test.json

{"data": [], "directed": false, "multigraph": false, "elements": {"nodes": [{"data": {"domainIds": "entrez.65220", "primaryDomainId": "entrez.65220", "geneType": "protein-coding", "displayName": "NAD kinase", "synonyms": "NAD kinase, poly(P)/ATP NAD kinase", "chromosome": "1", "description": "NAD kinase", "approvedSymbol": "NADK", "type": "Gene", "symbols": "dJ283E3.1", "mapLocation": "1p36.33", "graphics": {"fill": "#FFB6C1"}, "name": "NADK", "id": "entrez.65220", "value": "entrez.65220"}}, {"data": {"domainIds": "uniprot.Q6PJ22", "sequence": "GTRVVLRSRLKVRVVKELRGKKTAVHNGLGENGSQAAGLDMDVGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMIHPNVPAIMITPICPHSLSFRPIVVPAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVRDPVSDWFESLAQCLHWNVRKKQAHFEEEEEEEEEEG", "primaryDomainId": "uniprot.Q6PJ22", "displayName": "Q6PJ22_HUMAN", "synonyms": "FLJ13052 protein {ECO:0000313, EMBL:AAH24219.1}", "taxid": 9606, "geneName": "FLJ13052", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q6PJ22", "id": "uniprot.Q6PJ22", "value": "uniprot.Q6PJ22"}}, {"data": {"domainIds": "uniprot.A0A0A0MR98", "sequence": "MGRPRVRQAWPGCCGHTGRLPAGRGYLASHMCDPAGAELIGDGMSDPTPPSNACTGHIQDPASQRLTWNKSPKSVLVIKKMRDASLLQPFKELCTHLMEENMIVYVEKKVLEDPAIASDESFGAVKKKFCTFREDYDDISNQIDFIICLGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFSFENFQSQVTQVIEGNAAVVLRSRLKVRVVKELRGKKTAVHNGLGENGSQAAGLDMDVGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMIHPNVPAIMITPICPHSLSFRPIVVPAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVRDPVSDWFESLAQCLHWNVRKKQAHFEEEEEEEEEG", "primaryDomainId": "uniprot.A0A0A0MR98", "displayName": "A0A0A0MR98_HUMAN", "synonyms": "NAD kinase {ECO:0000313, Ensembl:ENSP00000339727}", "taxid": 9606, "geneName": "NADK", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A0A0MR98", "id": "uniprot.A0A0A0MR98", "value": "uniprot.A0A0A0MR98"}}, {"data": {"domainIds": "uniprot.A0A024R058", "sequence": "MEMEQEKMTMNKELSPDAAAYCCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFRRTRSLHGPCPVTTFGPKACVLQNPQTIMHIQDPASQRLTWNKSPKSVLVIKKMRDASLLQPFKELCTHLMEENMIVYVEKKVLEDPAIASDESFGAVKKKFCTFREDYDDISNQIDFIICLGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFSFENFQSQVTQVIEGNAAVVLRSRLKVRVVKELRGKKTAVHNGLGENGSQAAGLDMDVGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMIHPNVPAIMITPICPHSLSFRPIVVPAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVRDPVSDWFESLAQCLHWNVRKKQAHFEEEEEEEEEG", "primaryDomainId": "uniprot.A0A024R058", "displayName": "A0A024R058_HUMAN", "synonyms": "NAD kinase, isoform CRA_a {ECO:0000313, EMBL:EAW56155.1}", "taxid": 9606, "geneName": "NADK", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R058", "id": "uniprot.A0A024R058", "value": "uniprot.A0A024R058"}}, {"data": {"domainIds": "uniprot.O95544", "sequence": "MEMEQEKMTMNKELSPDAAAYCCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFRRTRSLHGPCPVTTFGPKACVLQNPQTIMHIQDPASQRLTWNKSPKSVLVIKKMRDASLLQPFKELCTHLMEENMIVYVEKKVLEDPAIASDESFGAVKKKFCTFREDYDDISNQIDFIICLGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFSFENFQSQVTQVIEGNAAVVLRSRLKVRVVKELRGKKTAVHNGLGENGSQAAGLDMDVGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMIHPNVPAIMITPICPHSLSFRPIVVPAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVRDPVSDWFESLAQCLHWNVRKKQAHFEEEEEEEEEG", "comments": "CATALYTIC ACTIVITY: Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,   ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,   ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;   Evidence={ECO:0000269|PubMed:11594753};\nCOFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;   Evidence={ECO:0000269|PubMed:11594753};\nBIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters:   KM=3.3 mM for ATP {ECO:0000269|PubMed:11594753};   KM=0.54 mM for NAD {ECO:0000269|PubMed:11594753};   Vmax=6.7 umol/min/mg enzyme {ECO:0000269|PubMed:11594753}; pH dependence:   Optimum pH is 7.5. {ECO:0000269|PubMed:11594753}; Temperature dependence:   Optimum temperature is 55 degrees Celsius.   {ECO:0000269|PubMed:11594753};\nINTERACTION: Q8TBB1:LNX1; NbExp=3; IntAct=EBI-743949, EBI-739832; O00560:SDCBP; NbExp=5; IntAct=EBI-743949, EBI-727004; P63104:YWHAZ; NbExp=2; IntAct=EBI-743949, EBI-347088;\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=O95544-1; Sequence=Displayed; Name=2;   IsoId=O95544-2; Sequence=VSP_047313, VSP_047314; Name=3;   IsoId=O95544-3; Sequence=VSP_047312;\nTISSUE SPECIFICITY: Widely expressed but not detected in skeletal muscle. {ECO:0000269|PubMed:11594753}.\nSIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.", "primaryDomainId": "uniprot.O95544", "displayName": "NADK_HUMAN", "synonyms": "NAD kinase, 2.7.1.23, Poly(P)/ATP NAD kinase", "taxid": 9606, "geneName": "NADK", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O95544", "id": "uniprot.O95544", "value": "uniprot.O95544"}}, {"data": {"domainIds": "entrez.8450", "primaryDomainId": "entrez.8450", "geneType": "protein-coding", "displayName": "cullin 4B", "synonyms": "cullin-4B", "chromosome": "X", "description": "cullin 4B", "approvedSymbol": "CUL4B", "type": "Gene", "symbols": "CUL-4B, MRXHF2, MRXS15, MRXSC, SFM2", "mapLocation": "Xq24", "graphics": {"fill": "#FFB6C1"}, "name": "CUL4B", "id": "entrez.8450", "value": "entrez.8450"}}, {"data": {"domainIds": "uniprot.K4DI93", "sequence": "MKSVCPVTSGFSSPSPSAAAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSNSSNEREDFDSTSSSSSTPPLQPRDSASPSTSSFCLGVSVAASSHVPIQKKLRFEDTLEFVGFDAKMAEESSSSSSSSSPTAATSQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA", "comments": "SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE- ProRule:PRU00330, ECO:0000256|RuleBase:RU003829, ECO:0000256|SAAS:SAAS00585788}.", "primaryDomainId": "uniprot.K4DI93", "displayName": "K4DI93_HUMAN", "synonyms": "Cullin 4B, isoform CRA_e {ECO:0000313, EMBL:EAX11880.1}, Cullin-4B {ECO:0000313, Ensembl:ENSP00000338919}", "taxid": 9606, "geneName": "CUL4B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "K4DI93", "id": "uniprot.K4DI93", "value": "uniprot.K4DI93"}}, {"data": {"domainIds": "uniprot.Q13620", "sequence": "MMSQSSGSGDGNDDEATTSKDGGFSSPSPSAAAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSNSSNEREDFDSTSSSSSTPPLQPRDSASPSTSSFCLGVSVAASSHVPIQKKLRFEDTLEFVGFDAKMAEESSSSSSSSSPTAATSQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA", "comments": "FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of- rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8. With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:16322693, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18235224, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544, ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:26711351}.\nPATHWAY: Protein modification; protein ubiquitination.\nSUBUNIT: Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin- protein ligase complexes that seem to be formed of DDB1, CUL4A or CUL4B, RBX1 and a variable substrate recognition component which seems to belong to a protein family described as DCAF (Ddb1- and Cul4- associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Component of the DCX(DTL) complex with the putative substrate recognition component DTL. Component of the DCX(DDB2) complex with the putative substrate recognition component DDB2. Part of a complex with RBX1 and TIP120A/CAND1. Interacts with RBX1 GRWD1, MLST8, SMU1, TLE2, TLE3, DCAF1, DDA1, DCAF6, DCAF17, DDB2, DCAF8, TIP120A/CAND1 and TMEM113. Interacts with cyclin E and with importins alpha-1 (KPNA2), alpha-3 (KPNA4), alpha-5 (KPNA1) and beta-1 (KPNB1). May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76 and WDR5. {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:16322693, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:18235224, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544, ECO:0000269|PubMed:22118460}.\nINTERACTION: Q86VP6:CAND1; NbExp=5; IntAct=EBI-456067, EBI-456077; Q16543:CDC37; NbExp=2; IntAct=EBI-456067, EBI-295634; Q16531:DDB1; NbExp=17; IntAct=EBI-456067, EBI-350322; P62877:RBX1; NbExp=5; IntAct=EBI-456067, EBI-398523; O94888:UBXN7; NbExp=3; IntAct=EBI-456067, EBI-1993627; Q9H898-2:ZMAT4; NbExp=3; IntAct=EBI-456067, EBI-11529334;\nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q13620-2; Sequence=Displayed; Name=2;   IsoId=Q13620-1; Sequence=VSP_039085; Name=3;   IsoId=Q13620-3; Sequence=VSP_039084, VSP_039086;\nPTM: Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. {ECO:0000269|PubMed:10597293}.\nDISEASE: Mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:300354]: A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span. {ECO:0000269|PubMed:17236139, ECO:0000269|PubMed:17273978, ECO:0000269|PubMed:19377476, ECO:0000269|PubMed:20002452}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE- ProRule:PRU00330}.\nSEQUENCE CAUTION: Sequence=AAB67315.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=AAK16812.1; Type=Frameshift; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q13620", "displayName": "CUL4B_HUMAN", "synonyms": "Cullin-4B, CUL-4B", "taxid": 9606, "geneName": "CUL4B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q13620", "id": "uniprot.Q13620", "value": "uniprot.Q13620"}}, {"data": {"domainIds": "entrez.3383", "primaryDomainId": "entrez.3383", "geneType": "protein-coding", "displayName": "intercellular adhesion molecule 1", "synonyms": "intercellular adhesion molecule 1, ICAM-1, cell surface glycoprotein P3.58, epididymis secretory sperm binding protein, intercellular adhesion molecule 1 (CD54), human rhinovirus receptor, major group rhinovirus receptor", "chromosome": "19", "description": "intercellular adhesion molecule 1", "approvedSymbol": "ICAM1", "type": "Gene", "symbols": "BB2, CD54, P3.58", "mapLocation": "19p13.2", "graphics": {"fill": "#FFB6C1"}, "name": "ICAM1", "id": "entrez.3383", "value": "entrez.3383"}}, {"data": {"domainIds": "uniprot.A0A384MEK5", "sequence": "MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP", "primaryDomainId": "uniprot.A0A384MEK5", "displayName": "A0A384MEK5_HUMAN", "synonyms": "Epididymis secretory sperm binding protein {ECO:0000313, EMBL:ADO22559.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A384MEK5", "id": "uniprot.A0A384MEK5", "value": "uniprot.A0A384MEK5"}}, {"data": {"domainIds": "uniprot.P05362", "sequence": "MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP", "comments": "FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:17875742}.\nFUNCTION: (Microbial infection) Acts as a receptor for major receptor group rhinovirus A-B capsid proteins. {ECO:0000269|PubMed:1968231, ECO:0000269|PubMed:2538243}.\nFUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus A21 capsid proteins. {ECO:0000269|PubMed:11160747, ECO:0000269|PubMed:16004874, ECO:0000269|PubMed:9539703}.\nFUNCTION: (Microbial infection) Upon Kaposi's sarcoma-associated herpesvirus/HHV-8 infection, is degraded by viral E3 ubiquitin ligase MIR2, presumably to prevent lysis of infected cells by cytotoxic T- lymphocytes and NK cell. {ECO:0000269|PubMed:11413168}.\nSUBUNIT: Homodimer (Probable). Interacts with MUC1 and promotes cell aggregation in epithelial cells. Interacts with ARHGEF26/SGEF. Interacts (on T cell side) with CD81, CD247 and CD9 at immunological synapses between antigen-presenting cells and T cells. {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:15099525, ECO:0000269|PubMed:17875742, ECO:0000269|PubMed:23858057, ECO:0000305}.\nSUBUNIT: (Microbial infection) Interacts with major receptor group rhinovirus A-B capsid proteins (PubMed:1968231, PubMed:2538243). {ECO:0000269|PubMed:1968231, ECO:0000269|PubMed:2538243}.\nSUBUNIT: (Microbial infection) Interacts with Coxsackievirus A21 capsid proteins (PubMed:11160747, PubMed:16004874, PubMed:9539703). {ECO:0000269|PubMed:11160747, ECO:0000269|PubMed:16004874, ECO:0000269|PubMed:9539703}.\nINTERACTION: P20701:ITGAL; NbExp=2; IntAct=EBI-1035358, EBI-961214;\nSUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.\nPTM: Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis.\nPOLYMORPHISM: Homozygotes with ICAM1-Kalifi Met-56 seem to have an increased risk for cerebral malaria [MIM:611162]. {ECO:0000269|PubMed:9259284}.\nSIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family. {ECO:0000305}.\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/ICAM1ID40909ch19p13.html\";\nWEB RESOURCE: Name=Wikipedia; Note=Intercellular adhesion molecule entry; URL=\"https://en.wikipedia.org/wiki/Intercellular_adhesion_molecule\";\nWEB RESOURCE: Name=SeattleSNPs; URL=\"http://pga.gs.washington.edu/data/icam1/\";\nWEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid structure; URL=\"http://viperdb.scripps.edu/info_page.php?VDB=1z7z\";\nWEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=ICAM-1; URL=\"http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_261\";", "primaryDomainId": "uniprot.P05362", "displayName": "ICAM1_HUMAN", "synonyms": "Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54", "taxid": 9606, "geneName": "ICAM1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P05362", "id": "uniprot.P05362", "value": "uniprot.P05362"}}, {"data": {"domainIds": "entrez.5711", "primaryDomainId": "entrez.5711", "geneType": "protein-coding", "displayName": "proteasome 26S subunit, non-ATPase 5", "synonyms": "26S proteasome non-ATPase regulatory subunit 5, 26S protease subunit S5 basic, 26S proteasome subunit S5B, proteasome (prosome, macropain) 26S subunit, non-ATPase, 5", "chromosome": "9", "description": "proteasome 26S subunit, non-ATPase 5", "approvedSymbol": "PSMD5", "type": "Gene", "symbols": "S5B", "mapLocation": "9q33.2", "graphics": {"fill": "#FFB6C1"}, "name": "PSMD5", "id": "entrez.5711", "value": "entrez.5711"}}, {"data": {"domainIds": "uniprot.Q16401", "sequence": "MAAQALALLREVARLEAPLEELRALHSVLQAVPLNELRQQAAELRLGPLFSLLNENHREKTTLCVSILERLLQAMEPVHVARNLRVDLQRGLIHPDDSVKILTLSQIGRIVENSDAVTEILNNAELLKQIVYCIGGENLSVAKAAIKSLSRISLTQAGLEALFESNLLDDLKSVMKTNDIVRYRVYELIIEISSVSPESLNYCTTSGLVTQLLRELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSSFYLPGFVKFFGNLAVMDSPQQICERYPIFVEKVFEMIESQDPTMIGVAVDTVGILGSNVEGKQVLQKTGTRFERLLMRIGHQSKNAPVELKIRCLDAISSLLYLPPEQQTDDLLRMTESWFSSLSRDPLELFRGISSQPFPELHCAALKVFTAIANQPWAQKLMFNSPGFVEYVVDRSVEHDKASKDAKYELVKALANSKTIAEIFGNPNYLRLRTYLSEGPYYVKPVSTTAVEGAE", "comments": "FUNCTION: 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. {ECO:0000269|PubMed:19412159, ECO:0000269|PubMed:19490896}.\nSUBUNIT: 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. {ECO:0000269|PubMed:19217412, ECO:0000269|PubMed:19412159, ECO:0000269|PubMed:19490896}.\nINTERACTION: P62191:PSMC1; NbExp=10; IntAct=EBI-752143, EBI-357598; P35998:PSMC2; NbExp=21; IntAct=EBI-752143, EBI-359710; Q12800:TFCP2; NbExp=3; IntAct=EBI-752143, EBI-717422;\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q16401-1; Sequence=Displayed; Name=2;   IsoId=Q16401-2; Sequence=VSP_045176;\nDOMAIN: Rich in dileucine repeats, which have been implicated in trafficking of a variety of transmembrane proteins.\nSIMILARITY: Belongs to the proteasome subunit S5B/HSM3 family. {ECO:0000305}.\nCAUTION: Was initially identified as a genuine component of the 26S proteasome. {ECO:0000305}.", "primaryDomainId": "uniprot.Q16401", "displayName": "PSMD5_HUMAN", "synonyms": "26S proteasome non-ATPase regulatory subunit 5, 26S protease subunit S5 basic, 26S proteasome subunit S5B", "taxid": 9606, "geneName": "PSMD5", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q16401", "id": "uniprot.Q16401", "value": "uniprot.Q16401"}}, {"data": {"domainIds": "entrez.144100", "primaryDomainId": "entrez.144100", "geneType": "protein-coding", "displayName": "pleckstrin homology domain containing A7", "synonyms": "pleckstrin homology domain-containing family A member 7, PH domain-containing family A member 7, pleckstrin homology domain containing, family A member 2, pleckstrin homology domain containing, family A member 7, pleckstrin homology domain-containing family A member 6", "chromosome": "11", "description": "pleckstrin homology domain containing A7", "approvedSymbol": "PLEKHA7", "type": "Gene", "symbols": "-", "mapLocation": "11p15.2-p15.1", "graphics": {"fill": "#FFB6C1"}, "name": "PLEKHA7", "id": "entrez.144100", "value": "entrez.144100"}}, {"data": {"domainIds": "uniprot.E9PKC0", "sequence": "MAAATVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRTGEPVNSGHMIRSDLPRGWEEGFTEEGASYFIDHNQQTTAFRHPVTGQFSPENSEFILQEEPNPHMSKQDRNQRPSSMVSETSTAGTASTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNPNVPVVVRGWLHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKYSFKAVHTGMRALIYNSSTAGSQAEQSGMRTYYFSADTQEDMNAWVRAMNQAAQVLSRSSLKRDMEKVERQAVPQANHTESCHECGRVGPGHTRDCPHRGHDDIVNFERQEQEGEQYRSQRDPLEGKRDRSKARSPYSPAEEDALFMDLPTGPRGQQAQPQRAEKNGMLPASYGPGEQNGTGGYQRAFPPRTNPEKHSQRKSNLAQVEHWARAQKGDSRSLPLDQTLPRQGPGQSLSFPENYQTLPKSTRHPSGGSSPPPRNLPSDYKYAQDRASHLKMSSEERRAHRDGTVWQLYEWQQRQQFRHGSPTAPICLGSPEFTDQGRSRSMLEVPRSISVPPSPSDIPPPGPPRVFPPRRPHTPAERVTVKPPDQRRSVDISLGDSPRRARGHAVKNSSHVDRRSMPSMGYMTHTVSAPSLHGKSADDTYLQLKKDLEYLDLKMTGRDLLKDRSLKPVKIAESDTDVKLSIFCEQDRVLQDLEDKIRALKENKDQLESVLEVLHRQMEQYRDQPQHLEKIAYQQKLLQEDLVHIRAELSRESTEMENAWNEYLKLENDVEQLKQTLQEQHRRAFFFQEKSQIQKDLWRIEDVTAGLSANKENFRILVESVKNPERKTVPLFPHPPVPSLSTSESKPPPQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVTSPLQSPTKAKPKVEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDRELGQCVNGDSRVELRSYVSEPELATLSGDMAQPSLGLVGPESRYQTLPGRGLSGSTSRLQQSSTIAPYVTLRRGLNAESSKATFPRPKSALERLYSGDHQRGKMSAEEQLERMKRHQKALVRERKRTLGQGERTGLPSSRYLSRPLPGDLGSWKREQDFDLQLLERVVQGEKKDKEENGWLKVQAMPVTELDLEPQDYDLDISRELSKPEKVSIPERYVELDPEEPPSLEELQARYRKAEKIRNILARSSMCNLQPTSGQDQNSVADLDLQLQEQERIINISYALASEASQRSKQVAAQAVTDP", "primaryDomainId": "uniprot.E9PKC0", "displayName": "E9PKC0_HUMAN", "synonyms": "Pleckstrin homology domain-containing family A member 7 {ECO:0000313, Ensembl:ENSP00000435389}", "taxid": 9606, "geneName": "PLEKHA7", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "E9PKC0", "id": "uniprot.E9PKC0", "value": "uniprot.E9PKC0"}}, {"data": {"domainIds": "uniprot.Q6IQ23", "sequence": "MAAATVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRTGEPVNSGHMIRSDLPRGWEEGFTEEGASYFIDHNQQTTAFRHPVTGQFSPENSEFILQEEPNPHMSKQDRNQRPSSMVSETSTAGTASTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNPNVPVVVRGWLHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKYSFKAVHTGMRALIYNSSTAGSQAEQSGMRTYYFSADTQEDMNAWVRAMNQAAQVLSRSSLKRDMEKVERQAVPQANHTESCHECGRVGPGHTRDCPHRGHDDIVNFERQEQEGEQYRSQRDPLEGKRDRSKARSPYSPAEEDALFMDLPTGPRGQQAQPQRAEKNGMLPASYGPGEQNGTGGYQRAFPPRTNPEKHSQRKSNLAQVEHWARAQKGDSRSLPLDQTLPRQGPGQSLSFPENYQTLPKSTRHPSGGSSPPPRNLPSDYKYAQDRASHLKMSSEERRAHRDGTVWQLYEWQQRQQFRHGSPTAPICLGSPEFTDQGRSRSMLEVPRSISVPPSPSDIPPPGPPRVFPPRRPHTPAERVTVKPPDQRRSVDISLGDSPRRARGHAVKNSSHVDRRSMPSMGYMTHTVSAPSLHGKSADDTYLQLKKDLEYLDLKMTGRDLLKDRSLKPVKIAESDTDVKLSIFCEQDRVLQDLEDKIRALKENKDQLESVLEVLHRQMEQYRDQPQHLEKIAYQQKLLQEDLVHIRAELSRESTEMENAWNEYLKLENDVEQLKQTLQEQHRRAFFFQEKSQIQKDLWRIEDVTAGLSANKENFRILVESVKNPERKTVPLFPHPPVPSLSTSESKPPPQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVTSPLQSPTKAKPKVEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDRELGQCVNGDSRVELRSYVSEPELATLSGDMAQPSLGLVGPESRYQTLPGRGLSGSTSRLQQSSTIAPYVTLRRGLNAESSKATFPRPKSALERLYSGDHQRGKMSAEEQLERMKRHQKALVRERKRTLGQGERTGLPSSRYLSRPLPGDLGSVC", "comments": "FUNCTION: Required for zonula adherens biogenesis and maintenance (PubMed:19041755). Acts via its interaction with CAMSAP3, which anchors microtubules at their minus-ends to zonula adherens, leading to the recruitment of KIFC3 kinesin to the junctional site (PubMed:19041755). Mediates docking of ADAM10 to zonula adherens through a PDZD11- dependent interaction with the ADAM10-binding protein TSPAN33 (PubMed:30463011). {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:30463011}.\nSUBUNIT: Interacts with CAMSAP3 and CTNND1 (PubMed:19041755). Interacts (via WW domains) with TSPAN33 (via cytoplasmic domain) and with PDZD11; the interaction with TSPAN33 is dependent on PDZD11 being bound to PLEKHA7 and facilitates the docking of ADAM10 to zonula adherens through interaction of TSPAN33 with ADAM10 (PubMed:30463011). {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:30463011}.\nINTERACTION: Q9UKV8:AGO2; NbExp=7; IntAct=EBI-2125301, EBI-528269; O60716:CTNND1; NbExp=3; IntAct=EBI-2125301, EBI-701927;\nSUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:30463011}. Cytoplasm {ECO:0000269|PubMed:19041755}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19041755}. Note=Localizes to zonula adherens, recruited via its interaction with CTNND1. {ECO:0000269|PubMed:19041755}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q6IQ23-1; Sequence=Displayed; Name=2;   IsoId=Q6IQ23-2; Sequence=VSP_025592; Name=3;   IsoId=Q6IQ23-3; Sequence=VSP_039543, VSP_025592;\nSEQUENCE CAUTION: Sequence=AAH33239.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAG62985.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q6IQ23", "displayName": "PKHA7_HUMAN", "synonyms": "Pleckstrin homology domain-containing family A member 7, PH domain-containing family A member 7", "taxid": 9606, "geneName": "PLEKHA7", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q6IQ23", "id": "uniprot.Q6IQ23", "value": "uniprot.Q6IQ23"}}, {"data": {"domainIds": "entrez.64599", "primaryDomainId": "entrez.64599", "geneType": "protein-coding", "displayName": "GRB10 interacting GYF protein 1", "synonyms": "GRB10-interacting GYF protein 1, PERQ amino acid-rich with GYF domain-containing protein 1, postmeiotic segregation increased 2-like 12", "chromosome": "7", "description": "GRB10 interacting GYF protein 1", "approvedSymbol": "GIGYF1", "type": "Gene", "symbols": "GYF1, PERQ1", "mapLocation": "7q22.1", "graphics": {"fill": "#FFB6C1"}, "name": "GIGYF1", "id": "entrez.64599", "value": "entrez.64599"}}, {"data": {"domainIds": "uniprot.O75420", "sequence": "MAAETLNFGPEWLRALSGGGSVASPPPSPAMPKYKLADYRYGREEMLALYVKENKVPEELQDKEFAAVLQDEPLQPLALEPLTEEEQRNFSLSVNSVAVLRLMGKGAGPPLAGTSRGRGSTRSRGRGRGDSCFYQRSIEEGDGAFGRSPREIQRSQSWDDRGERRFEKSARRDGARCGFEEGGAGPRKEHARSDSENWRSLREEQEEEEEGSWRLGAGPRRDGDRWRSASPDGGPRSAGWREHGERRRKFEFDLRGDRGGCGEEEGRGGGGSSHLRRCRAPEGFEEDKDGLPEWCLDDEDEEMGTFDASGAFLPLKKGPKEPIPEEQELDFQGLEEEEEPSEGLEEEGPEAGGKELTPLPPQEEKSSSPSPLPTLGPLWGTNGDGDETAEKEPPAAEDDIRGIQLSPGVGSSAGPPGDLEDDEGLKHLQQEAEKLVASLQDSSLEEEQFTAAMQTQGLRHSAAATALPLSHGAARKWFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKRGCDEGFQPLGEVIKMWGRVPFAPGPSPPPLLGNMDQERLKKQQELAAAALYQQLQHQQFLQLVSSRQLPQCALREKAALGDLTPPPPPPPQQQQQQLTAFLQQLQALKPPRGGDQNLLPTMSRSLSVPDSGRLWDVHTSASSQSGGEASLWDIPINSSTQGPILEQLQLQHKFQERREVELRAKREEEERKRREEKRRQQQQEEQKRRQEEEELFRRKHVRQQELLLKLLQQQQAVPVPPAPSSPPPLWAGLAKQGLSMKTLLELQLEGERQLHKQPPPREPARAQAPNHRVQLGGLGTAPLNQWVSEAGPLWGGPDKSGGGSSGLGLWEDTPKSGGSLVRGLGLKNSRSSPSLSDSYSHLSGRPIRKKTEEEEKLLKLLQGIPRPQDGFTQWCEQMLHTLSATGSLDVPMAVAILKEVESPYDVHDYIRSCLGDTLEAKEFAKQFLERRAKQKASQQRQQQQEAWLSSASLQTAFQANHSTKLGPGEGSKAKRRALMLHSDPSILGYSLHGSSGEIESVDDY", "comments": "FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling. May increase IGF1 receptor phosphorylation under IGF1 stimulation as well as phosphorylation of IRS1 and SHC1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:12771153}.\nSUBUNIT: Interacts with GRB10. This transient binding is increased under IGF1 stimulation and leads to recruitment of GIGYF1/GRB10 complex to IGF1 receptor (By similarity). {ECO:0000250}.\nDOMAIN: The GYF domain interacts with GRB10. {ECO:0000250}.\nSIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAC78792.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=AAL55738.1; Type=Frameshift; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.O75420", "displayName": "GGYF1_HUMAN", "synonyms": "GRB10-interacting GYF protein 1, PERQ amino acid-rich with GYF domain-containing protein 1", "taxid": 9606, "geneName": "GIGYF1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O75420", "id": "uniprot.O75420", "value": "uniprot.O75420"}}, {"data": {"domainIds": "entrez.1499", "primaryDomainId": "entrez.1499", "geneType": "protein-coding", "displayName": "catenin beta 1", "synonyms": "catenin beta-1, catenin (cadherin-associated protein), beta 1, 88kDa", "chromosome": "3", "description": "catenin beta 1", "approvedSymbol": "CTNNB1", "type": "Gene", "symbols": "CTNNB, EVR7, MRD19, NEDSDV, armadillo", "mapLocation": "3p22.1", "graphics": {"fill": "#FFB6C1"}, "name": "CTNNB1", "id": "entrez.1499", "value": "entrez.1499"}}, {"data": {"domainIds": "uniprot.A0A024R2Q3", "sequence": "MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL", "primaryDomainId": "uniprot.A0A024R2Q3", "displayName": "A0A024R2Q3_HUMAN", "synonyms": "Catenin (Cadherin-associated protein), beta 1, 88kDa, isoform CRA_a {ECO:0000313, EMBL:EAW64628.1}", "taxid": 9606, "geneName": "CTNNB1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R2Q3", "id": "uniprot.A0A024R2Q3", "value": "uniprot.A0A024R2Q3"}}, {"data": {"domainIds": "uniprot.P35222", "sequence": "MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL", "comments": "FUNCTION: Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2- mediated sumoylation of PML (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22647378, PubMed:22699938, PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938}.\nSUBUNIT: Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E- cadherin:catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Another cytoplasmic pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts with GLIS2 and MUC1. Interacts with SLC30A9. Interacts with XIRP1. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with SCRIB. Interacts with RAPGEF2. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain). Interacts with EMD. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. Interacts with PTPRJ. Interacts with PKT7 and CDK2. Interacts with FAT1 (via the cytoplasmic domain). Interacts with NANOS1 and NDRG2. Interacts with isoform 1 of NEK2. Interacts with both isoform 1 and isoform 2 of CDK5. Interacts with PTK6. Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. Identified in a complex with HINT1 and MITF. Interacts with FHIT. The CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4). Interacts with FERMT2. Identified in a complex with TCF7L2/TCF4 and FERMT2. Interacts with RORA. May interact with P-cadherin/CDH3. Interacts with RNF220 (PubMed:25266658). Interacts with CTNND2 (PubMed:25807484). Interacts (via the C-terminal region) with CBY1 (PubMed:12712206, PubMed:16424001). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (PubMed:25169422). Interacts with DLG5 (By similarity). Interacts with FAM53B; promoting translocation to the nucleus (PubMed:25183871). Interacts with TMEM170B (PubMed:29367600). Interacts with AHI1 (PubMed:21623382). Interacts with GID8 (PubMed:28829046). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha- catenin/CTNNA1 and p120 catenin/CTNND1 (PubMed:28051089). Forms a complex comprising APPL1, RUVBL2, APPL2, HDAC1 and HDAC2 (PubMed:19433865). Interacts with IRF2BPL; mediates the ubiquitination and degradation of CTNNB1 (PubMed:29374064). Interacts with AMFR (By similarity). Interacts with LMBR1L (PubMed:31073040). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11279024, ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:11389840, ECO:0000269|PubMed:11590244, ECO:0000269|PubMed:11713475, ECO:0000269|PubMed:11713476, ECO:0000269|PubMed:11751639, ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12408824, ECO:0000269|PubMed:12420223, ECO:0000269|PubMed:12501215, ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:12830000, ECO:0000269|PubMed:14595118, ECO:0000269|PubMed:16424001, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:17052462, ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18378692, ECO:0000269|PubMed:18819930, ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:19693690, ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:19996314, ECO:0000269|PubMed:20026641, ECO:0000269|PubMed:20164195, ECO:0000269|PubMed:21132015, ECO:0000269|PubMed:21247902, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:21623382, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:25183871, ECO:0000269|PubMed:25266658, ECO:0000269|PubMed:25807484, ECO:0000269|PubMed:28051089, ECO:0000269|PubMed:28829046, ECO:0000269|PubMed:29367600, ECO:0000269|PubMed:29374064, ECO:0000269|PubMed:29432739, ECO:0000269|PubMed:7982500, ECO:0000305|PubMed:31073040}.\nSUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein vPK; this interaction inhibits the Wnt signaling pathway. {ECO:0000269|PubMed:29432739}.\nINTERACTION: P00519:ABL1; NbExp=2; IntAct=EBI-491549, EBI-375543; O43707:ACTN4; NbExp=7; IntAct=EBI-491549, EBI-351526; Q5JTC6:AMER1; NbExp=9; IntAct=EBI-491549, EBI-6169747; P25054:APC; NbExp=19; IntAct=EBI-491549, EBI-727707; P10275:AR; NbExp=11; IntAct=EBI-491549, EBI-608057; O15169:AXIN1; NbExp=44; IntAct=EBI-491549, EBI-710484; O35625:Axin1 (xeno); NbExp=4; IntAct=EBI-491549, EBI-2365912; Q9YGY0:axin1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-1037449; Q9Y2T1:AXIN2; NbExp=2; IntAct=EBI-491549, EBI-4400025; O00512:BCL9; NbExp=2; IntAct=EBI-491549, EBI-533127; A1Z199:BCR/ABL fusion; NbExp=2; IntAct=EBI-491549, EBI-7286259; Q9Y297:BTRC; NbExp=8; IntAct=EBI-491549, EBI-307461; P33724:CAV1 (xeno); NbExp=5; IntAct=EBI-491549, EBI-79998; Q6P1J9:CDC73; NbExp=10; IntAct=EBI-491549, EBI-930143; P12830:CDH1; NbExp=14; IntAct=EBI-491549, EBI-727477; P19022:CDH2; NbExp=8; IntAct=EBI-491549, EBI-2256711; P33151:CDH5; NbExp=7; IntAct=EBI-491549, EBI-2903122; Q92793:CREBBP; NbExp=2; IntAct=EBI-491549, EBI-81215; P35221:CTNNA1; NbExp=3; IntAct=EBI-491549, EBI-701918; P26231:Ctnna1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-647895; Q9UI47:CTNNA3; NbExp=2; IntAct=EBI-491549, EBI-3937546; Q9NSA3:CTNNBIP1; NbExp=12; IntAct=EBI-491549, EBI-747082; Q9NYF0:DACT1; NbExp=3; IntAct=EBI-491549, EBI-3951744; P26358:DNMT1; NbExp=8; IntAct=EBI-491549, EBI-719459; P18146:EGR1; NbExp=7; IntAct=EBI-491549, EBI-2834611; P50402:EMD; NbExp=3; IntAct=EBI-491549, EBI-489887; P29317:EPHA2; NbExp=2; IntAct=EBI-491549, EBI-702104; Q9UKB1:FBXW11; NbExp=4; IntAct=EBI-491549, EBI-355189; Q96AC1:FERMT2; NbExp=13; IntAct=EBI-491549, EBI-4399465; P11362:FGFR1; NbExp=2; IntAct=EBI-491549, EBI-1028277; P49789:FHIT; NbExp=4; IntAct=EBI-491549, EBI-741760; P17948:FLT1; NbExp=2; IntAct=EBI-491549, EBI-1026718; Q08050:FOXM1; NbExp=16; IntAct=EBI-491549, EBI-866480; Q9BZE0:GLIS2; NbExp=6; IntAct=EBI-491549, EBI-7251368; P49841:GSK3B; NbExp=19; IntAct=EBI-491549, EBI-373586; Q9UBN7:HDAC6; NbExp=4; IntAct=EBI-491549, EBI-301697; Q16665:HIF1A; NbExp=4; IntAct=EBI-491549, EBI-447269; P42858:HTT; NbExp=5; IntAct=EBI-491549, EBI-466029; P08069:IGF1R; NbExp=3; IntAct=EBI-491549, EBI-475981; P18012:ipaC (xeno); NbExp=4; IntAct=EBI-491549, EBI-491541; P46940:IQGAP1; NbExp=3; IntAct=EBI-491549, EBI-297509; O75564:JRK; NbExp=3; IntAct=EBI-491549, EBI-8607681; P14923:JUP; NbExp=3; IntAct=EBI-491549, EBI-702484; Q14678:KANK1; NbExp=2; IntAct=EBI-491549, EBI-2556221; Q2LD37:KIAA1109; NbExp=2; IntAct=EBI-491549, EBI-2683809; Q9UJU2:LEF1; NbExp=10; IntAct=EBI-491549, EBI-926131; P27782:Lef1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-984464; Q8WVC0:LEO1; NbExp=2; IntAct=EBI-491549, EBI-932432; Q9JHQ5:Lztfl1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-6142879; Q9GZQ8:MAP1LC3B; NbExp=5; IntAct=EBI-491549, EBI-373144; P55197:MLLT10; NbExp=4; IntAct=EBI-491549, EBI-1104952; Q92597:NDRG1; NbExp=3; IntAct=EBI-491549, EBI-716486; P19838:NFKB1; NbExp=3; IntAct=EBI-491549, EBI-300010; P29474:NOS3; NbExp=4; IntAct=EBI-491549, EBI-1391623; O00482-1:NR5A2; NbExp=5; IntAct=EBI-491549, EBI-15960777; P49757:NUMB; NbExp=2; IntAct=EBI-491549, EBI-915016; P49757-3:NUMB; NbExp=3; IntAct=EBI-491549, EBI-10692196; Q8TEW0:PARD3; NbExp=2; IntAct=EBI-491549, EBI-81968; P16284:PECAM1; NbExp=3; IntAct=EBI-491549, EBI-716404; Q99697:PITX2; NbExp=2; IntAct=EBI-491549, EBI-1175211; P14618:PKM; NbExp=4; IntAct=EBI-491549, EBI-353408; P14618-1:PKM; NbExp=3; IntAct=EBI-491549, EBI-4304679; Q03431:PTH1R; NbExp=4; IntAct=EBI-491549, EBI-2860297; Q13308:PTK7; NbExp=5; IntAct=EBI-491549, EBI-2803245; P08575:PTPRC; NbExp=2; IntAct=EBI-491549, EBI-1341; P23470:PTPRG; NbExp=2; IntAct=EBI-491549, EBI-2258115; Q12913:PTPRJ; NbExp=2; IntAct=EBI-491549, EBI-2264500; P49023:PXN; NbExp=4; IntAct=EBI-491549, EBI-702209; Q04206:RELA; NbExp=3; IntAct=EBI-491549, EBI-73886; Q13761:RUNX3; NbExp=12; IntAct=EBI-491549, EBI-925990; Q9Y265:RUVBL1; NbExp=3; IntAct=EBI-491549, EBI-353675; Q01887:Ryk (xeno); NbExp=2; IntAct=EBI-491549, EBI-16110594; Q01826:SATB1; NbExp=9; IntAct=EBI-491549, EBI-743747; P63208:SKP1; NbExp=3; IntAct=EBI-491549, EBI-307486; Q9H6I2:SOX17; NbExp=2; IntAct=EBI-491549, EBI-9106753; P12931:SRC; NbExp=2; IntAct=EBI-491549, EBI-621482; P15884:TCF4; NbExp=22; IntAct=EBI-491549, EBI-533224; P36402:TCF7; NbExp=4; IntAct=EBI-491549, EBI-2119465; Q9NQB0:TCF7L2; NbExp=27; IntAct=EBI-491549, EBI-924724; O14746:TERT; NbExp=2; IntAct=EBI-491549, EBI-1772203; Q9UKE5:TNIK; NbExp=3; IntAct=EBI-491549, EBI-1051794; P11388:TOP2A; NbExp=5; IntAct=EBI-491549, EBI-539628; Q13625:TP53BP2; NbExp=5; IntAct=EBI-491549, EBI-77642; O95071:UBR5; NbExp=6; IntAct=EBI-491549, EBI-358329; Q9GZV5:WWTR1; NbExp=4; IntAct=EBI-491549, EBI-747743; Q9EPK5:Wwtr1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-1211920; P46937:YAP1; NbExp=13; IntAct=EBI-491549, EBI-1044059; P46937-3:YAP1; NbExp=2; IntAct=EBI-491549, EBI-6558686;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25183871}. Nucleus {ECO:0000269|PubMed:24342833, ECO:0000269|PubMed:25183871, ECO:0000269|PubMed:28829046, ECO:0000269|PubMed:29367600}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:B6V8E6}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q02248}. Cell junction {ECO:0000250|UniProtKB:B6V8E6}. Cell membrane {ECO:0000269|PubMed:24342833}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Cell junction, synapse {ECO:0000250|UniProtKB:Q02248}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q02248}. Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization. The majority of beta-catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Interaction with FAM53B promotes translocation to the nucleus (PubMed:25183871). {ECO:0000250|UniProtKB:B6V8E6, ECO:0000269|PubMed:25183871}.\nTISSUE SPECIFICITY: Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level). Expressed in breast cancer tissues (at protein level) (PubMed:29367600). {ECO:0000269|PubMed:11703283, ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:29367600}.\nPTM: Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription (By similarity). Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding. Phosphorylated on Ser-33 and Ser-37 by HIPK2 and GSK3B, this phosphorylation triggers proteasomal degradation (PubMed:25169422). Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization. Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11279024, ECO:0000269|PubMed:12027456, ECO:0000269|PubMed:12051714, ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:12640114, ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:20026641, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:25169422}.\nPTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity). {ECO:0000250}.\nPTM: S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions. {ECO:0000250|UniProtKB:Q02248}.\nPTM: O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1. {ECO:0000269|PubMed:24342833}.\nPTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000269|PubMed:24824780}.\nDISEASE: 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. {ECO:0000269|PubMed:9065402}. Note=The gene represented in this entry may be involved in disease pathogenesis.\nDISEASE: Note=Activating mutations in CTNNB1 have oncogenic activity resulting in tumor development. Somatic mutations are found in various tumor types, including colon cancers, ovarian and prostate carcinomas, hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant embryonal tumors mainly affecting young children in the first three years of life.\nDISEASE: Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor. {ECO:0000269|PubMed:10192393, ECO:0000269|PubMed:11703283, ECO:0000269|PubMed:12027456}. Note=The gene represented in this entry is involved in disease pathogenesis.\nDISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:10666372, ECO:0000269|PubMed:12027456}. Note=The gene represented in this entry may be involved in disease pathogenesis.\nDISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:10391090}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.\nDISEASE: Note=A chromosomal aberration involving CTNNB1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.\nDISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:11464291}. Note=The gene represented in this entry may be involved in disease pathogenesis.\nDISEASE: Neurodevelopmental disorder with spastic diplegia and visual defects (NEDSDV) [MIM:615075]: An autosomal dominant disorder characterized by global developmental delay, severe intellectual disability with absent or very limited speech, microcephaly, spasticity, and visual abnormalities. {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:25326669, ECO:0000269|PubMed:28514307}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Vitreoretinopathy, exudative 7 (EVR7) [MIM:617572]: A form of exudative vitreoretinopathy, 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. {ECO:0000269|PubMed:28575650}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAG35511.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; Sequence=BAB93475.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/CTNNB1ID71.html\";\nWEB RESOURCE: Name=NIEHS-SNPs; URL=\"http://egp.gs.washington.edu/data/ctnnb1/\";\nWEB RESOURCE: Name=Wikipedia; Note=Beta-catenin entry; URL=\"https://en.wikipedia.org/wiki/Beta-catenin\";", "primaryDomainId": "uniprot.P35222", "displayName": "CTNB1_HUMAN", "synonyms": "Catenin beta-1, Beta-catenin", "taxid": 9606, "geneName": "CTNNB1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P35222", "id": "uniprot.P35222", "value": "uniprot.P35222"}}, {"data": {"domainIds": "uniprot.B4DGU4", "sequence": "MELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL", "primaryDomainId": "uniprot.B4DGU4", "displayName": "B4DGU4_HUMAN", "synonyms": "Catenin beta-1 {ECO:0000313, Ensembl:ENSP00000411226}, cDNA FLJ57878, highly similar to Beta-catenin {ECO:0000313, EMBL:BAG57905.1}", "taxid": 9606, "geneName": "CTNNB1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DGU4", "id": "uniprot.B4DGU4", "value": "uniprot.B4DGU4"}}, {"data": {"domainIds": "entrez.57706", "primaryDomainId": "entrez.57706", "geneType": "protein-coding", "displayName": "DENN domain containing 1A", "synonyms": "DENN domain-containing protein 1A, DENN/MADD domain containing 1A, connecdenn 1", "chromosome": "9", "description": "DENN domain containing 1A", "approvedSymbol": "DENND1A", "type": "Gene", "symbols": "FAM31A, KIAA1608", "mapLocation": "9q33.3", "graphics": {"fill": "#FFB6C1"}, "name": "DENND1A", "id": "entrez.57706", "value": "entrez.57706"}}, {"data": {"domainIds": "uniprot.Q9HCG4", "sequence": "QQTEIRVLPLIFRSEELLLYLKENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITVHFGQVRPPRPHVVKRPKSNIAVEGRRTSVPSPEHLVKPLRHYAVFLSEDSSDDECQREEGPSSGFTESFFFSAPFEWPQPYRTLRESDSAEGDEAESPEQQVRKSTGPVPAPPDRAASIDLLEDVFSNLDMEAALQPLGQAKSLEDLRAPKDLREQPGTFDYQRLDLGGSERSRGVTVALKLTHPYNKLWSLGQDDMAIPSKPPAASPEKPSALLGNSLALPRRPQNRDSILNPSDKEEVPTPTLGSITIPRPQGRKTPELGIVPPPPIPRPAKLQAAGAALGDVSERLQTDRDRRAALSPGLLPGVVPQGPTELLQPLSPGPGAAGTSSDALLALLDPLSTAWSGSTLPSRPATPNVATPFTPQFSFPPAGTPTPFPQPPLNPFVPSMPAAPPTLPLVSTPAGPFGAPPASLGPAFASGLLLSSAGFCAPHRSQPNLSALSMPNLFGQMPMGTHTSPLQPLGPPAVAPSRIRTLPLARSSARAAETKQGLALRPGDPPLLPPRPPQGLEPTLQPSAPQQARDPFEDLLQKTKQDVSPSPALAPAPDSVEQLRKQWETFE", "primaryDomainId": "uniprot.Q9HCG4", "displayName": "Q9HCG4_HUMAN", "synonyms": "KIAA1608 protein {ECO:0000313, EMBL:BAB13434.2}", "taxid": 9606, "geneName": "KIAA1608", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9HCG4", "id": "uniprot.Q9HCG4", "value": "uniprot.Q9HCG4"}}, {"data": {"domainIds": "uniprot.Q8TEH3", "sequence": "MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLSSGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITVHFGQVRPPRPHVVKRPKSNIAVEGRRTSVPSPEQPQPYRTLRESDSAEGDEAESPEQQVRKSTGPVPAPPDRAASIDLLEDVFSNLDMEAALQPLGQAKSLEDLRAPKDLREQPGTFDYQRLDLGGSERSRGVTVALKLTHPYNKLWSLGQDDMAIPSKPPAASPEKPSALLGNSLALPRRPQNRDSILNPSDKEEVPTPTLGSITIPRPQGRKTPELGIVPPPPIPRPAKLQAAGAALGDVSERLQTDRDRRAALSPGLLPGVVPQGPTELLQPLSPGPGAAGTSSDALLALLDPLSTAWSGSTLPSRPATPNVATPFTPQFSFPPAGTPTPFPQPPLNPFVPSMPAAPPTLPLVSTPAGPFGAPPASLGPAFASGLLLSSAGFCAPHRSQPNLSALSMPNLFGQMPMGTHTSPLQPLGPPAVAPSRIRTLPLARSSARAAETKQGLALRPGDPPLLPPRPPQGLEPTLQPSAPQQARDPFEDLLQKTKQDVSPSPALAPAPDSVEQLRKQWETFE", "comments": "FUNCTION: Guanine nucleotide exchange factor (GEF) regulating clathrin- mediated endocytosis through RAB35 activation. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP- bound form. Regulates clathrin-mediated endocytosis of synaptic vesicles and mediates exit from early endosomes (PubMed:20154091, PubMed:20937701). Binds phosphatidylinositol-phosphates (PtdInsPs), with some preference for PtdIns(3)P (By similarity). {ECO:0000250|UniProtKB:Q8K382, ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}.\nACTIVITY REGULATION: The guanine nucleotide exchange factor (GEF) activity is autoinhibited. Autoinhibition may be the result of intramolecular interaction between the DENN domain and the C-terminus, which is disrupted upon phosphorylation. Activation is regulated by Akt activation. {ECO:0000269|PubMed:26055712}.\nSUBUNIT: Interacts with RAB35 (PubMed:20154091). Interacts with clathrin and with the adapter protein complex 2, AP-2 (PubMed:20154091, PubMed:20937701). Interacts with ITSN1 AND SH3GL2 (By similarity). Interacts (when phosphorylated) with YWHAE (PubMed:26055712). {ECO:0000250|UniProtKB:Q8K382, ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:26055712}.\nSUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}; Peripheral membrane protein {ECO:0000269|PubMed:20937701}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:20937701}. Note=Associates to membranes via lipid- binding activity. {ECO:0000250|UniProtKB:Q8K382}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=7; Name=1;   IsoId=Q8TEH3-1; Sequence=Displayed; Name=2;   IsoId=Q8TEH3-2; Sequence=VSP_019464, VSP_019465; Name=3;   IsoId=Q8TEH3-3; Sequence=VSP_034513, VSP_034514; Name=4;   IsoId=Q8TEH3-4; Sequence=VSP_034509, VSP_034512, VSP_034513,                            VSP_034514; Name=5;   IsoId=Q8TEH3-5; Sequence=VSP_034510, VSP_034511, VSP_019464,                            VSP_019465; Name=6;   IsoId=Q8TEH3-6; Sequence=VSP_034509, VSP_040666, VSP_040668; Name=7;   IsoId=Q8TEH3-7; Sequence=VSP_040667, VSP_040668;\nPTM: Phosphorylated on serine and/or threonine in an Akt-dependent manner. Phosphorylation probably regulates the guanine nucleotide exchange factor (GEF) activity, possibly by disrupting an intramolecular interaction between the DENN domain and the C-terminus of the protein, thereby relieving the autoinhibition. {ECO:0000269|PubMed:26055712}.\nDISEASE: Note=Genetic variants in DENND1A may play a role in susceptibility to polycystic ovary syndrome (PCOS), the most common endocrine disease among premenopausal women. PCOS is a complex disorder characterized by infertility, hirsutism, obesity, various menstrual disturbances, and enlarged ovaries studded with atretic follicles. {ECO:0000269|PubMed:22180642, ECO:0000269|PubMed:23208300, ECO:0000269|PubMed:24086769, ECO:0000269|PubMed:25626177}.\nSEQUENCE CAUTION: Sequence=AAH09616.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=AAH28061.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BAH13155.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q8TEH3", "displayName": "DEN1A_HUMAN", "synonyms": "DENN domain-containing protein 1A {ECO:0000312, HGNC:HGNC:29324}, Connecdenn 1 {ECO:0000303, PubMed:20154091}, Connecdenn {ECO:0000303, PubMed:20154091}, Protein FAM31A", "taxid": 9606, "geneName": "DENND1A", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q8TEH3", "id": "uniprot.Q8TEH3", "value": "uniprot.Q8TEH3"}}, {"data": {"domainIds": "entrez.93185", "primaryDomainId": "entrez.93185", "geneType": "protein-coding", "displayName": "immunoglobulin superfamily member 8", "synonyms": "immunoglobulin superfamily member 8, CD81 partner 3, glu-Trp-Ile EWI motif-containing protein 2, keratinocytes-associated transmembrane protein 4, prostaglandin regulatory-like protein", "chromosome": "1", "description": "immunoglobulin superfamily member 8", "approvedSymbol": "IGSF8", "type": "Gene", "symbols": "CD316, CD81P3, EWI-2, EWI2, KCT-4, LIR-D1, PGRL", "mapLocation": "1q23.2", "graphics": {"fill": "#FFB6C1"}, "name": "IGSF8", "id": "entrez.93185", "value": "entrez.93185"}}, {"data": {"domainIds": "uniprot.Q969P0", "sequence": "MGALRPTLLPPSLPLLLLLMLGMGCWAREVLVPEGPLYRVAGTAVSISCNVTGYEGPAQQNFEWFLYRPEAPDTALGIVSTKDTQFSYAVFKSRVVAGEVQVQRLQGDAVVLKIARLQAQDAGIYECHTPSTDTRYLGSYSGKVELRVLPDVLQVSAAPPGPRGRQAPTSPPRMTVHEGQELALGCLARTSTQKHTHLAVSFGRSVPEAPVGRSTLQEVVGIRSDLAVEAGAPYAERLAAGELRLGKEGTDRYRMVVGGAQAGDAGTYHCTAAEWIQDPDGSWAQIAEKRAVLAHVDVQTLSSQLAVTVGPGERRIGPGEPLELLCNVSGALPPAGRHAAYSVGWEMAPAGAPGPGRLVAQLDTEGVGSLGPGYEGRHIAMEKVASRTYRLRLEAARPGDAGTYRCLAKAYVRGSGTRLREAASARSRPLPVHVREEGVVLEAVAWLAGGTVYRGETASLLCNISVRGGPPGLRLAASWWVERPEDGELSSVPAQLVGGVGQDGVAELGVRPGGGPVSVELVGPRSHRLRLHSLGPEDEGVYHCAPSAWVQHADYSWYQAGSARSGPVTVYPYMHALDTLFVPLLVGTGVALVTGATVLGTITCCFMKRLRKR", "comments": "FUNCTION: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain. {ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:12750295, ECO:0000269|PubMed:12752121, ECO:0000269|PubMed:14662754, ECO:0000269|PubMed:15070678}.\nSUBUNIT: Interacts directly with CD82, CD81/tetraspanin-28 and CD9/tetraspanin-29. Also interacts with integrin alpha-3/beta-1 and integrin alpha-4/beta-1. {ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:12750295, ECO:0000269|PubMed:14662754, ECO:0000269|PubMed:15070678}.