ID UBE2C_HUMAN Reviewed; 179 AA. AC O00762; A6NP33; E1P5N7; G3XAB7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 218. DE RecName: Full=Ubiquitin-conjugating enzyme E2 C; DE EC=2.3.2.23 {ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:20061386}; DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme C; DE EC=2.3.2.24 {ECO:0000269|PubMed:17588522}; DE AltName: Full=E2 ubiquitin-conjugating enzyme C; DE AltName: Full=UbcH10; DE AltName: Full=Ubiquitin carrier protein C; DE AltName: Full=Ubiquitin-protein ligase C; GN Name=UBE2C; Synonyms=UBCH10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF CYS-114. RX PubMed=9122200; DOI=10.1073/pnas.94.6.2362; RA Townsley F.M., Aristarkhov A., Beck S., Hershko A., Ruderman J.V.; RT "Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 RT blocks cells in metaphase."; RL Proc. Natl. Acad. Sci. U.S.A. 94:2362-2367(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Lung adenocarcinoma, Lymph, Melanoma, Teratocarcinoma, and RC Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF CYS-114. RX PubMed=15558010; DOI=10.1038/nature03023; RA Rape M., Kirschner M.W.; RT "Autonomous regulation of the anaphase-promoting complex couples mitosis to RT S-phase entry."; RL Nature 432:588-595(2004). RN [7] RP CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME. RX PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014; RA Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.; RT "E3-independent monoubiquitination of ubiquitin-binding proteins."; RL Mol. Cell 26:891-898(2007). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=18485873; DOI=10.1016/j.cell.2008.04.012; RA Jin L., Williamson A., Banerjee S., Philipp I., Rape M.; RT "Mechanism of ubiquitin-chain formation by the human anaphase-promoting RT complex."; RL Cell 133:653-665(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP FUNCTION. RX PubMed=19820702; DOI=10.1038/ncb1983; RA Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P., RA Pines J., Venkitaraman A.R.; RT "UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic RT exit."; RL Nat. Cell Biol. 11:1363-1369(2009). RN [11] RP FUNCTION. RX PubMed=19822757; DOI=10.1073/pnas.0907887106; RA Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M.; RT "Identification of a physiological E2 module for the human anaphase- RT promoting complex."; RL Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20061386; DOI=10.1074/jbc.m109.089003; RA David Y., Ziv T., Admon A., Navon A.; RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to RT preferred lysines."; RL J. Biol. Chem. 285:8595-8604(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RX PubMed=11927573; DOI=10.1074/jbc.m109398200; RA Lin Y., Hwang W.C., Basavappa R.; RT "Structural and functional analysis of the human mitotic-specific RT ubiquitin-conjugating enzyme, UbcH10."; RL J. Biol. Chem. 277:21913-21921(2002). RN [17] {ECO:0007744|PDB:5L9U} RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) IN COMPLEX WITH APC/C, RP INTERACTION WITH ANAPC2, AND FUNCTION. RX PubMed=27259151; DOI=10.1016/j.cell.2016.05.037; RA Brown N.G., VanderLinden R., Watson E.R., Weissmann F., Ordureau A., RA Wu K.P., Zhang W., Yu S., Mercredi P.Y., Harrison J.S., Davidson I.F., RA Qiao R., Lu Y., Dube P., Brunner M.R., Grace C.R., Miller D.J., RA Haselbach D., Jarvis M.A., Yamaguchi M., Yanishevski D., Petzold G., RA Sidhu S.S., Kuhlman B., Kirschner M.W., Harper J.W., Peters J.M., Stark H., RA Schulman B.A.; RT "Dual RING E3 architectures regulate multiubiquitination and ubiquitin RT chain elongation by APC/C."; RL Cell 165:1440-1453(2016). CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its CC covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and CC 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the CC anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated CC ubiquitin ligase that controls progression through mitosis. Acts by CC initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, CC leading to the degradation of APC/C substrates by the proteasome and CC promoting mitotic exit. {ECO:0000269|PubMed:15558010, CC ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:19820702, CC ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:20061386, CC ECO:0000269|PubMed:27259151}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin- CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE- CC ProRule:PRU10133, ECO:0000269|PubMed:18485873, CC ECO:0000269|PubMed:20061386}; CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L- CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.24; Evidence={ECO:0000269|PubMed:17588522}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:18485873}. CC -!