\nINTERACTION: P60372:KRTAP10-4; NbExp=3; IntAct=EBI-8293590, EBI-10178153; P60409:KRTAP10-7; NbExp=3; IntAct=EBI-8293590, EBI-10172290; P60410:KRTAP10-8; NbExp=5; IntAct=EBI-8293590, EBI-10171774; P60411:KRTAP10-9; NbExp=3; IntAct=EBI-8293590, EBI-10172052;\nSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q969P0-1; Sequence=Displayed; Name=2;   IsoId=Q969P0-2; Sequence=VSP_017429, VSP_017430; Name=3;   IsoId=Q969P0-3; Sequence=VSP_017431;\nTISSUE SPECIFICITY: Expressed in brain, kidney, testis, liver and placenta with moderate expression in all other tissues. Detected on a majority of B-cells, T-cells, and natural killer cells but not on monocytes, polynuclear cells and platelets. {ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:12708969, ECO:0000269|PubMed:12750295}.\nDOMAIN: The Ig-like C2-type domains 3 and 4 are required for interaction with CD81. {ECO:0000250}.\nDOMAIN: The short cytoplasmic domain is very basic, interacts with membrane PIPs, and mediates plasma membrane localization. {ECO:0000250}.\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/IGSF8ID45820ch1q23.html\";", "primaryDomainId": "uniprot.Q969P0", "displayName": "IGSF8_HUMAN", "synonyms": "Immunoglobulin superfamily member 8, IgSF8, CD81 partner 3, Glu-Trp-Ile EWI motif-containing protein 2, EWI-2, Keratinocytes-associated transmembrane protein 4, KCT-4, LIR-D1, Prostaglandin regulatory-like protein, PGRL, CD316", "taxid": 9606, "geneName": "IGSF8", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q969P0", "id": "uniprot.Q969P0", "value": "uniprot.Q969P0"}}, {"data": {"domainIds": "entrez.9462", "primaryDomainId": "entrez.9462", "geneType": "protein-coding", "displayName": "RAS protein activator like 2", "synonyms": "ras GTPase-activating protein nGAP, RASAL2/ACVR1 fusion, Ras protein activator like 1", "chromosome": "1", "description": "RAS protein activator like 2", "approvedSymbol": "RASAL2", "type": "Gene", "symbols": "NGAP", "mapLocation": "1q25.2", "graphics": {"fill": "#FFB6C1"}, "name": "RASAL2", "id": "entrez.9462", "value": "entrez.9462"}}, {"data": {"domainIds": "uniprot.A8K2P3", "sequence": "MQTPEVPAERSPRRRSISGTSTSEKPNSMDTANTSPFKVPGFFSKRLKGSIKRTKSQSKLDRNTSFRLPSPRSTDDRSRGLPKLKESRSHESLLSPCSTVECLDLGRGEPVSVKPLHSSILGQDFCFEVTYLSGSKCFSCNSASERDKWMENLRRTVQPNKDNCRRAENVLRLWIIEAKDLAPKKKYFCELCLDDTLFARTTSKTKADNIFWGEHFEFFSLPPLHSITVHIYKDVEKRKKKDKNNYVGLVNIPTASVTGRQFVEKWYPVSTPTPNKGKTGGPSIRIKSRFQTITILPMEQYKESAEFVTSNYTMLCSVLEPVISVRNKEELACALVHILQSTGRAKDFLTDLVMSEVDRCGEHDVLIFRENTIATKSIEEYLKLVGQQYLHDALGEFIKALYESDENCEVDPSKCSSSELIDHQSNLKMCCELAFCKIINSYCVFPRELKEVFASWKQQCLNRGKQDISERLISASLFLRFLCPAIMSPSLFNLMQEYPDDRTSRTLTLIAKVIQNLANFAKFGNKEEYMAFMNDFLEHEWGGMKRFLLEISNPDTISNTPGFDGYIDLGRELSVLHSLLWEVVSQLDKGENSFLQATVAKLGPLPRVLADITKSLTNPTPIQQQLRRFTEHNSSPNVSGSLSSGLQKIFEDPTDSDLHKLKSPSQDNTDSYFRGKTLLLVQQASSQSMTYSEKDERESSLPNGRSVSLMDLQDTHAAQVEHASVMLDVPIRLTGSQLSITQVASIKQLRETQSTPQSAPQVRRPLHPALNQPGGLQPLSFQNPVYHLNNPIPAMPKASIDSSLENLSTASSRSQSNSEDFKLSGPSNSSMEDFTKRSTQSEDFSRRHTVPDRHIPLALPRQNSTGQAQIRKVDQGGLGARAKAPPSLPHSASLRSTGSMSVVSAALVAEPVQNGSRSRQQSSSSRESPVPKVRAIQRQQTQQVQSPVDSATMSPVERTAAWVLNNGQYEEDVEETEQNLDEAKHAEKYE", "primaryDomainId": "uniprot.A8K2P3", "displayName": "A8K2P3_HUMAN", "synonyms": "cDNA FLJ77041, highly similar to Homo sapiens RAS protein activator like 2 (RASAL2), transcript variant 1, mRNA {ECO:0000313, EMBL:BAF82997.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A8K2P3", "id": "uniprot.A8K2P3", "value": "uniprot.A8K2P3"}}, {"data": {"domainIds": "uniprot.Q9UJF2", "sequence": "MQTPEVPAERSPRRRSISGTSTSEKPNSMDTANTSPFKVPGFFSKRLKGSIKRTKSQSKLDRNTSFRLPSLRSTDDRSRGLPKLKESRSHESLLSPCSTVECLDLGRGEPVSVKPLHSSILGQDFCFEVTYLSGSKCFSCNSASERDKWMENLRRTVQPNKDNCRRAENVLRLWIIEAKDLAPKKKYFCELCLDDTLFARTTSKTKADNIFWGEHFEFFSLPPLHSITVHIYKDVEKKKKKDKNNYVGLVNIPTASVTGRQFVEKWYPVSTPTPNKGKTGGPSIRIKSRFQTITILPMEQYKEFAEFVTSNYTMLCSVLEPVISVRNKEELACALVHILQSTGRAKDFLTDLVMSEVDRCGEHDVLIFRENTIATKSIEEYLKLVGQQYLHDALGEFIKALYESDENCEVDPSKCSSSELIDHQSNLKMCCELAFCKIINSYCVFPRELKEVFASWKQQCLNRGKQDISERLISASLFLRFLCPAIMSPSLFNLMQEYPDDRTSRTLTLIAKVIQNLANFAKFGNKEEYMAFMNDFLEHEWGGMKRFLLEISNPDTISNTPGFDGYIDLGRELSVLHSLLWEVVSQLDKGENSFLQATVAKLGPLPRVLADITKSLTNPTPIQQQLRRFTEHNSSPNVSGSLSSGLQKIFEDPTDSDLHKLKSPSQDNTDSYFRGKTLLLVQQASSQSMTYSEKDERESSLPNGRSVSLMDLQDTHAAQVEHASVMLDVPIRLTGSQLSITQVASIKQLRETQSTPQSAPQVRRPLHPALNQPGGLQPLSFQNPVYHLNNPIPAMPKASIDSSLENLSTASSRSQSNSEDFKLSGPSNSSMEDFTKRSTQSEDFSRRHTVPDRHIPLALPRQNSTGQAQIRKVDQGGLGARAKAPPSLPHSASLRSTGSMSVVSAALVAEPVQNGSRSRQQSSSSRESPVPKVRAIQRQQTQQVQSPVDSATMSPVERTAAWVLNNGQYEEDVEETEQNLDEAKHAEKYEQEITKLKERLRVSSRRLEEYERRLLVQEQQMQKLLLEYKARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDHAEMQAVIDAKQKIIDAQEKRIVSLDSANTRLMSALTQVKERYSMQVRNGISPTNPTKLSITENGEFKNSSC", "comments": "FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.\nINTERACTION: Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-359444, EBI-6863741; Q96PC5:MIA2; NbExp=3; IntAct=EBI-359444, EBI-1050253; Q13077:TRAF1; NbExp=3; IntAct=EBI-359444, EBI-359224; Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-359444, EBI-739895;\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q9UJF2-1; Sequence=Displayed; Name=2;   IsoId=Q9UJF2-2; Sequence=VSP_045777, VSP_045778;\nSEQUENCE CAUTION: Sequence=AAI10612.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9UJF2", "displayName": "NGAP_HUMAN", "synonyms": "Ras GTPase-activating protein nGAP, RAS protein activator-like 2", "taxid": 9606, "geneName": "RASAL2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9UJF2", "id": "uniprot.Q9UJF2", "value": "uniprot.Q9UJF2"}}, {"data": {"domainIds": "entrez.9644", "primaryDomainId": "entrez.9644", "geneType": "protein-coding", "displayName": "SH3 and PX domains 2A", "synonyms": "SH3 and PX domain-containing protein 2A, SH3 multiple domains 1, adapter protein TKS5, adaptor protein TKS5, five SH3 domain-containing protein, tyrosine kinase substrate with five SH3 domains", "chromosome": "10", "description": "SH3 and PX domains 2A", "approvedSymbol": "SH3PXD2A", "type": "Gene", "symbols": "FISH, SH3MD1, TKS5", "mapLocation": "10q24.33", "graphics": {"fill": "#FFB6C1"}, "name": "SH3PXD2A", "id": "entrez.9644", "value": "entrez.9644"}}, {"data": {"domainIds": "uniprot.B3KPL1", "sequence": "MQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDVNPPKEDYGSSKRKSVWLSSWAESPKKDVTGADATAEPMILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNGTRDDSDINTSKTGEEEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYLKKAKDDLPTRKKNLAGPVEIIGNIMEISNLLNKKASGDKETPPAEGEGHEAPIAKKEISLPILCNASNGSAVGVPDRTVSRLAQGSPAVARIAPQRAQISSPNLRTRPPPRRESSLGFQLPKPPEPPSVEVEYYTIAEFQSCISDGISFRGGQKAEVIDKNSGGWWYVQIGEKEGWAPASYIDKRKKPNLSRRTSTLTRPKVPPPAPPSKPKEAEEGPTWASESQDSPRKLKYEEPEYDIPAFGFDSEPELSEEPVEDRASGERRPAQPHRPSPASSLQRARFKVGESSEDVALEEETIYENEGFRPYAEDTLSARGSSGDSDSPGSSSLSLTRKNSPKSGSPKSSSLLKLKAEKNAQAEMGKNHSSASFSSSITINTTCCSSSSSSSSSLSKTSGDLKPRSASDAGIRGTPKVRAKKDADANAGLTSCPRAKPSVRPKPFLNRAESQSQEKMDISTLRRQLRPTGQLRGGLKGSKSEDSELPPQTASEAPSEGSRRSSSDLITLPATTPPCPTKKEWEGPATSYMTCSAYQKVQDSEISFPAGVEVQVLEKQESGWWYVRFGELEGWAPSHYLVLDENEQPDPSGKELDTVPAKGRQNEGKSDSLEKIERRVQALNTVNQSKKATPPIPSKPPGGFGKTSGTPAVKMRNGVRQVAVRPQSVFVSPPPKDNNLSCALRRNESLTATDGLRGVRRNSSFSTARSAAAEAKGRLAERAASQGSDSPLLPAQRNSIPVSPVRPKPIEKSQFIHNNLKDVYVSIADYEGDEETAGFQEGVSMEVLERNPNGWWYCQILDGVKPFKGWVPSNYLEKKN", "primaryDomainId": "uniprot.B3KPL1", "displayName": "B3KPL1_HUMAN", "synonyms": "cDNA FLJ31907 fis, clone NT2RP7004396, highly similar to Homo sapiens SH3 multiple domains 1 (SH3MD1), mRNA {ECO:0000313, EMBL:BAG51723.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B3KPL1", "id": "uniprot.B3KPL1", "value": "uniprot.B3KPL1"}}, {"data": {"domainIds": "uniprot.Q5TCZ1", "sequence": "MLAYCVQDATVVDVEKRRNPSKHYVYIINVTWSDSTSQTIYRRYSKFFDLQMQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDVNPPKEDYGSSKRKSVWLSSWAESPKKDVTGADATAEPMILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNGTRDDSDINTSKTGEVSKRRKAHLRRLDRRWTLGGMVNRQHSREEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYLKKAKDDLPTRKKNLAGPVEIIGNIMEISNLLNKKASGDKETPPAEGEGHEAPIAKKEISLPILCNASNGSAVGVPDRTVSRLAQGSPAVARIAPQRAQISSPNLRTRPPPRRESSLGFQLPKPPEPPSVEVEYYTIAEFQSCISDGISFRGGQKAEVIDKNSGGWWYVQIGEKEGWAPASYIDKRKKPNLSRRTSTLTRPKVPPPAPPSKPKEAEEGPTGASESQDSPRKLKYEEPEYDIPAFGFDSEPELSEEPVEDRASGERRPAQPHRPSPASSLQRARFKVGESSEDVALEEETIYENEGFRPYAEDTLSARGSSGDSDSPGSSSLSLTRKNSPKSGSPKSSSLLKLKAEKNAQAEMGKNHSSASFSSSITINTTCCSSSSSSSSSLSKTSGDLKPRSASDAGIRGTPKVRAKKDADANAGLTSCPRAKPSVRPKPFLNRAESQSQEKMDISTLRRQLRPTGQLRGGLKGSKSEDSELPPQTASEAPSEGSRRSSSDLITLPATTPPCPTKKEWEGPATSYMTCSAYQKVQDSEISFPAGVEVQVLEKQESGWWYVRFGELEGWAPSHYLVLDENEQPDPSGKELDTVPAKGRQNEGKSDSLEKIERRVQALNTVNQSKKATPPIPSKPPGGFGKTSGTPAVKMRNGVRQVAVRPQSVFVSPPPKDNNLSCALRRNESLTATDGLRGVRRNSSFSTARSAAAEAKGRLAERAASQGSDSPLLPAQRNSIPVSPVRPKPIEKSQFIHNNLKDVYVSIADYEGDEETAGFQEGVSMEVLERNPNGWWYCQILDGVKPFKGWVPSNYLEKKN", "comments": "FUNCTION: Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide. {ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15710328, ECO:0000269|PubMed:15710903, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497}.\nSUBUNIT: Interacts (via N-terminus) with CYBA (By similarity). Interacts with ADAM12, ADAM15 and ADAM19. Interacts with NOXO1. Interacts (via SH3 domains) with NOXA1. Interacts with FASLG. {ECO:0000250, ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15710903, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20609497}.\nINTERACTION: Q13444:ADAM15; NbExp=2; IntAct=EBI-2483234, EBI-77818; P21575:Dnm1 (xeno); NbExp=2; IntAct=EBI-7014859, EBI-80070; Q07889:SOS1; NbExp=5; IntAct=EBI-7014859, EBI-297487;\nSUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC- transformed cells.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q5TCZ1-1; Sequence=Displayed; Name=2;   IsoId=Q5TCZ1-2; Sequence=VSP_023312, VSP_023313; Name=3;   IsoId=Q5TCZ1-3; Sequence=VSP_023313;\nTISSUE SPECIFICITY: Found in several cancer cell lines, particularly invasive breast carcinomas and melanomas. {ECO:0000269|PubMed:15710328}.\nDOMAIN: The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By similarity). {ECO:0000250}.\nDOMAIN: The fifth SH3 domain mediates binding with ADAM12, ADAM15 and ADAM19. {ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15710328}.\nPTM: Tyrosine phosphorylated by SRC. Phosphorylation plays a regulatory role in the protein localization. The intramolecular interaction of the PX domain with the third SH3 domain maintains the protein in the cytoplasm and phosphorylation disrupts this interaction, resulting in the redistribution of the protein from cytoplasm to the perimembrane region. Phosphorylated on serine upon DNA damage, probably by ATM or ATR.\nMISCELLANEOUS: [Isoform 3]: and partial transcript data. {ECO:0000305}.\nSIMILARITY: Belongs to the SH3PXD2 family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=BAA24848.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q5TCZ1", "displayName": "SPD2A_HUMAN", "synonyms": "SH3 and PX domain-containing protein 2A, Adapter protein TKS5, Five SH3 domain-containing protein, SH3 multiple domains protein 1, Tyrosine kinase substrate with five SH3 domains", "taxid": 9606, "geneName": "SH3PXD2A", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q5TCZ1", "id": "uniprot.Q5TCZ1", "value": "uniprot.Q5TCZ1"}}, {"data": {"domainIds": "entrez.5093", "primaryDomainId": "entrez.5093", "geneType": "protein-coding", "displayName": "poly(rC) binding protein 1", "synonyms": "poly(rC)-binding protein 1, alpha-CP1, epididymis secretory protein Li 85, heterogeneous nuclear ribonucleoprotein E1, heterogenous nuclear ribonucleoprotein E1, heterogenous nuclear ribonucleoprotein X, nucleic acid-binding protein SUB2.3", "chromosome": "2", "description": "poly(rC) binding protein 1", "approvedSymbol": "PCBP1", "type": "Gene", "symbols": "HEL-S-85, HNRPE1, HNRPX, hnRNP-E1, hnRNP-X", "mapLocation": "2p13.3", "graphics": {"fill": "#FFB6C1"}, "name": "PCBP1", "id": "entrez.5093", "value": "entrez.5093"}}, {"data": {"domainIds": "uniprot.Q53SS8", "sequence": "MDAGVTESGLNVTLTIRLLMHGKEVGSIIGKKGESVKRIREESGARINISEGNCPERIITLTGPTNAIFKAFAMIIDKLEEDINSSMTNSTAASRPPVTLRLVVPATQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGVPQSVTECVKQICLVMLETLSQSPQGRVMTIPYQPMPASSPVICAGGQDRCSDAAGYPHATHDLEGPPLDAYSIQGQHTISPLDLAKLNQVARQQSHFAMMHGGTGFAGIDSSSPEVKGYWASLDASTQTTHELTIPNNLIGCIIGRQGANINEIRQMSGAQIKIANPVEGSSGRQVTITGSAASISLAQYLINARLSSEKGMGCS", "primaryDomainId": "uniprot.Q53SS8", "displayName": "Q53SS8_HUMAN", "synonyms": "Epididymis secretory protein Li 85 {ECO:0000313, EMBL:ACI46021.1}, Poly(RC) binding protein 1 {ECO:0000313, EMBL:EAW99834.1}, cDNA, FLJ94964, highly similar to Homo sapiens poly(rC) binding protein 1 (PCBP1), mRNA {ECO:0000313, EMBL:BAG36897.1}", "taxid": 9606, "geneName": "PCBP1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q53SS8", "id": "uniprot.Q53SS8", "value": "uniprot.Q53SS8"}}, {"data": {"domainIds": "uniprot.Q15365", "sequence": "MDAGVTESGLNVTLTIRLLMHGKEVGSIIGKKGESVKRIREESGARINISEGNCPERIITLTGPTNAIFKAFAMIIDKLEEDINSSMTNSTAASRPPVTLRLVVPATQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGVPQSVTECVKQICLVMLETLSQSPQGRVMTIPYQPMPASSPVICAGGQDRCSDAAGYPHATHDLEGPPLDAYSIQGQHTISPLDLAKLNQVARQQSHFAMMHGGTGFAGIDSSSPEVKGYWASLDASTQTTHELTIPNNLIGCIIGRQGANINEIRQMSGAQIKIANPVEGSSGRQVTITGSAASISLAQYLINARLSSEKGMGCS", "comments": "FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. In case of infection by poliovirus, plays a role in initiation of viral RNA replication in concert with the viral protein 3CD (PubMed:12414943). {ECO:0000269|PubMed:12414943}.\nINTERACTION: O41951:GAMMAHV.ORF34 (xeno); NbExp=4; IntAct=EBI-946095, EBI-9640556; Q67020:PA (xeno); NbExp=2; IntAct=EBI-946095, EBI-11514477; Q13153:PAK1; NbExp=2; IntAct=EBI-946095, EBI-1307; Q13153-1:PAK1; NbExp=5; IntAct=EBI-946095, EBI-15628682; Q15366:PCBP2; NbExp=2; IntAct=EBI-946095, EBI-945799; Q13427:PPIG; NbExp=2; IntAct=EBI-946095, EBI-396072; Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-946095, EBI-538479; P26599:PTBP1; NbExp=2; IntAct=EBI-946095, EBI-350540; Q9UHX1:PUF60; NbExp=2; IntAct=EBI-946095, EBI-1053259; Q96PU8:QKI; NbExp=2; IntAct=EBI-946095, EBI-945792; Q14498:RBM39; NbExp=2; IntAct=EBI-946095, EBI-395290; Q14498-2:RBM39; NbExp=2; IntAct=EBI-946095, EBI-11032687; P09012:SNRPA; NbExp=5; IntAct=EBI-946095, EBI-607085; Q96EK4:THAP11; NbExp=4; IntAct=EBI-946095, EBI-1790529; Q9Y3Q8:TSC22D4; NbExp=2; IntAct=EBI-946095, EBI-739485; Q9Y2W2:WBP11; NbExp=2; IntAct=EBI-946095, EBI-714455; Q96NB3:ZNF830; NbExp=2; IntAct=EBI-946095, EBI-3920997;\nSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm.\nTISSUE SPECIFICITY: Abundantly expressed in skeletal muscle, thymus and peripheral blood leukocytes while a lower expression is observed in prostate, spleen, testis, ovary, small intestine, heart, liver, adrenal and thyroid glands.\nPTM: Phosphorylated; lowers poly(rC)-binding activity.\nSEQUENCE CAUTION: Sequence=CAA82631.1; Type=Frameshift; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q15365", "displayName": "PCBP1_HUMAN", "synonyms": "Poly(rC)-binding protein 1, Alpha-CP1, Heterogeneous nuclear ribonucleoprotein E1, hnRNP E1, Nucleic acid-binding protein SUB2.3", "taxid": 9606, "geneName": "PCBP1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q15365", "id": "uniprot.Q15365", "value": "uniprot.Q15365"}}, {"data": {"domainIds": "entrez.995", "primaryDomainId": "entrez.995", "geneType": "protein-coding", "displayName": "cell division cycle 25C", "synonyms": "M-phase inducer phosphatase 3, dual specificity phosphatase CDC25C, mitosis inducer CDC25, phosphotyrosine phosphatase, protein phosphatase 1, regulatory subunit 60", "chromosome": "5", "description": "cell division cycle 25C", "approvedSymbol": "CDC25C", "type": "Gene", "symbols": "CDC25, PPP1R60", "mapLocation": "5q31.2", "graphics": {"fill": "#FFB6C1"}, "name": "CDC25C", "id": "entrez.995", "value": "entrez.995"}}, {"data": {"domainIds": "uniprot.B4DX61", "sequence": "MSEEARFCFSPGENSKTMSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVLHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP", "primaryDomainId": "uniprot.B4DX61", "displayName": "B4DX61_HUMAN", "synonyms": "cDNA FLJ56262, highly similar to M-phase inducer phosphatase 3 {ECO:0000313, EMBL:BAG63273.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DX61", "id": "uniprot.B4DX61", "value": "uniprot.B4DX61"}}, {"data": {"domainIds": "uniprot.P30307", "sequence": "MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP", "comments": "FUNCTION: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity. {ECO:0000269|PubMed:8119945}.\nCATALYTIC ACTIVITY: 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;\nSUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated on Ser-129 and/or Thr-130, interacts with PLK1. {ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:12595692}.\nSUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr; this interaction inactivates CDC25C phosphatase activity. {ECO:0000269|PubMed:14972559}.\nINTERACTION: P06493:CDK1; NbExp=2; IntAct=EBI-974439, EBI-444308; O14757:CHEK1; NbExp=2; IntAct=EBI-974439, EBI-974488; Q9Y250:LZTS1; NbExp=2; IntAct=EBI-974439, EBI-1216080; P53350:PLK1; NbExp=5; IntAct=EBI-974439, EBI-476768; P31946:YWHAB; NbExp=4; IntAct=EBI-974439, EBI-359815;\nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:8119945}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=5; Name=1; Synonyms=CDC25C1;   IsoId=P30307-1; Sequence=Displayed; Name=2; Synonyms=CDC25C2;   IsoId=P30307-2; Sequence=VSP_000864; Name=3; Synonyms=CDC25C3;   IsoId=P30307-5; Sequence=Not described; Name=4; Synonyms=CDC25C4;   IsoId=P30307-3; Sequence=VSP_000863; Name=5; Synonyms=CDC25C5, Cdc25Cdm;   IsoId=P30307-4; Sequence=VSP_000863, VSP_000864;\nDEVELOPMENTAL STAGE: Expressed predominantly in G2 phase.\nPTM: Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 (PubMed:10557092). However, such phosphorylation by PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr- 67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M transition and is probably catalyzed by CDK1. Ser-168 phosphorylation levels are lower than those at the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased activity. {ECO:0000269|PubMed:10557092, ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:8119945}.\nSIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.\nWEB RESOURCE: Name=NIEHS-SNPs; URL=\"http://egp.gs.washington.edu/data/cdc25c/\";", "primaryDomainId": "uniprot.P30307", "displayName": "MPIP3_HUMAN", "synonyms": "M-phase inducer phosphatase 3, 3.1.3.48, Dual specificity phosphatase Cdc25C", "taxid": 9606, "geneName": "CDC25C", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P30307", "id": "uniprot.P30307", "value": "uniprot.P30307"}}, {"data": {"domainIds": "entrez.3608", "primaryDomainId": "entrez.3608", "geneType": "protein-coding", "displayName": "interleukin enhancer binding factor 2", "synonyms": "interleukin enhancer-binding factor 2, interleukin enhancer binding factor 2, 45kD, interleukin enhancer binding factor 2, 45kDa, nuclear factor of activated T-cells, 45-kDa", "chromosome": "1", "description": "interleukin enhancer binding factor 2", "approvedSymbol": "ILF2", "type": "Gene", "symbols": "NF45, PRO3063", "mapLocation": "1q21.3", "graphics": {"fill": "#FFB6C1"}, "name": "ILF2", "id": "entrez.3608", "value": "entrez.3608"}}, {"data": {"domainIds": "uniprot.F4ZW62", "sequence": "MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE", "comments": "INTERACTION: O95273:CCNDBP1; NbExp=3; IntAct=EBI-10177680, EBI-748961; P26641-2:EEF1G; NbExp=3; IntAct=EBI-10177680, EBI-10177695;", "primaryDomainId": "uniprot.F4ZW62", "displayName": "F4ZW62_HUMAN", "synonyms": "NF45 {ECO:0000313, EMBL:AEE02016.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "F4ZW62", "id": "uniprot.F4ZW62", "value": "uniprot.F4ZW62"}}, {"data": {"domainIds": "uniprot.Q53FG3", "sequence": "MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVVDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE", "primaryDomainId": "uniprot.Q53FG3", "displayName": "Q53FG3_HUMAN", "synonyms": "Interleukin enhancer binding factor 2 variant {ECO:0000313, EMBL:BAD97046.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q53FG3", "id": "uniprot.Q53FG3", "value": "uniprot.Q53FG3"}}, {"data": {"domainIds": "uniprot.B4DY09", "sequence": "MAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE", "primaryDomainId": "uniprot.B4DY09", "displayName": "B4DY09_HUMAN", "synonyms": "Interleukin enhancer-binding factor 2 {ECO:0000313, Ensembl:ENSP00000482909}, cDNA FLJ51660, highly similar to Interleukin enhancer-binding factor 2 {ECO:0000313, EMBL:BAG63571.1}", "taxid": 9606, "geneName": "ILF2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DY09", "id": "uniprot.B4DY09", "value": "uniprot.B4DY09"}}, {"data": {"domainIds": "uniprot.Q12905", "sequence": "MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE", "comments": "FUNCTION: Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. {ECO:0000269|PubMed:10574923, ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:9442054}.\nSUBUNIT: Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a complex with ILF3, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. {ECO:0000269|PubMed:10574923, ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17890166, ECO:0000269|PubMed:9442054}.\nINTERACTION: Q08752:PPID; NbExp=4; IntAct=EBI-357925, EBI-716596;\nSUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Nucleus. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.\nSEQUENCE CAUTION: Sequence=AAA20993.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=AAF29591.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q12905", "displayName": "ILF2_HUMAN", "synonyms": "Interleukin enhancer-binding factor 2, Nuclear factor of activated T-cells 45 kDa", "taxid": 9606, "geneName": "ILF2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q12905", "id": "uniprot.Q12905", "value": "uniprot.Q12905"}}, {"data": {"domainIds": "entrez.10528", "primaryDomainId": "entrez.10528", "geneType": "protein-coding", "displayName": "NOP56 ribonucleoprotein", "synonyms": "nucleolar protein 56, NOP56 ribonucleoprotein homolog, nucleolar protein 5A (56kDa with KKE/D repeat)", "chromosome": "20", "description": "NOP56 ribonucleoprotein", "approvedSymbol": "NOP56", "type": "Gene", "symbols": "NOL5A, SCA36", "mapLocation": "20p13", "graphics": {"fill": "#FFB6C1"}, "name": "NOP56", "id": "entrez.10528", "value": "entrez.10528"}}, {"data": {"domainIds": "uniprot.O00567", "sequence": "MVLLHVLFEHAVGYALLALKEVEEISLLQPQVEESVLNLGKFHSIVRLVAFCPFASSQVALENANAVSEGVVHEDLRLLLETHLPSKKKKVLLGVGDPKIGAAIQEELGYNCQTGGVIAEILRGVRLHFHNLVKGLTDLSACKAQLGLGHSYSRAKVKFNVNRVDNMIIQSISLLDQLDKDINTFSMRVREWYGYHFPELVKIINDNATYCRLAQFIGNRRELNEDKLEKLEELTMDGAKAKAILDASRSSMGMDISAIDLINIESFSSRVVSLSEYRQSLHTYLRSKMSQVAPSLSALIGEAVGARLIAHAGSLTNLAKYPASTVQILGAEKALFRALKTRGNTPKYGLIFHSTFIGRAAAKNKGRISRYLANKCSIASRIDCFSEVPTSVFGEKLREQVEERLSFYETGEIPRKNLDVMKEAMVQAEEAAAEITRKLEKQEKKRLKKEKKRLAALALASSENSSSTPEECEEMSEKPKKKKKQKPQEVPQENGMEDPSISFSKPKKKKSFSKEELMSSDLEETAGSTSIPKRKKSTPKEETVNDPEEAGHRSGSKKKRKFSKEEPVSSGPEEAVGKSSSKKKKKFHKASQED", "comments": "FUNCTION: Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs. {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:15574333}.\nSUBUNIT: Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA species. Within this complex directly interacts with TCOF1 in an RNA-independent manner. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles; the core proteins SNU13, NOP56, NOP58 and FBL assemble stepwise onto the snoRNA. Interacts NOP1 and NOP58. Interacts with NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge the association of NOP56 with NUFIP1. {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:19620283}.\nSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:9372940}. Cytoplasm {ECO:0000250|UniProtKB:Q9D6Z1}. Nucleus, nucleoplasm {ECO:0000305|PubMed:15574333}.\nDISEASE: Spinocerebellar ataxia 36 (SCA36) [MIM:614153]: 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. SCA36 is characterized by complicated clinical features, with ataxia as the first symptom, followed by characteristic late-onset involvement of the motor neuron system. Ataxic symptoms, such as gait and truncal instability, ataxic dysarthria, and uncoordinated limbs, start in late forties to fifties. Characteristically, affected individuals exhibit tongue atrophy with fasciculation. Progression of motor neuron involvement is typically limited to the tongue and main proximal skeletal muscles in both upper and lower extremities. {ECO:0000269|PubMed:21683323}. Note=The disease is caused by mutations affecting the gene represented in this entry. Caused by large hexanucleotide CGCCTG repeat expansions within intron 1. These expansions induce RNA foci and sequester the RNA-binding protein SRSF2. In addition, the transcription of MIR1292, a microRNA gene located just 19 bp 3' of the GGCCTG repeat, is significantly decreased.\nSIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=CAA72789.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.O00567", "displayName": "NOP56_HUMAN", "synonyms": "Nucleolar protein 56, Nucleolar protein 5A", "taxid": 9606, "geneName": "NOP56", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O00567", "id": "uniprot.O00567", "value": "uniprot.O00567"}}, {"data": {"domainIds": "entrez.57622", "primaryDomainId": "entrez.57622", "geneType": "protein-coding", "displayName": "leucine rich repeat and fibronectin type III domain containing 1", "synonyms": "leucine-rich repeat and fibronectin type III domain-containing protein 1, CTC-246B18.8, synaptic adhesion-like molecule 2", "chromosome": "19", "description": "leucine rich repeat and fibronectin type III domain containing 1", "approvedSymbol": "LRFN1", "type": "Gene", "symbols": "SALM2", "mapLocation": "19q13.2", "graphics": {"fill": "#FFB6C1"}, "name": "LRFN1", "id": "entrez.57622", "value": "entrez.57622"}}, {"data": {"domainIds": "uniprot.Q9P244", "sequence": "MAPGPFSSALLSPPPAALPFLLLLWAGASRGQPCPGRCICQNVAPTLTMLCAKTGLLFVPPAIDRRVVELRLTDNFIAAVRRRDFANMTSLVHLTLSRNTIGQVAAGAFADLRALRALHLDSNRLAEVRGDQLRGLGNLRHLILGNNQIRRVESAAFDAFLSTVEDLDLSYNNLEALPWEAVGQMVNLNTLTLDHNLIDHIAEGTFVQLHKLVRLDMTSNRLHKLPPDGLFLRSQGTGPKPPTPLTVSFGGNPLHCNCELLWLRRLTREDDLETCATPEHLTDRYFWSIPEEEFLCEPPLITRQAGGRALVVEGQAVSLRCRAVGDPEPVVHWVAPDGRLLGNSSRTRVRGDGTLDVTITTLRDSGTFTCIASNAAGEATAPVEVCVVPLPLMAPPPAAPPPLTEPGSSDIATPGRPGANDSAAERRLVAAELTSNSVLIRWPAQRPVPGIRMYQVQYNSSVDDSLVYRMIPSTSQTFLVNDLAAGRAYDLCVLAVYDDGATALPATRVVGCVQFTTAGDPAPCRPLRAHFLGGTMIIAIGGVIVASVLVFIVLLMIRYKVYGDGDSRRVKGSRSLPRVSHVCSQTNGAGTGAAQAPALPAQDHYEALREVESQAAPAVAVEAKAMEAETASAEPEVVLGRSLGGSATSLCLLPSEETSGEESRAAVGPRRSRSGALEPPTSAPPTLALVPGGAAARPRPQQRYSFDGDYGALFQSHSYPRRARRTKRHRSTPHLDGAGGGAAGEDGDLGLGSARACLAFTSTEWMLESTV", "comments": "FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Involved in the regulation and maintenance of excitatory synapses. Induces the clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and GRIN1 (By similarity). {ECO:0000250}.\nSUBUNIT: Can form heteromeric complexes with LRFN2, LRFN3, LRFN4 and LRFN5 (By similarity). Forms homomeric complexes, but not across cell junctions (By similarity). Interacts with DLG1, DLG2, DLG3 and DLG4. Interacts with 2 AMPA receptor subunits GRIA1 and GRIA2 and NMDA receptor subunit GRIN1 (By similarity). {ECO:0000250}.\nSUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic density membrane {ECO:0000250}. Note=Detected in excitatory, but not inhibitory, synaptic plasma membrane. {ECO:0000250}.\nDOMAIN: The PDZ-binding motif is required for neurite outgrowth promotion and for DLG1-, DLG3- and DLG4-binding. {ECO:0000250}.\nPTM: Glycosylated. {ECO:0000250}.\nSIMILARITY: Belongs to the LRFN family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q9P244", "displayName": "LRFN1_HUMAN", "synonyms": "Leucine-rich repeat and fibronectin type III domain-containing protein 1, Synaptic adhesion-like molecule 2", "taxid": 9606, "geneName": "LRFN1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9P244", "id": "uniprot.Q9P244", "value": "uniprot.Q9P244"}}, {"data": {"domainIds": "entrez.23271", "primaryDomainId": "entrez.23271", "geneType": "protein-coding", "displayName": "calmodulin regulated spectrin associated protein family member 2", "synonyms": "calmodulin-regulated spectrin-associated protein 2, calmodulin-regulated spectrin-associated protein 1-like protein 1", "chromosome": "1", "description": "calmodulin regulated spectrin associated protein family member 2", "approvedSymbol": "CAMSAP2", "type": "Gene", "symbols": "CAMSAP1L1", "mapLocation": "1q32.1", "graphics": {"fill": "#FFB6C1"}, "name": "CAMSAP2", "id": "entrez.23271", "value": "entrez.23271"}}, {"data": {"domainIds": "uniprot.B3KTI4", "sequence": "MGDAADPREMRKTFIVPAIKPFDHYDFSRAKIACNLAWLVAKAFGTENVPEELQEPFYTDQYDQEHIKPPVVNLLLSAELYCRAGSLFLKSDAAKPLLGHDAVIQALAQKGLYVTDQEKLVTERDLHKKPIQMSAHLAMIDTLMMAYTVEMVSIEKVIACAQQYSAFFQATDLPYDIEDAVMYWINKVNEHLKDIMEQEQKLKEHHTVEAPGGQKARYRKEQTLLKQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYLNQCCHFTLEDMLYAASSIKSNYSVFMAELFWWFEVVKPSFVQPRVVRPQGAEPVKDMPSIPVLNAAKRNVLDSSSDFPSSGEGATFTQSHHHLPSRYSRPQAHSSASGGIRRSSSMSYVDGFIGTWPKEKRSSVHGVSFDISFDKEDSVQRSTPNRGITRSISNEGLTLNNSHVSKHIRKNLSFKPINGEEEAESIEEELNIDSHSDLKSCVPLNTNELNSNENIHYKLPNGALQNRILLDEFGNQIETPSIEEALQIIHDTEKSPHTPQPDQIANGFFLHSQEMSILNSNIKLNQSSPDNVTDTKGALSPITDNTEVDTGIHVPSEDIPETMDEDSSLRDYTVSLDSDMDDASKFLQDYDIRTGNTREALSPCPSTVSTKSQPGSSASSSSGVKMTSFAEQKFRKLNHTDGKSSGSSSQKTTPEGSELNIPHVVAWAQIPEETGLPQGRDTTQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKKKGDGISPLREEAAGAEDEKVYTDRA", "primaryDomainId": "uniprot.B3KTI4", "displayName": "B3KTI4_HUMAN", "synonyms": "cDNA FLJ38321 fis, clone FCBBF3024225, highly similar to Homo sapiens calmodulin regulated spectrin-associated protein 1-like 1 (CAMSAP1L1), mRNA {ECO:0000313, EMBL:BAG53096.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B3KTI4", "id": "uniprot.B3KTI4", "value": "uniprot.B3KTI4"}}, {"data": {"domainIds": "uniprot.Q08AD1", "sequence": "MGDAADPREMRKTFIVPAIKPFDHYDFSRAKIACNLAWLVAKAFGTENVPEELQEPFYTDQYDQEHIKPPVVNLLLSAELYCRAGSLILKSDAAKPLLGHDAVIQALAQKGLYVTDQEKLVTERDLHKKPIQMSAHLAMIDTLMMAYTVEMVSIEKVIACAQQYSAFFQATDLPYDIEDAVMYWINKVNEHLKDIMEQEQKLKEHHTVEAPGGQKSPSKWFWKLVPARYRKEQTLLKQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYLNQCCHFTLEDMLYAASSIKSNYLVFMAELFWWFEVVKPSFVQPRVVRPQGAEPVKDMPSIPVLNAAKRNVLDSSSDFPSSGEGATFTQSHHHLPSRYSRPQAHSSASGGIRRSSSMSYVDGFIGTWPKEKRSSVHGVSFDISFDKEDSVQRSTPNRGITRSISNEGLTLNNSHVSKHIRKNLSFKPINGEEEAESIEEELNIDSHSDLKSCVPLNTNELNSNENIHYKLPNGALQNRILLDEFGNQIETPSIEEALQIIHDTEKSPHTPQPDQIANGFFLHSQEMSILNSNIKLNQSSPDNVTDTKGALSPITDNTEVDTGIHVPSEDIPETMDEDSSLRDYTVSLDSDMDDASKFLQDYDIRTGNTREALSPCPSTVSTKSQPGSSASSSSGVKMTSFAEQKFRKLNHTDGKSSGSSSQKTTPEGSELNIPHVVAWAQIPEETGLPQGRDTTQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKKKGDGISPLREEAAGAEDEKVYTDRAKEKESQKTDGQRSKSLADIKESMENPQAKWLKSPTTPIDPEKQWNLASPSEETLNEGEILEYTKSIEKLNSSLHFLQQEMQRLSLQQEMLMQMREQQSWVISPPQPSPQKQIRDFKPSKQAGLSSAIAPFSSDSPRPTHPSPQSSNRKSASFSVKSQRTPRPNELKITPLNRTLTPPRSVDSLPRLRRFSPSQVPIQTRSFVCFGDDGEPQLKESKPKEEVKKEELESKGTLEQRGHNPEEKEIKPFESTVSEVLSLPVTETVCLTPNEDQLNQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVPVEKYDGESDKEQFDDDQKVCCGFFFKDDQKAENDMAMKRAALLEKRLRREKETQLRKQQLEAEMEHKKEETRRKTEEERQKKEDERARREFIRQEYMRRKQLKLMEDMDTVIKPRPQVVKQKKQRPKSIHRDHIESPKTPIKGPPVSSLSLASLNTGDNESVHSGKRTPRSESVEGFLSPSRCGSRNGEKDWENASTTSSVASGTEYTGPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIGPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKRPVTPKKLLPTKA", "comments": "FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus- ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). 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, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi- associated proteins AKAP9 and PDE4DIP, required to tether non- centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:24908486, ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28726242}.\nSUBUNIT: Interacts with CAMSAP3 (By similarity). Interacts with KATNA1 and KATNB1; leading to regulate the length of CAMSAP2-decorated microtubule stretches (PubMed:24486153). Interacts with a complex formed by AKAP9 and PDE4DIP isoform 13/MMG8/SMYLE, which recruits CAMSAP2 to the Golgi (PubMed:27666745, PubMed:28814570). Interacts with MAPRE1/EB1 (PubMed:28726242, PubMed:28814570). {ECO:0000250|UniProtKB:Q8C1B1, ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570}.\nINTERACTION: P29692:EEF1D; NbExp=2; IntAct=EBI-1051869, EBI-358607;\nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:24908486, ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28814570}. Golgi apparatus {ECO:0000269|PubMed:27666745}. Note=Associated with the minus-end of microtubules and also detected at the centrosomes (PubMed:23169647, PubMed:24486153, PubMed:24908486, PubMed:24706919, PubMed:27666745, PubMed:28814570). Decorates the minus-end of microtubules by decreasing the rate of tubulin incorporation and remaining bound (PubMed:24486153). The length of CAMSAP2-decorated stretches on the minus-end of microtubules depends on MAPRE1/EB1 and MAPRE3/EB3, which promote elongation of CAMSAP2-decorated microtubule stretches (PubMed:28814570). Recruited to the Golgi apparatus by AKAP9 and PDE4DIP isoform 13/MMG8/SMYLE (PubMed:27666745). In neurons, localizes to the minus-end of microtubules in axon and dendrites (PubMed:24908486). {ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28814570}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q08AD1-1; Sequence=Displayed; Name=2;   IsoId=Q08AD1-2; Sequence=VSP_030805, VSP_030806; Name=3;   IsoId=Q08AD1-3; Sequence=VSP_030805;\nDOMAIN: The CKK domain binds microtubules and specifically recognizes the minus-end of microtubules (PubMed:24486153). {ECO:0000255|PROSITE- ProRule:PRU00841, ECO:0000269|PubMed:24486153}.\nDOMAIN: The MBD (microtubule-binding domain) region can recognize some features of the microtubule lattice, which might contribute to the specific decoration of growing microtubule minus-ends by CAMSAP2. {ECO:0000269|PubMed:24486153}.\nDISEASE: Note=Defects in CAMSAP2 may be a cause of susceptibility to epilepsy in the Chinese population. {ECO:0000305|PubMed:22116939}.\nSIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE- ProRule:PRU00841}.\nSEQUENCE CAUTION: Sequence=AAH56910.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q08AD1", "displayName": "CAMP2_HUMAN", "synonyms": "Calmodulin-regulated spectrin-associated protein 2 {ECO:0000305}, Calmodulin-regulated spectrin-associated protein 1-like protein 1", "taxid": 9606, "geneName": "CAMSAP2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q08AD1", "id": "uniprot.Q08AD1", "value": "uniprot.Q08AD1"}}, {"data": {"domainIds": "entrez.9846", "primaryDomainId": "entrez.9846", "geneType": "protein-coding", "displayName": "GRB2 associated binding protein 2", "synonyms": "GRB2-associated-binding protein 2, Grb2-associated binder 2, growth factor receptor bound protein 2-associated protein 2, pp100", "chromosome": "11", "description": "GRB2 associated binding protein 2", "approvedSymbol": "GAB2", "type": "Gene", "symbols": "-", "mapLocation": "11q14.1", "graphics": {"fill": "#FFB6C1"}, "name": "GAB2", "id": "entrez.9846", "value": "entrez.9846"}}, {"data": {"domainIds": "uniprot.Q9UQC2", "sequence": "MSGGGDVVCTGWLRKSPPEKKLRRYAWKKRWFILRSGRMSGDPDVLEYYKNDHSKKPLRIINLNFCEQVDAGLTFNKKELQDSFVFDIKTSERTFYLVAETEEDMNKWVQSICQICGFNQAEESTDSLRNVSSAGHGPRSSPAELSSSSQHLLRERKSSAPSHSSQPTLFTFEPPVSNHMQPTLSTSAPQEYLYLHQCISRRAENARSASFSQGTRASFLMRSDTAVQKLAQGNGHCVNGISGQVHGFYSLPKPSRHNTEFRDSTYDLPRSLASHGHTKGSLTGSETDNEDVYTFKTPSNTLCREFGDLLVDNMDVPATPLSAYQIPRTFTLDKNHNAMTVATPGDSAIAPPPRPPKPSQAETPRWGSPQQRPPISENSRSVAATIPRRNTLPAMDNSRLHRASSCETYEYPQRGGESAGRSAESMSDGVGSFLPGKMIVGRSDSTNSEDNYVPMNPGSSTLLAMERAGDNSQSVYIPMSPGAHHFDSLGYPSTTLPVHRGPSRGSEIQPPPVNRNLKPDRKAKPTPLDLRNNTVIDELPFKSPITKSWSRANHTFNSSSSQYCRPISTQSITSTDSGDSEENYVPMQNPVSASPVPSGTNSPAPKKSTGSVDYLALDFQPSSPSPHRKPSTSSVTSDEKVDYVQVDKEKTQALQNTMQEWTDVRQSSEPSKGAKL", "comments": "FUNCTION: Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis. {ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738}.\nSUBUNIT: Interacts with SHC1; may mediate interaction with receptors (By similarity). Interacts with SYK (By similarity). Interacts with PI- 3 kinase. Interacts with GRB2 (via SH3 2 domain). Interacts (phosphorylated) with PTPN11. Interacts with TNFRSF11A (via cytoplasmic domain). Interacts (phosphorylated) with 14-3-3 family proteins SFN, YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ; prevents interaction with GRB2 and attenuates GAB2 signaling. Interacts with HCK. {ECO:0000250, ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:15010462, ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:19523899}.\nINTERACTION: P62993:GRB2; NbExp=10; IntAct=EBI-975200, EBI-401755; P62993-1:GRB2; NbExp=3; IntAct=EBI-15787947, EBI-15787932; Q06124:PTPN11; NbExp=4; IntAct=EBI-975200, EBI-297779; P31946:YWHAB; NbExp=4; IntAct=EBI-975200, EBI-359815;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19172738}. Cell membrane {ECO:0000269|PubMed:19172738}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q9UQC2-1; Sequence=Displayed; Name=2;   IsoId=Q9UQC2-2; Sequence=VSP_038520;\nDOMAIN: The SH3-binding motifs mediate interaction with SHC1 and GRB2. {ECO:0000250}.\nDOMAIN: The PH domain mediates phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate binding. {ECO:0000250}.\nPTM: Phosphorylated on tyrosine residue(s) by the thrombopoietin receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and B- cell antigen receptors, gp130, IL-2R and IL-3R (By similarity). Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL (By similarity). Phosphorylated upon EGF stimulation. Phosphorylated on tyrosine residues by HCK upon IL6 signaling. {ECO:0000250, ECO:0000269|PubMed:15010462, ECO:0000269|PubMed:19172738}.\nPTM: Dephosphorylated by PTPN11.\nSIMILARITY: Belongs to the GAB family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=BAA25497.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/GAB2ID40664ch11q14.html\";", "primaryDomainId": "uniprot.Q9UQC2", "displayName": "GAB2_HUMAN", "synonyms": "GRB2-associated-binding protein 2, GRB2-associated binder 2, Growth factor receptor bound protein 2-associated protein 2, pp100", "taxid": 9606, "geneName": "GAB2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9UQC2", "id": "uniprot.Q9UQC2", "value": "uniprot.Q9UQC2"}}, {"data": {"domainIds": "entrez.9978", "primaryDomainId": "entrez.9978", "geneType": "protein-coding", "displayName": "ring-box 1", "synonyms": "E3 ubiquitin-protein ligase RBX1, E3 ubiquitin-protein transferase RBX1, RING finger protein 75, RING-box protein 1, ZYP protein, regulator of cullins 1, ring-box 1, E3 ubiquitin protein ligase", "chromosome": "22", "description": "ring-box 1", "approvedSymbol": "RBX1", "type": "Gene", "symbols": "BA554C12.1, RNF75, ROC1", "mapLocation": "22q13.2", "graphics": {"fill": "#FFB6C1"}, "name": "RBX1", "id": "entrez.9978", "value": "entrez.9978"}}, {"data": {"domainIds": "uniprot.P62877", "sequence": "MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH", "comments": "FUNCTION: 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. {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10579999, ECO:0000269|PubMed:11027288, ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16751180, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:22748924, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:29769719}.\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:11027288};\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:11027288};\nPATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11027288, ECO:0000269|PubMed:22748924}.\nSUBUNIT: Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2 (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. 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. 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. Part of multisubunit complexes with elongin BC complex (ELOB and ELOC), elongin A/ELOA or SOCS1 or WSB1 and CUL5. Interacts directly with CUL1 and probably also with CUL2, CUL3, CUL4A, CUL4B, CUL5 and CUL7. 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. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or CUL4B. Interacts with UBE2M. Part of a SCF complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via FBXO3. Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and CDC34. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein. Part of the BCR(ENC1) complex containing ENC1. Part of the BCR(GAN) complex containing GAN. Part of the BCR(KLHL41) complex containing KLHL41. Part of the BCR(KEAP1) complex containing KEAP1. Interacts with DCUN1D3. 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). {ECO:0000269|PubMed:10213691, ECO:0000269|PubMed:10230406, ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:11384984, ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:12149480, ECO:0000269|PubMed:12481031, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18809579, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22748924, ECO:0000269|PubMed:23274085, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:29149593}.\nSUBUNIT: (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. {ECO:0000269|PubMed:19679664}.\nINTERACTION: Q13616:CUL1; NbExp=24; IntAct=EBI-398523, EBI-359390; Q13617:CUL2; NbExp=7; IntAct=EBI-398523, EBI-456179; Q13620:CUL4B; NbExp=5; IntAct=EBI-398523, EBI-456067; Q93034:CUL5; NbExp=3; IntAct=EBI-398523, EBI-1057139; Q92990:GLMN; NbExp=4; IntAct=EBI-398523, EBI-726150; P58004:SESN2; NbExp=3; IntAct=EBI-398523, EBI-3939642; Q13309:SKP2; NbExp=3; IntAct=EBI-398523, EBI-456291; P61081:UBE2M; NbExp=6; IntAct=EBI-398523, EBI-1041660;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11027288}. Nucleus {ECO:0000269|PubMed:11027288}.\nTISSUE SPECIFICITY: Widely expressed.\nDOMAIN: 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). {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:22748924}.\nSIMILARITY: Belongs to the RING-box family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAH17370.2; Type=Erroneous initiation; Evidence={ECO:0000305};\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/RBX1ID42075ch22q13.html\";", "primaryDomainId": "uniprot.P62877", "displayName": "RBX1_HUMAN", "synonyms": "E3 ubiquitin-protein ligase RBX1, 2.3.2.27 {ECO:0000269, PubMed:11027288}, 2.3.2.32 {ECO:0000269, PubMed:11027288}, E3 ubiquitin-protein transferase RBX1 {ECO:0000305}, Protein ZYP, RING finger protein 75, RING-box protein 1, Rbx1, Regulator of cullins 1, ROC1 {ECO:0000303, PubMed:10230407}", "taxid": 9606, "geneName": "RBX1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P62877", "id": "uniprot.P62877", "value": "uniprot.P62877"}}, {"data": {"domainIds": "entrez.5127", "primaryDomainId": "entrez.5127", "geneType": "protein-coding", "displayName": "cyclin dependent kinase 16", "synonyms": "cyclin-dependent kinase 16, PCTAIRE-motif protein kinase 1, cell division protein kinase 16, serine/threonine-protein kinase PCTAIRE-1, testis secretory sperm-binding protein Li 224n", "chromosome": "X", "description": "cyclin dependent kinase 16", "approvedSymbol": "CDK16", "type": "Gene", "symbols": "PCTAIRE, PCTAIRE1, PCTGAIRE, PCTK1", "mapLocation": "Xp11.3", "graphics": {"fill": "#FFB6C1"}, "name": "CDK16", "id": "entrez.5127", "value": "entrez.5127"}}, {"data": {"domainIds": "uniprot.A0A024R183", "sequence": "MQSEIAMDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF", "primaryDomainId": "uniprot.A0A024R183", "displayName": "A0A024R183_HUMAN", "synonyms": "PCTAIRE protein kinase 1, isoform CRA_b {ECO:0000313, EMBL:EAW59296.1}", "taxid": 9606, "geneName": "PCTK1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R183", "id": "uniprot.A0A024R183", "value": "uniprot.A0A024R183"}}, {"data": {"domainIds": "uniprot.Q9BRL4", "sequence": "MDRMKKIKRQLSMTLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF", "comments": "INTERACTION: Q92624:APPBP2; NbExp=3; IntAct=EBI-10296950, EBI-743771; Q8WXE1:ATRIP; NbExp=3; IntAct=EBI-10296950, EBI-747353; O43829:ZBTB14; NbExp=3; IntAct=EBI-10296950, EBI-10176632;\nSIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000256|RuleBase:RU000304}.", "primaryDomainId": "uniprot.Q9BRL4", "displayName": "Q9BRL4_HUMAN", "synonyms": "PCTK1 protein {ECO:0000313, EMBL:AAH06190.1}", "taxid": 9606, "geneName": "PCTK1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9BRL4", "id": "uniprot.Q9BRL4", "value": "uniprot.Q9BRL4"}}, {"data": {"domainIds": "uniprot.A0A140VK97", "sequence": "MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF", "comments": "SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000256|RuleBase:RU000304}.", "primaryDomainId": "uniprot.A0A140VK97", "displayName": "A0A140VK97_HUMAN", "synonyms": "Testis secretory sperm-binding protein Li 224n {ECO:0000313, EMBL:AEE61234.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A140VK97", "id": "uniprot.A0A140VK97", "value": "uniprot.A0A140VK97"}}, {"data": {"domainIds": "uniprot.Q00536", "sequence": "MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF", "comments": "FUNCTION: Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro). {ECO:0000250, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068}.\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189,   ECO:0000269|PubMed:22798068};\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:22184064,   ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068};\nSUBUNIT: Found in a complex containing CABLES1, CDK17 and TDRD7. Interacts with YWHAH, YWHAQ and YWHAZ. Interacts with NSF. Identified in a complex with NSF, syntaxin-1, synaptotagmin, SYN1, SYP and CDK5R1 (By similarity). Interacts with BRSK2. Interacts with CCNY; this increases the CDK16 kinase activity. {ECO:0000250, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068}.\nINTERACTION: Q92624:APPBP2; NbExp=3; IntAct=EBI-726261, EBI-743771; Q8ND76-1:CCNY; NbExp=7; IntAct=EBI-726261, EBI-11615526; Q8N7R7:CCNYL1; NbExp=3; IntAct=EBI-726261, EBI-10103094; Q15436:SEC23A; NbExp=3; IntAct=EBI-726261, EBI-81088; O43829:ZBTB14; NbExp=3; IntAct=EBI-726261, EBI-10176632;\nSUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q00536-1; Sequence=Displayed; Name=2;   IsoId=Q00536-2; Sequence=VSP_046134; Name=3;   IsoId=Q00536-3; Sequence=VSP_046342;\nTISSUE SPECIFICITY: Detected in pancreas islets (at protein level). Detected in brain and pancreas. {ECO:0000269|PubMed:22798068}.\nPTM: Phosphorylation at Ser-153 inhibits kinase activity. {ECO:0000269|PubMed:22798068}.\nSIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAH01048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAH15607.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q00536", "displayName": "CDK16_HUMAN", "synonyms": "Cyclin-dependent kinase 16, 2.7.11.22, Cell division protein kinase 16, PCTAIRE-motif protein kinase 1, Serine/threonine-protein kinase PCTAIRE-1", "taxid": 9606, "geneName": "CDK16", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q00536", "id": "uniprot.Q00536", "value": "uniprot.Q00536"}}, {"data": {"domainIds": "entrez.56623", "primaryDomainId": "entrez.56623", "geneType": "protein-coding", "displayName": "inositol polyphosphate-5-phosphatase E", "synonyms": "phosphatidylinositol polyphosphate 5-phosphatase type IV, 72 kDa inositol polyphosphate 5-phosphatase, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase, phosphatidylinositol-4,5-bisphosphate 5-phosphatase", "chromosome": "9", "description": "inositol polyphosphate-5-phosphatase E", "approvedSymbol": "INPP5E", "type": "Gene", "symbols": "CORS1, CPD4, JBTS1, MORMS, PPI5PIV, pharbin", "mapLocation": "9q34.3", "graphics": {"fill": "#FFB6C1"}, "name": "INPP5E", "id": "entrez.56623", "value": "entrez.56623"}}, {"data": {"domainIds": "uniprot.Q9NRR6", "sequence": "MPSKAENLRPSEPAPQPPEGRTLQGQLPGAPPAQRAGSPPDAPGSESPALACSTPATPSGEDPPARAAPIAPRPPARPRLERALSLDDKGWRRRRFRGSQEDLEARNGTSPSRGSVQSEGPGAPAHSCSPPCLSTSLQEIPKSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVAGSSPRLPSLLPPRPPPALSLDIASDSLRTANKVDSDLADYKLRAQPLLVRAHSSLGPGRPRSPLACDDCSLRSAKSSFSLLAPIRSKDVRSRSYLEGSLLASGALLGADELARYFPDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTSGDGKVAERLLDYTRTVQALVLPRNVPDTNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKVRPGRDNIPLAAGKFDRELYLLGIKRRISKEIQRQQALQSQNSSTICSVS", "comments": "FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:10764818) (By similarity). Specific for lipid substrates, inactive towards water soluble inositol phosphates (PubMed:10764818). Plays an essential role in the primary cilium by controlling ciliary growth and phosphoinositide 3-kinase (PI3K) signaling and stability (By similarity). {ECO:0000250|UniProtKB:Q9JII1, ECO:0000269|PubMed:10764818}.\nCATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-   bisphosphate) + H2O = 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={ECO:0000269|PubMed:10764818, ECO:0000269|PubMed:19668216}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765;   Evidence={ECO:0000305|PubMed:10764818, ECO:0000305|PubMed:19668216};\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:10764818}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529;   Evidence={ECO:0000305|PubMed:10764818};\nCATALYTIC ACTIVITY: 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={ECO:0000250|UniProtKB:Q9JII1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32956;   Evidence={ECO:0000250|UniProtKB:Q9JII1};\nACTIVITY REGULATION: Active in the presence of octyl-glucoside or Triton X-100, but completely inhibited by CTAB. {ECO:0000269|PubMed:10764818}.\nBIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters:   KM=0.65 uM for phosphatidylinositol-3,4,5-trisphosphate   {ECO:0000269|PubMed:10764818};   Vmax=0.1145 umol/min/mg enzyme with phosphatidylinositol-3,4,5-   trisphosphate as substrate {ECO:0000269|PubMed:10764818};\nSUBUNIT: Interacts (when prenylated) with PDE6D; this is important for normal location in cilia. {ECO:0000269|PubMed:24166846}.\nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19668215, ECO:0000269|PubMed:19668216, ECO:0000269|PubMed:24166846}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9JII1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JII1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JII1}. Cell membrane {ECO:0000250|UniProtKB:Q9WVR1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9WVR1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVR1}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9WVR1}. Cytoplasm {ECO:0000250|UniProtKB:Q9WVR1}. Note=Peripheral membrane protein associated with Golgi stacks. {ECO:0000250|UniProtKB:Q9JII1}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q9NRR6-1; Sequence=Displayed; Name=2;   IsoId=Q9NRR6-2; Sequence=VSP_009799;\nTISSUE SPECIFICITY: Detected in brain, heart, pancreas, testis and spleen. {ECO:0000269|PubMed:10764818}.\nDISEASE: Joubert syndrome 1 (JBTS1) [MIM:213300]: A 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 and renal disease. {ECO:0000269|PubMed:19668216, ECO:0000269|PubMed:23034536, ECO:0000269|PubMed:23386033, ECO:0000269|PubMed:29052317}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Mental retardation, truncal obesity, retinal dystrophy, and micropenis (MORMS) [MIM:610156]: An autosomal recessive disorder characterized by moderate mental retardation, truncal obesity, congenital non-progressive retinal dystrophy, and micropenis in males. The phenotype is similar to Bardet-Biedl syndrome and Cohen syndrome Distinguishing features are the age of onset, the non-progressive nature of the visual impairment, lack of dysmorphic facies, skin or gingival infection, microcephaly, mottled retina, polydactyly, and testicular anomalies. {ECO:0000269|PubMed:19668215}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type IV family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAB03215.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9NRR6", "displayName": "INP5E_HUMAN", "synonyms": "Phosphatidylinositol polyphosphate 5-phosphatase type IV {ECO:0000305}, 72 kDa inositol polyphosphate 5-phosphatase, Inositol polyphosphate-5-phosphatase E {ECO:0000303, PubMed:19668216}, Phosphatidylinositol 4,5-bisphosphate 5-phosphatase {ECO:0000305}, 3.1.3.36 {ECO:0000269, PubMed:10764818, ECO:0000269, PubMed:19668216}, Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase {ECO:0000305}, 3.1.3.86 {ECO:0000269, PubMed:10764818}", "taxid": 9606, "geneName": "INPP5E", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9NRR6", "id": "uniprot.Q9NRR6", "value": "uniprot.Q9NRR6"}}, {"data": {"domainIds": "entrez.55667", "primaryDomainId": "entrez.55667", "geneType": "protein-coding", "displayName": "DENN domain containing 4C", "synonyms": "DENN domain-containing protein 4C, DENN/MADD domain containing 4A pseudogene, DENN/MADD domain containing 4C", "chromosome": "9", "description": "DENN domain containing 4C", "approvedSymbol": "DENND4C", "type": "Gene", "symbols": "C9orf55, C9orf55B, RAB10GEF, bA513M16.3", "mapLocation": "9p22.1", "graphics": {"fill": "#FFB6C1"}, "name": "DENND4C", "id": "entrez.55667", "value": "entrez.55667"}}, {"data": {"domainIds": "uniprot.Q5VZ89", "sequence": "MIEDKGPRVTDYFVVAGLTDTSTLLDQEINRLDTKSTGPKAPITDIAIIIKSAGETVPEGYTCVEATPSALQANLNYGSLKSPELFLCYKRGRDKPPLTDIGVLYEGKERLIPGCEVILATPYGRCANVNNSSTTSQRIFITYRRAPPVRPQNSLAVTDICVIVTSKGETPPHTFCKVDKNLNCGMWGSSVFLCYKKSVPASNAIAYKAGLIFRYPEEDYESFPLSESDVPLFCLPMGATIECWDPETKYPLPVFSTFVLTGSSAKKVYGAAIQFYEPYSRELLSEKQLMHLGLLTPVERKMVSKSINTNKCICLLSHWPFFEAFRKFLMFIYKLSVSGPHPLPIEKHISHFMQNIPFPSPQRPRILVQLSVHDALILSQPVSTPLPLSGANFSTLLMNLGPENCATLLLFVLLESKILLHSLRPAVLTGVAEAVVAMIFPFQWQCPYIPLCPLSLAAVLSAPLPFIVGVDSRYFDLHDPPQDVVCIDLDTNMLYVSDEKKNMNWKQLPKKPCKNLLSTLKKLYPQLSSVHQKTQEGSAIDMTPIEADFSWQKKMTQLEMEIQEAFLRFMASILKGYRTYLRPITEAPSNKATAADSLFDRQGFLKSRDRAYAKFYTLLSKTQIFIRFIEECSFVSDKDTGLAFFDDCIEKLFPDKGTEKTDKVDFDSAEDTRLIELDDSQKSEHTVFIMPPEPPPDDGKDLSPKYSYKYFPRLDLKLFDRPQELKLCFSRHPTGNSITKSPPLMAKRTKQEIKTAHKLAKRCYTNPPQWAKCLFSHCYSLWFICLPAYVRVSHPKVRALQQAYDVLIKMRKTDVDPLDEVCYRVVMQLCGLWGHPVLAVRVLFEMKTARIKPNAITYGYYNKVVLESPWPSSTRSGIFLWTKVRNVVRGLAQFRQPLKKTVQRSQVSSISGGQSDQGYGSKDELIKDDAEIHVPEEQAARELITKTKMQTEEVCDASAIVAKHSQPSPEPHSPTEPPAWGSSIVKVPSGIFDVNSRKSSTGSISNVLFSTQDPVEDAVFGEATNLKKNGDRGEKRQKHFPERSCSFSSESRAGMLLKKSSLDSNSSEMAIMMGADAKILTAALTCPKTSLLHIARTHSFENVSCHLPDSRTCMSESTWNPEHRSSPVPEMLEESQELLEPVVDDVPKTTATVDTYESLLSDSNSNQSRDLKTVSKDLRNKRSSLYGIAKVVQREDVETGLDPLSLLATECTGGKTPDSEDKLFSPVIARNLADEIESYMNLKSPLGSKSSSMELHREENRESGMTTAFIHALERRSSLPLDHGSPAQENPESEKSSPAVSRSKTFTGRFKQQTPSRTHKERSTSLSALVRSSPHGSLGSVVNSLSGLKLDNILSGPKIDVLKSGMKQAATVASKMWVAVASAYSYSDDEEETNRDYSFPAGLEDHILGENISPNTSISGLVPSELTQSNTSLGSSSSSGDVGKLHYPTGEVPFPRGMKGQDFEKSDHGSSQNTSMSSIYQNCAMEVLMSSCSQCRACGALVYDEEIMAGWTADDSNLNTACPFCKSNFLPLLNIEFKDLRGSASFFLKPSTSGDSLQSGSIPLANESLEHKPVSSLAEPDLINFMDFPKHNQIITEETGSAVEPSDEIKRASGDVQTMKISSVPNSLSKRNVSLTRSHSVGGPLQNIDFTQRPFHGISTVSLPNSLQEVVDPLGKRPNPPPVSVPYLSPLVLRKELESLLENEGDQVIHTSSFINQHPIIFWNLVWYFRRLDLPSNLPGLILTSEHCNEGVQLPLSSLSQDSKLVYIQLLWDNINLHQEPREPLYVSWRNFNSEKKSSLLSEEQQETSTLVETIRQSIQHNNVLKPINLLSQQMKPGMKRQRSLYREILFLSLVSLGRENIDIEAFDNEYGIAYNSLSSEILERLQKIDAPPSASVEWCRKCFGAPLI", "comments": "FUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269|PubMed:20937701}.\nSUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Cell membrane. Cytoplasm, cytosol. Note=Associates with SLC2A4/GLUT4 storage vesicles.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=1;   IsoId=Q5VZ89-1; Sequence=Displayed; Name=3;   IsoId=Q5VZ89-3; Sequence=VSP_027384, VSP_027386; Name=5;   IsoId=Q5VZ89-5; Sequence=VSP_027382, VSP_027383; Name=2;   IsoId=Q5VZ89-7; Sequence=VSP_027379;\nPTM: Phosphorylated in response to insulin. {ECO:0000250}.\nSEQUENCE CAUTION: Sequence=BAA91294.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAA91478.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAA92039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAB15221.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAC86313.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=CAH10466.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q5VZ89", "displayName": "DEN4C_HUMAN", "synonyms": "DENN domain-containing protein 4C", "taxid": 9606, "geneName": "DENND4C", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q5VZ89", "id": "uniprot.Q5VZ89", "value": "uniprot.Q5VZ89"}}, {"data": {"domainIds": "entrez.7157", "primaryDomainId": "entrez.7157", "geneType": "protein-coding", "displayName": "tumor protein p53", "synonyms": "cellular tumor antigen p53, antigen NY-CO-13, mutant tumor protein 53, p53 tumor suppressor, phosphoprotein p53, transformation-related protein 53, tumor protein 53, tumor supressor p53", "chromosome": "17", "description": "tumor protein p53", "approvedSymbol": "TP53", "type": "Gene", "symbols": "BCC7, BMFS5, LFS1, P53, TRP53", "mapLocation": "17p13.1", "graphics": {"fill": "#FFB6C1"}, "name": "TP53", "id": "entrez.7157", "value": "entrez.7157"}}, {"data": {"domainIds": "uniprot.A0A087X1Q1", "sequence": "MAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD", "comments": "FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. {ECO:0000256|RuleBase:RU003304}.\nCOFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;   Evidence={ECO:0000256|RuleBase:RU003304}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003304};\nSUBUNIT: Binds DNA as a homotetramer. {ECO:0000256|RuleBase:RU003304}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.\nSIMILARITY: Belongs to the p53 family. {ECO:0000256|RuleBase:RU003304}.", "primaryDomainId": "uniprot.A0A087X1Q1", "displayName": "A0A087X1Q1_HUMAN", "synonyms": "Cellular tumor antigen p53 {ECO:0000256, RuleBase:RU003304}", "taxid": 9606, "geneName": "TP53", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A087X1Q1", "id": "uniprot.A0A087X1Q1", "value": "uniprot.A0A087X1Q1"}}, {"data": {"domainIds": "uniprot.A0A087WXZ1", "sequence": "MAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQDQTSFQKENC", "comments": "FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. {ECO:0000256|RuleBase:RU003304}.\nCOFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;   Evidence={ECO:0000256|RuleBase:RU003304}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003304};\nSUBUNIT: Binds DNA as a homotetramer. {ECO:0000256|RuleBase:RU003304}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.\nSIMILARITY: Belongs to the p53 family. {ECO:0000256|RuleBase:RU003304}.", "primaryDomainId": "uniprot.A0A087WXZ1", "displayName": "A0A087WXZ1_HUMAN", "synonyms": "Cellular tumor antigen p53 {ECO:0000256, RuleBase:RU003304}", "taxid": 9606, "geneName": "TP53", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A087WXZ1", "id": "uniprot.A0A087WXZ1", "value": "uniprot.A0A087WXZ1"}}, {"data": {"domainIds": "uniprot.H2EHT1", "sequence": "MDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD", "comments": "FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. {ECO:0000256|RuleBase:RU003304}.\nCOFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;   Evidence={ECO:0000256|RuleBase:RU003304}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003304};\nSUBUNIT: Binds DNA as a homotetramer. {ECO:0000256|RuleBase:RU003304}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.\nSIMILARITY: Belongs to the p53 family. {ECO:0000256|RuleBase:RU003304}.", "primaryDomainId": "uniprot.H2EHT1", "displayName": "H2EHT1_HUMAN", "synonyms": "Cellular tumor antigen p53 {ECO:0000256, RuleBase:RU003304}", "taxid": 9606, "geneName": "TP53", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "H2EHT1", "id": "uniprot.H2EHT1", "value": "uniprot.H2EHT1"}}, {"data": {"domainIds": "uniprot.A0A087WT22", "sequence": "MAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQMLLDLRWCYFLINSS", "comments": "FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. {ECO:0000256|RuleBase:RU003304}.\nCOFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;   Evidence={ECO:0000256|RuleBase:RU003304}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003304};\nSUBUNIT: Binds DNA as a homotetramer. {ECO:0000256|RuleBase:RU003304}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.\nSIMILARITY: Belongs to the p53 family. {ECO:0000256|RuleBase:RU003304}.", "primaryDomainId": "uniprot.A0A087WT22", "displayName": "A0A087WT22_HUMAN", "synonyms": "Cellular tumor antigen p53 {ECO:0000256, RuleBase:RU003304}", "taxid": 9606, "geneName": "TP53", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A087WT22", "id": "uniprot.A0A087WT22", "value": "uniprot.A0A087WT22"}}, {"data": {"domainIds": "uniprot.Q53GA5", "sequence": "YMCNSSCMGGMNGRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD", "primaryDomainId": "uniprot.Q53GA5", "displayName": "Q53GA5_HUMAN", "synonyms": "Tumor protein p53 variant {ECO:0000313, EMBL:BAD96746.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q53GA5", "id": "uniprot.Q53GA5", "value": "uniprot.Q53GA5"}}, {"data": {"domainIds": "uniprot.K7PPA8", "sequence": "MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD", "comments": "FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. {ECO:0000256|RuleBase:RU003304}.\nCOFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;   Evidence={ECO:0000256|RuleBase:RU003304}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003304};\nSUBUNIT: Binds DNA as a homotetramer. {ECO:0000256|RuleBase:RU003304}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.\nSIMILARITY: Belongs to the p53 family. {ECO:0000256|RuleBase:RU003304}.", "primaryDomainId": "uniprot.K7PPA8", "displayName": "K7PPA8_HUMAN", "synonyms": "Cellular tumor antigen p53 {ECO:0000256, RuleBase:RU003304}", "taxid": 9606, "geneName": "TP53", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "K7PPA8", "id": "uniprot.K7PPA8", "value": "uniprot.K7PPA8"}}, {"data": {"domainIds": "uniprot.P04637", "sequence": "MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD", "comments": "FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross- over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492, ECO:0000269|PubMed:9840937}.\nCOFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;\nSUBUNIT: Forms homodimers and homotetramers (PubMed:19011621). Binds DNA as a homotetramer. Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By similarity). Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID complex. Interacts with ING4; this interaction may be indirect. Found in a complex with CABLES1 and TP73. Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. May interact with HCV core protein. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity (By similarity). Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F1. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts (via DNA-binding domain) with MAML1 (via N- terminus). Interacts with MKRN1. Interacts with PML (via C-terminus). Interacts with MDM2; leading to ubiquitination and proteasomal degradation of TP53. Directly interacts with FBXO42; leading to ubiquitination and degradation of TP53. Interacts (phosphorylated at Ser-15 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent inhibition of cell proliferation. Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when monomethylated at Lys-382) with L3MBTL1. Isoform 1 interacts with isoform 2 and with isoform 4. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB, SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with PPIF; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by cyclosporin A (CsA). Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts with KAT6A. Interacts with UBC9. Interacts with ZNF385B; the interaction is direct. Interacts (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest. Interacts with ANKRD2. Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts with MTA1 and COP1. Interacts with CCAR2 (via N-terminus). Interacts with MORC3 (PubMed:17332504). Interacts (via C-terminus) with POU4F2 isoform 1 (via C-terminus) (PubMed:17145718). Interacts (via oligomerization region) with NOP53; the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of TP53 (PubMed:22522597). Interacts with AFG1L; mediates mitochondrial translocation of TP53 (PubMed:27323408). Interacts with UBD (PubMed:25422469). Interacts with TAF6 isoform 1 and isoform 4 (PubMed:20096117). Interacts with C10orf90/FATS; the interaction inhibits binding of TP53 and MDM2 (By similarity). Interacts with NUPR1; interaction is stress-dependent (PubMed:18690848). Forms a complex with EP300 and NUPR1; this complex binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848). Interacts with PRMT5 in response to DNA damage; the interaction is STRAP dependent (PubMed:19011621). Interacts with PPP1R13L (via SH3 domain and ANK repeats); the interaction inhibits pro-apoptotic activity of p53/TP53 (PubMed:12524540). Interacts with PPP1R13B/ASPP1 and TP53BP2/ASPP2; the interactions promotes pro-apototic activity (PubMed:12524540). {ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P10361, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12750254, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:12851404, ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15109303, ECO:0000269|PubMed:15136035, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:16219768, ECO:0000269|PubMed:16322561, ECO:0000269|PubMed:16376338, ECO:0000269|PubMed:16377624, ECO:0000269|PubMed:16402859, ECO:0000269|PubMed:16474402, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17121812, ECO:0000269|PubMed:17145718, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:17245430, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:17719541, ECO:0000269|PubMed:17904127, ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:18585004, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:18690848, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:19509332, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:19536131, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20096117, ECO:0000269|PubMed:20124405, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:20364130, ECO:0000269|PubMed:20385133, ECO:0000269|PubMed:20660729, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:21952639, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:22945289, ECO:0000269|PubMed:23431171, ECO:0000269|PubMed:25422469, ECO:0000269|PubMed:25732823, ECO:0000269|PubMed:27323408, ECO:0000269|PubMed:8875926, ECO:0000269|PubMed:8875929, ECO:0000269|PubMed:9840937}.\nSUBUNIT: (Microbial infection) Interacts with cancer-associated/HPV E6 viral proteins leading to ubiquitination and degradation of TP53 giving a possible model for cell growth regulation. This complex formation requires an additional factor, E6-AP, which stably associates with TP53 in the presence of E6. {ECO:0000269|PubMed:2175676}.\nSUBUNIT: (Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL123. {ECO:0000269|PubMed:19776115}.\nSUBUNIT: (Microbial infection) Interacts (via N-terminus) with human adenovirus 5 E1B-55K protein; this interaction leads to the inhibition of TP53 function and/or its degradation. {ECO:0000269|PubMed:25772236}.\nINTERACTION: Self; NbExp=25; IntAct=EBI-366083, EBI-366083; P03070:- (xeno); NbExp=20; IntAct=EBI-366083, EBI-617698; P26663:- (xeno); NbExp=9; IntAct=EBI-366083, EBI-6838571; Q7L7W2:-; NbExp=2; IntAct=EBI-366083, EBI-7210801; Q8QW27:- (xeno); NbExp=2; IntAct=EBI-366083, EBI-6863726; Q13155:AIMP2; NbExp=6; IntAct=EBI-366083, EBI-745226; O95376:ARIH2; NbExp=5; IntAct=EBI-366083, EBI-711158; P49407:ARRB1; NbExp=5; IntAct=EBI-366083, EBI-743313; P29066:Arrb1 (xeno); NbExp=3; IntAct=EBI-366083, EBI-4303019; Q9UBL3:ASH2L; NbExp=7; IntAct=EBI-366083, EBI-540797; O95352-2:ATG7; NbExp=4; IntAct=EBI-366083, EBI-15980880; O15169:AXIN1; NbExp=4; IntAct=EBI-366083, EBI-710484; Q8N9N5:BANP; NbExp=3; IntAct=EBI-366083, EBI-744695; P10415:BCL2; NbExp=5; IntAct=EBI-366083, EBI-77694; Q07817-1:BCL2L1; NbExp=26; IntAct=EBI-366083, EBI-287195; P11274:BCR; NbExp=2; IntAct=EBI-366083, EBI-712838; O14503:BHLHE40; NbExp=11; IntAct=EBI-366083, EBI-711810; P51587:BRCA2; NbExp=7; IntAct=EBI-366083, EBI-79792; Q9NPI1:BRD7; NbExp=9; IntAct=EBI-366083, EBI-711221; Q9BX70:BTBD2; NbExp=2; IntAct=EBI-366083, EBI-710091; Q9Y297:BTRC; NbExp=2; IntAct=EBI-366083, EBI-307461; Q9ESJ1:Cables1 (xeno); NbExp=3; IntAct=EBI-366083, EBI-604411; Q9BWC9:CCDC106; NbExp=3; IntAct=EBI-366083, EBI-711501; P38936:CDKN1A; NbExp=3; IntAct=EBI-366083, EBI-375077; P17676:CEBPB; NbExp=4; IntAct=EBI-366083, EBI-969696; Q92793:CREBBP; NbExp=11; IntAct=EBI-366083, EBI-81215; P45481:Crebbp (xeno); NbExp=9; IntAct=EBI-366083, EBI-296306; P55060:CSE1L; NbExp=5; IntAct=EBI-366083, EBI-286709; P68400:CSNK2A1; NbExp=2; IntAct=EBI-366083, EBI-347804; Q14999:CUL7; NbExp=5; IntAct=EBI-366083, EBI-308606; Q8IWT3:CUL9; NbExp=4; IntAct=EBI-366083, EBI-311123; Q9P0U4:CXXC1; NbExp=7; IntAct=EBI-366083, EBI-949911; Q9UER7:DAXX; NbExp=12; IntAct=EBI-366083, EBI-77321; Q92841:DDX17; NbExp=3; IntAct=EBI-366083, EBI-746012; P17844:DDX5; NbExp=6; IntAct=EBI-366083, EBI-351962; Q9NRR4:DROSHA; NbExp=5; IntAct=EBI-366083, EBI-528367; Q9BV47:DUSP26; NbExp=9; IntAct=EBI-366083, EBI-2924519; O14641:DVL2; NbExp=4; IntAct=EBI-366083, EBI-740850; P03126:E6 (xeno); NbExp=5; IntAct=EBI-366083, EBI-1177242; P06463:E6 (xeno); NbExp=3; IntAct=EBI-366083, EBI-1186926; Q09472:EP300; NbExp=20; IntAct=EBI-366083, EBI-447295; P15036:ETS2; NbExp=4; IntAct=EBI-366083, EBI-1646991; Q86XK2:FBXO11; NbExp=4; IntAct=EBI-366083, EBI-1047804; O43524:FOXO3; NbExp=2; IntAct=EBI-366083, EBI-1644164; P49841:GSK3B; NbExp=3; IntAct=EBI-366083, EBI-373586; P32780:GTF2H1; NbExp=12; IntAct=EBI-366083, EBI-715539; Q13547:HDAC1; NbExp=7; IntAct=EBI-366083, EBI-301834; Q86Z02:HIPK1; NbExp=2; IntAct=EBI-366083, EBI-692891; P09429:HMGB1; NbExp=9; IntAct=EBI-366083, EBI-389432; P61978:HNRNPK; NbExp=2; IntAct=EBI-366083, EBI-304185; P61978-2:HNRNPK; NbExp=2; IntAct=EBI-366083, EBI-7060731; P02829:HSP82 (xeno); NbExp=8; IntAct=EBI-366083, EBI-8659; P34931:HSPA1L; NbExp=2; IntAct=EBI-366083, EBI-354912; P38646:HSPA9; NbExp=6; IntAct=EBI-366083, EBI-354932; P04792:HSPB1; NbExp=3; IntAct=EBI-366083, EBI-352682; P42858:HTT; NbExp=4; IntAct=EBI-366083, EBI-466029; Q7Z6Z7:HUWE1; NbExp=3; IntAct=EBI-366083, EBI-625934; Q16666-2:IFI16; NbExp=6; IntAct=EBI-366083, EBI-6273540; Q08619:Ifi205b (xeno); NbExp=2; IntAct=EBI-366083, EBI-8064290; O14920:IKBKB; NbExp=2; IntAct=EBI-366083, EBI-81266; Q9UHH9:IP6K2; NbExp=4; IntAct=EBI-366083, EBI-747509; Q6NYC1:JMJD6; NbExp=7; IntAct=EBI-366083, EBI-8464037; Q92993:KAT5; NbExp=3; IntAct=EBI-366083, EBI-399080; Q9H7Z6:KAT8; NbExp=2; IntAct=EBI-366083, EBI-896414; O60341-1:KDM1A; NbExp=6; IntAct=EBI-366083, EBI-15599570; Q8IZD2:KMT2E; NbExp=4; IntAct=EBI-366083, EBI-2689959; Q16363:LAMA4; NbExp=2; IntAct=EBI-366083, EBI-711505; P43356:MAGEA2B; NbExp=7; IntAct=EBI-366083, EBI-5650739; Q9UBF1:MAGEC2; NbExp=3; IntAct=EBI-366083, EBI-5651487; P46821:MAP1B; NbExp=6; IntAct=EBI-366083, EBI-764611; Q15759:MAPK11; NbExp=2; IntAct=EBI-366083, EBI-298304; Q8IW41:MAPKAPK5; NbExp=2; IntAct=EBI-366083, EBI-1201460; Q00987:MDM2; NbExp=93; IntAct=EBI-366083, EBI-389668; O15151:MDM4; NbExp=19; IntAct=EBI-366083, EBI-398437; Q9UHC7:MKRN1; NbExp=8; IntAct=EBI-366083, EBI-373524; O75970:MPDZ; NbExp=3; IntAct=EBI-366083, EBI-821405; P04731:MT1A; NbExp=3; IntAct=EBI-366083, EBI-8045030; P19338:NCL; NbExp=2; IntAct=EBI-366083, EBI-346967; Q9Y618:NCOR2; NbExp=7; IntAct=EBI-366083, EBI-80830; P23511:NFYA; NbExp=11; IntAct=EBI-366083, EBI-389739; P25208:NFYB; NbExp=6; IntAct=EBI-366083, EBI-389728; Q9Y3T9:NOC2L; NbExp=8; IntAct=EBI-366083, EBI-751547; O60936:NOL3; NbExp=3; IntAct=EBI-366083, EBI-740992; P06748:NPM1; NbExp=6; IntAct=EBI-366083, EBI-78579; P06748-1:NPM1; NbExp=3; IntAct=EBI-366083, EBI-354150; Q15466:NR0B2; NbExp=3; IntAct=EBI-366083, EBI-3910729; P22736:NR4A1; NbExp=6; IntAct=EBI-366083, EBI-721550; O43847:NRDC; NbExp=6; IntAct=EBI-366083, EBI-2371631; P89055:NSP1 (xeno); NbExp=6; IntAct=EBI-366083, EBI-9522973; O60285:NUAK1; NbExp=5; IntAct=EBI-366083, EBI-1046789; P49757:NUMB; NbExp=5; IntAct=EBI-366083, EBI-915016; Q96FW1:OTUB1; NbExp=8; IntAct=EBI-366083, EBI-1058491; Q8TEW0:PARD3; NbExp=3; IntAct=EBI-366083, EBI-81968; P09874:PARP1; NbExp=3; IntAct=EBI-366083, EBI-355676; Q96KB5:PBK; NbExp=7; IntAct=EBI-366083, EBI-536853; P35232:PHB; NbExp=6; IntAct=EBI-366083, EBI-354213; O75925:PIAS1; NbExp=4; IntAct=EBI-366083, EBI-629434; O75928:PIAS2; NbExp=2; IntAct=EBI-366083, EBI-348555; Q8N2W9:PIAS4; NbExp=2; IntAct=EBI-366083, EBI-473160; Q13526:PIN1; NbExp=12; IntAct=EBI-366083, EBI-714158; P53350:PLK1; NbExp=6; IntAct=EBI-366083, EBI-476768; P29590:PML; NbExp=4; IntAct=EBI-366083, EBI-295890; P30405:PPIF; NbExp=4; IntAct=EBI-366083, EBI-5544229; P36873-1:PPP1CC; NbExp=2; IntAct=EBI-366083, EBI-356289; Q8WUF5:PPP1R13L; NbExp=12; IntAct=EBI-366083, EBI-5550163; P30153:PPP2R1A; NbExp=3; IntAct=EBI-366083, EBI-302388; Q13362:PPP2R5C; NbExp=4; IntAct=EBI-366083, EBI-1266156; Q05655:PRKCD; NbExp=4; IntAct=EBI-366083, EBI-704279; P61289:PSME3; NbExp=7; IntAct=EBI-366083, EBI-355546; Q05397:PTK2; NbExp=13; IntAct=EBI-366083, EBI-702142; Q06609:RAD51; NbExp=2; IntAct=EBI-366083, EBI-297202; Q06330:RBPJ; NbExp=5; IntAct=EBI-366083, EBI-632552; Q96PM5:RCHY1; NbExp=11; IntAct=EBI-366083, EBI-947779; Q6PCD5:RFWD3; NbExp=5; IntAct=EBI-366083, EBI-2129159; Q06587:RING1; NbExp=7; IntAct=EBI-366083, EBI-752313; P23396:RPS3; NbExp=4; IntAct=EBI-366083, EBI-351193; Q8N488:RYBP; NbExp=3; IntAct=EBI-366083, EBI-752324; P23297:S100A1; NbExp=2; IntAct=EBI-366083, EBI-743686; P29034:S100A2; NbExp=2; IntAct=EBI-366083, EBI-752230; P26447:S100A4; NbExp=7; IntAct=EBI-366083, EBI-717058; P04271:S100B; NbExp=2; IntAct=EBI-366083, EBI-458391; Q15424:SAFB; NbExp=5; IntAct=EBI-366083, EBI-348298; Q8WTS6:SETD7; NbExp=11; IntAct=EBI-366083, EBI-1268586; P31947:SFN; NbExp=4; IntAct=EBI-366083, EBI-476295; Q96ST3:SIN3A; NbExp=2; IntAct=EBI-366083, EBI-347218; Q96EB6:SIRT1; NbExp=18; IntAct=EBI-366083, EBI-1802965; Q923E4:Sirt1 (xeno); NbExp=4; IntAct=EBI-366083, EBI-1802585; Q15796:SMAD2; NbExp=7; IntAct=EBI-366083, EBI-1040141; Q9NRG4:SMYD2; NbExp=6; IntAct=EBI-366083, EBI-1055671; Q8R5A0:Smyd2 (xeno); NbExp=3; IntAct=EBI-366083, EBI-15612527; O95863:SNAI1; NbExp=2; IntAct=EBI-366083, EBI-1045459; Q06945:SOX4; NbExp=4; IntAct=EBI-366083, EBI-6672525; P08047:SP1; NbExp=3; IntAct=EBI-366083, EBI-298336; Q12772:SREBF2; NbExp=3; IntAct=EBI-366083, EBI-465059; Q96SB4:SRPK1; NbExp=3; IntAct=EBI-366083, EBI-539478; P63165:SUMO1; NbExp=3; IntAct=EBI-366083, EBI-80140; Q86TM6:SYVN1; NbExp=5; IntAct=EBI-366083, EBI-947849; P20226:TBP; NbExp=2; IntAct=EBI-366083, EBI-355371; P15884:TCF4; NbExp=2; IntAct=EBI-366083, EBI-533224; P32776:TFB1 (xeno); NbExp=7; IntAct=EBI-366083, EBI-19146; Q96GM8:TOE1; NbExp=3; IntAct=EBI-366083, EBI-717460; Q12888:TP53BP1; NbExp=6; IntAct=EBI-366083, EBI-396540; Q12888-1:TP53BP1; NbExp=17; IntAct=EBI-366083, EBI-8022649; Q13625:TP53BP2; NbExp=7; IntAct=EBI-366083, EBI-77642; Q9H3D4:TP63; NbExp=5; IntAct=EBI-366083, EBI-2337775; O88898:Tp63 (xeno); NbExp=2; IntAct=EBI-366083, EBI-2338025; P13693:TPT1; NbExp=7; IntAct=EBI-366083, EBI-1783169; O15164:TRIM24; NbExp=3; IntAct=EBI-366083, EBI-2130378; Q15672:TWIST1; NbExp=10; IntAct=EBI-366083, EBI-1797287; P26687:Twist1 (xeno); NbExp=4; IntAct=EBI-366083, EBI-6123119; P0CG48:UBC; NbExp=15; IntAct=EBI-366083, EBI-3390054; P63279:UBE2I; NbExp=3; IntAct=EBI-366083, EBI-80168; Q05086:UBE3A; NbExp=6; IntAct=EBI-366083, EBI-954357; Q96PU4:UHRF2; NbExp=3; IntAct=EBI-366083, EBI-625304; Q9H9J4:USP42; NbExp=2; IntAct=EBI-366083, EBI-2513638; Q9H9J4-2:USP42; NbExp=2; IntAct=EBI-366083, EBI-9118105; Q93009:USP7; NbExp=18; IntAct=EBI-366083, EBI-302474; P11473:VDR; NbExp=6; IntAct=EBI-366083, EBI-286357; Q99986:VRK1; NbExp=11; IntAct=EBI-366083, EBI-1769146; Q14191:WRN; NbExp=5; IntAct=EBI-366083, EBI-368417; Q9NZC7:WWOX; NbExp=2; IntAct=EBI-366083, EBI-4320739; O14980:XPO1; NbExp=3; IntAct=EBI-366083, EBI-355867; P12956:XRCC6; NbExp=2; IntAct=EBI-366083, EBI-353208; P61981:YWHAG; NbExp=5; IntAct=EBI-366083, EBI-359832; P63104:YWHAZ; NbExp=2; IntAct=EBI-366083, EBI-347088; Q8TAQ5:ZNF420; NbExp=4; IntAct=EBI-366083, EBI-3923307; Q9PST7:znf585b (xeno); NbExp=3; IntAct=EBI-366083, EBI-1782562;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:22726440}. Nucleus {ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19011621}. Nucleus, PML body {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12810724}. Endoplasmic reticulum {ECO:0000269|PubMed:17170702}. Mitochondrion matrix {ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:27323408}. Note=Interaction with BANP promotes nuclear localization (PubMed:15701641). Recruited into PML bodies together with CHEK2 (PubMed:12810724). Translocates to mitochondria upon oxidative stress (PubMed:22726440). Translocates to mitochondria in response to mitomycin C treatment (PubMed:27323408). {ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:27323408}.\nSUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm. Note=Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4.\nSUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Note=Localized mainly in the nucleus with minor staining in the cytoplasm.\nSUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Note=Localized in the nucleus in most cells but found in the cytoplasm in some cells.\nSUBCELLULAR LOCATION: [Isoform 4]: Nucleus. Cytoplasm. Note=Predominantly nuclear but translocates to the cytoplasm following cell stress.\nSUBCELLULAR LOCATION: [Isoform 7]: Nucleus. Cytoplasm. Note=Localized mainly in the nucleus with minor staining in the cytoplasm.\nSUBCELLULAR LOCATION: [Isoform 8]: Nucleus. Cytoplasm. Note=Localized in both nucleus and cytoplasm in most cells. In some cells, forms foci in the nucleus that are different from nucleoli.\nSUBCELLULAR LOCATION: [Isoform 9]: Cytoplasm.\nALTERNATIVE PRODUCTS: Event=Alternative promoter usage, Alternative splicing; Named isoforms=9; Name=1; Synonyms=p53, p53alpha;   IsoId=P04637-1; Sequence=Displayed; Name=2; Synonyms=I9RET, p53beta;   IsoId=P04637-2; Sequence=VSP_006535, VSP_006536; Name=3; Synonyms=p53gamma;   IsoId=P04637-3; Sequence=VSP_040560, VSP_040561; Name=4; Synonyms=Del40-p53, Del40-p53alpha, p47;   IsoId=P04637-4; Sequence=VSP_040832; Name=5; Synonyms=Del40-p53beta;   IsoId=P04637-5; Sequence=VSP_040832, VSP_006535, VSP_006536; Name=6; Synonyms=Del40-p53gamma;   IsoId=P04637-6; Sequence=VSP_040832, VSP_040560, VSP_040561; Name=7; Synonyms=Del133-p53, Del133-p53alpha;   IsoId=P04637-7; Sequence=VSP_040833; Name=8; Synonyms=Del133-p53beta;   IsoId=P04637-8; Sequence=VSP_040833, VSP_006535, VSP_006536; Name=9; Synonyms=Del133-p53gamma;   IsoId=P04637-9; Sequence=VSP_040833, VSP_040560, VSP_040561;\nTISSUE SPECIFICITY: Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine. {ECO:0000269|PubMed:16131611}.\nINDUCTION: Up-regulated in response to DNA damage. Isoform 2 is not induced in tumor cells in response to stress. {ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:16131611}.\nDOMAIN: The nuclear export signal acts as a transcriptional repression domain. The TADI and TADII motifs (residues 17 to 25 and 48 to 56) correspond both to 9aaTAD motifs which are transactivation domains present in a large number of yeast and animal transcription factors. {ECO:0000269|PubMed:17467953}.\nPTM: Acetylated. Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner. {ECO:0000269|PubMed:10656795, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:23431171}.\nPTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylated by HIPK1 (By similarity). Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser- 392 following UV but not gamma irradiation. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. Phosphorylated by NUAK1 at Ser-15 and Ser-392; was initially thought to be mediated by STK11/LKB1 but it was later shown that it is indirect and that STK11/LKB1-dependent phosphorylation is probably mediated by downstream NUAK1 (PubMed:21317932). It is unclear whether AMP directly mediates phosphorylation at Ser-15. Phosphorylated on Thr- 18 by isoform 1 and isoform 2 of VRK2. Phosphorylation on Thr-18 by isoform 2 of VRK2 results in a reduction in ubiquitination by MDM2 and an increase in acetylation by EP300. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser- 15, Ser-33 and Ser-46, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage. {ECO:0000250, ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11546806, ECO:0000269|PubMed:11551930, ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:16377624, ECO:0000269|PubMed:16704422, ECO:0000269|PubMed:1705009, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:18022393, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20124405, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:2141171, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:9372954}.\nPTM: Dephosphorylated by PP2A-PPP2R5C holoenzyme at Thr-55. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A.\nPTM: May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line. {ECO:0000269|PubMed:8632915}.\nPTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation (PubMed:10722742, PubMed:12810724, PubMed:15340061, PubMed:17170702, PubMed:19880522). Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome (PubMed:10722742, PubMed:12810724, PubMed:20173098). Ubiquitinated by MKRN1 at Lys-291 and Lys-292, which leads to proteasomal degradation (PubMed:19536131). Deubiquitinated by USP10, leading to its stabilization (PubMed:20096447). Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation (PubMed:19556538). Ubiquitination by TOPORS induces degradation (PubMed:19473992). Deubiquitination by USP7, leading to stabilization (PubMed:15053880). Isoform 4 is monoubiquitinated in an MDM2- independent manner (PubMed:15340061). Ubiquitinated by COP1, which leads to proteasomal degradation (PubMed:19837670). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (By similarity). {ECO:0000250|UniProtKB:P02340, ECO:0000269|PubMed:10722742, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19536131, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:25591766, ECO:0000269|PubMed:25732823}.\nPTM: Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation (PubMed:15525938, PubMed:16415881). Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity (PubMed:17108971). Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370 (PubMed:17108971). Dimethylated at Lys-373 by EHMT1 and EHMT2 (PubMed:20118233). Monomethylated at Lys-382 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity (PubMed:17707234). Dimethylation at Lys-370 and Lys-382 diminishes p53 ubiquitination, through stabilizing association with the methyl reader PHF20 (PubMed:22864287). Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53- mediated transcriptional activation (PubMed:17805299). Monomethylated at Arg-333 and dimethylated at Arg-335 and Arg-337 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (PubMed:19011621). {ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16415881, ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:22864287}.\nPTM: Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9. {ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37}.\nDISEASE: Note=TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers. TP53 defects are found in Barrett metaplasia a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma.\nDISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Li-Fraumeni syndrome (LFS) [MIM:151623]: An autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers. {ECO:0000269|PubMed:10484981, ECO:0000269|PubMed:1565144, ECO:0000269|PubMed:1737852, ECO:0000269|PubMed:1933902, ECO:0000269|PubMed:1978757, ECO:0000269|PubMed:2259385, ECO:0000269|PubMed:7887414, ECO:0000269|PubMed:8825920, ECO:0000269|PubMed:9452042}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. Note=The gene represented in this entry is involved in disease pathogenesis.\nDISEASE: 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=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Papilloma of choroid plexus (CPP) [MIM:260500]: A benign tumor of neuroectodermal origin that generally occurs in childhood, but has also been reported in adults. Although generally found within the ventricular system, choroid plexus papillomas can arise ectopically in the brain parenchyma or disseminate throughout the neuraxis. Patients present with signs and symptoms of increased intracranial pressure including headache, hydrocephalus, papilledema, nausea, vomiting, cranial nerve deficits, gait impairment, and seizures. {ECO:0000269|PubMed:12085209}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Adrenocortical carcinoma (ADCC) [MIM:202300]: A malignant neoplasm of the adrenal cortex and a rare childhood tumor. It occurs with increased frequency in patients with Beckwith-Wiedemann syndrome and Li-Fraumeni syndrome. {ECO:0000269|PubMed:11481490}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Basal cell carcinoma 7 (BCC7) [MIM:614740]: A common malignant skin neoplasm that typically appears on hair-bearing skin, most commonly on sun-exposed areas. It is slow growing and rarely metastasizes, but has potentialities for local invasion and destruction. It usually develops as a flat, firm, pale area that is small, raised, pink or red, translucent, shiny, and waxy, and the area may bleed following minor injury. Tumor size can vary from a few millimeters to several centimeters in diameter. {ECO:0000269|PubMed:21946351}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.\nDISEASE: Bone marrow failure syndrome 5 (BMFS5) [MIM:618165]: A form of bone marrow failure syndrome, a heterogeneous group of life-threatening disorders characterized by hematopoietic defects in association with a range of variable extra hematopoietic features. BMFS5 is an autosomal dominant form characterized by infantile onset of severe red cell anemia requiring transfusion. Additional features include hypogammaglobulinemia, poor growth with microcephaly, developmental delay, and seizures. {ECO:0000269|PubMed:30146126}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nMISCELLANEOUS: [Isoform 2]: Expressed in quiescent lymphocytes. Seems to be non-functional. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.\nMISCELLANEOUS: [Isoform 3]: Expressed in quiescent lymphocytes. Seems to be non-functional. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.\nMISCELLANEOUS: [Isoform 7]: Produced by alternative promoter usage. {ECO:0000305}.\nMISCELLANEOUS: [Isoform 8]: Produced by alternative promoter usage and alternative splicing. {ECO:0000305}.\nMISCELLANEOUS: [Isoform 9]: Produced by alternative promoter usage and alternative splicing. {ECO:0000305}.\nSIMILARITY: Belongs to the p53 family. {ECO:0000305}.\nWEB RESOURCE: Name=IARC TP53 mutation database; Note=Somatic and germline TP53 mutations in human cancers; URL=\"http://p53.iarc.fr/\";\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/P53ID88.html\";\nWEB RESOURCE: Name=NIEHS-SNPs; URL=\"http://egp.gs.washington.edu/data/tp53/\";\nWEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL=\"http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=TP53\";\nWEB RESOURCE: Name=Wikipedia; Note=P53 entry; URL=\"https://en.wikipedia.org/wiki/P53\";\nWEB RESOURCE: Name=Protein Spotlight; Note=On the right track - Issue 206 of August 2018; URL=\"https://web.expasy.org/spotlight/back_issues/206/\";", "primaryDomainId": "uniprot.P04637", "displayName": "P53_HUMAN", "synonyms": "Cellular tumor antigen p53, Antigen NY-CO-13, Phosphoprotein p53, Tumor suppressor p53", "taxid": 9606, "geneName": "TP53", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P04637", "id": "uniprot.P04637", "value": "uniprot.P04637"}}, {"data": {"domainIds": "entrez.9470", "primaryDomainId": "entrez.9470", "geneType": "protein-coding", "displayName": "eukaryotic translation initiation factor 4E family member 2", "synonyms": "eukaryotic translation initiation factor 4E type 2, eIF-4E type 2, eIF4E-like cap-binding protein, eIF4E-like protein 4E-LP, eukaryotic translation initiation factor 4E homologous protein, eukaryotic translation initiation factor 4E-like 3, mRNA cap-binding protein type 3", "chromosome": "2", "description": "eukaryotic translation initiation factor 4E family member 2", "approvedSymbol": "EIF4E2", "type": "Gene", "symbols": "4E-LP, 4EHP, EIF4EL3, IF4e, h4EHP", "mapLocation": "2q37.1", "graphics": {"fill": "#FFB6C1"}, "name": "EIF4E2", "id": "entrez.9470", "value": "entrez.9470"}}, {"data": {"domainIds": "uniprot.B9A023", "sequence": "MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKDNSSFRNTKITL", "comments": "SIMILARITY: Belongs to the eukaryotic initiation factor 4E family. {ECO:0000256|RuleBase:RU004374}.", "primaryDomainId": "uniprot.B9A023", "displayName": "B9A023_HUMAN", "synonyms": "Eukaryotic translation initiation factor 4E type 2 {ECO:0000313, Ensembl:ENSP00000386983}", "taxid": 9606, "geneName": "EIF4E2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B9A023", "id": "uniprot.B9A023", "value": "uniprot.B9A023"}}, {"data": {"domainIds": "uniprot.Q59FE1", "sequence": "GSGDSGGERMNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKDNSSFRNTKITL", "comments": "SIMILARITY: Belongs to the eukaryotic initiation factor 4E family. {ECO:0000256|RuleBase:RU004374}.", "primaryDomainId": "uniprot.Q59FE1", "displayName": "Q59FE1_HUMAN", "synonyms": "Eukaryotic translation initiation factor 4E member 2 variant {ECO:0000313, EMBL:BAD92756.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q59FE1", "id": "uniprot.Q59FE1", "value": "uniprot.Q59FE1"}}, {"data": {"domainIds": "uniprot.B8ZZ50", "sequence": "MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKAWEEFHGLVNSSGR", "comments": "SIMILARITY: Belongs to the eukaryotic initiation factor 4E family. {ECO:0000256|RuleBase:RU004374}.", "primaryDomainId": "uniprot.B8ZZ50", "displayName": "B8ZZ50_HUMAN", "synonyms": "Eukaryotic translation initiation factor 4E type 2 {ECO:0000313, Ensembl:ENSP00000387336}", "taxid": 9606, "geneName": "EIF4E2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B8ZZ50", "id": "uniprot.B8ZZ50", "value": "uniprot.B8ZZ50"}}, {"data": {"domainIds": "uniprot.B8ZZL3", "sequence": "MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP", "comments": "SIMILARITY: Belongs to the eukaryotic initiation factor 4E family. {ECO:0000256|RuleBase:RU004374}.", "primaryDomainId": "uniprot.B8ZZL3", "displayName": "B8ZZL3_HUMAN", "synonyms": "Eukaryotic translation initiation factor 4E type 2 {ECO:0000313, Ensembl:ENSP00000386424}", "taxid": 9606, "geneName": "EIF4E2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B8ZZL3", "id": "uniprot.B8ZZL3", "value": "uniprot.B8ZZL3"}}, {"data": {"domainIds": "uniprot.Q53RG0", "sequence": "MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP", "comments": "SIMILARITY: Belongs to the eukaryotic initiation factor 4E family. {ECO:0000256|RuleBase:RU004374}.", "primaryDomainId": "uniprot.Q53RG0", "displayName": "Q53RG0_HUMAN", "synonyms": "Eukaryotic translation initiation factor 4E member 2, isoform CRA_c {ECO:0000313, EMBL:EAW71009.1}, cDNA FLJ12456 fis, clone NT2RM1000661, highly similar to Eukaryotic translation initiation factor 4E type 3 {ECO:0000313, EMBL:BAG51083.1}", "taxid": 9606, "geneName": "tmp_locus_9", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q53RG0", "id": "uniprot.Q53RG0", "value": "uniprot.Q53RG0"}}, {"data": {"domainIds": "uniprot.O60573", "sequence": "MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP", "comments": "FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation (PubMed:9582349, PubMed:17368478, PubMed:25624349). Acts as a repressor of translation initiation (PubMed:22751931). In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity). {ECO:0000250|UniProtKB:Q8BMB3, ECO:0000269|PubMed:17368478, ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:25624349, ECO:0000269|PubMed:9582349}.