- SUBUNIT: Component of the APC/C complex, composed of at least 14 CC distinct subunits that assemble into a complex of at least 19 chains CC with a combined molecular mass of around 1.2 MDa. Within this complex, CC directly interacts with ANAPC2. {ECO:0000269|PubMed:19820702, CC ECO:0000269|PubMed:27259151}. CC -!- INTERACTION: CC O00762; P62879: GNB2; NbExp=3; IntAct=EBI-719691, EBI-356942; CC O00762; Q13164: MAPK7; NbExp=3; IntAct=EBI-719691, EBI-1213983; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O00762-1; Sequence=Displayed; CC Name=2; CC IsoId=O00762-2; Sequence=VSP_045647; CC Name=3; CC IsoId=O00762-3; Sequence=VSP_045648; CC Name=4; CC IsoId=O00762-4; Sequence=VSP_045649; CC -!- PTM: Autoubiquitinated by the APC/C complex, leading to its degradation CC by the proteasome. Its degradation plays a central role in APC/C CC regulation, allowing cyclin-A accumulation before S phase entry. APC/C CC substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its CC E2 function, hence APC/C remaining active until its substrates have CC been destroyed. {ECO:0000269|PubMed:15558010}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44079/UBE2C"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U73379; AAB53362.1; -; mRNA. DR EMBL; BT007300; AAP35964.1; -; mRNA. DR EMBL; AL050348; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75804.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75805.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75806.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75807.1; -; Genomic_DNA. DR EMBL; BC007656; AAH07656.1; -; mRNA. DR EMBL; BC016292; AAH16292.1; -; mRNA. DR EMBL; BC050736; AAH50736.1; -; mRNA. DR EMBL; BI858659; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BM556795; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BU844974; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS13370.1; -. [O00762-1] DR CCDS; CCDS13371.1; -. [O00762-4] DR CCDS; CCDS13372.1; -. [O00762-3] DR CCDS; CCDS13374.1; -. [O00762-2] DR RefSeq; NP_001268670.1; NM_001281741.1. DR RefSeq; NP_001268671.1; NM_001281742.1. DR RefSeq; NP_008950.1; NM_007019.3. [O00762-1] DR RefSeq; NP_861515.1; NM_181799.2. [O00762-4] DR RefSeq; NP_861516.1; NM_181800.2. [O00762-3] DR RefSeq; NP_861517.1; NM_181801.3. [O00762-2] DR PDB; 1I7K; X-ray; 1.95 A; A/B=1-179. DR PDB; 4YII; X-ray; 1.80 A; U=27-179. DR PDB; 5A31; EM; 4.30 A; Q=29-173. DR PDB; 5KHR; EM; 6.10 A; Q=1-179. DR PDB; 5L9U; EM; 6.40 A; U=1-179. DR PDB; 8TAR; EM; 4.00 A; Q=29-173. DR PDB; 8TAU; EM; 3.50 A; Q=1-179. DR PDBsum; 1I7K; -. DR PDBsum; 4YII; -. DR PDBsum; 5A31; -. DR PDBsum; 5KHR; -. DR PDBsum; 5L9U; -. DR PDBsum; 8TAR; -. DR PDBsum; 8TAU; -. DR AlphaFoldDB; O00762; -. DR EMDB; EMD-2925; -. DR EMDB; EMD-41140; -. DR EMDB; EMD-41142; -. DR SMR; O00762; -. DR BioGRID; 116249; 91. DR DIP; DIP-52725N; -. DR IntAct; O00762; 15. DR MINT; O00762; -. DR STRING; 9606.ENSP00000348838; -. DR ChEMBL; CHEMBL4105834; -. DR iPTMnet; O00762; -. DR PhosphoSitePlus; O00762; -. DR SwissPalm; O00762; -. DR BioMuta; UBE2C; -. DR CPTAC; CPTAC-1465; -. DR CPTAC; CPTAC-1466; -. DR CPTAC; CPTAC-1467; -. DR CPTAC; CPTAC-1468; -. DR CPTAC; CPTAC-3259; -. DR CPTAC; CPTAC-3260; -. DR CPTAC; CPTAC-715; -. DR CPTAC; CPTAC-716; -. DR EPD; O00762; -. DR jPOST; O00762; -. DR MassIVE; O00762; -. DR MaxQB; O00762; -. DR PaxDb; 9606-ENSP00000348838; -. DR PeptideAtlas; O00762; -. DR ProteomicsDB; 15210; -. DR ProteomicsDB; 1657; -. DR ProteomicsDB; 33704; -. DR ProteomicsDB; 48021; -. [O00762-1] DR Pumba; O00762; -. DR TopDownProteomics; O00762-1; -. [O00762-1] DR TopDownProteomics; O00762-3; -. [O00762-3] DR ABCD; O00762; 2 sequenced antibodies. DR Antibodypedia; 27753; 534 antibodies from 38 providers. DR CPTC; O00762; 3 antibodies. DR DNASU; 11065; -. DR Ensembl; ENST00000335046.7; ENSP00000335674.3; ENSG00000175063.17. [O00762-4] DR Ensembl; ENST00000352551.9; ENSP00000333975.5; ENSG00000175063.17. [O00762-3] DR Ensembl; ENST00000356455.9; ENSP00000348838.4; ENSG00000175063.17. [O00762-1] DR Ensembl; ENST00000372568.4; ENSP00000361649.4; ENSG00000175063.17. [O00762-2] DR GeneID; 11065; -. DR