\nSUBUNIT: Interacts with EIF4EBP1, EIF4EBP2 and EIF4EBP3 (PubMed:15153109, PubMed:17368478). Does not interact with eIF4G (EIF4G1, EIF4G2 or EIF4G3) (By similarity). Component of the 4EHP-GYF2 complex, at least composed of EIF4E2, GIGYF2 and ZNF598 (PubMed:22751931). Interacts with GIGYF2 (via the 4EHP-binding motif); the interaction is direct (PubMed:22751931). {ECO:0000250|UniProtKB:Q8BMB3, ECO:0000269|PubMed:15153109, ECO:0000269|PubMed:17368478, ECO:0000269|PubMed:22751931}.\nINTERACTION: Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-398610, EBI-10173507; Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-398610, EBI-10187270; Q9H257:CARD9; NbExp=3; IntAct=EBI-398610, EBI-751319; Q01850:CDR2; NbExp=3; IntAct=EBI-398610, EBI-1181367; Q9NRA8:EIF4ENIF1; NbExp=4; IntAct=EBI-398610, EBI-301024; Q99814:EPAS1; NbExp=2; IntAct=EBI-398610, EBI-447470; Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-398610, EBI-10172004; A1A4E9:KRT13; NbExp=3; IntAct=EBI-398610, EBI-10171552; P08727:KRT19; NbExp=3; IntAct=EBI-398610, EBI-742756; Q15323:KRT31; NbExp=3; IntAct=EBI-398610, EBI-948001; Q6A162:KRT40; NbExp=3; IntAct=EBI-398610, EBI-10171697; P60370:KRTAP10-5; NbExp=3; IntAct=EBI-398610, EBI-10172150; P60410:KRTAP10-8; NbExp=3; IntAct=EBI-398610, EBI-10171774; P60411:KRTAP10-9; NbExp=3; IntAct=EBI-398610, EBI-10172052; Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-398610, EBI-741037; Q9Y5V3:MAGED1; NbExp=3; IntAct=EBI-398610, EBI-716006; Q9UPY8:MAPRE3; NbExp=3; IntAct=EBI-398610, EBI-726739; Q8TD10:MIPOL1; NbExp=3; IntAct=EBI-398610, EBI-2548751; P15173:MYOG; NbExp=3; IntAct=EBI-398610, EBI-3906629; Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-398610, EBI-10172876; Q7Z3S9:NOTCH2NLA; NbExp=3; IntAct=EBI-398610, EBI-945833; Q9GZV8:PRDM14; NbExp=3; IntAct=EBI-398610, EBI-3957793; Q04864:REL; NbExp=3; IntAct=EBI-398610, EBI-307352; Q96R06:SPAG5; NbExp=3; IntAct=EBI-398610, EBI-413317; Q8NA61:SPERT; NbExp=3; IntAct=EBI-398610, EBI-741724; O43597:SPRY2; NbExp=3; IntAct=EBI-398610, EBI-742487; O75478:TADA2A; NbExp=3; IntAct=EBI-398610, EBI-742268; P15884:TCF4; NbExp=3; IntAct=EBI-398610, EBI-533224; Q08117:TLE5; NbExp=3; IntAct=EBI-398610, EBI-717810; O75069-4:TMCC2; NbExp=3; IntAct=EBI-398610, EBI-10177480; P14373:TRIM27; NbExp=3; IntAct=EBI-398610, EBI-719493; Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-398610, EBI-2130429; Q5T124:UBXN11; NbExp=3; IntAct=EBI-398610, EBI-746004; Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-398610, EBI-739895; Q70EL1:USP54; NbExp=3; IntAct=EBI-398610, EBI-946185; Q96C00:ZBTB9; NbExp=3; IntAct=EBI-398610, EBI-395708;\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=O60573-1; Sequence=Displayed; Name=2;   IsoId=O60573-2; Sequence=VSP_054783, VSP_054784;\nPTM: Ubiquitinated by ARIH1 (PubMed:14623119, PubMed:25624349). The consequences of ubiquitination are however unclear: according to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report ubiquitination leads to its subsequent degradation (PubMed:14623119). {ECO:0000269|PubMed:14623119, ECO:0000269|PubMed:25624349}.\nPTM: ISGylation enhances its cap structure-binding activity and translation-inhibition activity. {ECO:0000269|PubMed:17289916}.\nSIMILARITY: Belongs to the eukaryotic initiation factor 4E family. {ECO:0000305}.", "primaryDomainId": "uniprot.O60573", "displayName": "IF4E2_HUMAN", "synonyms": "Eukaryotic translation initiation factor 4E type 2, eIF-4E type 2, eIF4E type 2, Eukaryotic translation initiation factor 4E homologous protein, Eukaryotic translation initiation factor 4E-like 3, eIF4E-like protein 4E-LP, mRNA cap-binding protein 4EHP, h4EHP {ECO:0000303, PubMed:17368478}, mRNA cap-binding protein type 3", "taxid": 9606, "geneName": "EIF4E2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O60573", "id": "uniprot.O60573", "value": "uniprot.O60573"}}, {"data": {"domainIds": "entrez.10420", "primaryDomainId": "entrez.10420", "geneType": "protein-coding", "displayName": "testis associated actin remodelling kinase 2", "synonyms": "dual specificity testis-specific protein kinase 2, testicular protein kinase 2, testis-specific kinase 2", "chromosome": "1", "description": "testis associated actin remodelling kinase 2", "approvedSymbol": "TESK2", "type": "Gene", "symbols": "-", "mapLocation": "1p34.1", "graphics": {"fill": "#FFB6C1"}, "name": "TESK2", "id": "entrez.10420", "value": "entrez.10420"}}, {"data": {"domainIds": "uniprot.B4DFN2", "sequence": "MALKMNTLSSNRANMLKEVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINSGNLEQLLDSNLHLPWTVRVKLAYDIAVGLSYLHFKGIFHRDLTSKNCLIKRDENGYSAVVADFGLAEKIPDVSMGSEKLAVVGSPFWMAPEVLRDEPYNEKADVFSYGIILCEIIARIQADPDYLPRTENFGLDYDAFQHMVGDCPPDFLQLTFNCCNMDPKLRPSFVEIGKTLEEILSRLQEEEQERDRKLQPTARGLLEKAPGVKRLSSLDDKIPHKSPCPRRTIWLSRSQSDIFSRKPPRTVSVLDPYYRPRDGAARTPKVNPFSARQDLMGGKIKFFDLPSKSVISLVFDLDAPGPGTMPLADWQEPLAPPIRRWCSLPGSPEFLHQEACPFVGREESLSDGPPPRLSSLKYRVKEIPPFRASALPAAQAHEAMDCSILQEENGFGSRPQGTSPCPAGASEEMEVEERPAGSTPATFSTSGIGLQTQGKQDG", "primaryDomainId": "uniprot.B4DFN2", "displayName": "B4DFN2_HUMAN", "synonyms": "cDNA FLJ58133, highly similar to Dual specificity testis-specific protein kinase 2 {ECO:0000313, EMBL:BAG57493.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DFN2", "id": "uniprot.B4DFN2", "value": "uniprot.B4DFN2"}}, {"data": {"domainIds": "uniprot.Q96S53", "sequence": "MDRSKRNSIAGFPPRVERLEEFEGGGGGEGNVSQVGRVWPSSYRALISAFSRLTRLDDFTCEKIGSGFFSEVFKVRHRASGQVMALKMNTLSSNRANMLKEVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINSGNLEQLLDSNLHLPWTVRVKLAYDIAVGLSYLHFKGIFHRDLTSKNCLIKRDENGYSAVVADFGLAEKIPDVSMGSEKLAVVGSPFWMAPEVLRDEPYNEKADVFSYGIILCEIIARIQADPDYLPRTENFGLDYDAFQHMVGDCPPDFLQLTFNCCNMDPKLRPSFVEIGKTLEEILSRLQEEEQERDRKLQPTARGLLEKAPGVKRLSSLDDKIPHKSPCPRRTIWLSRSQSDIFSRKPPRTVSVLDPYYRPRDGAARTPKVNPFSARQDLMGGKIKFFDLPSKSVISLVFDLDAPGPGTMPLADWQEPLAPPIRRWRSLPGSPEFLHQEACPFVGREESLSDGPPPRLSSLKYRVKEIPPFRASALPAAQAHEAMDCSILQEENGFGSRPQGTSPCPAGASEEMEVEERPAGSTPATFSTSGIGLQTQGKQDG", "comments": "FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser- 3'. May play an important role in spermatogenesis.\nCATALYTIC ACTIVITY: 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=2.7.12.1;\nCATALYTIC ACTIVITY: 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=2.7.12.1;\nCATALYTIC ACTIVITY: 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=2.7.12.1;\nCOFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};\nCOFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};\nACTIVITY REGULATION: Activated by autophosphorylation on Ser-219. {ECO:0000250}.\nINTERACTION: P08238:HSP90AB1; NbExp=2; IntAct=EBI-1384110, EBI-352572;\nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11418599}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3;   Comment=Experimental confirmation may be lacking for some isoforms.; Name=1;   IsoId=Q96S53-1; Sequence=Displayed; Name=2;   IsoId=Q96S53-2; Sequence=VSP_004930; Name=3;   IsoId=Q96S53-3; Sequence=VSP_004931;\nTISSUE SPECIFICITY: Predominantly expressed in testis and prostate. Found predominantly in non-germinal Sertoli cells. {ECO:0000269|PubMed:10512679, ECO:0000269|PubMed:11418599}.\nSIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q96S53", "displayName": "TESK2_HUMAN", "synonyms": "Dual specificity testis-specific protein kinase 2, 2.7.12.1, Testicular protein kinase 2", "taxid": 9606, "geneName": "TESK2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q96S53", "id": "uniprot.Q96S53", "value": "uniprot.Q96S53"}}, {"data": {"domainIds": "entrez.23303", "primaryDomainId": "entrez.23303", "geneType": "protein-coding", "displayName": "kinesin family member 13B", "synonyms": "kinesin-like protein KIF13B, guanylate kinase associated kinesin, kinesin 13B, kinesin-like protein GAKIN", "chromosome": "8", "description": "kinesin family member 13B", "approvedSymbol": "KIF13B", "type": "Gene", "symbols": "GAKIN", "mapLocation": "8p12", "graphics": {"fill": "#FFB6C1"}, "name": "KIF13B", "id": "entrez.23303", "value": "entrez.23303"}}, {"data": {"domainIds": "uniprot.Q9NQT8", "sequence": "MGDSKVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNPVNTNLSKGDARGQPKVFAYDHCFWSMDESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNEDPNARIIRDLREEVEKLREQLTKAEAMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVGDDKCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKKKAEREDEDQDPSMKNENSSEQLDVDGDSSSEVSSEVNFNYEYAQMEVTMKALGSNDPMQSILNSLEQQHEEEKRSALERQRLMYEHELEQLRRRLSPEKQNCRSMDRFSFHSPSAQQRLRQWAEEREATLNNSLMRLREQIVKANLLVREANYIAEELDKRTEYKVTLQIPASSLDANRKRGSLLSEPAIQVRRKGKGKQIWSLEKLDNRLLDMRDLYQEWKECEEDNPVIRSYFKRADPFYDEQENHSLIGVANVFLESLFYDVKLQYAVPIINQKGEVAGRLHVEVMRLSGDVGERIAGGDEVAEVSFEKETQENKLVCMVKILQATGLPQHLSHFVFCKYSFWDQQEPVIVAPEVDTSSSSVSKEPHCMVVFDHCNEFSVNITEDFIEHLSEGALAIEVYGHKINDPRKNPALWDLGIIQAKTRSLRDRWSEVTRKLEFWVQILEQNENGEYCPVEVISAKDVPTGGIFQLRQGQSRRVQVEVKSVQESGTLPLMEECILSVGIGCVKVRPLRAPRTHETFHEEEEDMDSYQDRDLERLRRKWLNALTKRQEYLDQQLQKLVSKRDKTEDDADREAQLLEMRLTLTEERNAVMVPSAGSGIPGAPAEWTPVPGMETHIPVIFLDLNADDFSSQDNLDDPEAGGWDATLTGEEEEEFFELQIVKQHDGEVKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQLSHPADMQLVLRKRICVNVHGRQGFAQSLLKKMSHRSSIPGCGVTFEIVSNIPEDAQGVEEREALARMAANVENPASADSEAYIEKYLRSVLAVENLLTLDRLRQEVAVKEQLTGKGKLSRRSISSPNVNRLSGSRQDLIPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGPVRRRSTGLRLGAPEARRSATLSGSATNLASLTAALAKADRSHKNPENRKSWAS", "comments": "FUNCTION: Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes. {ECO:0000269|PubMed:20194617}.\nSUBUNIT: Binds to DLG1 and DLG4. Interacts (when phosphorylated at Ser- 1381 and Ser-1410) with 14-3-3. {ECO:0000269|PubMed:10859302, ECO:0000269|PubMed:20194617}.\nINTERACTION: O75689:ADAP1; NbExp=6; IntAct=EBI-766408, EBI-714732; Q12959-2:DLG1; NbExp=3; IntAct=EBI-766408, EBI-357500;\nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20194617}. Cell projection, axon {ECO:0000269|PubMed:20194617}. Note=accumulates at the distal part of the microtubules in the tips of axons, but not of dendrites.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q9NQT8-1; Sequence=Displayed; Name=2;   IsoId=Q9NQT8-2; Sequence=VSP_056360, VSP_056361;\nTISSUE SPECIFICITY: Ubiquitous.\nPTM: Phosphorylated at Ser-1381 and Ser-1410 by MARK2, promoting interaction with 14-3-3 and inhibiting microtubule-dependent accumulation and formation of axons. {ECO:0000269|PubMed:20194617}.\nSIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.\nSEQUENCE CAUTION: Sequence=BAA31614.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9NQT8", "displayName": "KI13B_HUMAN", "synonyms": "Kinesin-like protein KIF13B, Kinesin-like protein GAKIN", "taxid": 9606, "geneName": "KIF13B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9NQT8", "id": "uniprot.Q9NQT8", "value": "uniprot.Q9NQT8"}}, {"data": {"domainIds": "entrez.10749", "primaryDomainId": "entrez.10749", "geneType": "protein-coding", "displayName": "kinesin family member 1C", "synonyms": "kinesin-like protein KIF1C, spastic ataxia 2 (autosomal recessive)", "chromosome": "17", "description": "kinesin family member 1C", "approvedSymbol": "KIF1C", "type": "Gene", "symbols": "LTXS1, SATX2, SAX2, SPAX2, SPG58", "mapLocation": "17p13.2", "graphics": {"fill": "#FFB6C1"}, "name": "KIF1C", "id": "entrez.10749", "value": "entrez.10749"}}, {"data": {"domainIds": "uniprot.O43896", "sequence": "MAGASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKSFTFDYSYWSHTSTEDPQFASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEPGQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINEDPNARLIRELQEEVARLRELLMAQGLSASALEGLKTEEGSVRGALPAVSSPPAPVSPSSPTTHNGELEPSFSPNTESQIGPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERERGVPPPPGPPSEPVDWNFAQKELLEQQGIDIKLEMEKRLQDLENQYRKEKEEADLLLEQQRLYADSDSGDDSDKRSCEESWRLISSLREQLPPTTVQTIVKRCGLPSSGKRRAPRRVYQIPQRRRLQGKDPRWATMADLKMQAVKEICYEVALADFRHGRAEIEALAALKMRELCRTYGKPDGPGDAWRAVARDVWDTVGEEEGGGAGSGGGSEEGARGAEVEDLRAHIDKLTGILQEVKLQNSSKDRELQALRDRMLRMERVIPLAQDHEDENEEGGEVPWAPPEGSEAAEEAAPSDRMPSARPPSPPLSSWERVSRLMEEDPAFRRGRLRWLKQEQLRLQGLQGSGGRGGGLRRPPARFVPPHDCKLRFPFKSNPQHRESWPGMGSGEAPTPLQPPEEVTPHPATPARRPPSPRRSHHPRRNSLDGGGRSRGAGSAQPEPQHFQPKKHNSYPQPPQPYPAQRPPGPRYPPYTTPPRMRRQRSAPDLKESGAAV", "comments": "FUNCTION: Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:9685376}.\nSUBUNIT: Monomer. Interacts with BICD2. {ECO:0000269|PubMed:24482476, ECO:0000305}.\nINTERACTION: A0JNT9:Bicdl1 (xeno); NbExp=3; IntAct=EBI-1644048, EBI-7893170;\nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.\nTISSUE SPECIFICITY: Expressed in all tissues examined, with most abundant expression in heart and skeletal muscle. {ECO:0000269|PubMed:9685376}.\nPTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:9685376}.\nDISEASE: Spastic ataxia 2, autosomal recessive (SPAX2) [MIM:611302]: A neurologic disorder characterized by cerebellar ataxia, dysarthria, and variable spasticity of the lower limbs. Cognition is not affected. {ECO:0000269|PubMed:24319291, ECO:0000269|PubMed:24482476}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE- ProRule:PRU00283}.\nSEQUENCE CAUTION: Sequence=BAA31681.2; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.O43896", "displayName": "KIF1C_HUMAN", "synonyms": "Kinesin-like protein KIF1C", "taxid": 9606, "geneName": "KIF1C", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O43896", "id": "uniprot.O43896", "value": "uniprot.O43896"}}, {"data": {"domainIds": "entrez.5692", "primaryDomainId": "entrez.5692", "geneType": "protein-coding", "displayName": "proteasome 20S subunit beta 4", "synonyms": "proteasome subunit beta type-4, 26 kDa prosomal protein, hsBPROS26, macropain beta chain, multicatalytic endopeptidase complex beta chain, proteasome (prosome, macropain) subunit, beta type, 4, proteasome beta chain, proteasome chain 3, proteasome subunit HsN3, proteasome subunit beta 4, proteasome subunit beta7, proteasome subunit, beta type, 4, testis tissue sperm-binding protein Li 79P", "chromosome": "1", "description": "proteasome 20S subunit beta 4", "approvedSymbol": "PSMB4", "type": "Gene", "symbols": "HN3, HsN3, PRAAS3, PROS-26, PROS26", "mapLocation": "1q21.3", "graphics": {"fill": "#FFB6C1"}, "name": "PSMB4", "id": "entrez.5692", "value": "entrez.5692"}}, {"data": {"domainIds": "uniprot.A0A140VK46", "sequence": "MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE", "comments": "CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.;   EC=3.4.25.1; Evidence={ECO:0000256|PIRNR:PIRNR001213};\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001213}. Nucleus {ECO:0000256|PIRNR:PIRNR001213, ECO:0000256|SAAS:SAAS00551005}.\nSIMILARITY: Belongs to the peptidase T1B family. {ECO:0000256|PIRNR:PIRNR001213}.", "primaryDomainId": "uniprot.A0A140VK46", "displayName": "A0A140VK46_HUMAN", "synonyms": "Proteasome subunit beta {ECO:0000256, PIRNR:PIRNR001213}, 3.4.25.1 {ECO:0000256, PIRNR:PIRNR001213}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A140VK46", "id": "uniprot.A0A140VK46", "value": "uniprot.A0A140VK46"}}, {"data": {"domainIds": "uniprot.P28070", "sequence": "MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE", "comments": "FUNCTION: 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). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. {ECO:0000269|PubMed:12097147, ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.\nCATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.;   EC=3.4.25.1; Evidence={ECO:0000269|PubMed:27176742};\nSUBUNIT: 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. Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with PRPF19 (PubMed:11571290, PubMed:12097147). {ECO:0000269|PubMed:11571290, ECO:0000269|PubMed:12097147, ECO:0000269|PubMed:15660529, ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187, ECO:0000269|PubMed:9344905}.\nSUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax protein. {ECO:0000269|PubMed:8692272}.\nSUBUNIT: (Microbial infection) Interacts with HIV-1 Nef and Tat proteins. {ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:9344905}.\nINTERACTION: A1L4K1:FSD2; NbExp=3; IntAct=EBI-603350, EBI-5661036; P25788:PSMA3; NbExp=3; IntAct=EBI-603350, EBI-348380; P20618:PSMB1; NbExp=3; IntAct=EBI-603350, EBI-372273;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345}.\nINDUCTION: Up-regulated in fibrolamellar carcinomas. {ECO:0000269|PubMed:17367606}.\nDISEASE: Proteasome-associated autoinflammatory syndrome 3 (PRAAS3) [MIM:617591]: An autoinflammatory disorder characterized by onset in early infancy and recurrent fever, nodular dermatitis, myositis, panniculitis-induced lipodystrophy, lymphadenopathy, and immune dysregulation. Variable accompanying features may include joint contractures, hepatosplenomegaly, anemia, thrombocytopenia, recurrent infections, autoantibodies, and hypergammaglobulinemia. Some patients may have intracranial calcifications. PRAAS3 inheritance is autosomal recessive or digenic. {ECO:0000269|PubMed:26524591}. Note=The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.\nSIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- ProRule:PRU00809}.\nCAUTION: A report observed N-glycosylation at Asn-83 (PubMed:19139490). However, as the protein does not localize in an extracellular compartment of the cell, additional evidence is required to confirm this result. {ECO:0000305|PubMed:19139490}.", "primaryDomainId": "uniprot.P28070", "displayName": "PSB4_HUMAN", "synonyms": "Proteasome subunit beta type-4, 3.4.25.1 {ECO:0000269, PubMed:27176742}, 26 kDa prosomal protein, HsBPROS26, PROS-26, Macropain beta chain, Multicatalytic endopeptidase complex beta chain, Proteasome beta chain, Proteasome chain 3, HsN3", "taxid": 9606, "geneName": "PSMB4", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P28070", "id": "uniprot.P28070", "value": "uniprot.P28070"}}, {"data": {"domainIds": "entrez.83743", "primaryDomainId": "entrez.83743", "geneType": "protein-coding", "displayName": "glutamate rich WD repeat containing 1", "synonyms": "glutamate-rich WD repeat-containing protein 1, CUL4- and DDB1-associated WDR protein 4, WD repeat domain 28, glutamate rich WD repeat protein GRWD, regulator of ribosome biogenesis 1 homolog", "chromosome": "19", "description": "glutamate rich WD repeat containing 1", "approvedSymbol": "GRWD1", "type": "Gene", "symbols": "CDW4, GRWD, RRB1, WDR28", "mapLocation": "19q13.33", "graphics": {"fill": "#FFB6C1"}, "name": "GRWD1", "id": "entrez.83743", "value": "entrez.83743"}}, {"data": {"domainIds": "uniprot.Q9BQ67", "sequence": "MAARKGRRRTCETGEPMEAESGDTSSEGPAQVYLPGRGPPLREGEELVMDEEAYVLYHRAQTGAPCLSFDIVRDHLGDNRTELPLTLYLCAGTQAESAQSNRLMMLRMHNLHGTKPPPSEGSDEEEEEEDEEDEEERKPQLELAMVPHYGGINRVRVSWLGEEPVAGVWSEKGQVEVFALRRLLQVVEEPQALAAFLRDEQAQMKPIFSFAGHMGEGFALDWSPRVTGRLLTGDCQKNIHLWTPTDGGSWHVDQRPFVGHTRSVEDLQWSPTENTVFASCSADASIRIWDIRAAPSKACMLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRQFKSGSPVATFKQHVAPVTSVEWHPQDSGVFAASGADHQITQWDLAVERDPEAGDVEADPGLADLPQQLLFVHQGETELKELHWHPQCPGLLVSTALSGFTIFRTISV", "comments": "FUNCTION: Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness (PubMed:25990725). {ECO:0000269|PubMed:25990725}.\nSUBUNIT: Interacts with METTL18 (PubMed:23349634). Interacts with CDT1; origin binding of GRWD1 is dependent on CDT1 (PubMed:25990725). Interacts with CDC6; origin binding of GRWD1 is dependent on CDC6 (PubMed:25990725). Binds to histone H2A-H2B and H3-H4 complexes (PubMed:25990725). {ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:25990725}.\nSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Nucleus {ECO:0000269|PubMed:25990725}. Chromosome {ECO:0000269|PubMed:25990725}. Note=Present in the nucleus throughout interphase and is detached from chromatin at the onset of mitosis and rebinds at telophase when the pre-replication complexes (pre-RC) is formed (PubMed:25990725). {ECO:0000269|PubMed:25990725}.\nINDUCTION: Induced by E2F transcription factors (PubMed:14990995). {ECO:0000269|PubMed:14990995}.", "primaryDomainId": "uniprot.Q9BQ67", "displayName": "GRWD1_HUMAN", "synonyms": "Glutamate-rich WD repeat-containing protein 1", "taxid": 9606, "geneName": "GRWD1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9BQ67", "id": "uniprot.Q9BQ67", "value": "uniprot.Q9BQ67"}}, {"data": {"domainIds": "entrez.27005", "primaryDomainId": "entrez.27005", "geneType": "protein-coding", "displayName": "ubiquitin specific peptidase 21", "synonyms": "ubiquitin carboxyl-terminal hydrolase 21, NEDD8-specific protease, deubiquitinating enzyme 21, ubiquitin specific protease 21, ubiquitin thioesterase 21, ubiquitin thiolesterase 21, ubiquitin-specific processing protease 21, ubiquitin-specific protease 16", "chromosome": "1", "description": "ubiquitin specific peptidase 21", "approvedSymbol": "USP21", "type": "Gene", "symbols": "USP16, USP23", "mapLocation": "1q23.3", "graphics": {"fill": "#FFB6C1"}, "name": "USP21", "id": "entrez.27005", "value": "entrez.27005"}}, {"data": {"domainIds": "uniprot.Q9UK80", "sequence": "MPQASEHRLGRTREPPVNIQPRVGSKLPFAPRARSKERRNPASGPNPMLRPLPPRPGLPDERLKKLELGRGRTSGPRPRGPLRADHGVPLPGSPPPTVALPLPSRTNLARSKSVSSGDLRPMGIALGGHRGTGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLFSIRTEPPASHGSFHMISARSSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILANGPVPSPPRRGGALLEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPLQRLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLMQEPPRCL", "comments": "FUNCTION: Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates (PubMed:10799498). Deubiquitinates BAZ2A/TIP5 leading to its stabilization (PubMed:26100909). {ECO:0000250|UniProtKB:Q9QZL6, ECO:0000269|PubMed:10799498, ECO:0000269|PubMed:26100909}.\nCATALYTIC ACTIVITY: 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;\nSUBUNIT: Interacts with BEND3 and BAZ2A/TIP5. {ECO:0000269|PubMed:26100909}.\nINTERACTION: Q6A162:KRT40; NbExp=3; IntAct=EBI-373242, EBI-10171697;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21888622}. Nucleus {ECO:0000269|PubMed:21888622}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q9UK80-1; Sequence=Displayed; Name=2;   IsoId=Q9UK80-2; Sequence=VSP_036717, VSP_036718; Name=3;   IsoId=Q9UK80-3; Sequence=VSP_036719;\nTISSUE SPECIFICITY: Highly expressed in heart, pancreas and skeletal muscle. Also expressed in brain, placenta, liver and kidney, and at very low level in lung. {ECO:0000269|PubMed:10799498}.\nSIMILARITY: Belongs to the peptidase C19 family. USP21 subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAF61308.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=AAG17222.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAD92136.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9UK80", "displayName": "UBP21_HUMAN", "synonyms": "Ubiquitin carboxyl-terminal hydrolase 21, 3.4.19.12, Deubiquitinating enzyme 21, Ubiquitin thioesterase 21, Ubiquitin-specific-processing protease 21", "taxid": 9606, "geneName": "USP21", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9UK80", "id": "uniprot.Q9UK80", "value": "uniprot.Q9UK80"}}, {"data": {"domainIds": "entrez.284615", "primaryDomainId": "entrez.284615", "geneType": "protein-coding", "displayName": "ankyrin repeat domain 34A", "synonyms": "ankyrin repeat domain-containing protein 34A, ankyrin repeat domain 34", "chromosome": "1", "description": "ankyrin repeat domain 34A", "approvedSymbol": "ANKRD34A", "type": "Gene", "symbols": "ANKRD34", "mapLocation": "1q21.1", "graphics": {"fill": "#FFB6C1"}, "name": "ANKRD34A", "id": "entrez.284615", "value": "entrez.284615"}}, {"data": {"domainIds": "uniprot.Q69YU3", "sequence": "MLHTEGHALLRAVGQGKLRLARLLLEGGAYVNEGDAQGETALMAACRARYDDPQNKARMVRYLLEQGADPNIADRLGRTALMHACAGGGGAAVASLLLAHGADPSVRDHAGASALVHALDRGDRETLATLLDACKAKGTEVIIITTDTSPSGTKKTRQYLNSPPSPGVEDPAPASPSPGFCTSPSEIQLQTAGGGGRGMLSPRAQEEEEKRDVFEFPLPKPPDDPSPSEPLPKPPRHPPKPLKRLNSEPWGLVAPPQPVPPTEGRPGIERLTAEFNGLTLTGRPRLSRRHSTEGPEDPPPWAEKVTSGGPLSRRNTAPEAQESGPPSGLRQKLSRMEPVELDTPGHLCPDSPESSRLSLERRRYSASPLTLPPAGSAPSPRQSQESLPGAVSPLSGRRRSPGLLERRGSGTLLLDHISQTRPGFLPPLNVSPHPPIPDIRPQPGGRAPSLPAPPYAGAPGSPRTKRKLVRRHSMQTEQIRLLGGFQSLGGPGEPGR", "comments": "PTM: Methylated at Gln-15 by N6AMT1. {ECO:0000269|PubMed:26797129}.\nSIMILARITY: Belongs to the ANKRD34 family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q69YU3", "displayName": "AN34A_HUMAN", "synonyms": "Ankyrin repeat domain-containing protein 34A", "taxid": 9606, "geneName": "ANKRD34A", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q69YU3", "id": "uniprot.Q69YU3", "value": "uniprot.Q69YU3"}}, {"data": {"domainIds": "entrez.23380", "primaryDomainId": "entrez.23380", "geneType": "protein-coding", "displayName": "SLIT-ROBO Rho GTPase activating protein 2", "synonyms": "SLIT-ROBO Rho GTPase-activating protein 2, SLIT-ROBO GAP2, formin-binding protein 2, rho GTPase-activating protein 34", "chromosome": "1", "description": "SLIT-ROBO Rho GTPase activating protein 2", "approvedSymbol": "SRGAP2", "type": "Gene", "symbols": "ARHGAP34, FNBP2, SRGAP2A, SRGAP3", "mapLocation": "1q32.1", "graphics": {"fill": "#FFB6C1"}, "name": "SRGAP2", "id": "entrez.23380", "value": "entrez.23380"}}, {"data": {"domainIds": "uniprot.A0A075B7B5", "sequence": "MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTLIS", "primaryDomainId": "uniprot.A0A075B7B5", "displayName": "A0A075B7B5_HUMAN", "synonyms": "SLIT-ROBO Rho GTPase-activating protein 2 {ECO:0000313, Ensembl:ENSP00000473954}", "taxid": 9606, "geneName": "SRGAP2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A075B7B5", "id": "uniprot.A0A075B7B5", "value": "uniprot.A0A075B7B5"}}, {"data": {"domainIds": "uniprot.B4DFE5", "sequence": "MMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV", "primaryDomainId": "uniprot.B4DFE5", "displayName": "B4DFE5_HUMAN", "synonyms": "cDNA FLJ56407, highly similar to SLIT-ROBO Rho GTPase-activating protein 2 {ECO:0000313, EMBL:BAG57406.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DFE5", "id": "uniprot.B4DFE5", "value": "uniprot.B4DFE5"}}, {"data": {"domainIds": "uniprot.B7Z3G4", "sequence": "MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQRELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMREYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTLIS", "primaryDomainId": "uniprot.B7Z3G4", "displayName": "B7Z3G4_HUMAN", "synonyms": "cDNA FLJ60271, highly similar to SLIT-ROBO Rho GTPase-activating protein 2 {ECO:0000313, EMBL:BAH12200.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B7Z3G4", "id": "uniprot.B7Z3G4", "value": "uniprot.B7Z3G4"}}, {"data": {"domainIds": "uniprot.B7ZM87", "sequence": "MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV", "primaryDomainId": "uniprot.B7ZM87", "displayName": "B7ZM87_HUMAN", "synonyms": "SLIT-ROBO Rho GTPase-activating protein 2 {ECO:0000313, Ensembl:ENSP00000485517}, SRGAP2 protein {ECO:0000313, EMBL:AAI44344.1}", "taxid": 9606, "geneName": "SRGAP2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B7ZM87", "id": "uniprot.B7ZM87", "value": "uniprot.B7ZM87"}}, {"data": {"domainIds": "uniprot.O75044", "sequence": "MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV", "comments": "FUNCTION: RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. Its interaction and inhibition by SRGAP2C reduces the rate of spine maturation, alters dendritic spine morphology and density and indirectly increases neuronal migration. It may have implications for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia. {ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, ECO:0000269|PubMed:22559944}.\nSUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP1 and SRGAP3 through its F-BAR domain. Interacts (via SH3 domain) with GPHN (By similarity). Interacts with SRGAP2C; formation of the heterodimer alters SRGAP2 function. Interacts (via SH3 domain) with FMNL1 (activated by RAC1); regulates the actin filament severing activity of FMNL1 and actin dynamics. Interacts (via SH3 domain) with FMNL3. Interacts with RAC1; specifically stimulates RAC1 GTPase activity. Probably interacts with ROBO1 and ROBO2. Interacts with FASLG. Interacts with PRMT5. {ECO:0000250, ECO:0000269|PubMed:11672528, ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, ECO:0000269|PubMed:22559944, ECO:0000305}.\nINTERACTION: Self; NbExp=5; IntAct=EBI-1051034, EBI-1051034; P48023:FASLG; NbExp=2; IntAct=EBI-1051034, EBI-495538; O95466:FMNL1; NbExp=3; IntAct=EBI-1051034, EBI-720020; P42858:HTT; NbExp=3; IntAct=EBI-1051034, EBI-466029; O14744:PRMT5; NbExp=4; IntAct=EBI-1051034, EBI-351098; Q9Y6N7:ROBO1; NbExp=3; IntAct=EBI-1051034, EBI-399762; P63104:YWHAZ; NbExp=2; IntAct=EBI-1051034, EBI-347088;\nSUBCELLULAR LOCATION: Cell membrane. Cell projection, dendritic spine. Cell junction, synapse, postsynaptic density {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Cell projection, lamellipodium. Cytoplasmic vesicle, phagosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to actin-rich phagosomes during phagocytosis. Translocates from nucleus to cytoplasm during development. {ECO:0000250}.\nDOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions. {ECO:0000269|PubMed:22467852}.\nPTM: Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions. {ECO:0000269|PubMed:20810653}.\nDISEASE: Note=A chromosomal aberration disrupting SRGAP2 has been found in a patient with early infantile epileptic encephalopathy. Balanced translocation t(1;9)(q32;q13) (PubMed:22106086). {ECO:0000269|PubMed:22106086}.\nMISCELLANEOUS: There are 3 duplications of SRGAP2 in the human genome as a result of segmental gene duplications. SRGAP2C is the only one to be fixed at a diploid state in the human genome. Moreover, SRGAP2C is functional, interacts with and inhibits SRGAP2 and is human-specific. The appearance of SRGAP2C in the human genome is estimated to 2,4 million years ago, which corresponds to the beginning of neocortex expansion in human evolution and it may have played an important role in this process through its interaction with SRGAP2 function.\nSEQUENCE CAUTION: Sequence=BAA32301.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};\nWEB RESOURCE: Name=Protein Spotlight; Note=Branching out - Issue 143 of October 2012; URL=\"https://web.expasy.org/spotlight/back_issues/143\";", "primaryDomainId": "uniprot.O75044", "displayName": "SRGP2_HUMAN", "synonyms": "SLIT-ROBO Rho GTPase-activating protein 2, srGAP2, Formin-binding protein 2, Rho GTPase-activating protein 34", "taxid": 9606, "geneName": "SRGAP2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O75044", "id": "uniprot.O75044", "value": "uniprot.O75044"}}, {"data": {"domainIds": "entrez.51547", "primaryDomainId": "entrez.51547", "geneType": "protein-coding", "displayName": "sirtuin 7", "synonyms": "NAD-dependent protein deacetylase sirtuin-7, NAD-dependent deacetylase sirtuin-7, SIR2-like protein 7, regulatory protein SIR2 homolog 7, silent mating type information regulation 2, S.cerevisiae, homolog 7, sir2-related protein type 7, sirtuin type 7", "chromosome": "17", "description": "sirtuin 7", "approvedSymbol": "SIRT7", "type": "Gene", "symbols": "SIR2L7", "mapLocation": "17q25.3", "graphics": {"fill": "#FFB6C1"}, "name": "SIRT7", "id": "entrez.51547", "value": "entrez.51547"}}, {"data": {"domainIds": "uniprot.Q9NRC8", "sequence": "MAAGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESADLVTELQGRSRRREGLKRRQEEVCDDPEELRGKVRELASAVRNAKYLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRSVSAADLSEAEPTLTHMSITRLHEQKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCVPNREYVRVFDVTERTALHRHQTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASRADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVMRLLMAELGLEIPAYSRWQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT", "comments": "FUNCTION: NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase and deglutarylase), depending on the context (PubMed:22722849, PubMed:26907567, PubMed:30653310, PubMed:31542297). Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac) (PubMed:22722849, PubMed:30420520). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression (PubMed:22722849, PubMed:30653310). H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor (PubMed:22722849). Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells (PubMed:22722849). Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes (PubMed:30653310). Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53 (PubMed:24207024, PubMed:26867678, PubMed:28147277, PubMed:28886238, PubMed:28426094, PubMed:30540930, PubMed:31075303, PubMed:30944854, PubMed:28790157). Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex (PubMed:16618798, PubMed:19174463, PubMed:24207024). Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:16618798, PubMed:19174463, PubMed:24207024). In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription (PubMed:24207024). Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis (PubMed:19174463). Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3- 55K, a core subunit of the U3 snoRNP complex (PubMed:26867678). Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65 (PubMed:31075303). Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation (PubMed:30944854). Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B) (PubMed:28886238). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (PubMed:28426094). Deacetylates FBL, promoting histone- glutamine methyltransferase activity of FBL (PubMed:30540930). Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51 (PubMed:28147277). Required to prevent R- loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). In addition to protein deacetylase activity, also acts as protein-lysine deacylase (PubMed:27436229, PubMed:27997115, PubMed:31542297). Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (PubMed:31542297). Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double- strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair (PubMed:27436229). Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ) (By similarity). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina (PubMed:31226208). Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability (PubMed:29728458). Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity). {ECO:0000250|UniProtKB:Q8BKJ9, ECO:0000269|PubMed:16618798, ECO:0000269|PubMed:19174463, ECO:0000269|PubMed:22722849, ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:26907567, ECO:0000269|PubMed:27436229, ECO:0000269|PubMed:27997115, ECO:0000269|PubMed:28147277, ECO:0000269|PubMed:28426094, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:29728458, ECO:0000269|PubMed:30420520, ECO:0000269|PubMed:30540930, ECO:0000269|PubMed:30653310, ECO:0000269|PubMed:30944854, ECO:0000269|PubMed:31075303, ECO:0000269|PubMed:31226208, ECO:0000269|PubMed:31542297}.\nCATALYTIC ACTIVITY: 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={ECO:0000255|PROSITE-ProRule:PRU00236,   ECO:0000269|PubMed:22722849, ECO:0000269|PubMed:24207024,   ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:26907567,   ECO:0000269|PubMed:28147277, ECO:0000269|PubMed:28426094,   ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:28886238,   ECO:0000269|PubMed:30420520, ECO:0000269|PubMed:30540930,   ECO:0000269|PubMed:30653310, ECO:0000269|PubMed:30944854,   ECO:0000269|PubMed:31075303}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637;   Evidence={ECO:0000269|PubMed:22722849, ECO:0000269|PubMed:26867678,   ECO:0000269|PubMed:26907567, ECO:0000269|PubMed:28147277,   ECO:0000269|PubMed:28426094, ECO:0000269|PubMed:28790157,   ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:30420520,   ECO:0000269|PubMed:30540930, ECO:0000269|PubMed:30653310,   ECO:0000269|PubMed:30944854, ECO:0000269|PubMed:31075303};\nCATALYTIC ACTIVITY: Reaction=H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-   glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;   Xref=Rhea:RHEA:47664, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875,   ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,   ChEBI:CHEBI:57540, ChEBI:CHEBI:87828, ChEBI:CHEBI:87829;   Evidence={ECO:0000269|PubMed:31542297}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47665;   Evidence={ECO:0000269|PubMed:31542297};\nCATALYTIC ACTIVITY: Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-   succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;   Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877,   ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,   ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832;   Evidence={ECO:0000269|PubMed:27436229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47669;   Evidence={ECO:0000269|PubMed:27436229};\nCATALYTIC ACTIVITY: 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={ECO:0000250|UniProtKB:Q8BKJ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23501;   Evidence={ECO:0000250|UniProtKB:Q8BKJ9};\nCOFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;   Evidence={ECO:0000250|UniProtKB:Q9NXA8}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8};\nACTIVITY REGULATION: NAD-dependent protein-lysine deacetylase and deacylase activities are activated by nucleic acids (PubMed:26907567, PubMed:27997115). Histone deacetylase activity is activated by DNA (PubMed:27997115). Protein-lysine deacylase activity is activated by RNA (PubMed:26907567). H3K18Ac histone deacetylase activity is inhibited by methylation at Arg-388 (PubMed:30420520). H3K18Ac histone deacetylase activity is inhibited by deubiquitination by USP7 (PubMed:28655758). {ECO:0000269|PubMed:26907567, ECO:0000269|PubMed:27997115, ECO:0000269|PubMed:28655758, ECO:0000269|PubMed:30420520}.\nSUBUNIT: Interacts with UBTF and the RNA polymerase I complex (PubMed:16618798, PubMed:19174463). Interacts with components of the B- WICH complex, such as MYBBP1A, SMARCA5/SNF2H and BAZ1B/WSTF (PubMed:22586326). Interacts with ELK4, leading to stabilization at target promoters for H3K18Ac deacetylation (PubMed:22722849). Interacts with histone H2A and/or histone H2B (PubMed:22722849). Interacts with DNMT1 (By similarity). Interacts with SIRT1 (By similarity). {ECO:0000250|UniProtKB:Q8BKJ9, ECO:0000269|PubMed:16618798, ECO:0000269|PubMed:19174463, ECO:0000269|PubMed:22586326, ECO:0000269|PubMed:22722849}.\nINTERACTION: P28324:ELK4; NbExp=3; IntAct=EBI-716046, EBI-11277718; Q16656:NRF1; NbExp=2; IntAct=EBI-716046, EBI-2547810;\nSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:19174463, ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:28426094, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:30420520}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:31075303}. Chromosome {ECO:0000269|PubMed:27436229, ECO:0000269|PubMed:31226208}. Cytoplasm {ECO:0000269|PubMed:11953824}. Note=Mainly localizes in the nucleolus and nucleoplasm (PubMed:24207024, PubMed:28886238, PubMed:28790157, PubMed:31075303). Associated with rDNA promoter and transcribed region (PubMed:16079181, PubMed:19174463). Associated with nucleolar organizer regions during mitosis (PubMed:16079181, PubMed:19174463). In response to stress, released from nucleolus to nucleoplasm (PubMed:24207024). Associated with chromatin (PubMed:22722849). In response to DNA damage, recruited to DNA double-strand breaks (DSBs) sites (PubMed:27436229) (Probable). Located close to the nuclear membrane when in the cytoplasm (PubMed:11953824). {ECO:0000269|PubMed:11953824, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:19174463, ECO:0000269|PubMed:22722849, ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:27436229, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:31075303, ECO:0000305|PubMed:30944854}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q9NRC8-1; Sequence=Displayed; Name=2;   IsoId=Q9NRC8-2; Sequence=VSP_008736, VSP_008737; Name=3;   IsoId=Q9NRC8-3; Sequence=VSP_044396, VSP_044397;\nINDUCTION: Overexpressed in thyroid carcinoma cell lines and tissues, but not in adenomas. {ECO:0000269|PubMed:11953824}.\nPTM: Phosphorylated during mitosis. {ECO:0000305|PubMed:19174463}.\nPTM: Methylation at Arg-388 by PRMT6 inhibits the H3K18Ac histone deacetylase activity, promoting mitochondria biogenesis and maintaining mitochondria respiration. {ECO:0000269|PubMed:30420520}.\nPTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains (PubMed:28655758). Deubiquitinated by USP7, inhibiting the H3K18Ac histone deacetylase activity and regulating gluconeogenesis (PubMed:28655758). {ECO:0000269|PubMed:28655758}.\nSIMILARITY: Belongs to the sirtuin family. Class IV subfamily. {ECO:0000305}.\nCAUTION: Was originally termed SIR-T8/SIRT8 (PubMed:11953824). This was later retracted (PubMed:12454780, PubMed:12454781). {ECO:0000303|PubMed:11953824, ECO:0000303|PubMed:12454780, ECO:0000303|PubMed:12454781}.\nSEQUENCE CAUTION: Sequence=CAB70848.2; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9NRC8", "displayName": "SIR7_HUMAN", "synonyms": "NAD-dependent protein deacetylase sirtuin-7, 2.3.1.286 {ECO:0000269, PubMed:24207024, ECO:0000269, PubMed:26867678, ECO:0000269, PubMed:28426094, ECO:0000269, PubMed:28886238, ECO:0000269, PubMed:30540930, ECO:0000269, PubMed:31075303}, NAD-dependent protein deacylase sirtuin-7, 2.3.1.- {ECO:0000269, PubMed:27436229, ECO:0000269, PubMed:31542297}, Regulatory protein SIR2 homolog 7, SIR2-like protein 7", "taxid": 9606, "geneName": "SIRT7", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9NRC8", "id": "uniprot.Q9NRC8", "value": "uniprot.Q9NRC8"}}, {"data": {"domainIds": "entrez.1915", "primaryDomainId": "entrez.1915", "geneType": "protein-coding", "displayName": "eukaryotic translation elongation factor 1 alpha 1", "synonyms": "elongation factor 1-alpha 1, CTCL tumor antigen, EF-1-alpha-1, EF1a-like protein, cervical cancer suppressor 3, elongation factor 1 alpha subunit, elongation factor Tu, epididymis secretory sperm binding protein, eukaryotic elongation factor 1 A-1, eukaryotic translation elongation factor 1 alpha 1-like 14, glucocorticoid receptor AF-1 specific elongation factor, leukocyte receptor cluster (LRC) member 7, leukocyte receptor cluster member 7, prostate tumor-inducing protein 1, translation elongation factor 1 alpha 1-like 14", "chromosome": "6", "description": "eukaryotic translation elongation factor 1 alpha 1", "approvedSymbol": "EEF1A1", "type": "Gene", "symbols": "CCS-3, CCS3, EE1A1, EEF-1, EEF1A, EF-Tu, EF1A, GRAF-1EF, HNGC:16303, LENG7, PTI1, eEF1A-1", "mapLocation": "6q13", "graphics": {"fill": "#FFB6C1"}, "name": "EEF1A1", "id": "entrez.1915", "value": "entrez.1915"}}, {"data": {"domainIds": "uniprot.P68104", "sequence": "MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK", "comments": "FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. {ECO:0000269|PubMed:17177976}.\nSUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS1. May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7) (By similarity). Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation. Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner. Interacts with PPP1R16B (PubMed:26497934). Interacts with SPHK1 and SPHK2; both interactions increase SPHK1 and SPHK2 kinase activity (PubMed:18263879). {ECO:0000250, ECO:0000269|PubMed:12426392, ECO:0000269|PubMed:12426393, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17980171, ECO:0000269|PubMed:18029264, ECO:0000269|PubMed:18263879, ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:26497934, ECO:0000269|PubMed:8650580}.\nINTERACTION: Q8NFJ9:BBS1; NbExp=3; IntAct=EBI-352162, EBI-1805484; Q00987:MDM2; NbExp=9; IntAct=EBI-352162, EBI-389668; P12004:PCNA; NbExp=2; IntAct=EBI-352162, EBI-358311; P54725:RAD23A; NbExp=2; IntAct=EBI-352162, EBI-746453; Q9NYA1:SPHK1; NbExp=2; IntAct=EBI-352162, EBI-985303; Q14166:TTLL12; NbExp=3; IntAct=EBI-352162, EBI-923010; P63104:YWHAZ; NbExp=2; IntAct=EBI-352162, EBI-347088; Q05516:ZBTB16; NbExp=4; IntAct=EBI-352162, EBI-711925; Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-352162, EBI-524753;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:8650580}. Nucleus {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:8650580}. Nucleus, nucleolus {ECO:0000269|PubMed:8650580}. Cell membrane {ECO:0000269|PubMed:26497934}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery (PubMed:19158340). Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens (PubMed:8650580). Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B (PubMed:26497934). {ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:26497934, ECO:0000269|PubMed:8650580}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=P68104-1; Sequence=Displayed; Name=2;   IsoId=P68104-2; Sequence=VSP_057184;\nTISSUE SPECIFICITY: Brain, placenta, lung, liver, kidney, pancreas but barely detectable in heart and skeletal muscle.\nINDUCTION: By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress. {ECO:0000269|PubMed:9677419}.\nPTM: ISGylated. {ECO:0000269|PubMed:16139798}.\nPTM: Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2 (PubMed:26497934). {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17595531, ECO:0000269|PubMed:20832312, ECO:0000269|PubMed:26497934}.\nPTM: Trimethylated at Lys-79 by EEF1AKMT1 (PubMed:26545399). Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation (PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (PubMed:25144183). 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 Gly-2 by EEF1AKNMT (PubMed:30143613). Mono- and dimethylated at Lys-55 by EEF1AKNMT; dimethylated form is predominant (PubMed:30143613, PubMed:30612740). {ECO:0000269|PubMed:25144183, ECO:0000269|PubMed:26545399, ECO:0000269|PubMed:28108655, ECO:0000269|PubMed:28520920, ECO:0000269|PubMed:30143613, ECO:0000269|PubMed:30612740}.\nSIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAA52367.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/EEF1A1ID40407ch6q13.html\";", "primaryDomainId": "uniprot.P68104", "displayName": "EF1A1_HUMAN", "synonyms": "Elongation factor 1-alpha 1, EF-1-alpha-1, Elongation factor Tu, EF-Tu, Eukaryotic elongation factor 1 A-1, eEF1A-1, Leukocyte receptor cluster member 7", "taxid": 9606, "geneName": "EEF1A1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P68104", "id": "uniprot.P68104", "value": "uniprot.P68104"}}, {"data": {"domainIds": "uniprot.Q6IPS9", "sequence": "MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK", "comments": "FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000256|RuleBase:RU000325}.\nSIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000256|RuleBase:RU000325}.", "primaryDomainId": "uniprot.Q6IPS9", "displayName": "Q6IPS9_HUMAN", "synonyms": "Elongation factor 1-alpha {ECO:0000256, RuleBase:RU000325}", "taxid": 9606, "geneName": "EEF1A1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q6IPS9", "id": "uniprot.Q6IPS9", "value": "uniprot.Q6IPS9"}}, {"data": {"domainIds": "entrez.57530", "primaryDomainId": "entrez.57530", "geneType": "protein-coding", "displayName": "cingulin", "synonyms": "cingulin", "chromosome": "1", "description": "cingulin", "approvedSymbol": "CGN", "type": "Gene", "symbols": "-", "mapLocation": "1q21.3", "graphics": {"fill": "#FFB6C1"}, "name": "CGN", "id": "entrez.57530", "value": "entrez.57530"}}, {"data": {"domainIds": "uniprot.Q9P2M7", "sequence": "MAEPRGPVDHGVQIRFITEPVSGAEMGTLRRGGRRPAKDARASTYGVAVRVQGIAGQPFVVLNSGEKGGDSFGVQIKGANDQGASGALSSDLELPENPYSQVKGFPAPSQSSTSDEEPGAYWNGKLLRSHSQASLAGPGPVDPSNRSNSMLELAPKVASPGSTIDTAPLSSVDSLINKFDSQLGGQARGRTGRRTRMLPPEQRKRSKSLDSRLPRDTFEERERQSTNHWTSSTKYDNHVGTSKQPAQSQNLSPLSGFSRSRQTQDWVLQSFEEPRRSAQDPTMLQFKSTPDLLRDQQEAAPPGSVDHMKATIYGILREGSSESETSVRRKVSLVLEKMQPLVMVSSGSTKAVAGQGELTRKVEELQRKLDEEVKKRQKLEPSQVGLERQLEEKTEECSRLQELLERRKGEAQQSNKELQNMKRLLDQGEDLRHGLETQVMELQNKLKHVQGPEPAKEVLLKDLLETRELLEEVLEGKQRVEEQLRLRERELTALKGALKEEVASRDQEVEHVRQQYQRDTEQLRRSMQDATQDHAVLEAERQKMSALVRGLQRELEETSEETGHWQSMFQKNKEDLRATKQELLQLRMEKEEMEEELGEKIEVLQRELEQARASAGDTRQVEVLKKELLRTQEELKELQAERQSQEVAGRHRDRELEKQLAVLRVEADRGRELEEQNLQLQKTLQQLRQDCEEASKAKMVAEAEATVLGQRRAAVETTLRETQEENDEFRRRILGLEQQLKETRGLVDGGEAVEARLRDKLQRLEAEKQQLEEALNASQEEEGSLAAAKRALEARLEEAQRGLARLGQEQQTLNRALEEEGKQREVLRRGKAELEEQKRLLDRTVDRLNKELEKIGEDSKQALQQLQAQLEDYKEKARREVADAQRQAKDWASEAEKTSGGLSRLQDEIQRLRQALQASQAERDTARLDKELLAQRLQGLEQEAENKKRSQDDRARQLKGLEEKVSRLETELDEEKNTVELLTDRVNRGRDQVDQLRTELMQERSARQDLECDKISLERQNKDLKTRLASSEGFQKPSASLSQLESQNQLLQERLQAEEREKTVLQSTNRKLERKVKELSIQIEDERQHVNDQKDQLSLRVKALKRQVDEAEEEIERLDGLRKKAQREVEEQHEVNEQLQARIKSLEKDSWRKASRSAAESALKNEGLSSDEEFDSVYDPSSIASLLTESNLQTSSC", "comments": "FUNCTION: Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier.\nSUBUNIT: Homodimer (By similarity). Interacts with TJP1/ZO-1. {ECO:0000250, ECO:0000269|PubMed:12023291}.\nINTERACTION: P63104:YWHAZ; NbExp=3; IntAct=EBI-79537, EBI-347088;\nSUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Note=Localizes to the apical junction complex composed of tight and adherens junctions. {ECO:0000250}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q9P2M7-1; Sequence=Displayed; Name=2;   IsoId=Q9P2M7-2; Sequence=VSP_037039, VSP_037040;\nTISSUE SPECIFICITY: Localized on the cytoplasmic face of tight junctions of polarized epithelia and some endothelia. Expressed in pancreas, kidney, liver and lung, but not in skeletal muscle, placenta, brain or heart.\nDOMAIN: Deletion of the ZO-1 interaction motif (ZIM) decreases but does not abolish colocalization with ZO-1.\nMISCELLANEOUS: [Isoform 2]: May be due to an intron retention. {ECO:0000305}.\nSIMILARITY: Belongs to the cingulin family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAF74498.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=AAI52446.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAA92557.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAF82696.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=EAW53434.1; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9P2M7", "displayName": "CING_HUMAN", "synonyms": "Cingulin", "taxid": 9606, "geneName": "CGN", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9P2M7", "id": "uniprot.Q9P2M7", "value": "uniprot.Q9P2M7"}}, {"data": {"domainIds": "entrez.135295", "primaryDomainId": "entrez.135295", "geneType": "protein-coding", "displayName": "serine and arginine rich splicing factor 12", "synonyms": "serine/arginine-rich splicing factor 12, 35 kDa SR repressor protein, SR splicing factor 12, serine-arginine repressor protein (35 kDa), splicing factor, arginine/serine-rich 13B, splicing factor, arginine/serine-rich 19", "chromosome": "6", "description": "serine and arginine rich splicing factor 12", "approvedSymbol": "SRSF12", "type": "Gene", "symbols": "SFRS13B, SFRS19, SRrp35", "mapLocation": "6q15", "graphics": {"fill": "#FFB6C1"}, "name": "SRSF12", "id": "entrez.135295", "value": "entrez.135295"}}, {"data": {"domainIds": "uniprot.B3KVR7", "sequence": "MKSKERHPCSPSDHRRSRSPSQRRTRSRSSSWGRNRRRSDSLKESRHRRFSYSQSKSRSKSLPRRSTSARQSRTPRRNFGSRGRSRSKSLQKRSKSIGKSQSSSPQKQTSSGTKSRSHGRHSDSIARSPCKSPKGYTNSETKVQTAKHSHFRSHSRSRSYRHKNSW", "primaryDomainId": "uniprot.B3KVR7", "displayName": "B3KVR7_HUMAN", "synonyms": "Serine-arginine repressor protein (35 kDa), isoform CRA_b {ECO:0000313, EMBL:EAW48562.1}, cDNA FLJ41221 fis, clone BRAMY2028914, highly similar to 35 kDa SR repressor protein {ECO:0000313, EMBL:BAG53879.1}", "taxid": 9606, "geneName": "SRrp35", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B3KVR7", "id": "uniprot.B3KVR7", "value": "uniprot.B3KVR7"}}, {"data": {"domainIds": "uniprot.Q8WXF0", "sequence": "MSRYTRPPNTSLFIRNVADATRPEDLRREFGRYGPIVDVYIPLDFYTRRPRGFAYVQFEDVRDAEDALYNLNRKWVCGRQIEIQFAQGDRKTPGQMKSKERHPCSPSDHRRSRSPSQRRTRSRSSSWGRNRRRSDSLKESRHRRFSYSQSKSRSKSLPRRSTSARQSRTPRRNFGSRGRSRSKSLQKRSKSIGKSQSSSPQKQTSSGTKSRSHGRHSDSIARSPCKSPKGYTNSETKVQTAKHSHFRSHSRSRSYRHKNSW", "comments": "FUNCTION: Splicing factor that seems to antagonize SR proteins in pre- mRNA splicing regulation. {ECO:0000269|PubMed:11684676}.\nSUBCELLULAR LOCATION: Nucleus {ECO:0000305}.\nTISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:11684676}.\nSIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=EAW48561.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q8WXF0", "displayName": "SRS12_HUMAN", "synonyms": "Serine/arginine-rich splicing factor 12, 35 kDa SR repressor protein, SRrp35, Splicing factor, arginine/serine-rich 13B, Splicing factor, arginine/serine-rich 19", "taxid": 9606, "geneName": "SRSF12", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q8WXF0", "id": "uniprot.Q8WXF0", "value": "uniprot.Q8WXF0"}}, {"data": {"domainIds": "entrez.23031", "primaryDomainId": "entrez.23031", "geneType": "protein-coding", "displayName": "microtubule associated serine/threonine kinase 3", "synonyms": "microtubule-associated serine/threonine-protein kinase 3", "chromosome": "19", "description": "microtubule associated serine/threonine kinase 3", "approvedSymbol": "MAST3", "type": "Gene", "symbols": "-", "mapLocation": "19p13.11", "graphics": {"fill": "#FFB6C1"}, "name": "MAST3", "id": "entrez.23031", "value": "entrez.23031"}}, {"data": {"domainIds": "uniprot.O60307", "sequence": "MDESSLLRRRGLQKELSLPRRGRGCRSGNRKSLVVGTPSPTLSRPLSPLSVPTAGSSPLDSPRNFSAASALNFPFARRADGRRWSLASLPSSGYGTNTPSSTLSSSSSSRERLHQLPFQPTPDELHFLSKHFRSSENVLDEEGGRSPRLRPRSRSLSPGRATGTFDNEIVMMNHVYRERFPKATAQMEGRLQEFLTAYAPGARLALADGVLGFIHHQIVELARDCLAKSGENLVTSRYFLEMQEKLERLLQDAHERSDSEEVSFIVQLVRKLLIIISRPARLLECLEFDPEEFYHLLEAAEGHAREGQGIKTDLPQYIIGQLGLAKDPLEEMVPLSHLEEEQPPAPESPESRALVGQSRRKPCESDFETIKLISNGAYGAVYLVRHRDTRQRFAIKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMFCSFETRRHLCMVMEYVEGGDCATLLKNMGPLPVDMARLYFAETVLALEYLHNYGIVHRDLKPDNLLITSLGHIKLTDFGLSKIGLMSMATNLYEGHIEKDAREFIDKQVCGTPEYIAPEVIFRQGYGKPVDWWAMGVVLYEFLVGCVPFFGDTPEELFGQVVSDEIMWPEGDEALPADAQDLITRLLRQSPLDRLGTGGTHEVKQHPFFLALDWAGLLRHKAEFVPQLEAEDDTSYFDTRSERYRHLGSEDDETNDEESSTEIPQFSSCSHRFSKVYSSSEFLAVQPTPTFAERSFSEDREEGWERSEVDYGRRLSADIRLRSWTSSGSSCQSSSSQPERGPSPSLLNTISLDTMPKFAFSSEDEGVGPGPAGPKRPVFILGEPDPPPAATPVMPKPSSLSADTAALSHARLRSNSIGARHSTPRPLDAGRGRRLGGPRDPAPEKSRASSSGGSGGGSGGRVPKSASVSALSLIITADDGSGGPLMSPLSPRSLSSNPSSRDSSPSRDPSPVCGSLRPPIVIHSSGKKYGFSLRAIRVYMGDSDVYTVHHVVWSVEDGSPAQEAGLRAGDLITHINGESVLGLVHMDVVELLLKSGNKISLRTTALENTSIKVGPARKNVAKGRMARRSKRSRRRETQDRRKSLFKKISKQTSVLHTSRSFSSGLHHSLSSSESLPGSPTHSLSPSPTTPCRSPAPDVPADTTASPPSASPSSSSPASPAAAGHTRPSSLHGLAAKLGPPRPKTGRRKSTSSIPPSPLACPPISAPPPRSPSPLPGHPPAPARSPRLRRGQSADKLGTGERLDGEAGRRTRGPEAELVVMRRLHLSERRDSFKKQEAVQEVSFDEPQEEATGLPTSVPQIAVEGEEAVPVALGPTGRD", "comments": "CATALYTIC ACTIVITY: 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;\nCATALYTIC ACTIVITY: 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;\nCOFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};\nSUBUNIT: Interacts with PTEN. {ECO:0000269|PubMed:15951562}.\nINTERACTION: P60484:PTEN; NbExp=3; IntAct=EBI-311420, EBI-696162;\nSIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. {ECO:0000305}.\nCAUTION: It is uncertain whether Met-1, Met-171 or Met-172 is the initiator. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAC62830.1; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.O60307", "displayName": "MAST3_HUMAN", "synonyms": "Microtubule-associated serine/threonine-protein kinase 3, 2.7.11.1", "taxid": 9606, "geneName": "MAST3", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O60307", "id": "uniprot.O60307", "value": "uniprot.O60307"}}, {"data": {"domainIds": "entrez.9201", "primaryDomainId": "entrez.9201", "geneType": "protein-coding", "displayName": "doublecortin like kinase 1", "synonyms": "serine/threonine-protein kinase DCLK1, doublecortin domain-containing protein 3A, doublecortin-like and CAM kinase-like 1", "chromosome": "13", "description": "doublecortin like kinase 1", "approvedSymbol": "DCLK1", "type": "Gene", "symbols": "CL1, CLICK1, DCAMKL1, DCDC3A, DCLK", "mapLocation": "13q13.3", "graphics": {"fill": "#FFB6C1"}, "name": "DCLK1", "id": "entrez.9201", "value": "entrez.9201"}}, {"data": {"domainIds": "uniprot.B7Z5K4", "sequence": "MLELIEVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRSSQHGGSSTSLASTKVCSSMDENDGPGEEVSEEGFQIPATITERYKVGRTIGDGNFAVVKECVERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVGFPSPYWDNVSDSAKELITMMLLVDVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPNSTAAGVSVIATTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF", "comments": "SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000256|RuleBase:RU000304}.", "primaryDomainId": "uniprot.B7Z5K4", "displayName": "B7Z5K4_HUMAN", "synonyms": "cDNA FLJ50623, highly similar to Serine/threonine-protein kinase DCAMKL1 {ECO:0000313, EMBL:BAH12940.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B7Z5K4", "id": "uniprot.B7Z5K4", "value": "uniprot.B7Z5K4"}}, {"data": {"domainIds": "uniprot.Q5VZY9", "sequence": "MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGSPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASSSRRSTTKSPGPSRRSKSPASTSSVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRDLYRPLSSDDLDSVGDSV", "primaryDomainId": "uniprot.Q5VZY9", "displayName": "Q5VZY9_HUMAN", "synonyms": "Serine/threonine-protein kinase DCLK1 {ECO:0000313, Ensembl:ENSP00000369222}", "taxid": 9606, "geneName": "DCLK1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q5VZY9", "id": "uniprot.Q5VZY9", "value": "uniprot.Q5VZY9"}}, {"data": {"domainIds": "uniprot.O15075", "sequence": "MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGSPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASSSRRSTTKSPGPSRRSKSPASTSSVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRSSQHGGSSTSLASTKVCSSMDENDGPGEEVSEEGFQIPATITERYKVGRTIGDGNFAVVKECVERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELITMMLLVDVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPNSTAAGVSVIATTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF", "comments": "FUNCTION: Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.\nCATALYTIC ACTIVITY: 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;\nCATALYTIC ACTIVITY: 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;\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4;   Comment=Additional isoforms seem to exist. Type A (AS and AL) and   type B (BS and BL) isoforms differ respectively by the presence or   absence of the doublecortin domain. An alternative splicing occurring   in 3' of the mRNA produces the long (L) instead of the short (S)   isoforms.; Name=2; Synonyms=AL;   IsoId=O15075-1; Sequence=Displayed; Name=1; Synonyms=AS;   IsoId=O15075-2; Sequence=VSP_004907; Name=3; Synonyms=BS;   IsoId=O15075-3; Sequence=VSP_004905, VSP_004906, VSP_004907; Name=4; Synonyms=BL;   IsoId=O15075-4; Sequence=VSP_004905, VSP_004906;\nTISSUE SPECIFICITY: In fetal tissues, highly expressed in brain, detectable in lung and liver, but not in kidney. In adult tissues, expressed ubiquitously in the brain, detectable in the heart, liver, spleen, thymus, prostate, testis, ovary, small intestine and colon. The type A isoforms seem to be expressed predominantly in fetal brain whereas type B isoforms are expressed abundantly in both fetal and adult brain. {ECO:0000269|PubMed:10051403}.\nINDUCTION: Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). {ECO:0000269|PubMed:16548883}.\nSIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=BAA20824.2; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.O15075", "displayName": "DCLK1_HUMAN", "synonyms": "Serine/threonine-protein kinase DCLK1, 2.7.11.1, Doublecortin domain-containing protein 3A, Doublecortin-like and CAM kinase-like 1, Doublecortin-like kinase 1", "taxid": 9606, "geneName": "DCLK1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O15075", "id": "uniprot.O15075", "value": "uniprot.O15075"}}, {"data": {"domainIds": "entrez.4809", "primaryDomainId": "entrez.4809", "geneType": "protein-coding", "displayName": "small nuclear ribonucleoprotein 13", "synonyms": "NHP2-like protein 1, NHP2 non-histone chromosome protein 2-like 1, SNU13 homolog, small nuclear ribonucleoprotein (U4/U6.U5), U4/U6.U5 tri-snRNP 15.5 kDa protein, [U4/U6.U5] tri-snRNP 15.5 kD RNA binding protein, high mobility group-like nuclear protein 2 homolog 1, non-histone chromosome protein 2-like 1, sperm specific antigen 1", "chromosome": "22", "description": "small nuclear ribonucleoprotein 13", "approvedSymbol": "SNU13", "type": "Gene", "symbols": "15.5K, FA-1, FA1, NHP2L1, NHPX, OTK27, SNRNP15-5, SPAG12, SSFA1", "mapLocation": "22q13.2", "graphics": {"fill": "#FFB6C1"}, "name": "SNU13", "id": "entrez.4809", "value": "entrez.4809"}}, {"data": {"domainIds": "uniprot.Q6FHM6", "sequence": "MTEADVNPKAYPLADAHLTKKLLDLVQQSCNYKQLRKGANEATKTLNRGISEFIVMAADAEPLEIILHLPLLCEDKNVPYVFVRSKQALGRACGVSRPVIACSVTIKEGSQLKQQIQSIQQSIERLLV", "comments": "FUNCTION: Common component of the spliceosome and rRNA processing machinery. {ECO:0000256|RuleBase:RU366039}.\nSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|RuleBase:RU366039}.\nSIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family. {ECO:0000256|RuleBase:RU366039}.", "primaryDomainId": "uniprot.Q6FHM6", "displayName": "Q6FHM6_HUMAN", "synonyms": "Ribonucloprotein {ECO:0000256, RuleBase:RU366039}", "taxid": 9606, "geneName": "NHP2L1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q6FHM6", "id": "uniprot.Q6FHM6", "value": "uniprot.Q6FHM6"}}, {"data": {"domainIds": "uniprot.P55769", "sequence": "MTEADVNPKAYPLADAHLTKKLLDLVQQSCNYKQLRKGANEATKTLNRGISEFIVMAADAEPLEIILHLPLLCEDKNVPYVFVRSKQALGRACGVSRPVIACSVTIKEGSQLKQQIQSIQQSIERLLV", "comments": "FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:28781166). Binds to the 5'-stem-loop of U4 snRNA and thereby contributes to spliceosome assembly (PubMed:10545122, PubMed:17412961). The protein undergoes a conformational change upon RNA-binding (PubMed:17412961). {ECO:0000269|PubMed:10545122, ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:28781166}.\nSUBUNIT: Identified in the spliceosome B complex (PubMed:28781166). 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, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39 (PubMed:16723661, PubMed:26912367). Interacts with RAD17 and PRPF31 (PubMed:10593953, PubMed:17412961, PubMed:21784869). The complex formed by SNU13 and PRPF31 binds U4 snRNA (PubMed:17412961). The complex formed by SNU13 and PRPF31 binds also U4atac snRNA, a characteristic component of specific, less abundant spliceosomal complexes (PubMed:21784869). {ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:21784869, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.\nINTERACTION: P04591:gag (xeno); NbExp=2; IntAct=EBI-712228, EBI-6179727; Q9UHK0:NUFIP1; NbExp=2; IntAct=EBI-712228, EBI-2563549;\nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}. Nucleus, nucleolus {ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:12429849, ECO:0000269|Ref.7}. Note=Concentrated in the dense fibrillar component of the nucleolus. {ECO:0000269|PubMed:10593953}.\nTISSUE SPECIFICITY: Ubiquitous.\nSIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family. {ECO:0000305}.", "primaryDomainId": "uniprot.P55769", "displayName": "NH2L1_HUMAN", "synonyms": "NHP2-like protein 1, High mobility group-like nuclear protein 2 homolog 1, OTK27, SNU13 homolog, hSNU13, U4/U6.U5 small nuclear ribonucleoprotein SNU13 {ECO:0000312, HGNC:HGNC:7819}, U4/U6.U5 tri-snRNP 15.5 kDa protein", "taxid": 9606, "geneName": "SNU13", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P55769", "id": "uniprot.P55769", "value": "uniprot.P55769"}}, {"data": {"domainIds": "entrez.83541", "primaryDomainId": "entrez.83541", "geneType": "protein-coding", "displayName": "family with sequence similarity 110 member A", "synonyms": "protein FAM110A", "chromosome": "20", "description": "family with sequence similarity 110 member A", "approvedSymbol": "FAM110A", "type": "Gene", "symbols": "C20orf55, F10, bA371L19.3", "mapLocation": "20p13", "graphics": {"fill": "#FFB6C1"}, "name": "FAM110A", "id": "entrez.83541", "value": "entrez.83541"}}, {"data": {"domainIds": "uniprot.Q9BQ89", "sequence": "MPVHTLSPGAPSAPALPCRLRTRVPGYLLRGPADGGARKPSAVERLEADKAKYVKSLHVANTRQEPVQPLLSKQPLFSPETRRTVLTPSRRALPGPCRRPQLDLDILSSLIDLCDSPVSPAEASRTPGRAEGAGRPPPATPPRPPPSTSAVRRVDVRPLPASPARPCPSPGPAAASSPARPPGLQRSKSDLSERFSRAAADLERFFNFCGLDPEEARGLGVAHLARASSDIVSLAGPSAGPGSSEGGCSRRSSVTVEERARERVPYGVSVVERNARVIKWLYGLRQARESPAAEG", "comments": "SUBUNIT: May interact with CSPP1. {ECO:0000305}.\nINTERACTION: O95273:CCNDBP1; NbExp=3; IntAct=EBI-1752811, EBI-748961; Q01850:CDR2; NbExp=3; IntAct=EBI-1752811, EBI-1181367; Q08379:GOLGA2; NbExp=5; IntAct=EBI-1752811, EBI-618309; P19012:KRT15; NbExp=5; IntAct=EBI-1752811, EBI-739566; Q15323:KRT31; NbExp=5; IntAct=EBI-1752811, EBI-948001; Q13064:MKRN3; NbExp=5; IntAct=EBI-1752811, EBI-2340269; Q5JR59-3:MTUS2; NbExp=3; IntAct=EBI-1752811, EBI-11522433; P16333:NCK1; NbExp=2; IntAct=EBI-1752811, EBI-389883; Q8ND90:PNMA1; NbExp=3; IntAct=EBI-1752811, EBI-302345; Q6NUQ1:RINT1; NbExp=5; IntAct=EBI-1752811, EBI-726876; O75558:STX11; NbExp=3; IntAct=EBI-1752811, EBI-714135; P36406:TRIM23; NbExp=5; IntAct=EBI-1752811, EBI-740098; P14373:TRIM27; NbExp=3; IntAct=EBI-1752811, EBI-719493; Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-1752811, EBI-2130429; Q86WT6:TRIM69; NbExp=3; IntAct=EBI-1752811, EBI-749955; Q86WT6-2:TRIM69; NbExp=4; IntAct=EBI-1752811, EBI-11525489; Q8N6Y0:USHBP1; NbExp=5; IntAct=EBI-1752811, EBI-739895;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17499476}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17499476}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:17499476}. Note=Distributed throughout the cytoplasm during mitosis, accumulating at spindle poles.\nTISSUE SPECIFICITY: Detected in thyroid, lymph node, trachea, adrenal gland, bone marrow, spleen, thymus, prostate, and peripheral blood leukocyte. Detected at lower levels in stomach, testis and spinal cord. {ECO:0000269|PubMed:17499476}.\nDEVELOPMENTAL STAGE: During the cell cycle, expression is increased during S phase and G2/M phase. {ECO:0000269|PubMed:17499476}.\nINDUCTION: Up-regulated in stimulated lymphocytes. {ECO:0000269|PubMed:17499476}.\nSIMILARITY: Belongs to the FAM110 family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q9BQ89", "displayName": "F110A_HUMAN", "synonyms": "Protein FAM110A", "taxid": 9606, "geneName": "FAM110A", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9BQ89", "id": "uniprot.Q9BQ89", "value": "uniprot.Q9BQ89"}}, {"data": {"domainIds": "entrez.10075", "primaryDomainId": "entrez.10075", "geneType": "protein-coding", "displayName": "HECT, UBA and WWE domain containing E3 ubiquitin protein ligase 1", "synonyms": "E3 ubiquitin-protein ligase HUWE1, ARF-binding protein 1, BJ-HCC-24 tumor antigen, HECT domain protein LASU1, HECT, UBA and WWE domain containing 1, E3 ubiquitin protein ligase, HECT-type E3 ubiquitin transferase HUWE1, Mcl-1 ubiquitin ligase E3, URE-binding protein 1, homologous to E6AP carboxyl terminus homologous protein 9, large structure of UREB1, upstream regulatory element-binding protein 1", "chromosome": "X", "description": "HECT, UBA and WWE domain containing E3 ubiquitin protein ligase 1", "approvedSymbol": "HUWE1", "type": "Gene", "symbols": "ARF-BP1, HECTH9, HSPC272, Ib772, LASU1, MRXST, MULE, URE-B1, UREB1", "mapLocation": "Xp11.22", "graphics": {"fill": "#FFB6C1"}, "name": "HUWE1", "id": "entrez.10075", "value": "entrez.10075"}}, {"data": {"domainIds": "uniprot.A0A024R9W5", "sequence": "MKVDRTKLKKTPTEAPADCRALIDKLKVCNDEQLLLELQQIKTWNIGKCELYHWVDLLDRFDGILADAGQTVENMSWMLVCDRPEREQLKMLLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKRSNYITRLGSDKRTPLLTRLQHLAESWGGKENGFGLAECCRDLHMMKYPPSATTLHFEFYADPGAEVKIEKRTTSNTLHYIHIEQLDKISESPSEIMESLTKMYSIPKDKQMLLFTHIRLAHGFSNHRKRLQAVQARLHAISILVYSNALQESANSILYNGLIEELVDVLQITDKQLMEIKAASLRTLTSIVHLERTPKLSSIIDCTGTASYHGFLPVLVRNCIQAMIDPSMDPYPHQFATALFSFLYHLASYDAGGEALVSCGMMEALLKVIKFLGDEQDQITFVTRAVRVVDLITNLDMAAFQSHSGLSIFIYRLEHEVDLCRKECPFVIKPKIQRPNTTQEGEEMETDMDGVQCIPQRAALLKSMLNFLKKAIQDPAFSDGIRHVMDGSLPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRRRRSSDPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKYICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQAMQSFNSTQQNETEPNQQVVGTEERIPIPLMDYILNVMKFVESILSNNTTDDHCQEFVNQKGLLPLVTILGLPNLPIDFPTSAACQAVAGVCKSILTLSHEPKVLQEGLLQLDSILSSLEPLHRPIESPGGSVLLRELACAGNVADATLSAQATPLLHALTAAHAYIMMFVHTCRVGQSEIRSISVNQWGSQLGLSVLSKLSQLYCSLVWESTVLLSLCTPNSLPSGCEFGQADMQKLVPKDEKAGTTQGGKRSDGEQDGAAGSMDASTQGLLEGIGLDGDTLAPMETDEPTASDSKGKSKITPAMAARIKQIKPLLSASSRLGRALAELFGLLVKLCVGSPVRQRRSHHAASTTTAPTPAARSTASALTKLLTKGLSWQPPPYTPTPRFRLTFFICSVGFTSPMLFDERKYPYHLMLQKFLCSGGHNALFETFNWALSMGGKVPVSEGLEHSDLPDGTGEFLDAWLMLVEKMVNPTTVLESPHSLPAKLPGGVQNFPQFSALRFLVVTQKAAFTCIKNLWNRKPLKVYGGRMAESMLAILCHILRGEPVIRERLSKEKEGSRGEEDTGQEEGGSRREPQVNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHPPPIMGGVVRDLSMSEEDQMMRAIAMSLGQDIPMDQRAESPEEVACRKEEEERKAREKQEEEEAKCLEKFQDADPLEQDELHTFTDTMLPGCFHLLDELPDTVYRVCDLIMTAIKRNGADYRDMILKQVVNQVWEAADVLIKAALPLTTSDTKTVSEWISQMATLPQASNLATRILLLTLLFEELKLPCAWVVESSGILNVLIKLLEVVQPCLQAAKEQKEVQTPKWITPVLLLIDFYEKTAISSKRRAQMTKYLQSNSNNWRWFDDRSGRWCSYSASNNSTIDSAWKSGETSVRFTAGRRRYTVQFTTMVQVNEETGNRRPVMLTLLRVPRLNKNSKNSNGQELEKTLEESKEMDIKRKENKGNDTPLALESTNTEKETSLEETKIGEILIQGLTEDMVTVLIRACVSMLGVPVDPDTLHATLRLCLRLTRDHKYAMMFAELKSTRMILNLTQSSGFNGFTPLVTLLLRHIIEDPCTLRHTMEKVVRSAATSGAGSTTSGVVSGSLGSREINYILRVLGPAACRNPDIFTEVANCCIRIALPAPRGSGTASDDEFENLRIKGPNAVQLVKTTPLKPSPLPVIPDTIKEVIYDMLNALAAYHAPEEADKSDPKPGVMTQEVGQLLQDMGDDVYQQYRSLTRQSSDFDTQSGFSINSQVFAADGASTETSASGTSQGEASTPEESRDGKKDKEGDRASEEGKQKGKGSKPLMPTSTILRLLAELVRSYVGIATLIANYSYTVGQSELIKEDCSVLAFVLDHLLPHTQNAEDKDTPALARLFLASLAAAGSGTDAQVALVNEVKAALGRALAMAESTEKHARLQAVMCIISTIMESCPSTSSFYSSATAKTQHNGMNNIIRLFLKKGLVNDLARVPHSLDLSSPNMANTVNAALKPLETLSRIVNQPSSLFGSKSASSKNKSEQDAQGASQDSSSNQQDPGEPGEAEVQEEDHDVTQTEVADGDIMDGEAETDSVVIAGQPEVLSSQEMQVENELEDLIDELLERDGGSGNSTIIVSRSGEDESQEDVLMDEAPSNLSQASTLQANREDSMNILDPEDEEEHTQEEDSSGSNEDEDDSQDEEEEEEEDEEDDQEDDEGEEGDEDDDDDGSEMELDEDYPDMNASPLVRFERFDREDDLIIEFDNMFSSATDIPPSPGNIPTTHPLMVRHADHSSLTLGSGSSTTRLTQGIGRSQRTLRQLTANTGHTIHVHYPGNRQPNPPLILQRLLGPSAAADILQLSSSLPLQSRGRARLLVGNDDVHIIARSDDELLDDFFHDQSTATSQAGTLSSIPTALTRWTEECKVLDAESMHDCVSVVKVSIVNHLEFLRDEELEERREKRRKQLAEEETKITDKGKEDKENRDQSAQCTASKSNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTLQSSQQQPTLPTPPALGEVPQELQSPAGEGGSSTQLLMPVEPEELGPTRPSGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLEEAVGDTSAAGSSEQPRAGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQLGIRPPTRTAPSTNSSAPAVVGNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQRRELAQNASSDTPMDPVTFIQTLPSDLRRSVLEDMEDSVLAVMPPDIAAEAQALRREQEARQRQLMHERLFGHSSTSALSAILRSPAFTSRLSGNRGVQYTRLAVQRGGTFQMGGSSSHNRPSGSNVDTLLRLRGRLLLDHEALSCLLVLLFVDEPKLNTSRLHRVLRNLCYHAQTRHWVIRSLLSILQRSSESELCIETPKLTTSEEKGKKSSKSCGSSSHENRPLDLLHKMESKSSNQLSWLSVSMDAALGCRTNIFQIQRSGGRKHTEKHASGGSTVHIHPQAAPVVCRHVLDTLIQLAKVFPSHFTQQRTKETNCESDRERGNKACSPCSSQSSSSGICTDFWDLLVKLDNMNVSRKGKNSVKSVPVSAGGEGETSPYSLEASPLGQLMNMLSHPVIRRSSLLTEKLLRLLSLISIALPENKVSEAQANSGSGASSTTTATSTTSTTTTTAASTTPTPPTAPTPVTSAPALVAATAISTIVVAASTTVTTPTTATTTVSISPTTKGSKSPAKVSDGGSSSTDFKMVSSGLTENQLQLSVEVLTSHSCSEEGLEDAANVLLQLSRGDSGTRDTVLKLLLNGARHLGYTLCKQIGTLLAELREYNLEQQRRAQCETLSPDGLPEEQPQTTKLKGKMQSRFDMAENVVIVASQKRPLGGRELQLPSMSMLTSKTSTQKFFLRVLQVIIQLRDDTRRANKKAKQTGRLGSSGLGSASSIQAAVRQLEAEADAIIQMVREGQRARRQQQAATSESSQSEASVRREESPMDVDQPSPSAQDTQSIASDGTPQGEKEKEERPPELPLLSEQLSLDELWDMLGECLKELEESHDQHAVLVLQPAVEAFFLVHATERESKPPVRDTRESQLAHIKDEPPPLSPAPLTPATPSSLDPFFSREPSSMHISSSLPPDTQKFLRFAETHRTVLNQILRQSTTHLADGPFAVLVDYIRVLDFDVKRKYFRQELERLDEGLRKEDMAVHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEYHKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECSEGFGLA", "comments": "CATALYTIC ACTIVITY: 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; Evidence={ECO:0000256|SAAS:SAAS00628607};", "primaryDomainId": "uniprot.A0A024R9W5", "displayName": "A0A024R9W5_HUMAN", "synonyms": "HECT, UBA and WWE domain containing 1, isoform CRA_b {ECO:0000313, EMBL:EAW93166.1}", "taxid": 9606, "geneName": "HUWE1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R9W5", "id": "uniprot.A0A024R9W5", "value": "uniprot.A0A024R9W5"}}, {"data": {"domainIds": "uniprot.Q7Z6Z7", "sequence": "MKVDRTKLKKTPTEAPADCRALIDKLKVCNDEQLLLELQQIKTWNIGKCELYHWVDLLDRFDGILADAGQTVENMSWMLVCDRPEREQLKMLLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKRSNYITRLGSDKRTPLLTRLQHLAESWGGKENGFGLAECCRDLHMMKYPPSATTLHFEFYADPGAEVKIEKRTTSNTLHYIHIEQLDKISESPSEIMESLTKMYSIPKDKQMLLFTHIRLAHGFSNHRKRLQAVQARLHAISILVYSNALQESANSILYNGLIEELVDVLQITDKQLMEIKAASLRTLTSIVHLERTPKLSSIIDCTGTASYHGFLPVLVRNCIQAMIDPSMDPYPHQFATALFSFLYHLASYDAGGEALVSCGMMEALLKVIKFLGDEQDQITFVTRAVRVVDLITNLDMAAFQSHSGLSIFIYRLEHEVDLCRKECPFVIKPKIQRPNTTQEGEEMETDMDGVQCIPQRAALLKSMLNFLKKAIQDPAFSDGIRHVMDGSLPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRRRRSSDPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKYICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQAMQSFNSTQQNETEPNQQVVGTEERIPIPLMDYILNVMKFVESILSNNTTDDHCQEFVNQKGLLPLVTILGLPNLPIDFPTSAACQAVAGVCKSILTLSHEPKVLQEGLLQLDSILSSLEPLHRPIESPGGSVLLRELACAGNVADATLSAQATPLLHALTAAHAYIMMFVHTCRVGQSEIRSISVNQWGSQLGLSVLSKLSQLYCSLVWESTVLLSLCTPNSLPSGCEFGQADMQKLVPKDEKAGTTQGGKRSDGEQDGAAGSMDASTQGLLEGIGLDGDTLAPMETDEPTASDSKGKSKITPAMAARIKQIKPLLSASSRLGRALAELFGLLVKLCVGSPVRQRRSHHAASTTTAPTPAARSTASALTKLLTKGLSWQPPPYTPTPRFRLTFFICSVGFTSPMLFDERKYPYHLMLQKFLCSGGHNALFETFNWALSMGGKVPVSEGLEHSDLPDGTGEFLDAWLMLVEKMVNPTTVLESPHSLPAKLPGGVQNFPQFSALRFLVVTQKAAFTCIKNLWNRKPLKVYGGRMAESMLAILCHILRGEPVIRERLSKEKEGSRGEEDTGQEEGGSRREPQVNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHPPPIMGGVVRDLSMSEEDQMMRAIAMSLGQDIPMDQRAESPEEVACRKEEEERKAREKQEEEEAKCLEKFQDADPLEQDELHTFTDTMLPGCFHLLDELPDTVYRVCDLIMTAIKRNGADYRDMILKQVVNQVWEAADVLIKAALPLTTSDTKTVSEWISQMATLPQASNLATRILLLTLLFEELKLPCAWVVESSGILNVLIKLLEVVQPCLQAAKEQKEVQTPKWITPVLLLIDFYEKTAISSKRRAQMTKYLQSNSNNWRWFDDRSGRWCSYSASNNSTIDSAWKSGETSVRFTAGRRRYTVQFTTMVQVNEETGNRRPVMLTLLRVPRLNKNSKNSNGQELEKTLEESKEMDIKRKENKGNDTPLALESTNTEKETSLEETKIGEILIQGLTEDMVTVLIRACVSMLGVPVDPDTLHATLRLCLRLTRDHKYAMMFAELKSTRMILNLTQSSGFNGFTPLVTLLLRHIIEDPCTLRHTMEKVVRSAATSGAGSTTSGVVSGSLGSREINYILRVLGPAACRNPDIFTEVANCCIRIALPAPRGSGTASDDEFENLRIKGPNAVQLVKTTPLKPSPLPVIPDTIKEVIYDMLNALAAYHAPEEADKSDPKPGVMTQEVGQLLQDMGDDVYQQYRSLTRQSSDFDTQSGFSINSQVFAADGASTETSASGTSQGEASTPEESRDGKKDKEGDRASEEGKQKGKGSKPLMPTSTILRLLAELVRSYVGIATLIANYSYTVGQSELIKEDCSVLAFVLDHLLPHTQNAEDKDTPALARLFLASLAAAGSGTDAQVALVNEVKAALGRALAMAESTEKHARLQAVMCIISTIMESCPSTSSFYSSATAKTQHNGMNNIIRLFLKKGLVNDLARVPHSLDLSSPNMANTVNAALKPLETLSRIVNQPSSLFGSKSASSKNKSEQDAQGASQDSSSNQQDPGEPGEAEVQEEDHDVTQTEVADGDIMDGEAETDSVVIAGQPEVLSSQEMQVENELEDLIDELLERDGGSGNSTIIVSRSGEDESQEDVLMDEAPSNLSQASTLQANREDSMNILDPEDEEEHTQEEDSSGSNEDEDDSQDEEEEEEEDEEDDQEDDEGEEGDEDDDDDGSEMELDEDYPDMNASPLVRFERFDREDDLIIEFDNMFSSATDIPPSPGNIPTTHPLMVRHADHSSLTLGSGSSTTRLTQGIGRSQRTLRQLTANTGHTIHVHYPGNRQPNPPLILQRLLGPSAAADILQLSSSLPLQSRGRARLLVGNDDVHIIARSDDELLDDFFHDQSTATSQAGTLSSIPTALTRWTEECKVLDAESMHDCVSVVKVSIVNHLEFLRDEELEERREKRRKQLAEEETKITDKGKEDKENRDQSAQCTASKSNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTLQSSQQQPTLPTPPALGEVPQELQSPAGEGGSSTQLLMPVEPEELGPTRPSGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLEEAVGDTSAAGSSEQPRAGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQLGIRPPTRTAPSTNSSAPAVVGNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQRRELAQNASSDTPMDPVTFIQTLPSDLRRSVLEDMEDSVLAVMPPDIAAEAQALRREQEARQRQLMHERLFGHSSTSALSAILRSPAFTSRLSGNRGVQYTRLAVQRGGTFQMGGSSSHNRPSGSNVDTLLRLRGRLLLDHEALSCLLVLLFVDEPKLNTSRLHRVLRNLCYHAQTRHWVIRSLLSILQRSSESELCIETPKLTTSEEKGKKSSKSCGSSSHENRPLDLLHKMESKSSNQLSWLSVSMDAALGCRTNIFQIQRSGGRKHTEKHASGGSTVHIHPQAAPVVCRHVLDTLIQLAKVFPSHFTQQRTKETNCESDRERGNKACSPCSSQSSSSGICTDFWDLLVKLDNMNVSRKGKNSVKSVPVSAGGEGETSPYSLEASPLGQLMNMLSHPVIRRSSLLTEKLLRLLSLISIALPENKVSEAQANSGSGASSTTTATSTTSTTTTTAASTTPTPPTAPTPVTSAPALVAATAISTIVVAASTTVTTPTTATTTVSISPTTKGSKSPAKVSDGGSSSTDFKMVSSGLTENQLQLSVEVLTSHSCSEEGLEDAANVLLQLSRGDSGTRDTVLKLLLNGARHLGYTLCKQIGTLLAELREYNLEQQRRAQCETLSPDGLPEEQPQTTKLKGKMQSRFDMAENVVIVASQKRPLGGRELQLPSMSMLTSKTSTQKFFLRVLQVIIQLRDDTRRANKKAKQTGRLGSSGLGSASSIQAAVRQLEAEADAIIQMVREGQRARRQQQAATSESSQSEASVRREESPMDVDQPSPSAQDTQSIASDGTPQGEKEKEERPPELPLLSEQLSLDELWDMLGECLKELEESHDQHAVLVLQPAVEAFFLVHATERESKPPVRDTRESQLAHIKDEPPPLSPAPLTPATPSSLDPFFSREPSSMHISSSLPPDTQKFLRFAETHRTVLNQILRQSTTHLADGPFAVLVDYIRVLDFDVKRKYFRQELERLDEGLRKEDMAVHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEYHKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECSEGFGLA", "comments": "FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15989957, PubMed:19713937, PubMed:15567145, PubMed:15767685, PubMed:18488021, PubMed:17567951, PubMed:19037095, PubMed:20534529). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Binds to an upstream initiator-like sequence in the preprodynorphin gene. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). {ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:20534529}.\nCATALYTIC ACTIVITY: 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;\nPATHWAY: Protein modification; protein ubiquitination.\nSUBUNIT: Interacts with isoform p14ARF of CDKN2A which strongly inhibits HUWE1 ubiquitin ligase activity. Interacts with MYCN, POLB and CDC6. Interacts with isoform 2 of PA2G4. Interacts with NR1D1 (PubMed:20534529). {ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:20534529}.\nINTERACTION: Q8N726:CDKN2A; NbExp=5; IntAct=EBI-625934, EBI-625922; P04792:HSPB1; NbExp=3; IntAct=EBI-625934, EBI-352682; Q07820:MCL1; NbExp=6; IntAct=EBI-625934, EBI-1003422; P20393:NR1D1; NbExp=3; IntAct=EBI-625934, EBI-2811738; P04637:TP53; NbExp=3; IntAct=EBI-625934, EBI-366083; Q13107:USP4; NbExp=4; IntAct=EBI-625934, EBI-723290;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19713937}. Nucleus {ECO:0000269|PubMed:19713937}. Note=Mainly expressed in the cytoplasm of most tissues, except in the nucleus of spermatogonia, primary spermatocytes and neuronal cells (By similarity). Predominantly cytosolic or perinuclear in some colorectal carcinoma cells. {ECO:0000250|UniProtKB:Q7TMY8}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=LASU1, Large structure of UREB1;   IsoId=Q7Z6Z7-1; Sequence=Displayed; Name=2;   IsoId=Q7Z6Z7-2; Sequence=VSP_011146; Name=3;   IsoId=Q7Z6Z7-3; Sequence=VSP_015272;\nTISSUE SPECIFICITY: Weakly expressed in heart, brain and placenta but not in other tissues. Expressed in a number of cell lines, predominantly in those from colorectal carcinomas. {ECO:0000269|PubMed:15567145}.\nDOMAIN: The HECT domain mediates inhibition of the transcriptional activity of p53.\nPTM: Phosphorylated on tyrosine; phosphorylation is probably required for its ability to inhibit TP53 transactivation. {ECO:0000250|UniProtKB:Q7TMY8}.\nDISEASE: Mental retardation, X-linked, syndromic, Turner type (MRXST) [MIM:309590]: A X-linked neurodevelopmental disorder with highly variable clinical manifestations. Common features consist of moderate to profound intellectual disability, delayed or absent speech, short stature with small hands and feet, and non-specific but recurrent dysmorphic facial features such as macrocephaly, microcephaly, a broad nasal tip, deep set eyes, epicanthic folds, short palpebral fissures and a short philtrum. Patients may manifest other features, such as hypotonia, seizures and delayed bone age. {ECO:0000269|PubMed:18252223, ECO:0000269|PubMed:25985138, ECO:0000269|PubMed:27130160, ECO:0000269|PubMed:27884935, ECO:0000269|PubMed:29180823}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAC62492.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAF28950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=AAF28950.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAB13404.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA, contains the C-terminal part of ATP5ME.; Evidence={ECO:0000305}; Sequence=BAC06833.1; Type=Frameshift; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q7Z6Z7", "displayName": "HUWE1_HUMAN", "synonyms": "E3 ubiquitin-protein ligase HUWE1, 2.3.2.26, ARF-binding protein 1, ARF-BP1, HECT, UBA and WWE domain-containing protein 1, HECT-type E3 ubiquitin transferase HUWE1, Homologous to E6AP carboxyl terminus homologous protein 9, HectH9, Large structure of UREB1, LASU1, Mcl-1 ubiquitin ligase E3, Mule, Upstream regulatory element-binding protein 1, URE-B1, URE-binding protein 1", "taxid": 9606, "geneName": "HUWE1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q7Z6Z7", "id": "uniprot.Q7Z6Z7", "value": "uniprot.Q7Z6Z7"}}, {"data": {"domainIds": "entrez.51121", "primaryDomainId": "entrez.51121", "geneType": "protein-coding", "displayName": "ribosomal protein L26 like 1", "synonyms": "60S ribosomal protein L26-like 1, large ribosomal subunit protein uL24-like 1, ribosomal protein L26 homolog, ribosomal protein L26 pseudogene 1", "chromosome": "5", "description": "ribosomal protein L26 like 1", "approvedSymbol": "RPL26L1", "type": "Gene", "symbols": "RPL26P1", "mapLocation": "5q35.1", "graphics": {"fill": "#FFB6C1"}, "name": "RPL26L1", "id": "entrez.51121", "value": "entrez.51121"}}, {"data": {"domainIds": "uniprot.Q9UNX3", "sequence": "MKFNPFVTSDRSKNRKRHFNAPSHVRRKIMSSPLSKELRQKYNVRSMPIRKDDEVQVVRGHYKGQQIGKVVQVYRKKYVIYIERVQREKANGTTVHVGIHPSKVVITRLKLDKDRKKILERKAKSRQVGKEKGKYKEELIEKMQE", "comments": "SIMILARITY: Belongs to the universal ribosomal protein uL24 family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q9UNX3", "displayName": "RL26L_HUMAN", "synonyms": "60S ribosomal protein L26-like 1, Large ribosomal subunit protein uL24-like 1", "taxid": 9606, "geneName": "RPL26L1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9UNX3", "id": "uniprot.Q9UNX3", "value": "uniprot.Q9UNX3"}}, {"data": {"domainIds": "entrez.49854", "primaryDomainId": "entrez.49854", "geneType": "protein-coding", "displayName": "zinc finger and BTB domain containing 21", "synonyms": "zinc finger and BTB domain-containing protein 21, zinc finger protein 295", "chromosome": "21", "description": "zinc finger and BTB domain containing 21", "approvedSymbol": "ZBTB21", "type": "Gene", "symbols": "ZNF295", "mapLocation": "21q22.3", "graphics": {"fill": "#FFB6C1"}, "name": "ZBTB21", "id": "entrez.49854", "value": "entrez.49854"}}, {"data": {"domainIds": "uniprot.Q5H9S0", "sequence": "MEGLLHYINPAHAISLLSALNEERLKGQLCDVLLIVGDQKFRAHKNVLAASSEYFQSLFTNKENESQTVFQLDFCEPDAFDNVLNYIYSSSLFVEKSSLAAVQELGYSLGISFLTNIVSKTPQAPFPTCPNRKKVFVEDDENSSQKRSVIVCQSRNEAQGKTVSQNQPDVSHTSRPSPSIAVKANTNKPHVPKPIEPLHNLSLTEKSWPKDSSVVYAKSLEHSGSLDDPNRISLVKRNAVLPSKPLQDREATDDKPGVSGQLPKGKALELALKRPRPPVLSVCSSSETPYLLKETNKGNGQGEDRNLLYYSKLGLVIPSSGSGSGNQSIDRSGPLVKSLLRRSLSMDSQAPVYSPSIDLKSSQGSSSVSSDAPGNVLCALSQKSSLKDCSEKTALDDRPQVLQPHRLRSFSASQSTDREGASPVTEVRIKTEPSSPLSDPSDIIRVTVGDAATTAAASSSSVTRDLSLKTEDDQKDMSRLPAKRRFQADRRLPFKKLKVNEHGSPVSEDNFEEGSSPTLLDADFPDSDLNKDEFGELEGTRPNKKFKCKHCLKIFRSTAGLHRHVNMYHNPEKPYACDICHKRFHTNFKVWTHCQTQHGIVKNPSPASSSHAVLDEKFQRKLIDIVREREIKKALIIKLRRGKPGFQGQSSSQAQQVIKRNLRSRAKGAYICTYCGKAYRFLSQFKQHIKMHPGEKPLGVNKVAKPKEHAPLASPVENKEVYQCRLCNAKLSSLLEQGSHERLCRNAAVCPYCSLRFFSPELK", "primaryDomainId": "uniprot.Q5H9S0", "displayName": "Q5H9S0_HUMAN", "synonyms": "Uncharacterized protein DKFZp781N1974 {ECO:0000313, EMBL:CAI45954.1}", "taxid": 9606, "geneName": "DKFZp781N1974", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q5H9S0", "id": "uniprot.Q5H9S0", "value": "uniprot.Q5H9S0"}}, {"data": {"domainIds": "uniprot.Q9ULJ3", "sequence": "MEGLLHYINPAHAISLLSALNEERLKGQLCDVLLIVGDQKFRAHKNVLAASSEYFQSLFTNKENESQTVFQLDFCEPDAFDNVLNYIYSSSLFVEKSSLAAVQELGYSLGISFLTNIVSKTPQAPFPTCPNRKKVFVEDDENSSQKRSVIVCQSRNEAQGKTVSQNQPDVSHTSRPSPSIAVKANTNKPHVPKPIEPLHNLSLTEKSWPKDSSVVYAKSLEHSGSLDDPNRISLVKRNAVLPSKPLQDREAMDDKPGVSGQLPKGKALELALKRPRPPVLSVCSSSETPYLLKETNKGNGQGEDRNLLYYSKLGLVIPSSGSGSGNQSIDRSGPLVKSLLRRSLSMDSQVPVYSPSIDLKSSQGSSSVSSDAPGNVLCALSQKSSLKDCSEKTALDDRPQVLQPHRLRSFSASQSTDREGASPVTEVRIKTEPSSPLSDPSDIIRVTVGDAATTAAASSSSVTRDLSLKTEDDQKDMSRLPAKRRFQADRRLPFKKLKVNEHGSPVSEDNFEEGSSPTLLDADFPDSDLNKDEFGELEGTRPNKKFKCKHCLKIFRSTAGLHRHVNMYHNPEKPYACDICHKRFHTNFKVWTHCQTQHGIVKNPSPASSSHAVLDEKFQRKLIDIVREREIKKALIIKLRRGKPGFQGQSSSQAQQVIKRNLRSRAKGAYICTYCGKAYRFLSQFKQHIKMHPGEKPLGVNKVAKPKEHAPLASPVENKEVYQCRLCNAKLSSLLEQGSHERLCRNAAVCPYCSLRFFSPELKQEHESKCEYKKLTCLECMRTFKSSFSIWRHQVEVHNQNNMAPTENFSLPVLDHNGDVTGSSRPQSQPEPNKVNHIVTTKDDNVFSDSSEQVNFDSEDSSCLPEDLSLSKQLKIQVKEEPVEEAEEEAPEASTAPKEAGPSKEASLWPCEKCGKMFTVHKQLERHQELLCSVKPFICHVCNKAFRTNFRLWSHFQSHMSQASEESAHKESEVCPVPTNSPSPPPLPPPPPLPKIQPLEPDSPTGLSENPTPATEKLFVPQESDTLFYHAPPLSAITFKRQFMCKLCHRTFKTAFSLWSHEQTHN", "comments": "FUNCTION: Acts as a transcription repressor. {ECO:0000269|PubMed:15629158}.\nSUBUNIT: Homodimer. Interacts with ZBTB14. {ECO:0000269|PubMed:15629158}.\nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15629158}. Note=Colocalizes with ZBTB14 in nucleus in HEK293 cells.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=ZNF295L;   IsoId=Q9ULJ3-1; Sequence=Displayed; Name=2; Synonyms=ZNF295S;   IsoId=Q9ULJ3-2; Sequence=VSP_041349;\nTISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues. {ECO:0000269|PubMed:15629158}.\nSEQUENCE CAUTION: Sequence=BAA86541.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9ULJ3", "displayName": "ZBT21_HUMAN", "synonyms": "Zinc finger and BTB domain-containing protein 21, Zinc finger protein 295", "taxid": 9606, "geneName": "ZBTB21", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9ULJ3", "id": "uniprot.Q9ULJ3", "value": "uniprot.Q9ULJ3"}}, {"data": {"domainIds": "entrez.4763", "primaryDomainId": "entrez.4763", "geneType": "protein-coding", "displayName": "neurofibromin 1", "synonyms": "neurofibromin, neurofibromatosis 1, neurofibromatosis-related protein NF-1, truncated neurofibromin 1", "chromosome": "17", "description": "neurofibromin 1", "approvedSymbol": "NF1", "type": "Gene", "symbols": "NFNS, VRNF, WSS", "mapLocation": "17q11.2", "graphics": {"fill": "#FFB6C1"}, "name": "NF1", "id": "entrez.4763", "value": "entrez.4763"}}, {"data": {"domainIds": "uniprot.P21359", "sequence": "MAAHRPVEWVQAVVSRFDEQLPIKTGQQNTHTKVSTEHNKECLINISKYKFSLVISGLTTILKNVNNMRIFGEAAEKNLYLSQLIILDTLEKCLAGQPKDTMRLDETMLVKQLLPEICHFLHTCREGNQHAAELRNSASGVLFSLSCNNFNAVFSRISTRLQELTVCSEDNVDVHDIELLQYINVDCAKLKRLLKETAFKFKALKKVAQLAVINSLEKAFWNWVENYPDEFTKLYQIPQTDMAECAEKLFDLVDGFAESTKRKAAVWPLQIILLILCPEIIQDISKDVVDENNMNKKLFLDSLRKALAGHGGSRQLTESAAIACVKLCKASTYINWEDNSVIFLLVQSMVVDLKNLLFNPSKPFSRGSQPADVDLMIDCLVSCFRISPHNNQHFKICLAQNSPSTFHYVLVNSLHRIITNSALDWWPKIDAVYCHSVELRNMFGETLHKAVQGCGAHPAIRMAPSLTFKEKVTSLKFKEKPTDLETRSYKYLLLSMVKLIHADPKLLLCNPRKQGPETQGSTAELITGLVQLVPQSHMPEIAQEAMEALLVLHQLDSIDLWNPDAPVETFWEISSQMLFYICKKLTSHQMLSSTEILKWLREILICRNKFLLKNKQADRSSCHFLLFYGVGCDIPSSGNTSQMSMDHEELLRTPGASLRKGKGNSSMDSAAGCSGTPPICRQAQTKLEVALYMFLWNPDTEAVLVAMSCFRHLCEEADIRCGVDEVSVHNLLPNYNTFMEFASVSNMMSTGRAALQKRVMALLRRIEHPTAGNTEAWEDTHAKWEQATKLILNYPKAKMEDGQAAESLHKTIVKRRMSHVSGGGSIDLSDTDSLQEWINMTGFLCALGGVCLQQRSNSGLATYSPPMGPVSERKGSMISVMSSEGNADTPVSKFMDRLLSLMVCNHEKVGLQIRTNVKDLVGLELSPALYPMLFNKLKNTISKFFDSQGQVLLTDTNTQFVEQTIAIMKNLLDNHTEGSSEHLGQASIETMMLNLVRYVRVLGNMVHAIQIKTKLCQLVEVMMARRDDLSFCQEMKFRNKMVEYLTDWVMGTSNQAADDDVKCLTRDLDQASMEAVVSLLAGLPLQPEEGDGVELMEAKSQLFLKYFTLFMNLLNDCSEVEDESAQTGGRKRGMSRRLASLRHCTVLAMSNLLNANVDSGLMHSIGLGYHKDLQTRATFMEVLTKILQQGTEFDTLAETVLADRFERLVELVTMMGDQGELPIAMALANVVPCSQWDELARVLVTLFDSRHLLYQLLWNMFSKEVELADSMQTLFRGNSLASKIMTFCFKVYGATYLQKLLDPLLRIVITSSDWQHVSFEVDPTRLEPSESLEENQRNLLQMTEKFFHAIISSSSEFPPQLRSVCHCLYQATCHSLLNKATVKEKKENKKSVVSQRFPQNSIGAVGSAMFLRFINPAIVSPYEAGILDKKPPPRIERGLKLMSKILQSIANHVLFTKEEHMRPFNDFVKSNFDAARRFFLDIASDCPTSDAVNHSLSFISDGNVLALHRLLWNNQEKIGQYLSSNRDHKAVGRRPFDKMATLLAYLGPPEHKPVADTHWSSLNLTSSKFEEFMTRHQVHEKEEFKALKTLSIFYQAGTSKAGNPIFYYVARRFKTGQINGDLLIYHVLLTLKPYYAKPYEIVVDLTHTGPSNRFKTDFLSKWFVVFPGFAYDNVSAVYIYNCNSWVREYTKYHERLLTGLKGSKRLVFIDCPGKLAEHIEHEQQKLPAATLALEEDLKVFHNALKLAHKDTKVSIKVGSTAVQVTSAERTKVLGQSVFLNDIYYASEIEEICLVDENQFTLTIANQGTPLTFMHQECEAIVQSIIHIRTRWELSQPDSIPQHTKIRPKDVPGTLLNIALLNLGSSDPSLRSAAYNLLCALTCTFNLKIEGQLLETSGLCIPANNTLFIVSISKTLAANEPHLTLEFLEECISGFSKSSIELKHLCLEYMTPWLSNLVRFCKHNDDAKRQRVTAILDKLITMTINEKQMYPSIQAKIWGSLGQITDLLDVVLDSFIKTSATGGLGSIKAEVMADTAVALASGNVKLVSSKVIGRMCKIIDKTCLSPTPTLEQHLMWDDIAILARYMLMLSFNNSLDVAAHLPYLFHVVTFLVATGPLSLRASTHGLVINIIHSLCTCSQLHFSEETKQVLRLSLTEFSLPKFYLLFGISKVKSAAVIAFRSSYRDRSFSPGSYERETFALTSLETVTEALLEIMEACMRDIPTCKWLDQWTELAQRFAFQYNPSLQPRALVVFGCISKRVSHGQIKQIIRILSKALESCLKGPDTYNSQVLIEATVIALTKLQPLLNKDSPLHKALFWVAVAVLQLDEVNLYSAGTALLEQNLHTLDSLRIFNDKSPEEVFMAIRNPLEWHCKQMDHFVGLNFNSNFNFALVGHLLKGYRHPSPAIVARTVRILHTLLTLVNKHRNCDKFEVNTQSVAYLAALLTVSEEVRSRCSLKHRKSLLLTDISMENVPMDTYPIHHGDPSYRTLKETQPWSSPKGSEGYLAATYPTVGQTSPRARKSMSLDMGQPSQANTKKLLGTRKSFDHLISDTKAPKRQEMESGITTPPKMRRVAETDYEMETQRISSSQQHPHLRKVSVSESNVLLDEEVLTDPKIQALLLTVLATLVKYTTDEFDQRILYEYLAEASVVFPKVFPVVHNLLDSKINTLLSLCQDPNLLNPIHGIVQSVVYHEESPPQYQTSYLQSFGFNGLWRFAGPFSKQTQIPDYAELIVKFLDALIDTYLPGIDEETSEESLLTPTSPYPPALQSQLSITANLNLSNSMTSLATSQHSPGIDKENVELSPTTGHCNSGRTRHGSASQVQKQRSAGSFKRNSIKKIV", "comments": "FUNCTION: Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269|PubMed:2121371, ECO:0000269|PubMed:8417346}.\nSUBUNIT: Interacts with HTR6 (PubMed:23027611). {ECO:0000269|PubMed:23027611}.\nINTERACTION: P05067:APP; NbExp=3; IntAct=EBI-1172917, EBI-77613; P01112:HRAS; NbExp=2; IntAct=EBI-1172917, EBI-350145; P34741:SDC2; NbExp=4; IntAct=EBI-1172917, EBI-1172957; Q7Z699:SPRED1; NbExp=6; IntAct=EBI-1172917, EBI-5235340;\nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14988005}. Nucleus, nucleolus {ECO:0000269|PubMed:14988005}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=6;   Comment=Experimental confirmation may be lacking for some isoforms.; Name=2; Synonyms=Type II;   IsoId=P21359-1; Sequence=Displayed; Name=1; Synonyms=Type I;   IsoId=P21359-2; Sequence=VSP_001628; Name=3;   IsoId=P21359-3; Sequence=VSP_001629, VSP_001630; Name=4;   IsoId=P21359-4; Sequence=VSP_001631, VSP_001632; Name=5;   IsoId=P21359-5; Sequence=VSP_043467, VSP_043468; Name=6;   IsoId=P21359-6; Sequence=VSP_001628, VSP_053587;\nTISSUE SPECIFICITY: Detected in brain, peripheral nerve, lung, colon and muscle. {ECO:0000269|PubMed:8417346}.\nDOMAIN: Binds phospholipids via its C-terminal CRAL-TRIO domain. Binds primarily glycerophospholipids with monounsaturated C18:1 and/or C16:1 fatty acid moieties and a phosphatidylethanolamine or phosphatidylcholine headgroup. Has lesser affinity for lipids containing phosphatidylserine and phosphatidylinositol. {ECO:0000269|PubMed:16397625, ECO:0000269|PubMed:17187824, ECO:0000269|PubMed:21089070}.\nRNA EDITING: Modified_positions=1306 {ECO:0000269|PubMed:11727199, ECO:0000269|PubMed:8602361}; Note=The stop codon (UGA) at position 1306 is created by RNA editing. Various levels of RNA editing occurs in peripheral nerve-sheath tumor samples (PNSTs) from patients with NF1. Preferentially observed in transcripts containing exon 23A.;\nDISEASE: Neurofibromatosis 1 (NF1) [MIM:162200]: A disease characterized by patches of skin pigmentation (cafe-au-lait spots), Lisch nodules of the iris, tumors in the peripheral nervous system and fibromatous skin tumors. Individuals with the disorder have increased susceptibility to the development of benign and malignant tumors. {ECO:0000269|PubMed:10220149, ECO:0000269|PubMed:10336779, ECO:0000269|PubMed:10607834, ECO:0000269|PubMed:10712197, ECO:0000269|PubMed:10980545, ECO:0000269|PubMed:11258625, ECO:0000269|PubMed:11735023, ECO:0000269|PubMed:11857752, ECO:0000269|PubMed:12522551, ECO:0000269|PubMed:12552569, ECO:0000269|PubMed:12746402, ECO:0000269|PubMed:1302608, ECO:0000269|PubMed:15060124, ECO:0000269|PubMed:15146469, ECO:0000269|PubMed:15520408, ECO:0000269|PubMed:15523642, ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:17160901, ECO:0000269|PubMed:21089070, ECO:0000269|PubMed:2114220, ECO:0000269|PubMed:21838856, ECO:0000269|PubMed:23758643, ECO:0000269|PubMed:24413922, ECO:0000269|PubMed:7981679, ECO:0000269|PubMed:8081387, ECO:0000269|PubMed:8544190, ECO:0000269|PubMed:8807336, ECO:0000269|PubMed:8834249, ECO:0000269|PubMed:9003501, ECO:0000269|PubMed:9101300, ECO:0000269|PubMed:9150739, ECO:0000269|PubMed:9298829, ECO:0000269|PubMed:9668168}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Watson syndrome (WTSN) [MIM:193520]: A syndrome characterized by the presence of pulmonary stenosis, cafe-au-lait spots, and mental retardation. It is considered as an atypical form of neurofibromatosis. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Familial spinal neurofibromatosis (FSNF) [MIM:162210]: Considered to be an alternative form of neurofibromatosis, showing multiple spinal tumors. {ECO:0000269|PubMed:11704931}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Neurofibromatosis-Noonan syndrome (NFNS) [MIM:601321]: Characterized by manifestations of both NF1 and Noonan syndrome (NS). NS is a disorder characterized by dysmorphic facial features, short stature, hypertelorism, cardiac anomalies, deafness, motor delay, and a bleeding diathesis. {ECO:0000269|PubMed:12707950, ECO:0000269|PubMed:16380919, ECO:0000269|PubMed:19845691}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: 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. Note=The gene represented in this entry may be involved in disease pathogenesis.