KEGG; hsa:11065; -. DR MANE-Select; ENST00000356455.9; ENSP00000348838.4; NM_007019.4; NP_008950.1. DR UCSC; uc002xpl.5; human. [O00762-1] DR AGR; HGNC:15937; -. DR CTD; 11065; -. DR DisGeNET; 11065; -. DR GeneCards; UBE2C; -. DR HGNC; HGNC:15937; UBE2C. DR HPA; ENSG00000175063; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 605574; gene. DR neXtProt; NX_O00762; -. DR OpenTargets; ENSG00000175063; -. DR PharmGKB; PA38057; -. DR VEuPathDB; HostDB:ENSG00000175063; -. DR eggNOG; KOG0421; Eukaryota. DR GeneTree; ENSGT00930000150941; -. DR HOGENOM; CLU_030988_9_2_1; -. DR InParanoid; O00762; -. DR OMA; YNVQTIL; -. DR OrthoDB; 5389101at2759; -. DR PhylomeDB; O00762; -. DR TreeFam; TF101116; -. DR BRENDA; 2.3.2.23; 2681. DR BRENDA; 2.3.2.24; 2681. DR PathwayCommons; O00762; -. DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex. DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B. DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase. DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase. DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins. DR Reactome; R-HSA-176412; Phosphorylation of the APC/C. DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex. DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX. DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes. DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; O00762; -. DR SIGNOR; O00762; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 11065; 449 hits in 1173 CRISPR screens. DR ChiTaRS; UBE2C; human. DR EvolutionaryTrace; O00762; -. DR GeneWiki; UBE2C; -. DR GenomeRNAi; 11065; -. DR Pharos; O00762; Tbio. DR PRO; PR:O00762; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O00762; Protein. DR Bgee; ENSG00000175063; Expressed in ventricular zone and 160 other cell types or tissues. DR ExpressionAtlas; O00762; baseline and differential. DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI. DR GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:Reactome. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB. DR GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB. DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB. DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IDA:UniProt. DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; TAS:UniProtKB. DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR PANTHER; PTHR24067:SF338; UBIQUITIN-CONJUGATING ENZYME E2C; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS00183; UBC_1; 1. DR PROSITE; PS50127; UBC_2; 1. DR Genevisible; O00762; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle; KW Cell division; Mitosis; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT CHAIN 2..179 FT /note="Ubiquitin-conjugating enzyme E2 C" FT /id="PRO_0000082560" FT DOMAIN 30..175 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 114 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..39 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045647" FT VAR_SEQ 44..72 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045648" FT VAR_SEQ 73..140 FT /note="VYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSA FT LYDVRTILLSIQSLLG -> AVGSIRTSSTVCLLSGPRETQDSSKPLVWGLGWDMRLLL FT ELTLQLFLQMP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045649" FT VARIANT 25 FT /note="G -> D" FT /id="VAR_007694" FT MUTAGEN 114 FT /note="C->S: Loss of function; inhibition of cyclin-B FT degradation." FT /evidence="ECO:0000269|PubMed:15558010, FT ECO:0000269|PubMed:9122200" FT HELIX 30..45 FT /evidence="ECO:0007829|PDB:4YII" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:4YII" FT STRAND 61..68 FT /evidence="ECO:0007829|PDB:4YII" FT STRAND 78..84 FT /evidence="ECO:0007829|PDB:4YII" FT TURN 87..91 FT /evidence="ECO:0007829|PDB:4YII" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:4YII" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:4YII" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:4YII" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:4YII" FT HELIX 128..140 FT /evidence="ECO:0007829|PDB:4YII" FT HELIX 150..155 FT /evidence="ECO:0007829|PDB:4YII" FT HELIX 159..172 FT /evidence="ECO:0007829|PDB:4YII" SQ SEQUENCE 179 AA; 19652 MW; 0B6F58A1F0665D9A CRC64; MASQNRDPAA TSVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI SAFPESDNLF KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT PCYHPNVDTQ GNICLDILKE KWSALYDVRT ILLSIQSLLG EPNIDSPLNT HAAELWKNPT AFKKYLQETY SKQVTSQEP //