\nCAUTION: Was originally thought to be associated with LEOPARD (LS), an autosomal dominant syndrome. {ECO:0000305|PubMed:8807336}.\nSEQUENCE CAUTION: Sequence=AAA59923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/NF1ID134.html\";\nWEB RESOURCE: Name=NIEHS-SNPs; URL=\"http://egp.gs.washington.edu/data/nf1/\";\nWEB RESOURCE: Name=Mendelian genes neurofibromin 1 (NF1); Note=Leiden Open Variation Database (LOVD); URL=\"http://www.lovd.nl/NF1\";", "primaryDomainId": "uniprot.P21359", "displayName": "NF1_HUMAN", "synonyms": "Neurofibromin, Neurofibromatosis-related protein NF-1", "taxid": 9606, "geneName": "NF1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P21359", "id": "uniprot.P21359", "value": "uniprot.P21359"}}, {"data": {"domainIds": "entrez.9833", "primaryDomainId": "entrez.9833", "geneType": "protein-coding", "displayName": "maternal embryonic leucine zipper kinase", "synonyms": "maternal embryonic leucine zipper kinase, pEg3 kinase, protein kinase Eg3, protein kinase PK38, tyrosine-protein kinase MELK", "chromosome": "9", "description": "maternal embryonic leucine zipper kinase", "approvedSymbol": "MELK", "type": "Gene", "symbols": "HPK38", "mapLocation": "9p13.2", "graphics": {"fill": "#FFB6C1"}, "name": "MELK", "id": "entrez.9833", "value": "entrez.9833"}}, {"data": {"domainIds": "uniprot.B7Z1G6", "sequence": "MMNFSNIMNYMKLLGQSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV", "comments": "CATALYTIC ACTIVITY: 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={ECO:0000256|SAAS:SAAS01117232};\nCATALYTIC ACTIVITY: 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={ECO:0000256|SAAS:SAAS01117231};", "primaryDomainId": "uniprot.B7Z1G6", "displayName": "B7Z1G6_HUMAN", "synonyms": "Non-specific serine/threonine protein kinase {ECO:0000256, SAAS:SAAS00804148}, 2.7.11.1 {ECO:0000256, SAAS:SAAS00804148}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B7Z1G6", "id": "uniprot.B7Z1G6", "value": "uniprot.B7Z1G6"}}, {"data": {"domainIds": "uniprot.Q14680", "sequence": "MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV", "comments": "FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis. {ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:12400006, ECO:0000269|PubMed:14699119, ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:17280616}.\nCATALYTIC ACTIVITY: 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={ECO:0000255|PROSITE-ProRule:PRU10027,   ECO:0000269|PubMed:16216881};\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:16216881};\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:16216881};\nACTIVITY REGULATION: Activated by autophosphorylation of the T-loop at Thr-167 and Ser-171: in contrast to other members of the SNF1 subfamily, phosphorylation at Thr-167 is not mediated by STK11/LKB1 but via autophosphorylation instead. Inhibited by calcium-binding. Kinase activity is also regulated by reducing agents: dithiothreitol (DTT) or reduced glutathione are required for kinase activity in vitro; such dependence is however not due to the presence of disulfide bonds. {ECO:0000269|PubMed:16216881}.\nSUBUNIT: Monomer. Interacts with ZNF622 and PPP1R8. {ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:14699119}.\nINTERACTION: Q9BZR8:BCL2L14; NbExp=4; IntAct=EBI-1046702, EBI-1385773;\nSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16159311, ECO:0000269|PubMed:21145462}; Peripheral membrane protein {ECO:0000269|PubMed:16159311, ECO:0000269|PubMed:21145462}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=8; Name=1;   IsoId=Q14680-1; Sequence=Displayed; Name=2;   IsoId=Q14680-2; Sequence=VSP_044715; Name=3;   IsoId=Q14680-3; Sequence=VSP_045208; Name=4;   IsoId=Q14680-4; Sequence=VSP_045209; Name=5;   IsoId=Q14680-5; Sequence=VSP_045430; Name=6;   IsoId=Q14680-6; Sequence=VSP_045431; Name=7;   IsoId=Q14680-7; Sequence=VSP_046760; Name=8;   IsoId=Q14680-8; Sequence=VSP_046759;\nTISSUE SPECIFICITY: Expressed in placenta, kidney, thymus, testis, ovary and intestine. {ECO:0000269|PubMed:8724849}.\nDEVELOPMENTAL STAGE: Increases during G2/M phase compared to interphase. Protein level decreases when cells exit mitosis, probably due to degradation. {ECO:0000269|PubMed:20420823}.\nINDUCTION: Up-regulated in many cancers cells. Up-regulated upon treatment with radiation or 5-fluorouracil (5-FU) in colorectal cancer cells, suggesting that it might be associated with increased resistance of colorectal cells against radiation and 5-FU. Down-regulated upon siomycin A, a thiazole antibiotic, treatment, leading to inhibit tumor growth in vivo. {ECO:0000269|PubMed:21558073, ECO:0000269|PubMed:21806965}.\nDOMAIN: The KA1 domain mediates binding to phospholipids and targeting to membranes. {ECO:0000250}.\nPTM: Autophosphorylated: autophosphorylation of the T-loop at Thr-167 and Ser-171 is required for activation. Thr-478 phosphorylation during mitosis promotes interaction with PPP1R8 (Probable). {ECO:0000305|PubMed:14699119, ECO:0000305|PubMed:14976552, ECO:0000305|PubMed:16216881, ECO:0000305|PubMed:16628004, ECO:0000305|PubMed:20420823}.\nDISEASE: Note=Defects in MELK are associated with some cancers, such as brain or breast cancers. Expression is dramatically increased in aggressive undifferentiated tumors, correlating with poor patient outcome in breast and brain cancers, suggesting a role in tumor- initiating cells and proliferation via its function in cell proliferation regulation.\nMISCELLANEOUS: Potential therapeutic target for treatment of somatic tumors, such as brain and breast cancers, down-regulation of MELK inhibiting tumorigenesis (PubMed:17960622, PubMed:20861186). {ECO:0000305|PubMed:17960622, ECO:0000305|PubMed:20861186}.\nSIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=BAA11492.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/MELKID43360ch9p13.html\";", "primaryDomainId": "uniprot.Q14680", "displayName": "MELK_HUMAN", "synonyms": "Maternal embryonic leucine zipper kinase, hMELK, 2.7.11.1, Protein kinase Eg3, pEg3 kinase, Protein kinase PK38, hPK38, Tyrosine-protein kinase MELK, 2.7.10.2", "taxid": 9606, "geneName": "MELK", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q14680", "id": "uniprot.Q14680", "value": "uniprot.Q14680"}}, {"data": {"domainIds": "entrez.9820", "primaryDomainId": "entrez.9820", "geneType": "protein-coding", "displayName": "cullin 7", "synonyms": "cullin-7", "chromosome": "6", "description": "cullin 7", "approvedSymbol": "CUL7", "type": "Gene", "symbols": "3M1, CUL-7, KIAA0076, dJ20C7.5", "mapLocation": "6p21.1", "graphics": {"fill": "#FFB6C1"}, "name": "CUL7", "id": "entrez.9820", "value": "entrez.9820"}}, {"data": {"domainIds": "uniprot.Q14999", "sequence": "MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHKMLGEDGQVIGPSQESAGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDPRVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEELSGERGQLELEFSMAMGTLISELVQAMRWDQASDRPRSSARSPGSIFQPQLADVSPGLPAAQAQPSFRRSRRFRPRSEFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEFRQSNNGVPPVQVFWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQGAVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDTEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDEILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNQAYPSLLEAQEDVLLLDAQAQAKDSEDAAKVEAKEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRILKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELAQELRDMVFKCEKHAHLYRKLITNILGGCIQMVLGQIEDHRRTHQPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLHLSSRLNGALRQEQNFADRFLPDDEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAFFSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCWRAVVEKQVNNFLTSSWRDDDFVPRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCLQAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQELLKLEDTEKKIQVGLGASGKEHKSEKEEEAGAAAVVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHSWPVASICHTLNPRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEDGQNLEKRRNLLNCLIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVPVTVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYASCTATQSFSTFR", "comments": "FUNCTION: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (PubMed:24793696). Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (PubMed:21572988, PubMed:24362026). Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (PubMed:20139075). Does not promote polyubiquitination and proteasomal degradation of p53/TP53 (PubMed:16547496, PubMed:17332328). While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions. {ECO:0000269|PubMed:16547496, ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:18498745, ECO:0000269|PubMed:20139075, ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.\nPATHWAY: Protein modification; protein ubiquitination.\nSUBUNIT: Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Part of a Cul7-RING complex consisting of CUL7, RBX1, SKP1 and FBXW8. Interacts with a complex of SKP1 and FBXW8, but not with SKP1 alone. Interacts with CUL9; leading to inhibit CUL9 activity. Interacts with FBXW8; interaction is mutually exclusive of binding to CUL9 or p53/TP53. Interacts with p53/TP53; the interaction preferentially involves tetrameric and dimeric p53/TP53. The CUL7-CUL9 heterodimer seems to interact specifically with p53/TP53. Interacts with CUL1; the interactions seems to be mediated by FBXW8. Interacts with OBSL1. Interacts (as part of the 3M complex) with HDAC4 and HDAC5; it is negatively regulated by ANKRA2. {ECO:0000269|PubMed:12481031, ECO:0000269|PubMed:12904573, ECO:0000269|PubMed:15964813, ECO:0000269|PubMed:16547496, ECO:0000269|PubMed:17298945, ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:21737058, ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696, ECO:0000269|PubMed:25752541}.\nSUBUNIT: (Microbial infection) Interacts with SV40 Large T antigen; this interaction seems to inhibit CUL7. {ECO:0000269|PubMed:16140746}.\nINTERACTION: O75147-2:OBSL1; NbExp=4; IntAct=EBI-308606, EBI-15927144; P04637:TP53; NbExp=5; IntAct=EBI-308606, EBI-366083;\nSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Golgi apparatus. Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus (PubMed:24793695). CCDC8 is required for centrosomal location (PubMed:24793695). {ECO:0000269|PubMed:24793695}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q14999-1; Sequence=Displayed; Name=2;   IsoId=Q14999-2; Sequence=VSP_046105, VSP_046106;\nTISSUE SPECIFICITY: Highly expressed in fetal kidney and adult skeletal muscle. Also abundant in fetal brain, as well as in adult pancreas, kidney, placenta and heart. Detected in trophoblasts, lymphoblasts, osteoblasts, chondrocytes and skin fibroblasts. {ECO:0000269|PubMed:16142236}.\nDEVELOPMENTAL STAGE: Highly expressed in invasive placental villi during first trimester. {ECO:0000269|PubMed:20139075}.\nPTM: According to a report, may not be neddylated despite the conserved consensus site for neddylation at Lys-1576. {ECO:0000269|PubMed:17332328}.\nDISEASE: 3M syndrome 1 (3M1) [MIM:273750]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies. {ECO:0000269|PubMed:16142236, ECO:0000269|PubMed:17675530, ECO:0000269|PubMed:23018678}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE- ProRule:PRU00330}.\nSEQUENCE CAUTION: Sequence=BAA07551.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q14999", "displayName": "CUL7_HUMAN", "synonyms": "Cullin-7, CUL-7", "taxid": 9606, "geneName": "CUL7", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q14999", "id": "uniprot.Q14999", "value": "uniprot.Q14999"}}, {"data": {"domainIds": "entrez.27332", "primaryDomainId": "entrez.27332", "geneType": "protein-coding", "displayName": "zinc finger protein 638", "synonyms": "zinc finger protein 638, CTCL tumor antigen se33-1, CTCL-associated antigen se33-1, NP220 nuclear protein, cutaneous T-cell lymphoma-associated antigen se33-1, nuclear protein 220, zinc finger matrin-like protein", "chromosome": "2", "description": "zinc finger protein 638", "approvedSymbol": "ZNF638", "type": "Gene", "symbols": "NP220, ZFML, Zfp638", "mapLocation": "2p13.3-p13.2", "graphics": {"fill": "#FFB6C1"}, "name": "ZNF638", "id": "entrez.27332", "value": "entrez.27332"}}, {"data": {"domainIds": "uniprot.A8K583", "sequence": "MSRPRFNPRGDFPLQRPRAPNPSGMRPPGPFMRPGSMGLPRFYPAGRARGIPHRFAGHESYQNMGPQRMNVQVTQHRTDPRLTKEKLDFHEAQQKKGKPHGSRWDDEPHISASVAVKQSSVTQVTEQSPKVQSRYTKESASSILASFGLSNEDLEELSRYPDEQLTPENMPLILRDIRMRKMGRRLPNLPSQSRNKETLGSEAVSSNVIDYGHASKYGYTEDPLEVRIYDPEIPTDEVENEFQSQQNISASVPNPNVICNSMFPVEDVFRQMDFPGESSNNRSFFSVESGTKMSGLHISGGQSVLEPIKSVNQSINQTVSQTMSQSLIPPSMNQQPFSSELISSVSQQERIPHEPVINSSNVHVGSRGSKKNYQSQADIPIRSPFGIVKASWLPKFSHADAQKMKRLPTPSMMNDYYAASPRIFPHLCSLCNVECSHLKDWIQHQNTSTHIESCRQLRQQYPDWNPEILPSRRNEGNRKENETPRRRSHSPSPRRSRRSSSSHRFRRSRSPMHYMYRPRSRSPRICHRFISRYRSRSRSRSPYRIRNPFRGSPKCFRSVSPERMSRRSVRSSDRKKALEDVVQRSGHGTEFNKQKHLEAADKGHSPAQKPKTSSGTKPSVKPTSATKSDSNLGGHSIRCKSKNLEDDTLSECKQVSDKAVSLQRKLRKEQSLHYGSVLLITELPEDGCTEEDVRKLFQPFGKVNDVLIVPYRKEAYLEMEFKEAITAIMKYIETTPLTIKGKSVKICVPGKKKAQNKEVKKKTLESKKVSASTLKRDADASKAVEIVTSTSAAKTGQAKASVAKVNKSTGKSASSVKSVVTVAVKGNKASIKTAKSGGKKSLEAKKTGNVKNKDSNKPVTIPENSEIKTSIEVKATENCAKEAISDAALEATENEPLNKETEEMCVMLVSNLPNKGYSVEEVYDLAKPFGGLKDILILSSHKKAYIEINRKAAESMVKFYTCFPVLMDGNQLSISMAPENMNIKDEEAIFITLVKENDPEANIDTIYDRFVHLDNLPEDGLQCVLCVGLQFGKVDHHVFISNRNKAILQLDSPESAQSMYSFLKQNPQNIGDHMLTCSLSPKIDLPEVQIEHDPELEKESPGLKNSPIDESEVQTATDSPSVKPNELEEESTPSIQTETLVQQEEPCEEEAEKATCDSDFAVETLELETQGEEVKEEIPLVASASVSIEQFTENAEECALNQQMFNSDLEKKGAEIINPKTALLPSDSVFAEERNLKGILEESPSEAEDFISGITQTMVEAVAEVEKNETVSEILPSTCIVTLVPGIPTGDEKTVDKKNISEKKGNMDEKEEKEFNTKETRMDLQIGTEKAEKNEGRMDAEKVEKMAAMKEKPAENTLFKAYPNKGVGQANKPDETSKTSILAVSDVSSSKPSIKAVIVSSPKAKATVSKTENQKSFPKSVPRDQINAEKKLSAKEFGLLKPTSARSGLAESSSKFKPTQSSLTRGGSGRISALQGKLSKLDYRDITKQSQETEARPSIMKRDDSNNKTLAEQNTKNPKSTTGRSSKSKEEPLFPFNLDEFVTVDEVIEEVNPSQAKQNPLKGKRKETLKNVPFSELN", "primaryDomainId": "uniprot.A8K583", "displayName": "A8K583_HUMAN", "synonyms": "cDNA FLJ77126, highly similar to Homo sapiens zinc finger protein 638 (ZNF638), transcript variant 1, mRNA {ECO:0000313, EMBL:BAF83887.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A8K583", "id": "uniprot.A8K583", "value": "uniprot.A8K583"}}, {"data": {"domainIds": "uniprot.Q14966", "sequence": "MSRPRFNPRGDFPLQRPRAPNPSGMRPPGPFMRPGSMGLPRFYPAGRARGIPHRFAGHESYQNMGPQRMNVQVTQHRTDPRLTKEKLDFHEAQQKKGKPHGSRWDDEPHISASVAVKQSSVTQVTEQSPKVQSRYTKESASSILASFGLSNEDLEELSRYPDEQLTPENMPLILRDIRMRKMGRRLPNLPSQSRNKETLGSEAVSSNVIDYGHASKYGYTEDPLEVRIYDPEIPTDEVENEFQSQQNISASVPNPNVICNSMFPVEDVFRQMDFPGESSNNRSFFSVESGTKMSGLHISGGQSVLEPIKSVNQSINQTVSQTMSQSLIPPSMNQQPFSSELISSVSQQERIPHEPVINSSNVHVGSRGSKKNYQSQADIPIRSPFGIVKASWLPKFSHADAQKMKRLPTPSMMNDYYAASPRIFPHLCSLCNVECSHLKDWIQHQNTSTHIESCRQLRQQYPDWNPEILPSRRNEGNRKENETPRRRSHSPSPRRSRRSSSSHRFRRSRSPMHYMYRPRSRSPRICHRFISRYRSRSRSRSPYRIRNPFRGSPKCFRSVSPERMSRRSVRSSDRKKALEDVVQRSGHGTEFNKQKHLEAADKGHSPAQKPKTSSGTKPSVKPTSATKSDSNLGGHSIRCKSKNLEDDTLSECKQVSDKAVSLQRKLRKEQSLHYGSVLLITELPEDGCTEEDVRKLFQPFGKVNDVLIVPYRKEAYLEMEFKEAITAIMKYIETTPLTIKGKSVKICVPGKKKAQNKEVKKKTLESKKVSASTLKRDADASKAVEIVTSTSAAKTGQAKASVAKVNKSTGKSASSVKSVVTVAVKGNKASIKTAKSGGKKSLEAKKTGNVKNKDSNKPVTIPENSEIKTSIEVKATENCAKEAISDAALEATENEPLNKETEEMCVMLVSNLPNKGYSVEEVYDLAKPFGGLKDILILSSHKKAYIEINRKAAESMVKFYTCFPVLMDGNQLSISMAPENMNIKDEEAIFITLVKENDPEANIDTIYDRFVHLDNLPEDGLQCVLCVGLQFGKVDHHVFISNRNKAILQLDSPESAQSMYSFLKQNPQNIGDHMLTCSLSPKIDLPEVQIEHDPELEKESPGLKNSPIDESEVQTATDSPSVKPNELEEESTPSIQTETLVQQEEPCEEEAEKATCDSDFAVETLELETQGEEVKEEIPLVASASVSIEQFTENAEECALNQQMFNSDLEKKGAEIINPKTALLPSDSVFAEERNLKGILEESPSEAEDFISGITQTMVEAVAEVEKNETVSEILPSTCIVTLVPGIPTGDEKTVDKKNISEKKGNMDEKEEKEFNTKETRMDLQIGTEKAEKNEGRMDAEKVEKMAAMKEKPAENTLFKAYPNKGVGQANKPDETSKTSILAVSDVSSSKPSIKAVIVSSPKAKATVSKTENQKSFPKSVPRDQINAEKKLSAKEFGLLKPTSARSGLAESSSKFKPTQSSLTRGGSGRISALQGKLSKLDYRDITKQSQETEARPSIMKRDDSNNKTLAEQNTKNPKSTTGRSSKSKEEPLFPFNLDEFVTVDEVIEEVNPSQAKQNPLKGKRKETLKNVPFSELNLKKKKGKTSTPRGVEGELSFVTLDEIGEEEDAAAHLAQALVTVDEVIDEEELNMEEMVKNSNSLFTLDELIDQDDCISHSEPKDVTVLSVAEEQDLLKQERLVTVDEIGEVEELPLNESADITFATLNTKGNEGDTVRDSIGFISSQVPEDPSTLVTVDEIQDDSSDLHLVTLDEVTEEDEDSLADFNNLKEELNFVTVDEVGEEEDGDNDLKVELAQSKNDHPTDKKGNRKKRAVDTKKTKLESLSQVGPVNENVMEEDLKTMIERHLTAKTPTKRVRIGKTLPSEKAVVTEPAKGEEAFQMSEVDEESGLKDSEPERKRKKTEDSSSGKSVASDVPEELDFLVPKAGFFCPICSLFYSGEKAMTNHCKSTRHKQNTEKFMAKQRKEKEQNEAEERSSR", "comments": "FUNCTION: Transcription factor that binds to cytidine clusters in double-stranded DNA (PubMed:8647861, PubMed:30487602). Plays a key role in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Mediates transcriptional repression of unintegrated viral DNA by specifically binding to the cytidine clusters of retroviral DNA and mediating the recruitment of chromatin silencers, such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). May also regulate alternative splicing of target genes during adipogenesis (By similarity). {ECO:0000250|UniProtKB:Q61464, ECO:0000269|PubMed:30487602, ECO:0000269|PubMed:8647861}.\nSUBUNIT: Interacts with FHL2 (PubMed:11813260). Interacts with CEBPA, CEBPD and CEBPG (By similarity). Interacts with MPHOSPH8 and TASOR components of the HUSH complex; leading to recruitment of the HUSH complex (PubMed:30487602). Interacts with SETDB1 (PubMed:30487602). Interacts with HDAC1 (PubMed:30487602). Interacts with HDAC4 (PubMed:30487602). {ECO:0000250|UniProtKB:Q61464, ECO:0000269|PubMed:11813260, ECO:0000269|PubMed:30487602}.\nSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE- ProRule:PRU00130, ECO:0000269|PubMed:11813260, ECO:0000269|PubMed:8647861}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=6;   Comment=Additional isoforms seem to exist.; Name=1; Synonyms=Alpha;   IsoId=Q14966-1; Sequence=Displayed; Name=2;   IsoId=Q14966-2; Sequence=VSP_014802, VSP_014803; Name=3;   IsoId=Q14966-3; Sequence=VSP_014806; Name=4;   IsoId=Q14966-4; Sequence=VSP_014804, VSP_014805; Name=5;   IsoId=Q14966-5; Sequence=VSP_014801; Name=6;   IsoId=Q14966-6; Sequence=VSP_059342, VSP_059343;\nDOMAIN: The matrin-type zinc finger domain is required for localization to nuclear speckles. {ECO:0000250|UniProtKB:Q61464}.\nMISCELLANEOUS: [Isoform 5]: Tumor-associated antigen found in several cutaneous T-cell lymphoma (CTCL), and in particular in mycosis fungoides patients and in Sezary syndrome patients. {ECO:0000305|PubMed:11149944}.\nMISCELLANEOUS: [Isoform 5]: Broadly expressed. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAH64530.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q14966", "displayName": "ZN638_HUMAN", "synonyms": "Zinc finger protein 638, Cutaneous T-cell lymphoma-associated antigen se33-1 {ECO:0000303, PubMed:11149944}, CTCL-associated antigen se33-1 {ECO:0000303, PubMed:11149944}, Nuclear protein 220 {ECO:0000303, PubMed:8647861}, Zinc finger matrin-like protein", "taxid": 9606, "geneName": "ZNF638", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q14966", "id": "uniprot.Q14966", "value": "uniprot.Q14966"}}, {"data": {"domainIds": "entrez.6242", "primaryDomainId": "entrez.6242", "geneType": "protein-coding", "displayName": "rhotekin", "synonyms": "rhotekin", "chromosome": "2", "description": "rhotekin", "approvedSymbol": "RTKN", "type": "Gene", "symbols": "-", "mapLocation": "2p13.1", "graphics": {"fill": "#FFB6C1"}, "name": "RTKN", "id": "entrez.6242", "value": "entrez.6242"}}, {"data": {"domainIds": "uniprot.Q9BST9", "sequence": "MFSRNHRSRVTVARGSALEMEFKRGRFRLSLFSDLPEDTELQRKLDHEIRMREGACKLLAACSQREQALEATKSLLVCNSRILSYMGELQRRKEAQVLGKTSRRPSDSGPPAERSPCRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMILVDRTLTDISFQSNVLFAEAGPDFELRLELYGACVEEEGALTGGPKRLATKLSSSLGRSSGRRVRASLDSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQDGFRTHDLTLASHEENPAWLPLYGSVCCRLAAQPLCMTQPTASGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQALGRPFTLSISNQYGDDEVTHTLQTESREALQSWMEALWQLFFDMSQWKQCCDEIMKIETPAPRKPPQALAKQGSLYHEMAIEPLDDIAAVTDILTQREGARLETPPPWLAMFTDQPALPNPCSPASVAPAPDWTHPLPWGRPRTFSLDAVPPDHSPRARSVAPLPPQRSPRTRGLCSKGQPRTWLQSPV", "comments": "FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may confer increased resistance to apoptosis to cells in gastric tumorigenesis. May play a novel role in the organization of septin structures. {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:15480428, ECO:0000269|PubMed:16007136}.\nSUBUNIT: Interacts via its C-terminal region with the TAX1BP3 PDZ domain. This interaction facilitates Rho-mediated activation of the c- Fos serum response element (SRE). Interacts with SEPT9. Specifically binds to GTP-bound RHOA, RHOB and RHOC and inhibits their GTPase activity. {ECO:0000250|UniProtKB:Q8C6B2, ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16007136}.\nINTERACTION: P61586:RHOA; NbExp=6; IntAct=EBI-446694, EBI-446668; Q9QUI0:Rhoa (xeno); NbExp=2; IntAct=EBI-446694, EBI-643583; O60504:SORBS3; NbExp=3; IntAct=EBI-446694, EBI-741237; O60504-2:SORBS3; NbExp=3; IntAct=EBI-446694, EBI-1222956;\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1 {ECO:0000269|PubMed:10873388};   IsoId=Q9BST9-1; Sequence=Displayed; Name=2 {ECO:0000269|PubMed:15489334};   IsoId=Q9BST9-2; Sequence=VSP_052004; Name=3 {ECO:0000269|PubMed:10940294};   IsoId=Q9BST9-3; Sequence=VSP_052005;\nTISSUE SPECIFICITY: Highly expressed in prostate, moderately in kidney, heart, brain, spleen, testis, placenta, small intestine, pancreas, skeletal muscle and peripheral blood leukocytes, and weakly in ovary, colon and thymus. Weakly expressed in all normal cell lines tested. Overexpressed in various cancer cell lines. {ECO:0000269|PubMed:10873388, ECO:0000269|PubMed:15480428}.\nMISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000269|PubMed:10940294}.\nSEQUENCE CAUTION: Sequence=AAL16767.1; Type=Frameshift; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9BST9", "displayName": "RTKN_HUMAN", "synonyms": "Rhotekin", "taxid": 9606, "geneName": "RTKN", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9BST9", "id": "uniprot.Q9BST9", "value": "uniprot.Q9BST9"}}, {"data": {"domainIds": "entrez.6047", "primaryDomainId": "entrez.6047", "geneType": "protein-coding", "displayName": "ring finger protein 4", "synonyms": "E3 ubiquitin-protein ligase RNF4, E3 ubiquitin ligase RNF4, RING-type E3 ubiquitin transferase RNF4, small nuclear RING finger protein", "chromosome": "4", "description": "ring finger protein 4", "approvedSymbol": "RNF4", "type": "Gene", "symbols": "RES4-26, SLX5, SNURF", "mapLocation": "4p16.3", "graphics": {"fill": "#FFB6C1"}, "name": "RNF4", "id": "entrez.6047", "value": "entrez.6047"}}, {"data": {"domainIds": "uniprot.P78317", "sequence": "MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI", "comments": "FUNCTION: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys- 48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation. {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:19307308, ECO:0000269|PubMed:20026589, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20943951}.\nCATALYTIC ACTIVITY: 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;\nPATHWAY: Protein modification; protein ubiquitination.\nSUBUNIT: Homodimer (via RING-type zinc finger domain). Interacts with GSC2 (By similarity). Interacts with AR/the androgen receptor and TBP (By similarity). Interacts with TCF20 (By similarity). Interacts with PATZ1. Interacts with TRPS1; negatively regulates TRPS1 transcriptional repressor activity. Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent. Interacts with PARP1. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6). {ECO:0000250, ECO:0000269|PubMed:10713105, ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:15707587, ECO:0000269|PubMed:19779455, ECO:0000269|PubMed:20943951, ECO:0000269|PubMed:23028697}.\nINTERACTION: Self; NbExp=2; IntAct=EBI-2340927, EBI-2340927; Q13838:DDX39B; NbExp=4; IntAct=EBI-2340927, EBI-348622; Q9BQY4:RHOXF2; NbExp=4; IntAct=EBI-2340927, EBI-372094; Q9UHF7:TRPS1; NbExp=2; IntAct=EBI-2340927, EBI-2556151;\nSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body. Nucleus, nucleoplasm.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=P78317-1; Sequence=Displayed; Name=2;   IsoId=P78317-2; Sequence=VSP_045789, VSP_045790;\nTISSUE SPECIFICITY: Widely expressed at low levels in many tissues; highly expressed in testis. {ECO:0000269|PubMed:9479498}.\nDOMAIN: The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate. {ECO:0000269|PubMed:18408734}.\nDOMAIN: The RING-type zinc finger domain is required for the ubiquitination of polysumoylated substrates. {ECO:0000250|UniProtKB:O88846}.\nPTM: Sumoylated; conjugated by one or two SUMO1 moieties. {ECO:0000250}.\nPTM: Autoubiquitinated. {ECO:0000250}.", "primaryDomainId": "uniprot.P78317", "displayName": "RNF4_HUMAN", "synonyms": "E3 ubiquitin-protein ligase RNF4, 2.3.2.27, RING finger protein 4, RING-type E3 ubiquitin transferase RNF4 {ECO:0000305}, Small nuclear ring finger protein, Protein SNURF", "taxid": 9606, "geneName": "RNF4", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P78317", "id": "uniprot.P78317", "value": "uniprot.P78317"}}, {"data": {"domainIds": "entrez.25776", "primaryDomainId": "entrez.25776", "geneType": "protein-coding", "displayName": "chibby family member 1, beta catenin antagonist", "synonyms": "protein chibby homolog 1, ARPP-binding protein, PKD2 interactor, Golgi and endoplasmic reticulum-associated 1, chibby CTNNB1-mediated transcription inhibitor, chibby homolog 1, coiled-coil protein PIGEA-14, cytosolic leucine-rich protein, polycystin-2 interactor, Golgi- and endoplasmic reticulum-associated protein, 14 kDa", "chromosome": "22", "description": "chibby family member 1, beta catenin antagonist", "approvedSymbol": "CBY1", "type": "Gene", "symbols": "C22orf2, CBY, Chibby1, HS508I15A, PGEA1, PIGEA-14, PIGEA14, arb1", "mapLocation": "22q13.1", "graphics": {"fill": "#FFB6C1"}, "name": "CBY1", "id": "entrez.25776", "value": "entrez.25776"}}, {"data": {"domainIds": "uniprot.A0A087WUW0", "sequence": "MDKCQKHDVECEKPDANEDSLCNSVHVQWPGEGSTGFAFIRPKMPFFGNTFSPKKTPPRKSASLSNLHSLDRSTREVELGLEYGSPTMNLAGQSLKFENGQWIAETGVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISRKRK", "primaryDomainId": "uniprot.A0A087WUW0", "displayName": "A0A087WUW0_HUMAN", "synonyms": "Protein chibby homolog 1 {ECO:0000313, Ensembl:ENSP00000478962}", "taxid": 9606, "geneName": "CBY1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A087WUW0", "id": "uniprot.A0A087WUW0", "value": "uniprot.A0A087WUW0"}}, {"data": {"domainIds": "uniprot.A0A024R1L9", "sequence": "MPFFGNTFSPKKTPPRKSASLSNLHSLDRSTREVELGLEYGSPTMNLAGQSLKFENGQWIAETGVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISRKRK", "primaryDomainId": "uniprot.A0A024R1L9", "displayName": "A0A024R1L9_HUMAN", "synonyms": "HCG2010808, isoform CRA_b {ECO:0000313, EMBL:EAW60256.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R1L9", "id": "uniprot.A0A024R1L9", "value": "uniprot.A0A024R1L9"}}, {"data": {"domainIds": "uniprot.Q9Y3M2", "sequence": "MPFFGNTFSPKKTPPRKSASLSNLHSLDRSTREVELGLEYGSPTMNLAGQSLKFENGQWIAETGVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISRKRK", "comments": "FUNCTION: 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. {ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:15194699}.\nSUBUNIT: 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). {ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:15194699, ECO:0000269|PubMed:16424001, ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}.\nINTERACTION: Q96M91:CFAP53; NbExp=3; IntAct=EBI-947308, EBI-742422; A1XBS5:FAM92A; NbExp=3; IntAct=EBI-947308, EBI-2349888; Q15311:RALBP1; NbExp=3; IntAct=EBI-947308, EBI-749285; Q6PF05-3:TTC23L; NbExp=3; IntAct=EBI-947308, EBI-10182647; P62258:YWHAE; NbExp=3; IntAct=EBI-947308, EBI-356498; P63104:YWHAZ; NbExp=3; IntAct=EBI-947308, EBI-347088;\nSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16424001}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27528616}. Golgi apparatus. Golgi apparatus, trans- Golgi network {ECO:0000269|PubMed:16424001}.\nTISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:12712206}.\nMISCELLANEOUS: 'Chibby' is Japanese for 'small'; the gene was so named for the RNAi phenotype seen in flies.\nSIMILARITY: Belongs to the chibby family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q9Y3M2", "displayName": "CBY1_HUMAN", "synonyms": "Protein chibby homolog 1, ARPP-binding protein, Cytosolic leucine-rich protein, PIGEA-14, PKD2 interactor, Golgi and endoplasmic reticulum-associated 1", "taxid": 9606, "geneName": "CBY1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9Y3M2", "id": "uniprot.Q9Y3M2", "value": "uniprot.Q9Y3M2"}}, {"data": {"domainIds": "entrez.90102", "primaryDomainId": "entrez.90102", "geneType": "protein-coding", "displayName": "pleckstrin homology like domain family B member 2", "synonyms": "pleckstrin homology-like domain family B member 2, LL5 beta, protein LL5-beta", "chromosome": "3", "description": "pleckstrin homology like domain family B member 2", "approvedSymbol": "PHLDB2", "type": "Gene", "symbols": "LL5b, LL5beta", "mapLocation": "3q13.2", "graphics": {"fill": "#FFB6C1"}, "name": "PHLDB2", "id": "entrez.90102", "value": "entrez.90102"}}, {"data": {"domainIds": "uniprot.Q86SQ0", "sequence": "MEEHSYIQKELDLQNGSLEEDSVVHSVENDSQNMMESLSPKKYSSSLRFKANGDYSGSYLTLSQPVPAKRSPSPLGTSVRSSPSLAKIQGSKQFSYDGTDKNIPMKPPTPLLNTTSSLSGYPLGRADFDHYTGRDSERALRLSEKPPYSKYSSRHKSHDNVYSLGGLEGRKASGSLLAMWNGSSLSDAGPPPISRSGAASMPSSPKQARKMSIQDSLALQPKLTRHKELASENINLRTRKYSSSSLSHMGAYSRSLPRLYRATENQLTPLSLPPRNSLGNSKRTKLGEKDLPHSVIDNDNYLNFSSLSSGALPYKTSASEGNPYVSSTLSVPASPRVARKMLLASTSSCASDDFDQASYVGTNPSHSLLAGESDRVFATRRNFSCGSVEFDEADLESLRQASGTPQPALRERKSSISSISGRDDLMDYHRRQREERLREQEMERLERQRLETILSLCAEYTKPDSRLSTGTTVEDVQKINKELEKLQLSDEESVFEEALMSPDTRYRCHRKDSLPDADLASCGSLSQSSASFFTPRSTRNDELLSDLTRTPPPPSSTFPKASSESSYLSILPKTPEGISEEQRSQELAAMEETRIVILNNLEELKQKIKDINDQMDESFRELDMECALLDGEQKSETTELMKEKEILDHLNRKIAELEKNIVGEKTKEKVKLDAEREKLERLQELYSEQKTQLDNCPESMREQLQQQLKRDADLLDVESKHFEDLEFQQLEHESRLDEEKENLTQQLLREVAEYQRNIVSRKEKISALKKQANHIVQQAQREQDHFVKEKNNLIMMLQREKENLCNLEKKYSSLSGGKGFPVNPNTLKEGYISVNEINEPCGNSTNLSPSTQFPADADAVATEPATAVLASQPQSKEHFRSLEERKKQHKEGLYLSDTLPRKKTTSSISPHFSSATMGRSITPKAHLPLGQSNSCGSVLPPSLAAMAKDSESRRMLRGYNHQQMSEGHRQKSEFYNRTASESNVYLNSFHYPDHSYKDQAFDTLSLDSSDSMETSISACSPDNISSASTSNIARIEEMERLLKQAHAEKTRLLESREREMEAKKRALEEEKRRREILEKRLQEETSQRQKLIEKEVKIRERQRAQARPLTRYLPVRKEDFDLRSHVETAGHNIDTCYHVSITEKTCRGFLIKMGGKIKTWKKRWFVFDRNKRTFSYYADKHETKLKGVIYFQAIEEVYYDHLKNANKSPNPLLTFSVKTHDRIYYMVAPSPEAMRIWMDVIVTGAEGYTHFLL", "comments": "FUNCTION: Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). {ECO:0000250, ECO:0000269|PubMed:12376540}.\nSUBUNIT: Interacts with FLNC. {ECO:0000269|PubMed:12376540}.\nINTERACTION: P21333:FLNA; NbExp=3; IntAct=EBI-2798483, EBI-350432;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12376540}. Membrane {ECO:0000269|PubMed:12376540}; Peripheral membrane protein {ECO:0000269|PubMed:12376540}. Note=Translocates to the plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is translocated to vesicular compartments.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q86SQ0-1; Sequence=Displayed; Name=2;   IsoId=Q86SQ0-2; Sequence=VSP_016745; Name=3;   IsoId=Q86SQ0-3; Sequence=VSP_016744, VSP_016745;\nDOMAIN: The PH domain mediates the binding to phosphoinositides.\nSEQUENCE CAUTION: Sequence=AAH69194.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; Sequence=BAD93140.1; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q86SQ0", "displayName": "PHLB2_HUMAN", "synonyms": "Pleckstrin homology-like domain family B member 2, Protein LL5-beta", "taxid": 9606, "geneName": "PHLDB2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q86SQ0", "id": "uniprot.Q86SQ0", "value": "uniprot.Q86SQ0"}}, {"data": {"domainIds": "entrez.90362", "primaryDomainId": "entrez.90362", "geneType": "protein-coding", "displayName": "family with sequence similarity 110 member B", "synonyms": "protein FAM110B", "chromosome": "8", "description": "family with sequence similarity 110 member B", "approvedSymbol": "FAM110B", "type": "Gene", "symbols": "C8orf72", "mapLocation": "8q12.1", "graphics": {"fill": "#FFB6C1"}, "name": "FAM110B", "id": "entrez.90362", "value": "entrez.90362"}}, {"data": {"domainIds": "uniprot.B3KRT5", "sequence": "MPTETLQTGSMVKPVSPAGTFTSAVPLRILNKGPDYFRRQAEPNPKRLSAVERLEADKAKYVKSQEVINAKQEPVKPAVLAKPPVCPAAKRALGSPTLKVFGNHAKTESGVQRENLKLEILKNIINSSEGSSSGSGHKHSSRNWPPHRSEATDLHRHSFAESLKVYPTQGRRSPQEGGSHVGRRLLEQSAESFLHVSHSSSDIRKVTSVKPLKAIPCSSSPPPLPPKPKIAAIASMKSPEADPVEPACGVSRRPSLQRSKSDLSDRYFRVDADVERFFNYCGLDPEELENLGMENFARANSDIISLNFRSASMISSDCEQSQDSNSDLRNDDSANNRVPYGISAIERNARIIKWLYSIKQARESQKVSHV", "primaryDomainId": "uniprot.B3KRT5", "displayName": "B3KRT5_HUMAN", "synonyms": "cDNA FLJ34902 fis, clone NT2RI2000588 {ECO:0000313, EMBL:BAG52497.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B3KRT5", "id": "uniprot.B3KRT5", "value": "uniprot.B3KRT5"}}, {"data": {"domainIds": "uniprot.A0A024R7V5", "sequence": "MPTETLQTGSMVKPVSPAGTFTSAVPLRILNKGPDYFRRQAEPNPKRLSAVERLEADKAKYVKSQEVINAKQEPVKPAVLAKPPVCPAAKRALGSPTLKVFGNHAKTESGVQRENLKLEILKNIINSSEGSSSGSGHKHSSRNWPPHRSEATDLHRHSFAESLKVYPTQGRRSPQEGGSHVGRRLLEQSAESFLHVSHSSSDIRKVTSVKPLKAIPCSSSAPPLPPKPKIAAIASMKSPEADPVEPACGVSRRPSLQRSKSDLSDRYFRVDADVERFFNYCGLDPEELENLGMENFARANSDIISLNFRSASMISSDCEQSQDSNSDLRNDDSANDRVPYGISAIERNARIIKWLYSIKQARESQKVSHV", "primaryDomainId": "uniprot.A0A024R7V5", "displayName": "A0A024R7V5_HUMAN", "synonyms": "Chromosome 8 open reading frame 72, isoform CRA_a {ECO:0000313, EMBL:EAW86802.1}", "taxid": 9606, "geneName": "C8orf72", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R7V5", "id": "uniprot.A0A024R7V5", "value": "uniprot.A0A024R7V5"}}, {"data": {"domainIds": "uniprot.Q8TC76", "sequence": "MPTETLQTGSMVKPVSPAGTFTSAVPLRILNKGPDYFRRQAEPNPKRLSAVERLEADKAKYVKSQEVINAKQEPVKPAVLAKPPVCPAAKRALGSPTLKVFGNHAKTESGVQRENLKLEILKNIINSSEGSSSGSGHKHSSRNWPPHRSEATDLHRHSFAESLKVYPTQGRRSPQEGGSHVGRRLLEQSAESFLHVSHSSSDIRKVTSVKPLKAIPCSSSAPPLPPKPKIAAIASMKSPEADPVEPACGVSRRPSLQRSKSDLSDRYFRVDADVERFFNYCGLDPEELENLGMENFARANSDIISLNFRSASMISSDCEQSQDSNSDLRNDDSANDRVPYGISAIERNARIIKWLYSIKQARESQKVSHV", "comments": "FUNCTION: May be involved in tumor progression.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17499476}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17499476}.\nTISSUE SPECIFICITY: Detected in thyroid, spleen and testis, and at lower levels in stomach, spinal cord, lymph node, trachea, adrenal gland, prostate, ovary and intestine. {ECO:0000269|PubMed:17499476}.\nSIMILARITY: Belongs to the FAM110 family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAB50224.1; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q8TC76", "displayName": "F110B_HUMAN", "synonyms": "Protein FAM110B", "taxid": 9606, "geneName": "FAM110B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q8TC76", "id": "uniprot.Q8TC76", "value": "uniprot.Q8TC76"}}, {"data": {"domainIds": "entrez.116987", "primaryDomainId": "entrez.116987", "geneType": "protein-coding", "displayName": "ArfGAP with GTPase domain, ankyrin repeat and PH domain 1", "synonyms": "arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1, Arf GAP with GTP-binding protein-like, ANK repeat and PH domains 1, GTP-binding and GTPase-activating protein 1, centaurin, gamma 2", "chromosome": "2", "description": "ArfGAP with GTPase domain, ankyrin repeat and PH domain 1", "approvedSymbol": "AGAP1", "type": "Gene", "symbols": "AGAP-1, CENTG2, GGAP1, cnt-g2", "mapLocation": "2q37.2", "graphics": {"fill": "#FFB6C1"}, "name": "AGAP1", "id": "entrez.116987", "value": "entrez.116987"}}, {"data": {"domainIds": "uniprot.X5D293", "sequence": "MNYQQQLANSAAIRAEIQRFESVHPNIYSIYELLERVEEPVLQNQIREHVIAIEDAFVNSQEWTLSRSVPELKVGIVGNLASGKSALVHRYLTGTYVQEESPEDMDAGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKIVATRKKQQLSIGPCKSLPNSPSHSSVCSAQVSAVHISQTSNGGGSLSDYSSSVPSTPSTSQKELRIDVPPTANTPTPVRKQSKRRSNLFTSRKGSDPDKEKKGLESRADSIGSGRAIPIKQGMLLKRSGKSLNKEWKKKYVTLCDNGVLTYHPSLHDYMQNVHGKEIDLLRTTVKVPGKRPPRATSACAPISSPKTNGLSKDMSSLHISPNSDTGLGDSVCSSPSISSTTSPKLDPPPSPHANRKKHRRKKSTSNFKADGLSGTAEEQEENFEFIIVSLTGQTWHFEATTYEERDAWVQAIESQILASLQSCESSKNKSRLTSQSEAMALQSIRNMRGNSHCVDCETQNPNWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDWPVELIKVMSSIGNELANSVWEESSQGRTKPSVDSTREEKERWIRAKYEQKLFLAPLPCTELSLGQHLLRATADEDLRTAILLLAHGSRDEVNETCGEGDGRTALHLACRKGNVVLAQLLIWYGVDVTARDAHGNTALAYARQASSQECIDVLLQYGCPDERFVLMATPNLSRRNNNRNNSSGRVPTII", "primaryDomainId": "uniprot.X5D293", "displayName": "X5D293_HUMAN", "synonyms": "ArfGAP with GTPase domain, ankyrin repeat and PH domain 1 isoform A {ECO:0000313, EMBL:AHW56404.1}", "taxid": 9606, "geneName": "AGAP1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "X5D293", "id": "uniprot.X5D293", "value": "uniprot.X5D293"}}, {"data": {"domainIds": "uniprot.B2RZG9", "sequence": "MNYQQQLANSAAIRAEIQRFESVHPNIYSIYELLERVEEPVLQNQIREHVIAIEDAFVNSQEWTLSRSVPELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKIVATRKKQQLSIGPCKSLPNSPSHSSVCSAQVSAVHISQTSNGGGSLSDYSSSVPSTPSISQKELRIDVPPTANTPTPVRKQSKRRSNLFTSRKGSDPDKEKKGLESRADSIGSGRAIPIKQGMLLKRSGKSLNKEWKKKYVTLCDNGVLTYHPSLHDYMQNVHGKEIDLLRTTVKVPGKRPPRATSACAPISSPKTNGLSKDMSSLHISPNSDTGLGDSVCSSPSISSTTSPKLDPPPSPHANRKKHRRKKSTSNFKADGLSGTAEEQEENFEFIIVSLTGQTWHFEATTYEERDAWVQAIESQILASLQSCESSKNKSRLTSQSEAMALQSIRNMRGNSHCVDCETQNPNWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDWPIELIKVMSSIGNELANSVWEESSQGRTKPSVDSTREEKERWIRAKYEQKLFLAPLPCTELSLGQHLLRATADEDLRTAILLLAHGSRDEVNETCGEGDGRTALHLACRKGNVVLAQLLIWYGVDVTARDAHGNTALAYARQASSQECIDVLLQYGCPDERFVLMATPNLSRRNNNRNNSSGRVPTII", "primaryDomainId": "uniprot.B2RZG9", "displayName": "B2RZG9_HUMAN", "synonyms": "ArfGAP with GTPase domain, ankyrin repeat and PH domain 1 {ECO:0000313, EMBL:AAI67153.1}", "taxid": 9606, "geneName": "AGAP1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B2RZG9", "id": "uniprot.B2RZG9", "value": "uniprot.B2RZG9"}}, {"data": {"domainIds": "uniprot.Q9UPQ3", "sequence": "MNYQQQLANSAAIRAEIQRFESVHPNIYSIYELLERVEEPVLQNQIREHVIAIEDAFVNSQEWTLSRSVPELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKIVATRKKQQLSIGPCKSLPNSPSHSSVCSAQVSAVHISQTSNGGGSLSDYSSSVPSTPSTSQKELRIDVPPTANTPTPVRKQSKRRSNLFTSRKGSDPDKEKKGLESRADSIGSGRAIPIKQGMLLKRSGKSLNKEWKKKYVTLCDNGVLTYHPSLHDYMQNVHGKEIDLLRTTVKVPGKRPPRATSACAPISSPKTNGLSKDMSSLHISPNSGNVTSASGSQMASGISLVSFNSRPDGMHQRSYSVSSADQWSEATVIANSAISSDTGLGDSVCSSPSISSTTSPKLDPPPSPHANRKKHRRKKSTSNFKADGLSGTAEEQEENFEFIIVSLTGQTWHFEATTYEERDAWVQAIESQILASLQSCESSKNKSRLTSQSEAMALQSIRNMRGNSHCVDCETQNPNWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDWPVELIKVMSSIGNELANSVWEESSQGRTKPSVDSTREEKERWIRAKYEQKLFLAPLPCTELSLGQHLLRATADEDLRTAILLLAHGSRDEVNETCGEGDGRTALHLACRKGNVVLAQLLIWYGVDVTARDAHGNTALAYARQASSQECIDVLLQYGCPDERFVLMATPNLSRRNNNRNNSSGRVPTII", "comments": "FUNCTION: GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)- dependent trafficking of proteins in the endosomal-lysosomal system. {ECO:0000269|PubMed:12640130}.\nACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol 3,4,5-trisphosphate (PIP3) and, to a lesser extent, by phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid potentiates PIP2 stimulation.\nSUBUNIT: Homodimer. Interacts with several subunits of the AP-3 protein complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3. {ECO:0000269|PubMed:12967569, ECO:0000269|PubMed:15381706}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12388557, ECO:0000269|PubMed:12640130}. Note=Associates with the endocytic compartment.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q9UPQ3-1; Sequence=Displayed; Name=2;   IsoId=Q9UPQ3-2; Sequence=VSP_011183; Name=3;   IsoId=Q9UPQ3-3; Sequence=VSP_011181, VSP_011182;\nTISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12388557, ECO:0000269|PubMed:12640130, ECO:0000269|PubMed:15381706, ECO:0000269|PubMed:16079295}.\nDOMAIN: The PH domain mediates AP-3 binding.\nPTM: Phosphorylated on tyrosines. {ECO:0000269|PubMed:15381706}.\nSIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAH60814.1; Type=Miscellaneous discrepancy; Note=A 4-nucleotides insertion of unknown origin disrupts the reading frame.; Evidence={ECO:0000305}; Sequence=BAA83051.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BAA91862.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9UPQ3", "displayName": "AGAP1_HUMAN", "synonyms": "Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1, AGAP-1, Centaurin-gamma-2, Cnt-g2, GTP-binding and GTPase-activating protein 1, GGAP1", "taxid": 9606, "geneName": "AGAP1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9UPQ3", "id": "uniprot.Q9UPQ3", "value": "uniprot.Q9UPQ3"}}, {"data": {"domainIds": "entrez.9223", "primaryDomainId": "entrez.9223", "geneType": "protein-coding", "displayName": "membrane associated guanylate kinase, WW and PDZ domain containing 1", "synonyms": "membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1, BAI1-associated protein 1, WW domain-containing protein 3, atrophin-1-interacting protein 3, membrane-associated guanylate kinase inverted 1, trinucleotide repeat-containing gene 19 protein", "chromosome": "3", "description": "membrane associated guanylate kinase, WW and PDZ domain containing 1", "approvedSymbol": "MAGI1", "type": "Gene", "symbols": "AIP-3, AIP3, BAIAP1, BAP-1, BAP1, MAGI-1, MAGI-1b, Magi1d, TNRC19, WWP3", "mapLocation": "3p14.1", "graphics": {"fill": "#FFB6C1"}, "name": "MAGI1", "id": "entrez.9223", "value": "entrez.9223"}}, {"data": {"domainIds": "uniprot.Q96QZ7", "sequence": "MSKVIQKKNHWTSRVHECTVKRGPQGELGVTVLGGAEHGEFPYVGAVAAVEAAGLPGGGEGPRLGEGELLLEVQGVRVSGLPRYDVLGVIDSCKEAVTFKAVRQGGRLNKDLRHFLNQRFQKGSPDHELQQTIRDNLYRHAVPCTTRSPREGEVPGVDYNFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALHSLQSGSKQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGEQEEHTLQETALPPVNSSIIAAPITDPSQKFPQYLPLSAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGIYYVDHINRKTQYENPVLEAKRKKQLEQQQQQQQQQQQQQQQQQQQQTEEWTEDHSALVPPVIPNHPPSNPEPAREVPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVNGMKDARPSSPADVASNSSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLVECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEFPPAEAQAPDQTDSSGQKKPDPFKIWAQSRSMYENRPMSPSPASGLSKGEREREINSTNFGECPIPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAVPKTENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHTPSQQGTQETRNTTKPKQESQFEFKAPQATQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLKRGDGSVPEYDPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEKRAHARDPKGSREYSRQPNEHHTWNGTSRKPDSGACRPKDRAPEGRRDAQAERAAAANGPKRRSPEKRREGTRSADNTLERREKHEKRRDVSPERRRERSPTRRRDGSPSRRRRSLERLLEQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNREDRASHREREEANLKQDAGRSSRHPPEQRRRPYKECSTDLSI", "comments": "FUNCTION: May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity). {ECO:0000250}.\nSUBUNIT: Interacts through its WW 2 domain with SYNPO and through its PDZ 5 domain with ACTN4 (PubMed:12042308). Interacts with cytoplasmic domain of ADGRB1 (PubMed:9647739). Interacts via its WW domains with DRPLA (PubMed:9647693). Interacts with ESAM, LRP2 and CXADR (By similarity). May interact with CTNNB1 (By similarity). Interacts through its PDZ 1 domain with NET1 (By similarity). Interacts with ASIC3 and AMOT (PubMed:15317815, PubMed:16043488). Interacts with FCHSD2 (PubMed:14627983). Interacts with IGSF5/JAM4 and through its PDZ 2 and 3 domains with NPHS1 forming a tripartite complex (By similarity) (PubMed:12773569). Interacts with DDN (PubMed:16751601). Isoform 3 (via PDZ domain) interacts with RAPGEF2 (PubMed:11168587). Interacts with DLL1 (By similarity). Interacts with KCNJ10 and possibly with KCNJ10/KCNJ16 heterodimer; this interaction may facilitate KCNJ10/KCNJ16 potassium channel expression at the basolateral membrane in kidney tubular cells. {ECO:0000250|UniProtKB:Q4L1J4, ECO:0000250|UniProtKB:Q6RHR9, ECO:0000269|PubMed:11168587, ECO:0000269|PubMed:12042308, ECO:0000269|PubMed:12773569, ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:16043488, ECO:0000269|PubMed:16751601, ECO:0000269|PubMed:9647693, ECO:0000269|PubMed:9647739}.\nINTERACTION: P06463:E6 (xeno); NbExp=3; IntAct=EBI-924464, EBI-1186926; O94868:FCHSD2; NbExp=5; IntAct=EBI-924464, EBI-1215612; P46940:IQGAP1; NbExp=4; IntAct=EBI-924464, EBI-297509; O60333-3:KIF1B; NbExp=3; IntAct=EBI-924464, EBI-465669; Q9Y4G8:RAPGEF2; NbExp=2; IntAct=EBI-8769674, EBI-307079;\nSUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11969287}. Cell membrane {ECO:0000269|PubMed:11969287}; Peripheral membrane protein {ECO:0000269|PubMed:11969287}. Note=Localizes to epithelial cells tight junctions.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=7;   Comment=Additional isoforms seem to exist.; Name=1; Synonyms=MAGI-1C-alpha-beta1;   IsoId=Q96QZ7-1; Sequence=Displayed; Name=2; Synonyms=MAGI-1C-beta;   IsoId=Q96QZ7-2; Sequence=VSP_011664, VSP_011666; Name=3; Synonyms=MAGI-1A-alpha-beta1;   IsoId=Q96QZ7-3; Sequence=VSP_011670, VSP_011671, VSP_011672; Name=4; Synonyms=MAGI-1A-alpha;   IsoId=Q96QZ7-4; Sequence=VSP_011664, VSP_011666, VSP_011667,                            VSP_011668, VSP_011670, VSP_011671,                            VSP_011672; Name=5; Synonyms=MAGI-1B-alpha-beta;   IsoId=Q96QZ7-5; Sequence=VSP_011666, VSP_011669, VSP_011672; Name=6; Synonyms=MAGI-1C-beta2;   IsoId=Q96QZ7-6; Sequence=VSP_011664, VSP_011666, VSP_011667; Name=7; Synonyms=MAGI-1C-beta3;   IsoId=Q96QZ7-7; Sequence=VSP_011664, VSP_011665;\nTISSUE SPECIFICITY: Widely expressed with the exception of skeletal muscle. Isoform 1, isoform 2 and isoform 6 are highly expressed in colon, kidney, lung, liver, and pancreas. Isoform 5 is predominantly expressed in brain and heart. Isoform 3 and isoform 4 are highly expressed in pancreas and brain. {ECO:0000269|PubMed:11969287, ECO:0000269|PubMed:9647693, ECO:0000269|PubMed:9647739}.", "primaryDomainId": "uniprot.Q96QZ7", "displayName": "MAGI1_HUMAN", "synonyms": "Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1, Atrophin-1-interacting protein 3, AIP-3, BAI1-associated protein 1, BAP-1, Membrane-associated guanylate kinase inverted 1, MAGI-1, Trinucleotide repeat-containing gene 19 protein, WW domain-containing protein 3, WWP3", "taxid": 9606, "geneName": "MAGI1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q96QZ7", "id": "uniprot.Q96QZ7", "value": "uniprot.Q96QZ7"}}, {"data": {"domainIds": "entrez.84451", "primaryDomainId": "entrez.84451", "geneType": "protein-coding", "displayName": "mitogen-activated protein kinase kinase kinase 21", "synonyms": "mitogen-activated protein kinase kinase kinase 21, mitogen-activated protein kinase kinase kinase MLK4, mixed lineage kinase 4", "chromosome": "1", "description": "mitogen-activated protein kinase kinase kinase 21", "approvedSymbol": "MAP3K21", "type": "Gene", "symbols": "MLK4, dJ862P8.3", "mapLocation": "1q42.2", "graphics": {"fill": "#FFB6C1"}, "name": "MAP3K21", "id": "entrez.84451", "value": "entrez.84451"}}, {"data": {"domainIds": "uniprot.Q5TCX8", "sequence": "MALRGAAGATDTPVSSAGGAPGGSASSSSTSSGGSASAGAGLWAALYDYEARGEDELSLRRGQLVEVLSQDAAVSGDEGWWAGQVQRRLGIFPANYVAPCRPAASPAPPPSRPSSPVHVAFERLELKELIGAGGFGQVYRATWQGQEVAVKAARQDPEQDAAAAAESVRREARLFAMLRHPNIIELRGVCLQQPHLCLVLEFARGGALNRALAAANAAPDPRAPGPRRARRIPPHVLVNWAVQIARGMLYLHEEAFVPILHRDLKSSNILLLEKIEHDDICNKTLKITDFGLAREWHRTTKMSTAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMKECWQQDPHIRPSFALILEQLTAIEGAVMTEMPQESFHSMQDDWKLEIQQMFDELRTKEKELRSREEELTRAALQQKSQEELLKRREQQLAEREIDVLERELNILIFQLNQEKPKVKKRKGKFKRSRLKLKDGHRISLPSDFQHKITVQASPNLDKRRSLNSSSSSPPSSPTMMPRLRAIQLTSDESNKTWGRNTVFRQEEFEDVKRNFKKKGCTWGPNSIQMKDRTDCKERIRPLSDGNSPWSTILIKNQKTMPLASLFVDQPGSCEEPKLSPDGLEHRKPKQIKLPSQAYIDLPLGKDAQRENPAEAESWEEAASANAATVSIEMTPTNSLSRSPQRKKTESALYGCTVLLASVALGLDLRELHKAQAAEEPLPKEEKKKREGIFQRASKSRRSASPPTSLPSTCGEASSPPSLPLSSALGILSTPSFSTKCLLQMDSEDPLVDSAPVTCDSEMLTPDFCPTAPGSGREPALMPRLDTDCSVSRNLPSSFLQQTCGNVPYCASSKHRPSHHRRTMSDGNPTPTGATIISATGASALPLCPSPAPHSHLPREVSPKKHSTVHIVPQRRPASLRSRSDLPQAYPQTAVSQLAQTACVVGRPGPHPTQFLAAKERTKSHVPSLLDADVEGQSRDYTVPLCRMRSKTSRPSIYELEKEFLS", "comments": "FUNCTION: Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways. {ECO:0000269|PubMed:21602844}.\nCATALYTIC ACTIVITY: 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=2.7.11.25;   Evidence={ECO:0000305};\nCATALYTIC ACTIVITY: 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=2.7.11.25; Evidence={ECO:0000305};\nCOFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;   Evidence={ECO:0000250|UniProtKB:P80192};\nACTIVITY REGULATION: Homodimerization via the leucine zipper domains is required for autophosphorylation and subsequent activation. {ECO:0000250|UniProtKB:Q16584}.\nSUBUNIT: Homodimer (By similarity). Interacts with TLR4. {ECO:0000250, ECO:0000269|PubMed:21602844}.\nINTERACTION: O15111:CHUK; NbExp=2; IntAct=EBI-1057380, EBI-81249;\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1 {ECO:0000269|Ref.1}; Synonyms=MLK4beta;   IsoId=Q5TCX8-1; Sequence=Displayed; Name=2 {ECO:0000269|Ref.1}; Synonyms=MLK4alpha;   IsoId=Q5TCX8-2; Sequence=VSP_051733, VSP_051734; Name=3;   IsoId=Q5TCX8-3; Sequence=VSP_051731, VSP_051732;\nPTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. {ECO:0000250|UniProtKB:Q16584}.\nSIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=BAB47433.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q5TCX8", "displayName": "M3K21_HUMAN", "synonyms": "Mitogen-activated protein kinase kinase kinase 21, 2.7.11.25, Mitogen-activated protein kinase kinase kinase MLK4, Mixed lineage kinase 4", "taxid": 9606, "geneName": "MAP3K21", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q5TCX8", "id": "uniprot.Q5TCX8", "value": "uniprot.Q5TCX8"}}, {"data": {"domainIds": "entrez.1025", "primaryDomainId": "entrez.1025", "geneType": "protein-coding", "displayName": "cyclin dependent kinase 9", "synonyms": "cyclin-dependent kinase 9, CDC2-related kinase, cell division cycle 2-like protein kinase 4, cell division protein kinase 9, serine/threonine protein kinase PITALRE, tat-associated kinase complex catalytic subunit", "chromosome": "9", "description": "cyclin dependent kinase 9", "approvedSymbol": "CDK9", "type": "Gene", "symbols": "C-2k, CDC2L4, CTK1, PITALRE, TAK", "mapLocation": "9q34.11", "graphics": {"fill": "#FFB6C1"}, "name": "CDK9", "id": "entrez.1025", "value": "entrez.1025"}}, {"data": {"domainIds": "uniprot.A0A024R880", "sequence": "MAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF", "comments": "SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000256|RuleBase:RU000304}.", "primaryDomainId": "uniprot.A0A024R880", "displayName": "A0A024R880_HUMAN", "synonyms": "Cyclin-dependent kinase 9 (CDC2-related kinase), isoform CRA_a {ECO:0000313, EMBL:EAW87697.1}", "taxid": 9606, "geneName": "CDK9", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R880", "id": "uniprot.A0A024R880", "value": "uniprot.A0A024R880"}}, {"data": {"domainIds": "uniprot.P50750", "sequence": "MAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF", "comments": "FUNCTION: Protein kinase involved in the regulation of transcription (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094). Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094). This complex is inactive when in the 7SK snRNP complex form (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094). Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR and the negative elongation factors DSIF and NELF (PubMed:9857195, PubMed:10912001, PubMed:11112772, PubMed:12037670, PubMed:20081228, PubMed:20980437, PubMed:21127351). Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6- inducible STAT3 signaling) (PubMed:17956865, PubMed:18362169). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis (PubMed:10393184, PubMed:11112772). P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export (PubMed:15564463, PubMed:19575011, PubMed:19844166). Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing (PubMed:15564463, PubMed:19575011, PubMed:19844166). The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro (PubMed:21127351). Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage (PubMed:20493174). In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6 (PubMed:20493174). Promotes cardiac myocyte enlargement (PubMed:20081228). RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription (PubMed:21127351). AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect (PubMed:9857195, PubMed:10912001, PubMed:11112772). The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation (PubMed:12037670). {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11145967, ECO:0000269|PubMed:11575923, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:11884399, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15564463, ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18362169, ECO:0000269|PubMed:19575011, ECO:0000269|PubMed:19844166, ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:20930849, ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:28426094, ECO:0000269|PubMed:9857195}.\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:20980437}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;   Evidence={ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:20980437};\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:12037670,   ECO:0000269|PubMed:20980437}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;   Evidence={ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:20980437};\nCATALYTIC ACTIVITY: 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={ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:28426094}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217;   Evidence={ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:28426094};\nACTIVITY REGULATION: Inhibited by CDKI-71, CR8, GPC-286199, AG-024322, flavopiridol (alvocidib), RBG-286147, anilinopyrimidine 32, arylazopyrazole 31b, indirubin 3'-monoxime, meriolin 3,P276-00, olomoucine II, pyrazolotriazine, meriolin, variolin, thiazolyl- pyrimidine, thiazolyl-pyrimidine, indirubin-30-monoxime, ZK 304709, AG- 012986, AT7519, R547, RGB-286638, imidazole pyrimidine, EXEL-3700, EXEL-8647, 5,6-dichloro-1-b-ribofur-anosyl-benzimidazole (DRB), P276- 00, roscovitine (seliciclib, CYC202) and SNS-032 (BMS-387032). Activation by Thr-186 phosphorylation is calcium Ca(2+) signaling pathway-dependent; actively inactivated by dephosphorylation mediated by PPP1CA, PPM1A and PPM1B. Reversibly repressed by acetylation at Lys- 44 and Lys-48. {ECO:0000269|PubMed:18250157, ECO:0000269|PubMed:18483222, ECO:0000269|PubMed:19238148, ECO:0000269|PubMed:21448926, ECO:0000269|PubMed:21484792, ECO:0000269|PubMed:21779453}.\nSUBUNIT: 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). Associates with CCNT1/cyclin-T1, CCNT2/cyclin-T2 (isoform A and isoform B) or CCNK/cyclin-K to form active P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31 and is part of the super elongation complex (SEC). Component of a complex which is composed of at least 5 members: HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H and NCL/nucleolin. Associates with UBR5 and forms a transcription regulatory complex composed of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulate target gene transcription (e.g. gamma fibrinogen/FGG) by recruiting their promoters. Component of the 7SK snRNP inactive complex which is composed of at least 8 members: P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, LARP7, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. This inactive 7SK snRNP complex can also interact with NCOR1 and HDAC3, probably to regulate CDK9 acetylation. Release of P-TEFb from P-TEFb/7SK snRNP complex requires both PP2B to transduce calcium Ca(2+) signaling in response to stimuli (e.g. UV or hexamethylene bisacetamide (HMBA)) and PPP1CA to dephosphorylate Thr-186. This released P-TEFb remains inactive in the pre-initiation complex with BRD4 until new Thr-186 phosphorylation occurs after the synthesis of a short RNA (PubMed:10393184, PubMed:10574912, PubMed:12037670, PubMed:11884399, PubMed:12065898, PubMed:12718890, PubMed:15965233, PubMed:16109376, PubMed:17452463, PubMed:17643375, PubMed:18249148, PubMed:18483222, PubMed:18566585, PubMed:20159561, PubMed:20471948, PubMed:21127351, PubMed:21779453, PubMed:22195968, PubMed:9491887). Interacts with BRD4; to target chromatin binding (PubMed:16109376, PubMed:16109377, PubMed:18483222). Interacts with JMJD6 (PubMed:24360279). Interacts with activated nuclear STAT3 and RELA/p65 (PubMed:17956865, PubMed:18362169). Binds to AR and MYOD1 (PubMed:12037670, PubMed:20980437). Forms a complex composed of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes (PubMed:20081228). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (By similarity). Interacts with HSF1 (PubMed:27189267). Interacts with TBX21 (By similarity). Isoform 3: binds to KU70/XRCC6 (PubMed:20535204). Interacts with WDR43 (By similarity). {ECO:0000250|UniProtKB:Q99J95, ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:11884399, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:12065898, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15965233, ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:17452463, ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18249148, ECO:0000269|PubMed:18362169, ECO:0000269|PubMed:18483222, ECO:0000269|PubMed:18566585, ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:20535204, ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:21779453, ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:24360279, ECO:0000269|PubMed:27189267, ECO:0000269|PubMed:9491887}.\nSUBUNIT: (Microbial infection) Interacts with the acidic/proline-rich region of HIV-1 and HIV-2 Tat via T-loop region and is thus required for HIV to hijack host transcription machinery during its replication through cooperative binding to viral TAR RNA (PubMed:10958691, PubMed:9491887). Interacts with herpes simplex virus 1 protein ICP22; this interaction inhibits the positive transcription elongation factor b (P-TEFb) (PubMed:23029222). {ECO:0000269|PubMed:10958691, ECO:0000269|PubMed:23029222, ECO:0000269|PubMed:9491887}.\nINTERACTION: Q13535:ATR; NbExp=3; IntAct=EBI-1383449, EBI-968983; Q8WXE1:ATRIP; NbExp=3; IntAct=EBI-1383449, EBI-747353; O60885-1:BRD4; NbExp=9; IntAct=EBI-1383449, EBI-9345088; O60563:CCNT1; NbExp=21; IntAct=EBI-1383449, EBI-2479671; Q16543:CDC37; NbExp=3; IntAct=EBI-1383449, EBI-295634; Q9HAW4:CLSPN; NbExp=3; IntAct=EBI-1383449, EBI-1369377; Q13451:FKBP5; NbExp=4; IntAct=EBI-1383449, EBI-306914; O94992:HEXIM1; NbExp=10; IntAct=EBI-1383449, EBI-2832510; P07900:HSP90AA1; NbExp=2; IntAct=EBI-1383449, EBI-296047; P08238:HSP90AB1; NbExp=2; IntAct=EBI-1383449, EBI-352572; Q6NYC1:JMJD6; NbExp=5; IntAct=EBI-1383449, EBI-8464037; Q4G0J3:LARP7; NbExp=11; IntAct=EBI-1383449, EBI-2371923; P53041:PPP5C; NbExp=3; IntAct=EBI-1383449, EBI-716663; P40763:STAT3; NbExp=2; IntAct=EBI-1383449, EBI-518675; P04608:tat (xeno); NbExp=8; IntAct=EBI-1383449, EBI-6164389;\nSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, PML body. Note=Accumulates on chromatin in response to replication stress. Complexed with CCNT1 in nuclear speckles, but uncomplexed form in the cytoplasm. The translocation from nucleus to cytoplasm is XPO1/CRM1- dependent. Associates with PML body when acetylated.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=P50750-1; Sequence=Displayed; Name=2;   IsoId=P50750-2; Sequence=VSP_016288;\nTISSUE SPECIFICITY: Ubiquitous.\nINDUCTION: By replication stress, in chromatin. Probably degraded by the proteasome upon Thr-186 dephosphorylation.\nPTM: Autophosphorylation at Thr-186, Ser-347, Thr-350, Ser-353, Thr-354 and Ser-357 triggers kinase activity by promoting cyclin and substrate binding (e.g. HIV TAT) upon conformational changes. Thr-186 phosphorylation requires the calcium Ca(2+) signaling pathway, including CaMK1D and calmodulin. This inhibition is relieved by Thr-29 dephosphorylation. However, phosphorylation at Thr-29 is inhibitory within the HIV transcription initiation complex. Phosphorylation at Ser-175 inhibits kinase activity. Can be phosphorylated on either Thr- 362 or Thr-363 but not on both simultaneously (PubMed:18566585). {ECO:0000269|PubMed:10958691, ECO:0000269|PubMed:15965233, ECO:0000269|PubMed:18483222, ECO:0000269|PubMed:18566585, ECO:0000269|PubMed:18829461, ECO:0000269|PubMed:20535204, ECO:0000269|PubMed:20851342, ECO:0000269|PubMed:21448926, ECO:0000269|PubMed:21533037, ECO:0000269|PubMed:21779453}.\nPTM: Dephosphorylation of Thr-186 by PPM1A and PPM1B blocks CDK9 activity and may lead to CDK9 proteasomal degradation. However, PPP1CA- mediated Thr-186 dephosphorylation is required to release P-TEFb from its inactive P-TEFb/7SK snRNP complex. Dephosphorylation of C-terminus Thr and Ser residues by protein phosphatase-1 (PP1) triggers CDK9 activity, contributing to the activation of HIV-1 transcription.\nPTM: N6-acetylation of Lys-44 promotes kinase activity, whereas acetylation of both Lys-44 and Lys-48 mediated by PCAF/KAT2B and GCN5/KAT2A reduces kinase activity (PubMed:17452463, PubMed:18250157). The acetylated form associates with PML bodies in the nuclear matrix and with the transcriptionally silent HIV-1 genome; deacetylated upon transcription stimulation (PubMed:17452463, PubMed:18250157). Deacetylated by SIRT7, promoting the kinase activity and subsequent 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (PubMed:28426094). {ECO:0000269|PubMed:17452463, ECO:0000269|PubMed:18250157, ECO:0000269|PubMed:28426094}.\nPTM: Polyubiquitinated and thus activated by UBR5. This ubiquitination is promoted by TFIIS/TCEA1 and favors 'Ser-2' phosphorylation of RPB1/POLR2A CTD. {ECO:0000269|PubMed:21127351}.\nDISEASE: Note=Chronic activation of CDK9 causes cardiac myocyte enlargement leading to cardiac hypertrophy and confers predisposition to heart failure.\nMISCELLANEOUS: CDK9 inhibition contributes to the anticancer activity of most CDK inhibitors under clinical investigation (PubMed:18423896 and PubMed:21779453). As a retroviruses target during the hijack of host transcription (e.g. HIV), CDK9 inhibitors might become specific antiretroviral agents (PubMed:18423896). May be a target for cardiac hypertrophy future treatments (PubMed:19757441 and PubMed:18423896). May also be a target in anti-inflammatory therapy in innate immunity and systemic inflammation (PubMed:18728388). {ECO:0000305|PubMed:18423896, ECO:0000305|PubMed:18728388}.\nSIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.\nWEB RESOURCE: Name=NIEHS-SNPs; URL=\"http://egp.gs.washington.edu/data/cdk9/\";", "primaryDomainId": "uniprot.P50750", "displayName": "CDK9_HUMAN", "synonyms": "Cyclin-dependent kinase 9, 2.7.11.22 {ECO:0000269, PubMed:12037670, ECO:0000269, PubMed:20980437}, 2.7.11.23 {ECO:0000269, PubMed:21127351, ECO:0000269, PubMed:28426094}, C-2K, Cell division cycle 2-like protein kinase 4, Cell division protein kinase 9, Serine/threonine-protein kinase PITALRE, Tat-associated kinase complex catalytic subunit", "taxid": 9606, "geneName": "CDK9", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P50750", "id": "uniprot.P50750", "value": "uniprot.P50750"}}, {"data": {"domainIds": "entrez.6235", "primaryDomainId": "entrez.6235", "geneType": "protein-coding", "displayName": "ribosomal protein S29", "synonyms": "40S ribosomal protein S29, small ribosomal subunit protein uS14", "chromosome": "14", "description": "ribosomal protein S29", "approvedSymbol": "RPS29", "type": "Gene", "symbols": "DBA13, S29, uS14", "mapLocation": "14q21.3", "graphics": {"fill": "#FFB6C1"}, "name": "RPS29", "id": "entrez.6235", "value": "entrez.6235"}}, {"data": {"domainIds": "uniprot.P62273", "sequence": "MGHQQLYWSHPRKFGQGSRSCRVCSNRHGLIRKYGLNMCRQCFRQYAKDIGFIKLD", "comments": "COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;   Evidence={ECO:0000269|PubMed:25957688}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:25957688};\nSUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688}.\nSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}. Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6QAP6}. Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q6QAP6, ECO:0000269|PubMed:25957688}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=P62273-1; Sequence=Displayed; Name=2;   IsoId=P62273-2; Sequence=VSP_042844;\nDISEASE: Diamond-Blackfan anemia 13 (DBA13) [MIM:615909]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre- Robin syndrome and cleft palate), thumb and urogenital anomalies. {ECO:0000269|PubMed:24829207}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the universal ribosomal protein uS14 family. {ECO:0000305}.", "primaryDomainId": "uniprot.P62273", "displayName": "RS29_HUMAN", "synonyms": "40S ribosomal protein S29, Small ribosomal subunit protein uS14 {ECO:0000303, PubMed:24524803}", "taxid": 9606, "geneName": "RPS29", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P62273", "id": "uniprot.P62273", "value": "uniprot.P62273"}}, {"data": {"domainIds": "entrez.7074", "primaryDomainId": "entrez.7074", "geneType": "protein-coding", "displayName": "TIAM Rac1 associated GEF 1", "synonyms": "T-lymphoma invasion and metastasis-inducing protein 1, T cell lymphoma invasion and metastasis 1, human T-lymphoma invasion and metastasis inducing TIAM1 protein", "chromosome": "21", "description": "TIAM Rac1 associated GEF 1", "approvedSymbol": "TIAM1", "type": "Gene", "symbols": "TIAM-1", "mapLocation": "21q22.11", "graphics": {"fill": "#FFB6C1"}, "name": "TIAM1", "id": "entrez.7074", "value": "entrez.7074"}}, {"data": {"domainIds": "uniprot.A0A2X0TW27", "sequence": "MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDSTGPQLATMRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPKQQHSSTLESYLIKPIQRILKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTTVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEDWDPFRFRHMIPTEALQVRALASADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKAVHSILRDKHRRQLLKTESLPSSQQYVPFGGKRLCALKGARPAMSRAVSAPSKSLGRRRRRLARNRFTIDSDAVSASSPEKESQQPPGGGDTDRWVEEQFDLAQYEEQDDIKETDILSDDDEFCESVKGASVDRDLQERLQATSISQRERGRKTLDSHASRMAQLKKQAALSGINGGLESASEEVIWVRREDFAPSRKLNTEI", "primaryDomainId": "uniprot.A0A2X0TW27", "displayName": "A0A2X0TW27_HUMAN", "synonyms": "T-cell lymphoma invasion and metastasis 1 {ECO:0000313, EMBL:EAX09895.1}, TIAM1 {ECO:0000313, EMBL:SPT35806.1}", "taxid": 9606, "geneName": "TIAM1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A2X0TW27", "id": "uniprot.A0A2X0TW27", "value": "uniprot.A0A2X0TW27"}}, {"data": {"domainIds": "uniprot.Q13009", "sequence": "MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDSTGPQLATMRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPKQQHSSTLESYLIKPIQRILKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTTVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEDWDPFRFRHMIPTEALQVRALASADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKAVHSILRDKHRRQLLKTESLPSSQQYVPFGGKRLCALKGARPAMSRAVSAPSKSLGRRRRRLARNRFTIDSDAVSASSPEKESQQPPGGGDTDRWVEEQFDLAQYEEQDDIKETDILSDDDEFCESVKGASVDRDLQERLQATSISQRERGRKTLDSHASRMAQLKKQAALSGINGGLESASEEVIWVRREDFAPSRKLNTEI", "comments": "FUNCTION: Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP- dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates RAC1, CDC42, and to a lesser extent RHOA. Required for normal cell adhesion and cell migration. {ECO:0000269|PubMed:20361982}.\nSUBUNIT: Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with NTRK2; mediates the activation of RAC1 by BDNF. Interacts with MAPK8IP2 and CD44 (By similarity). Interacts with BAIAP2. Interacts with EPHA8; regulates clathrin-mediated endocytosis of EPHA8. Interacts with PARD3. Interacts (via PDZ domain) with CNTNAP4, SDC1 and SDC3 (via C-terminus). {ECO:0000250, ECO:0000269|PubMed:15899863, ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:20361982, ECO:0000269|PubMed:20496116, ECO:0000269|PubMed:23395182, ECO:0000269|PubMed:23832200, ECO:0000269|PubMed:7753201}.\nINTERACTION: Q9C0A0-1:CNTNAP4; NbExp=2; IntAct=EBI-1050007, EBI-16035743; P54763:Ephb2 (xeno); NbExp=3; IntAct=EBI-1050007, EBI-537711; P18827:SDC1; NbExp=5; IntAct=EBI-1050007, EBI-2855248;\nSUBCELLULAR LOCATION: Cell junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Detected at the boundary between cells with actin-rich protrusions (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. {ECO:0000250}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q13009-1; Sequence=Displayed; Name=2;   IsoId=Q13009-2; Sequence=VSP_055865, VSP_055866;\nTISSUE SPECIFICITY: Found in virtually all analyzed tumor cell lines including B- and T-lymphomas, neuroblastomas, melanomas and carcinomas.\nDOMAIN: The first PH domain mediates interaction with membranes enriched in phosphoinositides. {ECO:0000250}.\nSIMILARITY: Belongs to the TIAM family. {ECO:0000305}.\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/TIAM1ID42557ch21q22.html\";", "primaryDomainId": "uniprot.Q13009", "displayName": "TIAM1_HUMAN", "synonyms": "T-lymphoma invasion and metastasis-inducing protein 1, TIAM-1", "taxid": 9606, "geneName": "TIAM1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q13009", "id": "uniprot.Q13009", "value": "uniprot.Q13009"}}, {"data": {"domainIds": "entrez.51307", "primaryDomainId": "entrez.51307", "geneType": "protein-coding", "displayName": "family with sequence similarity 53 member C", "synonyms": "protein FAM53C, putative nuclear protein", "chromosome": "5", "description": "family with sequence similarity 53 member C", "approvedSymbol": "FAM53C", "type": "Gene", "symbols": "C5orf6", "mapLocation": "5q31.2", "graphics": {"fill": "#FFB6C1"}, "name": "FAM53C", "id": "entrez.51307", "value": "entrez.51307"}}, {"data": {"domainIds": "uniprot.Q9NYF3", "sequence": "MITLITEQLQKQTLDELKCTRFSISLPLPDHADISNCGNSFQLVSEGASWRGLPHCSCAEFQDSLNFSYHPSGLSLHLRPPSRGNSPKEQPFSQVLRPEPPDPEKLPVPPAPPSKRHCRSLSVPVDLSRWQPVWRPAPSKLWTPIKHRGSGGGGGPQVPHQSPPKRVSSLRFLQAPSASSQCAPAHRPYSPPFFSLALAQDSSRPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPASSPELPWRPRGLRNLPRSRSQPCDLDARKTGVKRRHEEDPRRLRPSLDFDKMNQKPYSGGLCLQETAREGSSISPPWFMACSPPPLSASCSPTGGSSQVLSESEEEEEGAVRWGRQALSKRTLCQRDFGDLDLNLIEEN", "comments": "INTERACTION: V9HW98:HEL2; NbExp=3; IntAct=EBI-1644252, EBI-10190883; O43639:NCK2; NbExp=5; IntAct=EBI-1644252, EBI-713635; P31947:SFN; NbExp=3; IntAct=EBI-1644252, EBI-476295; P61981:YWHAG; NbExp=6; IntAct=EBI-1644252, EBI-359832;\nSIMILARITY: Belongs to the FAM53 family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q9NYF3", "displayName": "FA53C_HUMAN", "synonyms": "Protein FAM53C {ECO:0000305}", "taxid": 9606, "geneName": "FAM53C", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9NYF3", "id": "uniprot.Q9NYF3", "value": "uniprot.Q9NYF3"}}, {"data": {"domainIds": "entrez.79109", "primaryDomainId": "entrez.79109", "geneType": "protein-coding", "displayName": "MAPK associated protein 1", "synonyms": "target of rapamycin complex 2 subunit MAPKAP1, MEKK2-interacting protein 1, SAPK-interacting protein 1, TORC2 subunit MAPKAP1, mSIN1, mitogen-activated protein kinase 2-associated protein 1, mitogen-activated protein kinase associated protein 1, ras inhibitor MGC2745, stress-activated map kinase interacting protein 1, stress-activated protein kinase-interacting 1", "chromosome": "9", "description": "MAPK associated protein 1", "approvedSymbol": "MAPKAP1", "type": "Gene", "symbols": "JC310, MIP1, SIN1, SIN1b, SIN1g", "mapLocation": "9q33.3", "graphics": {"fill": "#FFB6C1"}, "name": "MAPKAP1", "id": "entrez.79109", "value": "entrez.79109"}}, {"data": {"domainIds": "uniprot.A0A024R863", "sequence": "MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ", "primaryDomainId": "uniprot.A0A024R863", "displayName": "A0A024R863_HUMAN", "synonyms": "Mitogen-activated protein kinase associated protein 1, isoform CRA_a {ECO:0000313, EMBL:EAW87633.1}", "taxid": 9606, "geneName": "MAPKAP1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024R863", "id": "uniprot.A0A024R863", "value": "uniprot.A0A024R863"}}, {"data": {"domainIds": "uniprot.Q9BPZ7", "sequence": "MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ", "comments": "FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. {ECO:0000269|PubMed:15988011, ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:17043309, ECO:0000269|PubMed:17054722, ECO:0000269|PubMed:17303383, ECO:0000269|PubMed:23727834}.\nSUBUNIT: All isoforms except isoform 4 can be incorporated into the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Interacts with ATF2, MAP3K2 and MAPK8. Interacts with GTP-bound HRAS and KRAS. Interacts with IFNAR2 and SGK1. Isoform 2 interacts with NBN. Isoform 1 interacts with CCDC28B. {ECO:0000269|PubMed:15988011, ECO:0000269|PubMed:16919458, ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:17054722, ECO:0000269|PubMed:17303383, ECO:0000269|PubMed:23727834, ECO:0000269|PubMed:23762398}.\nINTERACTION: P78527:PRKDC; NbExp=2; IntAct=EBI-749938, EBI-352053;\nSUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasmic vesicle. Nucleus.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=6; Name=1; Synonyms=beta, gamma;   IsoId=Q9BPZ7-1; Sequence=Displayed; Name=2; Synonyms=alpha, beta;   IsoId=Q9BPZ7-2; Sequence=VSP_006098; Name=3;   IsoId=Q9BPZ7-3; Sequence=VSP_033204; Name=4;   IsoId=Q9BPZ7-4; Sequence=VSP_033202; Name=5; Synonyms=alpha;   IsoId=Q9BPZ7-5; Sequence=VSP_033203, VSP_033207; Name=6; Synonyms=gamma;   IsoId=Q9BPZ7-6; Sequence=VSP_033205, VSP_033206;\nTISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in heart and skeletal muscle. {ECO:0000269|PubMed:15988011}.\nMISCELLANEOUS: [Isoform 4]: Not involved in a TORC2 complex. {ECO:0000305}.\nSIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.", "primaryDomainId": "uniprot.Q9BPZ7", "displayName": "SIN1_HUMAN", "synonyms": "Target of rapamycin complex 2 subunit MAPKAP1, TORC2 subunit MAPKAP1, Mitogen-activated protein kinase 2-associated protein 1, Stress-activated map kinase-interacting protein 1, SAPK-interacting protein 1, mSIN1", "taxid": 9606, "geneName": "MAPKAP1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9BPZ7", "id": "uniprot.Q9BPZ7", "value": "uniprot.Q9BPZ7"}}, {"data": {"domainIds": "entrez.57460", "primaryDomainId": "entrez.57460", "geneType": "protein-coding", "displayName": "protein phosphatase, Mg2+/Mn2+ dependent 1H", "synonyms": "protein phosphatase 1H, neurite extension-related protein phosphatase related to PP2C, protein phosphatase 1H (PP2C domain containing), ras homolog gene family, member C like 1", "chromosome": "12", "description": "protein phosphatase, Mg2+/Mn2+ dependent 1H", "approvedSymbol": "PPM1H", "type": "Gene", "symbols": "ARHCL1, NERPP-2C, URCC2", "mapLocation": "12q14.1-q14.2", "graphics": {"fill": "#FFB6C1"}, "name": "PPM1H", "id": "entrez.57460", "value": "entrez.57460"}}, {"data": {"domainIds": "uniprot.Q9ULR3", "sequence": "MLTRVKSAVANFMGGIMAGSSGSEHGGGSCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKAGAVTSTPNRNSSKRRSSLPNGEGLQLKENSESEGVSCHYWSLFDGHAGSGAAVVASRLLQHHITEQLQDIVDILKNSAVLPPTCLGEEPENTPANSRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSSYNISGGCTALIVICLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDEDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRIYDLSKYDHGSDDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS", "comments": "FUNCTION: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation. {ECO:0000269|PubMed:22586611}.\nCATALYTIC ACTIVITY: 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;\nCATALYTIC ACTIVITY: 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;\nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22586611}. Cytoplasm {ECO:0000269|PubMed:22586611}.\nMISCELLANEOUS: May act as a suppressor of trastuzumab resistance. {ECO:0000303|PubMed:22586611}.\nSIMILARITY: Belongs to the PP2C family. {ECO:0000305}.\nCAUTION: 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. {ECO:0000305|PubMed:19139490}.", "primaryDomainId": "uniprot.Q9ULR3", "displayName": "PPM1H_HUMAN", "synonyms": "Protein phosphatase 1H, 3.1.3.16", "taxid": 9606, "geneName": "PPM1H", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9ULR3", "id": "uniprot.Q9ULR3", "value": "uniprot.Q9ULR3"}}, {"data": {"domainIds": "entrez.5691", "primaryDomainId": "entrez.5691", "geneType": "protein-coding", "displayName": "proteasome 20S subunit beta 3", "synonyms": "proteasome subunit beta type-3, epididymis secretory sperm binding protein, proteasome (prosome, macropain) subunit, beta type, 3, proteasome chain 13, proteasome component C10-II, proteasome subunit beta 3, proteasome theta chain", "chromosome": "17", "description": "proteasome 20S subunit beta 3", "approvedSymbol": "PSMB3", "type": "Gene", "symbols": "HC10-II", "mapLocation": "17q12", "graphics": {"fill": "#FFB6C1"}, "name": "PSMB3", "id": "entrez.5691", "value": "entrez.5691"}}, {"data": {"domainIds": "uniprot.A0A384NL22", "sequence": "MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD", "comments": "CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.;   EC=3.4.25.1; Evidence={ECO:0000256|RuleBase:RU004203};\nSUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. {ECO:0000256|RuleBase:RU004203}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203, ECO:0000256|SAAS:SAAS00551005}.\nSIMILARITY: Belongs to the peptidase T1B family. {ECO:0000256|RuleBase:RU004203}.", "primaryDomainId": "uniprot.A0A384NL22", "displayName": "A0A384NL22_HUMAN", "synonyms": "Proteasome subunit beta {ECO:0000256, RuleBase:RU004203}, 3.4.25.1 {ECO:0000256, RuleBase:RU004203}", "taxid": 9606, "geneName": "PSMB3", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A384NL22", "id": "uniprot.A0A384NL22", "value": "uniprot.A0A384NL22"}}, {"data": {"domainIds": "uniprot.P49720", "sequence": "MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD", "comments": "FUNCTION: 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). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.\nCATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.;   EC=3.4.25.1; Evidence={ECO:0000269|PubMed:27176742};\nSUBUNIT: 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. {ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187}.\nSUBUNIT: (Microbial infection) Interacts with HIV-1 TAT protein. {ECO:0000269|PubMed:14550573}.\nINTERACTION: Q9Y244:POMP; NbExp=3; IntAct=EBI-603340, EBI-696895; O14818:PSMA7; NbExp=3; IntAct=EBI-603340, EBI-603272; P20618:PSMB1; NbExp=3; IntAct=EBI-603340, EBI-372273; P40306:PSMB10; NbExp=3; IntAct=EBI-603340, EBI-603329; P49721:PSMB2; NbExp=5; IntAct=EBI-603340, EBI-359335; P28074:PSMB5; NbExp=3; IntAct=EBI-603340, EBI-357828; P14373:TRIM27; NbExp=5; IntAct=EBI-603340, EBI-719493;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345}.\nINDUCTION: Up-regulated in asthenozoospermic sperm. {ECO:0000269|PubMed:18281682}.\nSIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- ProRule:PRU00809}.", "primaryDomainId": "uniprot.P49720", "displayName": "PSB3_HUMAN", "synonyms": "Proteasome subunit beta type-3, 3.4.25.1 {ECO:0000269, PubMed:27176742}, Proteasome chain 13, Proteasome component C10-II, Proteasome theta chain", "taxid": 9606, "geneName": "PSMB3", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P49720", "id": "uniprot.P49720", "value": "uniprot.P49720"}}, {"data": {"domainIds": "entrez.11047", "primaryDomainId": "entrez.11047", "geneType": "protein-coding", "displayName": "adhesion regulating molecule 1", "synonyms": "proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, M(r) 110,000 surface antigen, proteasome regulatory particle non-ATPase 13, rpn13 homolog", "chromosome": "20", "description": "adhesion regulating molecule 1", "approvedSymbol": "ADRM1", "type": "Gene", "symbols": "ARM-1, ARM1, GP110", "mapLocation": "20q13.33", "graphics": {"fill": "#FFB6C1"}, "name": "ADRM1", "id": "entrez.11047", "value": "entrez.11047"}}, {"data": {"domainIds": "uniprot.A0A087WX59", "sequence": "MTTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD", "primaryDomainId": "uniprot.A0A087WX59", "displayName": "A0A087WX59_HUMAN", "synonyms": "Proteasomal ubiquitin receptor ADRM1 {ECO:0000313, Ensembl:ENSP00000480756}", "taxid": 9606, "geneName": "ADRM1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A087WX59", "id": "uniprot.A0A087WX59", "value": "uniprot.A0A087WX59"}}, {"data": {"domainIds": "uniprot.Q16186", "sequence": "MTTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD", "comments": "FUNCTION: 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. Within the complex, functions as a proteasomal ubiquitin receptor. Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation. UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex. {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817, ECO:0000269|PubMed:24752541, ECO:0000269|PubMed:25702870, ECO:0000269|PubMed:25702872}.\nSUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP) (PubMed:16990800). Interacts with the proteasomal scaffolding protein PSMD1 (PubMed:16990800,PubMed:16815440, PubMed:16906146, PubMed:20471946). Interacts with deubiquitinase UCHL5; this interaction activates the auto-inhibited UCHL5 by deoligomerizing it (PubMed:17139257, PubMed:24752541, PubMed:25702870, PubMed:25702872). Interacts with UBQLN2 and ubiquitin (PubMed:27396824). {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817, ECO:0000269|PubMed:20471946, ECO:0000269|PubMed:24752541, ECO:0000269|PubMed:25702872, ECO:0000269|PubMed:27396824}.\nINTERACTION: P48510:DSK2 (xeno); NbExp=4; IntAct=EBI-954387, EBI-6174; O35593:Psmd14 (xeno); NbExp=2; IntAct=EBI-954387, EBI-772796; Q13200:PSMD2; NbExp=3; IntAct=EBI-954387, EBI-357648; P55036:PSMD4; NbExp=5; IntAct=EBI-954387, EBI-359318; P54727:RAD23B; NbExp=2; IntAct=EBI-954387, EBI-954531; P0CG48:UBC; NbExp=10; IntAct=EBI-954387, EBI-3390054; Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-954387, EBI-741480; Q9UHD9:UBQLN2; NbExp=5; IntAct=EBI-954387, EBI-947187; Q9Y5K5:UCHL5; NbExp=20; IntAct=EBI-954387, EBI-1051183; Q9Y5K5-3:UCHL5; NbExp=5; IntAct=EBI-954387, EBI-11749875;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16990800}. Nucleus {ECO:0000269|PubMed:16990800}.\nDOMAIN: The Pru (pleckstrin-like receptor for ubiquitin) domain mediates interactions with PSMD1 and ubiquitin. Preferential binding to the proximal subunit of K48-linked diubiquitin allows UCHL5 access to the distal subunit. {ECO:0000269|PubMed:18497817}.\nSIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.\nCAUTION: Although initially described as a cell membrane glycoprotein, ADRM1 is intracellular and non-glycosylated, and has probably no direct role in cell adhesion. {ECO:0000305}.", "primaryDomainId": "uniprot.Q16186", "displayName": "ADRM1_HUMAN", "synonyms": "Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog", "taxid": 9606, "geneName": "ADRM1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q16186", "id": "uniprot.Q16186", "value": "uniprot.Q16186"}}, {"data": {"domainIds": "entrez.26037", "primaryDomainId": "entrez.26037", "geneType": "protein-coding", "displayName": "signal induced proliferation associated 1 like 1", "synonyms": "signal-induced proliferation-associated 1-like protein 1, SIPA1-like protein 1, high-risk human papilloma viruses E6 oncoproteins targeted protein 1, spine-associated RapGAP 1", "chromosome": "14", "description": "signal induced proliferation associated 1 like 1", "approvedSymbol": "SIPA1L1", "type": "Gene", "symbols": "E6TP1, SPAR1", "mapLocation": "14q24.2", "graphics": {"fill": "#FFB6C1"}, "name": "SIPA1L1", "id": "entrez.26037", "value": "entrez.26037"}}, {"data": {"domainIds": "uniprot.O43166", "sequence": "MTSLKRSQTERPLATDRASVVGTDGTPKVHTDDFYMRRFRSQNGSLGSSVMAPVGPPRSEGSHHITSTPGVPKMGVRARIADWPPRKENIKESSRSSQEIETSSCLDSLSSKSSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTRPSENMDSRFLMPEAYPSSPRKALRRIRQRSNSDITISELDVDSFDECISPTYKTGPSLHREYGSTSSIDKQGTSGESFFDLLKGYKDDKSDRGPTPTKLSDFLITGGGKGSGFSLDVIDGPISQRENLRLFKEREKPLKRRSKSETGDSSIFRKLRNAKGEELGKSSDLEDNRSEDSVRPWTCPKCFAHYDVQSILFDLNEAIMNRHNVIKRRNTTTGASAAAVASLVSGPLSHSASFSSPMGSTEDLNSKGSLSMDQGDDKSNELVMSCPYFRNEIGGEGERKISLSKSNSGSFSGCESASFESTLSSHCTNAGVAVLEVPKENLVLHLDRVKRYIVEHVDLGAYYYRKFFYQKEHWNYFGADENLGPVAVSIRREKPDEMKENGSPYNYRIIFRTSELMTLRGSVLEDAIPSTAKHSTARGLPLKEVLEHVVPELNVQCLRLAFNTPKVTEQLMKLDEQGLNYQQKVGIMYCKAGQSTEEEMYNNESAGPAFEEFLQLLGERVRLKGFEKYRAQLDTKTDSTGTHSLYTTYKDYEIMFHVSTMLPYTPNNKQQLLRKRHIGNDIVTIVFQEPGAQPFSPKNIRSHFQHVFVIVRVHNPCSDSVCYSVAVTRSRDVPSFGPPIPKGVTFPKSNVFRDFLLAKVINAENAAHKSEKFRAMATRTRQEYLKDLAEKNVTNTPIDPSGKFPFISLASKKKEKSKPYPGAELSSMGAIVWAVRAEDYNKAMELDCLLGISNEFIVLIEQETKSVVFNCSCRDVIGWTSTDTSLKIFYERGECVSVGSFINIEEIKEIVKRLQFVSKGCESVEMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVIIPPHDDCTPRRSCSETYRMPVMEYKMNEGVSYEFKFPFRNNNKWQRNASKGPHSPQVPSQVQSPMTSRLNAGKGDGKMPPPERAANIPRSISSDGRPLERRLSPGSDIYVTVSSMALARSQCRNSPSNLSSSSDTGSVGGTYRQKSMPEGFGVSRRSPASIDRQNTQSDIGGSGKSTPSWQRSEDSIADQMAYSYRGPQDFNSFVLEQHEYTEPTCHLPAVSKVLPAFRESPSGRLMRQDPVVHLSPNKQGHSDSHYSSHSSSNTLSSNASSAHSDEKWYDGDRTESELNSYNYLQGTSADSGIDTTSYGPSHGSTASLGAATSSPRSGPGKEKVAPLWHSSSEVISMADRTLETESHGLDRKTESSLSLDIHSKSQAGSTPLTRENSTFSINDAASHTSTMSSRHSASPVVFTSARSSPKEELHPAAPSQLAPSFSSSSSSSSGPRSFYPRQGATSKYLIGWKKPEGTINSVGFMDTRKRHQSDGNEIAHTRLRASTRDLRASPKPTSKSTIEEDLKKLIDLESPTPESQKSFKFHALSSPQSPFPSTPTSRRALHRTLSDESIYNSQREHFFTSRASLLDQALPNDVLFSSTYPSLPKSLPLRRPSYTLGMKSLHGEFSASDSSLTDIQETRRQPMPDPGLMPLPDTAADLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEDQALAQMKPYSSSKDSSPTLASKVDQLEGMLKMLREDLKKEKEDKAHLQAEVQHLREDNLRLQEESQNASDKLKKFTEWVFNTIDMS", "comments": "FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.\nSUBUNIT: Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with the actin cytoskeleton (By similarity). Interacts (via PDZ domain) with EPHA4 (via PDZ motif); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Interacts with HPV E6. {ECO:0000250, ECO:0000269|PubMed:18094260, ECO:0000269|PubMed:9858596}.\nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, synapse, postsynaptic density {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons (By similarity). {ECO:0000250}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=E6TP1 beta;   IsoId=O43166-1; Sequence=Displayed; Name=2; Synonyms=E6TP1 alpha;   IsoId=O43166-2; Sequence=VSP_010917; Name=3;   IsoId=O43166-3; Sequence=VSP_010917, VSP_054774;\nTISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9858596}.\nPTM: Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2. {ECO:0000250}.\nPTM: Phosphorylated at Ser-1349 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}.\nSEQUENCE CAUTION: Sequence=BAA23712.2; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.O43166", "displayName": "SI1L1_HUMAN", "synonyms": "Signal-induced proliferation-associated 1-like protein 1, SIPA1-like protein 1, High-risk human papilloma viruses E6 oncoproteins targeted protein 1, E6-targeted protein 1", "taxid": 9606, "geneName": "SIPA1L1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "O43166", "id": "uniprot.O43166", "value": "uniprot.O43166"}}, {"data": {"domainIds": "entrez.51474", "primaryDomainId": "entrez.51474", "geneType": "protein-coding", "displayName": "LIM domain and actin binding 1", "synonyms": "LIM domain and actin-binding protein 1, 1110021C24Rik, epithelial protein lost in neoplasm beta, sterol regulatory element binding protein 3", "chromosome": "12", "description": "LIM domain and actin binding 1", "approvedSymbol": "LIMA1", "type": "Gene", "symbols": "EPLIN, LDLCQ8, SREBP3", "mapLocation": "12q13.12", "graphics": {"fill": "#FFB6C1"}, "name": "LIMA1", "id": "entrez.51474", "value": "entrez.51474"}}, {"data": {"domainIds": "uniprot.Q9UHB6", "sequence": "MESSPFNRRQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEETNMEKKRSNTENLSQHFRKGTLTVLKKKWENPGLGAESHTDSLRNSSTEIRHRADHPPAEVTSHAASGAKADQEEQIHPRSRLRSPPEALVQGRYPHIKDGEDLKDHSTESKKMENCLGESRHEVEKSEISENTDASGKIEKYNVPLNRLKMMFEKGEPTQTKILRAQSRSASGRKISENSYSLDDLEIGPGQLSSSTFDSEKNESRRNLELPRLSETSIKDRMAKYQAAVSKQSSSTNYTNELKASGGEIKIHKMEQKENVPPGPEVCITHQEGEKISANENSLAVRSTPAEDDSRDSQVKSEVQQPVHPKPLSPDSRASSLSESSPPKAMKKFQAPARETCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHRPHKDLWASKNENEEILERPAQLANARETPHSPGVEDAPIAKVGVLAASMEAKASSQQEKEDKPAETKKLRIAWPPPTELGSSGSALEEGIKMSKPKWPPEDEISKPEVPEDVDLDLKKLRRSSSLKERSRPFTVAASFQSTSVKSPKTVSPPIRKGWSMSEQSEESVGGRVAERKQVENAKASKKNGNVGKTTWQNKESKGETGKRSKEGHSLEMENENLVENGADSDEDDNSFLKQQSPQEPKSLNWSSFVDNTFAEEFTTQNQKSQDVELWEGEVVKELSVEEQIKRNRYYDEDEDEE", "comments": "FUNCTION: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000269|PubMed:12566430}.\nSUBUNIT: Interacts with NPCL1; bridges NPC1L1 with MYO5B (PubMed:29880681). Interacts with MYO5B; bridges NPC1L1 with MYO5B (PubMed:29880681). Interacts with PXN; this complex stabilizes actin dynamics (PubMed:24694988). Interacts with F-actin and G-actin (PubMed:12566430). {ECO:0000269|PubMed:12566430, ECO:0000269|PubMed:24694988, ECO:0000269|PubMed:29880681}.\nINTERACTION: P12830:CDH1; NbExp=2; IntAct=EBI-351479, EBI-727477; P35221:CTNNA1; NbExp=2; IntAct=EBI-351479, EBI-701918; O46385:SVIL (xeno); NbExp=3; IntAct=EBI-351479, EBI-6995105;\nSUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion {ECO:0000269|PubMed:10618726, ECO:0000269|PubMed:24694988}. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:10618726}. Cell membrane {ECO:0000250|UniProtKB:Q9ERG0}. Note=Expressed in the brush border membrane of the small intestine and colocalizes with NPC1L1 and MYO5B (PubMed:29880681). Colocalizes with PXN at focal adhesions in mesangial cells (PubMed:24694988). Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (By similarity). {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000269|PubMed:24694988, ECO:0000269|PubMed:29880681}.\nALTERNATIVE PRODUCTS: Event=Alternative promoter usage, Alternative splicing; Named isoforms=5; Name=Beta;   IsoId=Q9UHB6-1; Sequence=Displayed; Name=Alpha;   IsoId=Q9UHB6-2; Sequence=VSP_003116; Name=3;   IsoId=Q9UHB6-3; Sequence=VSP_003117; Name=4;   IsoId=Q9UHB6-4; Sequence=VSP_040136; Name=5;   IsoId=Q9UHB6-5; Sequence=VSP_003116, VSP_040136;\nTISSUE SPECIFICITY: Highly expressed in placenta, kidney, pancreas, prostate, ovary, spleen and heart. Also detected in lung, liver, brain, skeletal muscle, thymus, testis and intestine. Not detected in leukocytes. Isoform Beta expressed generally at very low levels. Isoform Alpha abundant in epithelial cells from mammary gland, prostate and in normal oral keratinocytes. Low levels in aortic endothelial cells and dermal fibroblasts. Not detectable in myocardium. {ECO:0000269|PubMed:24694988}.\nINDUCTION: Down-regulated in some cancer cell lines. Isoform Alpha is induced by serum. Isoform Beta is constitutively expressed. {ECO:0000269|PubMed:10806352}.\nDOMAIN: Contains at least 2 actin-binding domains, one on each side of the LIM domain. Both domains bind actin monomers and filaments. The C- terminal domain binds filaments more efficiently than the N-terminus. {ECO:0000269|PubMed:12566430}.\nPTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces its association with F-actin and contributes to actin filament reorganization and enhances cell motility. {ECO:0000250|UniProtKB:Q9ERG0}.\nPOLYMORPHISM: Genetic variations in LIMA1 influence low density lipoprotein cholesterol (LDL-C) variability and contribute to the low density lipoprotein cholesterol level quantitative trait locus 8 (LDLCQ8) [MIM:618079]. {ECO:0000269|PubMed:29880681}.\nMISCELLANEOUS: [Isoform Beta]: Produced by alternative promoter usage.\nMISCELLANEOUS: [Isoform Alpha]: Produced by alternative promoter usage. {ECO:0000305}.\nMISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform Beta. {ECO:0000305}.\nMISCELLANEOUS: [Isoform 4]: Produced by alternative splicing. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAG17267.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAA91120.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAD92749.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9UHB6", "displayName": "LIMA1_HUMAN", "synonyms": "LIM domain and actin-binding protein 1, Epithelial protein lost in neoplasm", "taxid": 9606, "geneName": "LIMA1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9UHB6", "id": "uniprot.Q9UHB6", "value": "uniprot.Q9UHB6"}}, {"data": {"domainIds": "entrez.5685", "primaryDomainId": "entrez.5685", "geneType": "protein-coding", "displayName": "proteasome 20S subunit alpha 4", "synonyms": "proteasome subunit alpha type-4, macropain subunit C9, multicatalytic endopeptidase complex subunit C9, proteasome (prosome, macropain) subunit, alpha type, 4, proteasome component C9, proteasome subunit HC9, proteasome subunit L, proteasome subunit alpha 4, proteasome subunit alpha3", "chromosome": "15", "description": "proteasome 20S subunit alpha 4", "approvedSymbol": "PSMA4", "type": "Gene", "symbols": "HC9, HsT17706, PSC9", "mapLocation": "15q25.1", "graphics": {"fill": "#FFB6C1"}, "name": "PSMA4", "id": "entrez.5685", "value": "entrez.5685"}}, {"data": {"domainIds": "uniprot.H0YN18", "sequence": "MSRRYDSRTTIFSPEAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK", "comments": "CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.;   EC=3.4.25.1; Evidence={ECO:0000256|PROSITE-ProRule:PRU00808};\nSIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE- ProRule:PRU00808}.", "primaryDomainId": "uniprot.H0YN18", "displayName": "H0YN18_HUMAN", "synonyms": "Proteasome endopeptidase complex {ECO:0000256, PROSITE-ProRule:PRU00808}, 3.4.25.1 {ECO:0000256, PROSITE-ProRule:PRU00808}", "taxid": 9606, "geneName": "PSMA4", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "H0YN18", "id": "uniprot.H0YN18", "value": "uniprot.H0YN18"}}, {"data": {"domainIds": "uniprot.H0YLC2", "sequence": "MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAWKLQH", "comments": "CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.;   EC=3.4.25.1; Evidence={ECO:0000256|PROSITE-ProRule:PRU00808,   ECO:0000256|RuleBase:RU000551};\nSUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. {ECO:0000256|RuleBase:RU000551}.\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551, ECO:0000256|SAAS:SAAS00594407}.\nSIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE- ProRule:PRU00808, ECO:0000256|RuleBase:RU000551}.", "primaryDomainId": "uniprot.H0YLC2", "displayName": "H0YLC2_HUMAN", "synonyms": "Proteasome subunit alpha type {ECO:0000256, RuleBase:RU000551}, 3.4.25.1 {ECO:0000256, RuleBase:RU000551}", "taxid": 9606, "geneName": "PSMA4", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "H0YLC2", "id": "uniprot.H0YLC2", "value": "uniprot.H0YLC2"}}, {"data": {"domainIds": "uniprot.P25789", "sequence": "MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK", "comments": "FUNCTION: 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). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.\nCATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.;   EC=3.4.25.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00808,   ECO:0000269|PubMed:27176742};\nSUBUNIT: 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. {ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187}.\nSUBUNIT: (Microbial infection) Interaction with HTLV-1 TAX protein favors NFKB1 activation. {ECO:0000269|PubMed:8692272}.\nINTERACTION: Q99PV5:Bhlhe41 (xeno); NbExp=2; IntAct=EBI-359310, EBI-6143801; Q08379:GOLGA2; NbExp=3; IntAct=EBI-359310, EBI-618309; Q16665:HIF1A; NbExp=4; IntAct=EBI-359310, EBI-447269; Q13422:IKZF1; NbExp=3; IntAct=EBI-359310, EBI-745305; P25786:PSMA1; NbExp=7; IntAct=EBI-359310, EBI-359352; P25787:PSMA2; NbExp=7; IntAct=EBI-359310, EBI-603262; P25788:PSMA3; NbExp=4; IntAct=EBI-359310, EBI-348380; P60900:PSMA6; NbExp=5; IntAct=EBI-359310, EBI-357793; O14818:PSMA7; NbExp=10; IntAct=EBI-359310, EBI-603272;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345}. Note=Colocalizes with TRIM5 in the cytoplasmic bodies. {ECO:0000250|UniProtKB:Q9R1P0}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=P25789-1; Sequence=Displayed; Name=2;   IsoId=P25789-2; Sequence=VSP_043102;\nINDUCTION: Down-regulated by antioxidants BO-653 and probucol. {ECO:0000269|PubMed:11521686}.\nSIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE- ProRule:PRU00808}.", "primaryDomainId": "uniprot.P25789", "displayName": "PSA4_HUMAN", "synonyms": "Proteasome subunit alpha type-4, 3.4.25.1 {ECO:0000269, PubMed:27176742}, Macropain subunit C9, Multicatalytic endopeptidase complex subunit C9, Proteasome component C9, Proteasome subunit L", "taxid": 9606, "geneName": "PSMA4", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P25789", "id": "uniprot.P25789", "value": "uniprot.P25789"}}, {"data": {"domainIds": "entrez.3845", "primaryDomainId": "entrez.3845", "geneType": "protein-coding", "displayName": "KRAS proto-oncogene, GTPase", "synonyms": "GTPase KRas, K-ras p21 protein, Kirsten rat sarcoma viral oncogene homolog, Kirsten rat sarcoma viral proto-oncogene, PR310 c-K-ras oncogene, c-Kirsten-ras protein, cellular c-Ki-ras2 proto-oncogene, cellular transforming proto-oncogene, oncogene KRAS2, transforming protein p21, v-Ki-ras2 Kirsten rat sarcoma 2 viral oncogene homolog", "chromosome": "12", "description": "KRAS proto-oncogene, GTPase", "approvedSymbol": "KRAS", "type": "Gene", "symbols": "'C-K-RAS, C-K-RAS, CFC2, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, K-Ras, K-Ras 2, KI-RAS, KRAS1, KRAS2, NS, NS3, OES, RALD, RASK2, c-Ki-ras, c-Ki-ras2", "mapLocation": "12p12.1", "graphics": {"fill": "#FFB6C1"}, "name": "KRAS", "id": "entrez.3845", "value": "entrez.3845"}}, {"data": {"domainIds": "uniprot.A0A024RAV5", "sequence": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEKMSKDGKKKKKKSKTKCVIM", "primaryDomainId": "uniprot.A0A024RAV5", "displayName": "A0A024RAV5_HUMAN", "synonyms": "V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog, isoform CRA_b {ECO:0000313, EMBL:EAW96513.1}", "taxid": 9606, "geneName": "KRAS", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "A0A024RAV5", "id": "uniprot.A0A024RAV5", "value": "uniprot.A0A024RAV5"}}, {"data": {"domainIds": "uniprot.I1SRC5", "sequence": "MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQGLLKMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM", "comments": "SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. {ECO:0000256|RuleBase:RU362109, ECO:0000256|SAAS:SAAS00805669}.", "primaryDomainId": "uniprot.I1SRC5", "displayName": "I1SRC5_HUMAN", "synonyms": "UBE2L3/KRAS fusion protein {ECO:0000313, EMBL:AEA35014.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "I1SRC5", "id": "uniprot.I1SRC5", "value": "uniprot.I1SRC5"}}, {"data": {"domainIds": "uniprot.L7RSL8", "sequence": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM", "primaryDomainId": "uniprot.L7RSL8", "displayName": "L7RSL8_HUMAN", "synonyms": "V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog {ECO:0000313, EMBL:AGC09594.1}, V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog, isoform CRA_a {ECO:0000313, EMBL:EAW96514.1}", "taxid": 9606, "geneName": "KRAS", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "L7RSL8", "id": "uniprot.L7RSL8", "value": "uniprot.L7RSL8"}}, {"data": {"domainIds": "uniprot.P01116", "sequence": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM", "comments": "FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation (PubMed:23698361, PubMed:22711838). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (PubMed:24623306). {ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24623306, ECO:0000305}.\nACTIVITY REGULATION: 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). Interaction with SOS1 promotes exchange of bound GDP by GTP. {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:22566140, ECO:0000269|PubMed:22711838}.\nSUBUNIT: Interacts with PHLPP. Interacts (active GTP-bound form preferentially) with RGS14 (By similarity). Interacts (when farnesylated) with PDE6D; this promotes dissociation from the cell membrane (PubMed:23698361). Interacts with SOS1 (PubMed:22431598). {ECO:0000250|UniProtKB:P08644, ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361}.\nINTERACTION: Q96II5:ARAF; NbExp=3; IntAct=EBI-367415, EBI-9383168; Q04631:Fnta (xeno); NbExp=3; IntAct=EBI-367427, EBI-602447; P04049:RAF1; NbExp=3; IntAct=EBI-367427, EBI-365996; P50749:RASSF2; NbExp=2; IntAct=EBI-367415, EBI-960081;\nSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361}; Lipid-anchor {ECO:0000305|PubMed:23698361}; Cytoplasmic side {ECO:0000305|PubMed:23698361}. Cytoplasm, cytosol {ECO:0000269|PubMed:23698361}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2;   Comment=Isoforms differ in the C-terminal region which is encoded by   two alternative exons (IVA and IVB).; Name=2A; Synonyms=K-Ras4A;   IsoId=P01116-1; Sequence=Displayed; Name=2B; Synonyms=K-Ras4B;   IsoId=P01116-2, P01118-1;   Sequence=VSP_011140, VSP_011141;\nPTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000269|PubMed:22711838, ECO:0000269|Ref.17}.\nPTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000305|PubMed:30442762, ECO:0000305|PubMed:30442766}.\nDISEASE: 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. {ECO:0000269|PubMed:8955068}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:17332249}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Noonan syndrome 3 (NS3) [MIM:609942]: 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. {ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:16773572, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:17468812, ECO:0000269|PubMed:19396835, ECO:0000269|PubMed:20949621}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:7773929}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Note=Defects in KRAS are a cause of pylocytic astrocytoma (PA). Pylocytic astrocytomas are neoplasms of the brain and spinal cord derived from glial cells which vary from histologically benign forms to highly anaplastic and malignant tumors. {ECO:0000269|PubMed:16247081}.\nDISEASE: Cardiofaciocutaneous syndrome 2 (CFC2) [MIM:615278]: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis- like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. CFC2 patients often do not have the skin abnormalities, such as ichthyosis, hyperkeratosis, and hemangioma observed in CFC1. {ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:21797849}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nDISEASE: Note=KRAS mutations are involved in cancer development. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:1553789, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:3627975, ECO:0000269|PubMed:6092920, ECO:0000269|PubMed:6695174, ECO:0000269|PubMed:7773929}.\nSIMILARITY: Belongs to the small GTPase superfamily. Ras family. {ECO:0000305}.\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/KRASID91.html\";\nWEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL=\"http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=KRAS\";", "primaryDomainId": "uniprot.P01116", "displayName": "RASK_HUMAN", "synonyms": "GTPase KRas, K-Ras 2, Ki-Ras, c-K-ras, c-Ki-ras", "taxid": 9606, "geneName": "KRAS", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P01116", "id": "uniprot.P01116", "value": "uniprot.P01116"}}, {"data": {"domainIds": "entrez.994", "primaryDomainId": "entrez.994", "geneType": "protein-coding", "displayName": "cell division cycle 25B", "synonyms": "M-phase inducer phosphatase 2, dual specificity phosphatase Cdc25B", "chromosome": "20", "description": "cell division cycle 25B", "approvedSymbol": "CDC25B", "type": "Gene", "symbols": "-", "mapLocation": "20p13", "graphics": {"fill": "#FFB6C1"}, "name": "CDC25B", "id": "entrez.994", "value": "entrez.994"}}, {"data": {"domainIds": "uniprot.B4DRC3", "sequence": "MHSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "primaryDomainId": "uniprot.B4DRC3", "displayName": "B4DRC3_HUMAN", "synonyms": "cDNA FLJ56140, highly similar to M-phase inducer phosphatase 2 {ECO:0000313, EMBL:BAG61235.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DRC3", "id": "uniprot.B4DRC3", "value": "uniprot.B4DRC3"}}, {"data": {"domainIds": "uniprot.E1YMX4", "sequence": "MDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "primaryDomainId": "uniprot.E1YMX4", "displayName": "E1YMX4_HUMAN", "synonyms": "Isoform CDC25B7 {ECO:0000313, EMBL:CBX26629.1}, 3.1.3.48 {ECO:0000313, EMBL:CBX26629.1}", "taxid": 9606, "geneName": "CDC25B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "E1YMX4", "id": "uniprot.E1YMX4", "value": "uniprot.E1YMX4"}}, {"data": {"domainIds": "uniprot.G8JLH2", "sequence": "MHSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "primaryDomainId": "uniprot.G8JLH2", "displayName": "G8JLH2_HUMAN", "synonyms": "M-phase inducer phosphatase 2 {ECO:0000313, Ensembl:ENSP00000368918}", "taxid": 9606, "geneName": "CDC25B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "G8JLH2", "id": "uniprot.G8JLH2", "value": "uniprot.G8JLH2"}}, {"data": {"domainIds": "uniprot.B4DQZ3", "sequence": "MHSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGRFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMDHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "primaryDomainId": "uniprot.B4DQZ3", "displayName": "B4DQZ3_HUMAN", "synonyms": "cDNA FLJ55479, highly similar to M-phase inducer phosphatase 2 {ECO:0000313, EMBL:BAG61105.1}", "taxid": 9606, "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DQZ3", "id": "uniprot.B4DQZ3", "value": "uniprot.B4DQZ3"}}, {"data": {"domainIds": "uniprot.Q6MZW8", "sequence": "FEQAIQAASRIIRNEQFAIRRFQSMPDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPDMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "primaryDomainId": "uniprot.Q6MZW8", "displayName": "Q6MZW8_HUMAN", "synonyms": "Uncharacterized protein DKFZp686G14213 {ECO:0000313, EMBL:CAE45909.2}", "taxid": 9606, "geneName": "DKFZp686G14213", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q6MZW8", "id": "uniprot.Q6MZW8", "value": "uniprot.Q6MZW8"}}, {"data": {"domainIds": "uniprot.B3KS38", "sequence": "MDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "primaryDomainId": "uniprot.B3KS38", "displayName": "B3KS38_HUMAN", "synonyms": "HCG39252, isoform CRA_g {ECO:0000313, EMBL:EAX10500.1}, Isoform CDC25B6 {ECO:0000313, EMBL:CBX26628.1}, 3.1.3.48 {ECO:0000313, EMBL:CBX26628.1}, cDNA FLJ35394 fis, clone SKNSH2002768, highly similar to M-PHASE INDUCER PHOSPHATASE 2 {ECO:0000313, EMBL:BAG52600.1}", "taxid": 9606, "geneName": "CDC25B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B3KS38", "id": "uniprot.B3KS38", "value": "uniprot.B3KS38"}}, {"data": {"domainIds": "uniprot.B4DIG0", "sequence": "MHSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "primaryDomainId": "uniprot.B4DIG0", "displayName": "B4DIG0_HUMAN", "synonyms": "M-phase inducer phosphatase 2 {ECO:0000313, Ensembl:ENSP00000339125}, cDNA FLJ53333, highly similar to M-phase inducer phosphatase 2 {ECO:0000313, EMBL:BAG58472.1}", "taxid": 9606, "geneName": "CDC25B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "B4DIG0", "id": "uniprot.B4DIG0", "value": "uniprot.B4DIG0"}}, {"data": {"domainIds": "uniprot.P30305", "sequence": "MEVPQPEPAPGSALSPAGVCGGAQRPGHLPGLLLGSHGLLGSPVRAAASSPVTTLTQTMHDLAGLGSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ", "comments": "FUNCTION: Tyrosine protein phosphatase which functions as a dosage- dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2- dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity. {ECO:0000269|PubMed:17332740}.\nCATALYTIC ACTIVITY: 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;\nACTIVITY REGULATION: Stimulated by B-type cyclins.\nSUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. {ECO:0000269|PubMed:11333986}.\nINTERACTION: P31946:YWHAB; NbExp=5; IntAct=EBI-1051746, EBI-359815; P61981:YWHAG; NbExp=3; IntAct=EBI-1051746, EBI-359832; Q04917:YWHAH; NbExp=5; IntAct=EBI-1051746, EBI-306940; P63104:YWHAZ; NbExp=7; IntAct=EBI-1051746, EBI-347088;\nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15908796}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15908796}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=3; Synonyms=CDC25B3;   IsoId=P30305-1; Sequence=Displayed; Name=1; Synonyms=CDC25B1;   IsoId=P30305-2; Sequence=VSP_000861; Name=2; Synonyms=CDC25B2;   IsoId=P30305-3; Sequence=VSP_000862; Name=4;   IsoId=P30305-4; Sequence=VSP_000861, VSP_012587;\nPTM: Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-353 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-169 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-323 and Ser-375 by MAPK14 is required for binding to 14-3-3 proteins. {ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:12400006, ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:17332740}.\nSIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.\nWEB RESOURCE: Name=NIEHS-SNPs; URL=\"http://egp.gs.washington.edu/data/cdc25b/\";", "primaryDomainId": "uniprot.P30305", "displayName": "MPIP2_HUMAN", "synonyms": "M-phase inducer phosphatase 2, 3.1.3.48, Dual specificity phosphatase Cdc25B", "taxid": 9606, "geneName": "CDC25B", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P30305", "id": "uniprot.P30305", "value": "uniprot.P30305"}}, {"data": {"domainIds": "entrez.26058", "primaryDomainId": "entrez.26058", "geneType": "protein-coding", "displayName": "GRB10 interacting GYF protein 2", "synonyms": "GRB10-interacting GYF protein 2, PERQ amino acid rich, with GYF domain 3, PERQ amino acid-rich with GYF domain-containing protein 2, Parkinson disease (autosomal recessive, early onset) 11, trinucleotide repeat-containing gene 15 protein", "chromosome": "2", "description": "GRB10 interacting GYF protein 2", "approvedSymbol": "GIGYF2", "type": "Gene", "symbols": "GYF2, PARK11, PERQ2, PERQ3, TNRC15", "mapLocation": "2q37.1", "graphics": {"fill": "#FFB6C1"}, "name": "GIGYF2", "id": "entrez.26058", "value": "entrez.26058"}}, {"data": {"domainIds": "uniprot.Q6Y7W6", "sequence": "MAAETQTLNFGPEWLRALSSGGSITSPPLSPALPKYKLADYRYGREEMLALFLKDNKIPSDLLDKEFLPILQEEPLPPLALVPFTEEEQRNFSMSVNSAAVLRLTGRGGGGTVVGAPRGRSSSRGRGRGRGECGFYQRSFDEVEGVFGRGGGREMHRSQSWEERGDRRFEKPGRKDVGRPNFEEGGPTSVGRKHEFIRSESENWRIFREEQNGEDEDGGWRLAGSRRDGERWRPHSPDGPRSAGWREHMERRRRFEFDFRDRDDERGYRRVRSGSGSIDDDRDSLPEWCLEDAEEEMGTFDSSGAFLSLKKVQKEPIPEEQEMDFRPVDEGEECSDSEGSHNEEAKEPDKTNKKEGEKTDRVGVEASEETPQTSSSSARPGTPSDHQSQEASQFERKDEPKTEQTEKAEEETRMENSLPAKVPSRGDEMVADVQQPLSQIPSDTASPLLILPPPVPNPSPTLRPVETPVVGAPGMGSVSTEPDDEEGLKHLEQQAEKMVAYLQDSALDDERLASKLQEHRAKGVSIPLMHEAMQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGRVPFSPGPAPPPHMGELDQERLTRQQELTALYQMQHLQYQQFLIQQQYAQVLAQQQKAALSSQQQQQLALLLQQFQTLKMRISDQNIIPSVTRSVSVPDTGSIWELQPTASQPTVWEGGSVWDLPLDTTTPGPALEQLQQLEKAKAAKLEQERREAEMRAKREEEERKRQEELRRQQEEILRRQQEEERKRREEEELARRKQEEALRRQREQEIALRRQREEEERQQQEEALRRLEERRREEEERRKQEELLRKQEEEAAKWAREEEEAQRRLEENRLRMEEEAARLRHEEEERKRKELEVQRQKELMRQRQQQQEALRRLQQQQQQQQLAQMKLPSSSTWGQQSNTTACQSQATLSLAEIQKLEEERERQLREEQRRQQRELMKALQQQQQQQQQKLSGWGNVSKPSGTTKSLLEIQQEEARQMQKQQQQQQQHQQPNRARNNTHSNLHTSIGNSVWGSINTGPPNQWASDLVSSIWSNADTKNSNMGFWDDAVKEVGPRNSTNKNKNNASLSKSVGVSNRQNKKVEEEEKLLKLFQGVNKAQDGFTQWCEQMLHALNTANNLDVPTFVSFLKEVESPYEVHDYIRAYLGDTSEAKEFAKQFLERRAKQKANQQRQQQQLPQQQQQQPPQQPPQQPQQQDSVWGMNHSTLHSVFQTNQSNNQQSNFEAVQSGKKKKKQKMVRADPSLLGFSVNASSERLNMGEIETLDDY", "comments": "FUNCTION: Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931). In 4EHP-GYF2 the complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (By similarity). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153). {ECO:0000250|UniProtKB:Q6Y7W8, ECO:0000269|PubMed:12771153, ECO:0000269|PubMed:22751931}.\nSUBUNIT: Component of the 4EHP-GYF2 complex, at least composed of EIF4E2, GIGYF2 and ZNF598 (PubMed:22751931). Interacts (via the 4EHP- binding motif) with EIF4E2; the interaction is direct (PubMed:22751931). Interacts with ZFP36/TTP (via P-P-P-P-G repeats); the interaction is direct (By similarity). Interacts with GRB10 (By similarity). {ECO:0000250|UniProtKB:Q6Y7W8, ECO:0000269|PubMed:22751931}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=1;   IsoId=Q6Y7W6-1; Sequence=Displayed; Name=2;   IsoId=Q6Y7W6-3; Sequence=VSP_022244, VSP_043471; Name=3;   IsoId=Q6Y7W6-4; Sequence=VSP_044996, VSP_044997; Name=4;   IsoId=Q6Y7W6-5; Sequence=VSP_044996;\nDISEASE: Parkinson disease 11 (PARK11) [MIM:607688]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology 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. {ECO:0000269|PubMed:18358451, ECO:0000269|PubMed:20060621, ECO:0000269|PubMed:20178831, ECO:0000269|PubMed:26134514}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry. Its association with Parkinson disease is however unclear. According to a number of studies, variations affecting this gene are not a frequent cause of Parkinson disease, suggesting that GIGYF2 does not play a major role in Parkinson disease etiology (PubMed:19279319, PubMed:19429085, PubMed:19638301, PubMed:19482505, PubMed:20004041, PubMed:19321232, PubMed:20060621). {ECO:0000269|PubMed:19279319, ECO:0000269|PubMed:19321232, ECO:0000269|PubMed:19429085, ECO:0000269|PubMed:19482505, ECO:0000269|PubMed:19638301, ECO:0000269|PubMed:20004041, ECO:0000269|PubMed:20060621}.\nSIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=BAA31617.2; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAA91873.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q6Y7W6", "displayName": "GGYF2_HUMAN", "synonyms": "GRB10-interacting GYF protein 2 {ECO:0000303, PubMed:12771153}, PERQ amino acid-rich with GYF domain-containing protein 2, Trinucleotide repeat-containing gene 15 protein {ECO:0000303, PubMed:18358451}", "taxid": 9606, "geneName": "GIGYF2", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q6Y7W6", "id": "uniprot.Q6Y7W6", "value": "uniprot.Q6Y7W6"}}, {"data": {"domainIds": "entrez.9759", "primaryDomainId": "entrez.9759", "geneType": "protein-coding", "displayName": "histone deacetylase 4", "synonyms": "histone deacetylase 4, histone deacetylase A", "chromosome": "2", "description": "histone deacetylase 4", "approvedSymbol": "HDAC4", "type": "Gene", "symbols": "AHO3, BDMR, HA6116, HD4, HDAC-4, HDAC-A, HDACA", "mapLocation": "2q37.3", "graphics": {"fill": "#FFB6C1"}, "name": "HDAC4", "id": "entrez.9759", "value": "entrez.9759"}}, {"data": {"domainIds": "uniprot.P56524", "sequence": "MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL", "comments": "FUNCTION: 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 via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1 (PubMed:27708256). {ECO:0000269|PubMed:10523670, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:27708256}.\nCATALYTIC ACTIVITY: 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;\nSUBUNIT: Homodimer. Homodimerization via its N-terminal domain (PubMed:12032081). Interacts with MEF2A (PubMed:10487761). Interacts with MEF2C and MEF2D (PubMed:10523670). Interacts with AHRR (By similarity). Interacts with NR2C1 (PubMed:11463856). Interacts with HDAC7 (By similarity). Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner (PubMed:10958686). Interacts with BTBD14B (By similarity). Interacts with KDM5B (PubMed:17373667). Interacts with MYOCD (By similarity). Interacts with MORC2 (PubMed:20110259). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats). Interacts with CUL7 (as part of the 3M complex); negatively regulated by ANKRA2 (PubMed:25752541). Interacts with EP300 in the presence of TFAP2C (PubMed:24413532). Interacts with HSPA1A and HSPA1B leading to their deacetylation at 'Lys-77' (PubMed:27708256). Interacts with ZBTB7B; the interaction allows the recruitment of HDAC4 on CD8 loci for deacetylation and possible inhibition of CD8 genes expression (By similarity). Interacts with DHX36 (By similarity). Interacts with SIK3; this interaction leads to HDAC4 retention in the cytoplasm (By similarity). Interacts with ZNF638 (PubMed:30487602). {ECO:0000250|UniProtKB:Q6NZM9, ECO:0000250|UniProtKB:Q99P99, ECO:0000269|PubMed:10487761, ECO:0000269|PubMed:10523670, ECO:0000269|PubMed:10958686, ECO:0000269|PubMed:11463856, ECO:0000269|PubMed:17373667, ECO:0000269|PubMed:20110259, ECO:0000269|PubMed:22649097, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:25752541, ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:30487602}.\nINTERACTION: Self; NbExp=4; IntAct=EBI-308629, EBI-308629; Q9H9E1:ANKRA2; NbExp=3; IntAct=EBI-308629, EBI-10215533; P10275:AR; NbExp=4; IntAct=EBI-308629, EBI-608057; P15336:ATF2; NbExp=2; IntAct=EBI-308629, EBI-1170906; P41182:BCL6; NbExp=3; IntAct=EBI-308629, EBI-765407; Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-308629, EBI-714781; Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-308629, EBI-10171416; Q01850:CDR2; NbExp=3; IntAct=EBI-308629, EBI-1181367; O54946-2:Dnajb6 (xeno); NbExp=2; IntAct=EBI-308629, EBI-13941040; Q8AZK7:EBNA-LP (xeno); NbExp=5; IntAct=EBI-308629, EBI-1185167; O95967:EFEMP2; NbExp=3; IntAct=EBI-308629, EBI-743414; Q08379:GOLGA2; NbExp=3; IntAct=EBI-308629, EBI-618309; P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-308629, EBI-6148881; Q15323:KRT31; NbExp=3; IntAct=EBI-308629, EBI-948001; O76015:KRT38; NbExp=3; IntAct=EBI-308629, EBI-1047263; Q6A162:KRT40; NbExp=3; IntAct=EBI-308629, EBI-10171697; O95751:LDOC1; NbExp=3; IntAct=EBI-308629, EBI-740738; A9UHW6:MIF4GD; NbExp=4; IntAct=EBI-308629, EBI-373498; Q5JR59:MTUS2; NbExp=3; IntAct=EBI-308629, EBI-742948; Q8ND90:PNMA1; NbExp=3; IntAct=EBI-308629, EBI-302345; Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-308629, EBI-726876; Q13761:RUNX3; NbExp=9; IntAct=EBI-308629, EBI-925990; P31947:SFN; NbExp=4; IntAct=EBI-308629, EBI-476295; P63279:UBE2I; NbExp=3; IntAct=EBI-308629, EBI-80168; P31946:YWHAB; NbExp=3; IntAct=EBI-308629, EBI-359815; P62258:YWHAE; NbExp=4; IntAct=EBI-308629, EBI-356498; P61981:YWHAG; NbExp=8; IntAct=EBI-308629, EBI-359832; Q04917:YWHAH; NbExp=5; IntAct=EBI-308629, EBI-306940; P27348:YWHAQ; NbExp=3; IntAct=EBI-308629, EBI-359854; P63104:YWHAZ; NbExp=6; IntAct=EBI-308629, EBI-347088;\nSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-246, Ser-467 and Ser-632 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation. Interaction with SIK3 leads to HDAC4 retention in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q6NZM9}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=P56524-1; Sequence=Displayed; Name=2;   IsoId=P56524-2; Sequence=VSP_057290, VSP_057291;\nTISSUE SPECIFICITY: Ubiquitous.\nDOMAIN: The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.\nDOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of ANKRA2. {ECO:0000269|PubMed:22649097}.\nPTM: Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-350, within the PxLPxI/L motif, impairs the binding of ANKRA2 but generates a high- affinity docking site for 14-3-3. {ECO:0000269|PubMed:10958686, ECO:0000269|PubMed:22649097}.\nPTM: Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4. {ECO:0000269|PubMed:12032081}.\nDISEASE: Brachydactyly-mental retardation syndrome (BDMR) [MIM:600430]: A syndrome resembling the physical anomalies found in Albright hereditary osteodystrophy. Common features are mild facial dysmorphism, congenital heart defects, distinct brachydactyly type E, mental retardation, developmental delay, seizures, autism spectrum disorder, and stocky build. Soft tissue ossification is absent, and there are no abnormalities in parathyroid hormone or calcium metabolism. {ECO:0000269|PubMed:20691407, ECO:0000269|PubMed:23188045, ECO:0000269|PubMed:24715439}. Note=The gene represented in this entry is involved in disease pathogenesis. HDAC4 point mutations and chromosomal microdeletions encompassing this gene have been found in BDMR patients (PubMed:20691407, PubMed:24715439, PubMed:23188045). However, HDAC4 haploinsufficiency is not fully penetrant and multiple genes may contribute to manifestation of the full phenotypic spectrum (PubMed:24715439, PubMed:23188045). {ECO:0000269|PubMed:20691407, ECO:0000269|PubMed:23188045, ECO:0000269|PubMed:24715439}.\nSIMILARITY: Belongs to the histone deacetylase family. HD type 2 subfamily. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=BAA22957.2; Type=Erroneous initiation; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.P56524", "displayName": "HDAC4_HUMAN", "synonyms": "Histone deacetylase 4, HD4, 3.5.1.98", "taxid": 9606, "geneName": "HDAC4", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P56524", "id": "uniprot.P56524", "value": "uniprot.P56524"}}, {"data": {"domainIds": "entrez.7283", "primaryDomainId": "entrez.7283", "geneType": "protein-coding", "displayName": "tubulin gamma 1", "synonyms": "tubulin gamma-1 chain, gamma-tubulin complex component 1, tubulin, gamma polypeptide", "chromosome": "17", "description": "tubulin gamma 1", "approvedSymbol": "TUBG1", "type": "Gene", "symbols": "CDCBM4, GCP-1, TUBG, TUBGCP1", "mapLocation": "17q21.2", "graphics": {"fill": "#FFB6C1"}, "name": "TUBG1", "id": "entrez.7283", "value": "entrez.7283"}}, {"data": {"domainIds": "uniprot.P23258", "sequence": "MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFERTCRQYDKLRKREAFLEQFRKEDMFKDNFDEMDTSREIVQQLIDEYHAATRPDYISWGTQEQ", "comments": "FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation.\nSUBUNIT: Interacts with TUBGCP2 and TUBGCP3 (PubMed:9566969, PubMed:9566969). Interacts with B9D2 (By similarity). Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of TUBG1 and CDK5RAP2 (PubMed:17959831). Interacts with PIFO (PubMed:20643351). Interacts with SAS6 and NUP62 at the centrosome (PubMed:24107630). {ECO:0000250|UniProtKB:P83887, ECO:0000269|PubMed:17959831, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:24107630, ECO:0000269|PubMed:9566967, ECO:0000269|PubMed:9566969}.\nINTERACTION: Self; NbExp=6; IntAct=EBI-302589, EBI-302589; O15169:AXIN1; NbExp=4; IntAct=EBI-302589, EBI-710484; Q96L34:MARK4; NbExp=4; IntAct=EBI-302589, EBI-302319; Q08AG7:MZT1; NbExp=4; IntAct=EBI-302589, EBI-2637198; Q6NZ67:MZT2B; NbExp=4; IntAct=EBI-302589, EBI-1052566; Q9UGJ1-2:TUBGCP4; NbExp=2; IntAct=EBI-302589, EBI-10964469;\nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:24107630, ECO:0000269|PubMed:9566967, ECO:0000269|PubMed:9566969}.\nPTM: Phosphorylation at Ser-131 by BRSK1 regulates centrosome duplication, possibly by mediating relocation of gamma-tubulin and its associated proteins from the cytoplasm to the centrosome. {ECO:0000250}.\nMASS SPECTROMETRY: Mass=51197.98; Method=MALDI; Evidence={ECO:0000269|PubMed:11840567};\nDISEASE: Cortical dysplasia, complex, with other brain malformations 4 (CDCBM4) [MIM:615412]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset seizures, microcephaly, spastic tetraplegia, and various malformations of cortical development, such as agyria, posterior or frontal pachygyria, thick cortex, and subcortical band heterotopia and thin corpus callosum in some patients. {ECO:0000269|PubMed:23603762}. Note=The disease is caused by mutations affecting the gene represented in this entry.\nSIMILARITY: Belongs to the tubulin family. {ECO:0000305}.", "primaryDomainId": "uniprot.P23258", "displayName": "TBG1_HUMAN", "synonyms": "Tubulin gamma-1 chain, Gamma-1-tubulin, Gamma-tubulin complex component 1, GCP-1", "taxid": 9606, "geneName": "TUBG1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "P23258", "id": "uniprot.P23258", "value": "uniprot.P23258"}}, {"data": {"domainIds": "entrez.51133", "primaryDomainId": "entrez.51133", "geneType": "protein-coding", "displayName": "potassium channel tetramerization domain containing 3", "synonyms": "BTB/POZ domain-containing protein KCTD3, NY-REN-45 antigen, potassium channel tetramerisation domain containing 3, renal carcinoma antigen NY-REN-45", "chromosome": "1", "description": "potassium channel tetramerization domain containing 3", "approvedSymbol": "KCTD3", "type": "Gene", "symbols": "NY-REN-45", "mapLocation": "1q41", "graphics": {"fill": "#FFB6C1"}, "name": "KCTD3", "id": "entrez.51133", "value": "entrez.51133"}}, {"data": {"domainIds": "uniprot.Q9Y597", "sequence": "MAGGHCGSFPAAAAGSGEIVQLNVGGTRFSTSRQTLMWIPDSFFSSLLSGRISTLRDETGAIFIDRDPAAFAPILNFLRTKELDLRGVSINVLRHEAEFYGITPLVRRLLLCEELERSSCGSVLFHGYLPPPGIPSRKINNTVRSADSRNGLNSTEGEARGNGTQPVLSGTGEETVRLGFPVDPRKVLIVAGHHNWIVAAYAHFAVCYRIKESSGWQQVFTSPYLDWTIERVALNAKVVGGPHGDKDKMVAVASESSIILWSVQDGGSGSEIGVFSLGVPVDALFFIGNQLVATSHTGKVGVWNAVTQHWQVQDVVPITSYDTAGSFLLLGCNNGSIYYIDMQKFPLRMKDNDLLVTELYHDPSNDAITALSVYLTPKTSVSGNWIEIAYGTSSGAVRVIVQHPETVGSGPQLFQTFTVHRSPVTKIMLSEKHLVSVCADNNHVRTWTVTRFRGMISTQPGSTPLASFKILSLEETESHGSYSSGNDIGPFGERDDQQVFIQKVVPITNKLFVRLSSTGKRICEIQAVDCTTISSFTVRECEGSSRMGSRPRRYLFTGHTNGSIQMWDLTTAMDMVNKSEDKDVGGPTEEELLKLLDQCDLSTSRCATPNISPATSVVQHSHLRESNSSLQLQHHDTTHEAATYGSMRPYRESPLLARARRTESFHSYRDFQTINLNRNVERAVPENGNLGPIQAEVKGATGECNISERKSPGVEIKSLRELDSGLEVHKIAEGFSESKKRSSEDENENKIEFRKKGGFEGGGFLGRKKVPYLASSPSTSDGGTDSPGTASPSPTKTTPSPRHKKSDSSGQEYSL", "comments": "FUNCTION: Accessory subunit of potassium/sodium hyperpolarization- activated cyclic nucleotide-gated channel 3 (HCN3) upregulating its cell-surface expression and current density without affecting its voltage dependence and kinetics. {ECO:0000250|UniProtKB:Q8BFX3}.\nSUBUNIT: Interacts with HCN3. {ECO:0000250|UniProtKB:Q8BFX3}.\nSUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BFX3}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1;   IsoId=Q9Y597-1; Sequence=Displayed; Name=2;   IsoId=Q9Y597-2; Sequence=VSP_020069; Name=3;   IsoId=Q9Y597-3; Sequence=VSP_020068;\nTISSUE SPECIFICITY: Broadly expressed in normal tissues. {ECO:0000269|PubMed:10508479}.\nMISCELLANEOUS: Reacts with sera from 5-25 per cent of cancer patients but not with sera from normal donors. Seventy per cent of renal cancer patients have antibodies against one or a panel of these antigens.\nSIMILARITY: Belongs to the KCTD3 family. {ECO:0000305}.\nSEQUENCE CAUTION: Sequence=AAH13868.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};", "primaryDomainId": "uniprot.Q9Y597", "displayName": "KCTD3_HUMAN", "synonyms": "BTB/POZ domain-containing protein KCTD3, Renal carcinoma antigen NY-REN-45", "taxid": 9606, "geneName": "KCTD3", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q9Y597", "id": "uniprot.Q9Y597", "value": "uniprot.Q9Y597"}}, {"data": {"domainIds": "entrez.85360", "primaryDomainId": "entrez.85360", "geneType": "protein-coding", "displayName": "synapse defective Rho GTPase homolog 1", "synonyms": "rho GTPase-activating protein SYDE1, protein syd-1 homolog 1, synapse defective 1, Rho GTPase, homolog 1, synapse defective protein 1 homolog 1", "chromosome": "19", "description": "synapse defective Rho GTPase homolog 1", "approvedSymbol": "SYDE1", "type": "Gene", "symbols": "7h3, SYD1", "mapLocation": "19p13.12", "graphics": {"fill": "#FFB6C1"}, "name": "SYDE1", "id": "entrez.85360", "value": "entrez.85360"}}, {"data": {"domainIds": "uniprot.Q6ZW31", "sequence": "MAEPLLRKTFSRLRGREKLPRKKSDAKERGHPAQRPEPSPPEPEPQAPEGSQAGAEGPSSPEASRSPARGAYLQSLEPSSRRWVLGGAKPAEDTSLGPGVPGTGEPAGEIWYNPIPEEDPRPPAPEPPGPQPGSAESEGLAPQGAAPASPPTKASRTKSPGPARRLSIKMKKLPELRRRLSLRGPRAGRERERAAPAGSVISRYHLDSSVGGPGPAAGPGGTRSPRAGYLSDGDSPERPAGPPSPTSFRPYEVGPAARAPPAALWGRLSLHLYGLGGLRPAPGATPRDLCCLLQVDGEARARTGPLRGGPDFLRLDHTFHLELEAARLLRALVLAWDPGVRRHRPCAQGTVLLPTVFRGCQAQQLAVRLEPQGLLYAKLTLSEQQEAPATAEPRVFGLPLPLLVERERPPGQVPLIIQKCVGQIERRGLRVVGLYRLCGSAAVKKELRDAFERDSAAVCLSEDLYPDINVITGILKDYLRELPTPLITQPLYKVVLEAMARDPPNRVPPTTEGTRGLLSCLPDVERATLTLLLDHLRLVSSFHAYNRMTPQNLAVCFGPVLLPARQAPTRPRARSSGPGLASAVDFKHHIEVLHYLLQSWPDPRLPRQSPDVAPYLRPKRQPPLHLPLADPEVVTRPRGRGGPESPPSNRYAGDWSVCGRDFLPCGRDFLSGPDYDHVTGSDSEDEDEEVGEPRVTGDFEDDFDAPFNPHLNLKDFDALILDLERELSKQINVCL", "comments": "FUNCTION: GTPase activator for the Rho-type GTPases. As a GCM1 downstream effector, it is involved in placental development and positively regulates trophoblast cells migration. It regulates cytoskeletal remodeling by controlling the activity of Rho GTPases including RHOA, CDC42 and RAC1 (PubMed:27917469). {ECO:0000269|PubMed:27917469}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1;   IsoId=Q6ZW31-1; Sequence=Displayed; Name=2;   IsoId=Q6ZW31-2; Sequence=VSP_029717;\nTISSUE SPECIFICITY: Expressed in trophoblast cells of placental villi. {ECO:0000269|PubMed:27917469}.", "primaryDomainId": "uniprot.Q6ZW31", "displayName": "SYDE1_HUMAN", "synonyms": "Rho GTPase-activating protein SYDE1, Synapse defective protein 1 homolog 1, Protein syd-1 homolog 1", "taxid": 9606, "geneName": "SYDE1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q6ZW31", "id": "uniprot.Q6ZW31", "value": "uniprot.Q6ZW31"}}, {"data": {"domainIds": "entrez.8844", "primaryDomainId": "entrez.8844", "geneType": "protein-coding", "displayName": "kinase suppressor of ras 1", "synonyms": "kinase suppressor of Ras 1", "chromosome": "17", "description": "kinase suppressor of ras 1", "approvedSymbol": "KSR1", "type": "Gene", "symbols": "KSR, RSU2", "mapLocation": "17q11.2", "graphics": {"fill": "#FFB6C1"}, "name": "KSR1", "id": "entrez.8844", "value": "entrez.8844"}}, {"data": {"domainIds": "uniprot.Q8IVT5", "sequence": "MDRAALRAAAMGEKKEGGGGGDAAAAEGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKCAVSNDLTQQEIRTLEAKLVRYICKQRQCKLSVAPGERTPELNSYPRFSDWLYTFNVRPEVVQEIPRDLTLDALLEMNEAKVKETLRRCGASGDECGRLQYALTCLRKVTGLGGEHKEDSSWSSLDARRESGSGPSTDTLSAASLPWPPGSSQLGRAGNSAQGPRSISVSALPASDSPTPSFSEGLSDTCIPLHASGRLTPRALHSFITPPTTPQLRRHTKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDDVSSMRFDLSHGSPQMVRRDIGLSVTHRFSTKSWLSQVCHVCQKSMIFGVKCKHCRLKCHNKCTKEAPACRISFLPLTRLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNHLDSSSNPSSTTSSTPSSPAPFPTSSNPSSATTPPNPSPGQRDSRFNFPAAYFIHHRQQFIFPVPSAGHCWKCLLIAESLKENAFNISAFAHAAPLPEAADGTRLDDQPKADVLEAHEAEAEEPEAGKSEAEDDEDEVDDLPSSRRPWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREGRRENQLKLSHDWLCYLAPEIVREMTPGKDEDQLPFSKAADVYAFGTVWYELQARDWPLKNQAAEASIWQIGSGEGMKRVLTSVSLGKEVSEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSADINSSKVVPRFERFGLGVLESSNPKM", "comments": "FUNCTION: Part of a multiprotein signaling complex which promotes phosphorylation of Raf family members and activation of downstream MAP kinases (By similarity). Independently of its kinase activity, acts as MAP2K1/MEK1 and MAP2K2/MEK2-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1 or MAP2K2/MEK2, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 and/or MAP2K2/MEK2 (PubMed:29433126). Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP (By similarity). Its kinase activity is unsure (By similarity). Some protein kinase activity has been detected in vitro, however the physiological relevance of this activity is unknown (By similarity). {ECO:0000250|UniProtKB:Q61097, ECO:0000269|PubMed:29433126}.\nCATALYTIC ACTIVITY: 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={ECO:0000250|UniProtKB:Q61097};\nCATALYTIC ACTIVITY: 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={ECO:0000250|UniProtKB:Q61097};\nSUBUNIT: Homodimer (PubMed:29433126). Heterodimerizes (via N-terminus) with BRAF (via N-terminus) in a MAP2K1/MEK1 or MAP2K2/MEK2-dependent manner (PubMed:29433126). Interacts with MAP2K1/MEK1 and MAP2K2/MEK2 (PubMed:10409742, PubMed:29433126). Binding to MAP2K1/MEK1 releases the intramolecular inhibitory interaction between KSR1 N-terminus and kinase domains which is required for the subsequent RSK1 dimerization with BRAF (PubMed:29433126). Identified in a complex with AKAP13, MAP2K1 and BRAF (By similarity). Interacts with AKAP13 and BRAF (PubMed:21102438). Interacts with RAF and MAPK/ERK, in a Ras-dependent manner (By similarity). Interacts with 14-3-3 proteins including YWHAB (By similarity). Interacts with HSP90AA1/HSP90, YWHAE/14-3-3 and CDC37 (PubMed:10409742, PubMed:29433126). The binding of 14-3-3 proteins to phosphorylated KSR1 prevents the membrane localization (By similarity). Interacts with MARK3 (By similarity). Interacts with PPP2R1A and PPP2CA (By similarity). Interacts with isoform 1 of VRK2 (PubMed:20679487). {ECO:0000250|UniProtKB:Q61097, ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:20679487, ECO:0000269|PubMed:21102438, ECO:0000269|PubMed:29433126}.\nINTERACTION: P36507:MAP2K2; NbExp=6; IntAct=EBI-486984, EBI-1056930; Q86Y07:VRK2; NbExp=4; IntAct=EBI-486984, EBI-1207615;\nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20679487}. Membrane {ECO:0000269|PubMed:20679487}; Peripheral membrane protein {ECO:0000269|PubMed:20679487}. Cell membrane {ECO:0000250|UniProtKB:Q61097}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q61097}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q61097}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20679487}. Note=In unstimulated cells, where the phosphorylated form is bound to a 14-3-3 protein, sequestration in the cytoplasm occurs. Following growth factor treatment, the protein is free for membrane translocation, and it moves from the cytoplasm to the cell periphery. {ECO:0000305|PubMed:12007434}.\nALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=1;   IsoId=Q8IVT5-1; Sequence=Displayed; Name=2;   IsoId=Q8IVT5-2; Sequence=VSP_055656, VSP_055657; Name=3;   IsoId=Q8IVT5-3; Sequence=VSP_055655; Name=4;   IsoId=Q8IVT5-4; Sequence=VSP_055655, VSP_055657;\nDOMAIN: The protein kinase domain is predicted to be catalytically inactive. The domain is sufficient for KSR1 and KSR1-mediated MAP2K1 and MAP2K2 membrane localization. The domain is required but not sufficient for MAP kinase-mediated inhibition of ELK1 phosphorylation (PubMed:10409742). {ECO:0000255, ECO:0000269|PubMed:10409742}.\nDOMAIN: The N-terminal region mediates interaction with BRAF (PubMed:29433126). Also mediates membrane localization (By similarity). {ECO:0000250|UniProtKB:Q61097, ECO:0000269|PubMed:29433126}.\nPTM: Phosphorylated on Ser-311 and, to a higher extent, on Ser-406 by MARK3. Dephosphorylated on Ser-406 by PPP2CA. In resting cells, phosphorylated KSR1 is cytoplasmic and in stimulated cells, dephosphorylated KSR1 is membrane-associated. Phosphorylated by PKA at Ser-888. Phosphorylation at Ser-888 is required for cAMP-dependent activation of MAPK1 and/or MAPK3 (By similarity). {ECO:0000250|UniProtKB:Q61097}.\nSIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. {ECO:0000305}.\nCAUTION: Although it belongs to the protein kinase superfamily, the ATP-binding motif VAIK has an arginine instead of a lysine residue suggesting that KSR1 can not bind ATP and therefore lacks protein kinase activity. However, KSR1 is capable of binding ATP (PubMed:29433126). Has protein kinase activity towards MAP2K1 in the presence of RAF1/c-RAF in vitro (By similarity). {ECO:0000250|UniProtKB:Q61097, ECO:0000269|PubMed:29433126, ECO:0000305}.\nWEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL=\"http://atlasgeneticsoncology.org/Genes/KSR1ID41107ch17q11.html\";", "primaryDomainId": "uniprot.Q8IVT5", "displayName": "KSR1_HUMAN", "synonyms": "Kinase suppressor of Ras 1, 2.7.11.1 {ECO:0000250, UniProtKB:Q61097}", "taxid": 9606, "geneName": "KSR1", "type": "Protein", "graphics": {"fill": "#FFB6C1"}, "name": "Q8IVT5", "id": "uniprot.Q8IVT5", "value": "uniprot.Q8IVT5"}}, {"data": {"id": "entrez.66489", "value": "entrez.66489", "name": "entrez.66489"}}, {"data": {"id": "entrez.13669", "value": "entrez.13669", "name": "entrez.13669"}}], "edges": [{"data": {"type": "ProteinEncodedBy", "source": "entrez.65220", "target": "uniprot.Q6PJ22"}}, {"data": {"type": "ProteinEncodedBy", "source": "entrez.65220", "target": "uniprot.A0A0A0MR98"}}, {"data": {"type": "ProteinEncodedBy", "source": "entrez.65220", "target": "uniprot.A0A024R058"}}, {"data": {"type": "ProteinEncodedBy", "source": "entrez.65220", "target": "uniprot.O95544"}}, {"data": {"SUID": 332922, "shared name": "65220 (interacts with) 85360", "shared interaction": "interacts with", "Confidence score": 4.314327917938276, "Experimental type1": "Affinity Capture-MS", "name": "65220 (interacts with) 85360", "selected": false, "interaction": "interacts with", "type": "IsFunctionallyRelatedTo", "source": "entrez.65220", "target": "entrez.85360"}}, {"data": {"SUID": 332919, "shared name": "65220 (interacts with) 135295", "shared interaction": "interacts with", "Confidence score": 4.314327917938276, "Experimental type1": "Affinity Capture-MS", "name": "65220 (interacts with) 135295", "selected": false, "interaction": "interacts with", "type": "IsFunctionallyRelatedTo", "source": "entrez.65220", "target": "entrez.135295"}}, {"data": {"SUID": 332920, "shared name": "65220 (interacts with) 83541", "shared interaction": "interacts with", "Confidence score": 4.314327917938276, "Experimental type1": "Affinity Capture-MS", "name": "65220 (interacts with) 83541", "selected": false, "interaction": "interacts with", "type": "IsFunctionallyRelatedTo", "source": "entrez.65220", "target": "entrez.83541"}}, {"data": {"SUID": 332913, "shared name": "65220 (interacts with) 9201", "shared interaction": "interacts with", "Confidence score": 4.314327917938276, "Experimental type1": "Affinity Capture-MS", "name": "65220 (interacts with) 9201", "selected": false, "interaction": "interacts with", "type": "IsFunctionallyRelatedTo", "source": "entrez.65220", "target": "entrez.9201"}}, {"data": {"SUID": 332914, "shared name": "65220 (interacts with) 9223", "shared interaction": "interacts with", "Confidence score": 4.314327917938276, "Experimental type1": "Affinity Capture-MS", "name": "65220 (interacts with) 9223", "selected": false, "interaction": "interacts with", "type": "IsFunctionallyRelatedTo", "source": "entrez.65220", "target": "entrez.9223"}}, {"data": {"SUID": 332911, "shared name": "65220 (interacts with) 26058", "shared interaction": "interacts with", "Confidence score": 4.314327917938276, "Experimental type1": "Affinity Capture-MS", "name": "65220 (interacts with) 26058", "selected": false, "interaction": "interacts with", "type": "IsFunctionallyRelatedTo", "source": "entrez.65220", "target": "entrez.26058"}}, {"data": {"SUID": 332912, "shared name": "65220 (interacts with) 26037", "shared interaction": "interacts with", "Confidence score": 4.314327917938276, "Experimental type1": "Affinity Capture-MS", "name": "65220 (interacts with) 26037", "selected": false, "interaction": "interacts with", "type": "IsFunctionallyRelatedTo", "source": "entrez.65220", "target": "entrez.26037"}}, {"data": {"SUID": 332917, "shared name": "65220 (interacts with) 57622", "shared interaction": "interacts with", "Confidence score": 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