UBE2C_HUMAN
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 03-AUG-2022, entry version 209.
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 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="http://atlasgeneticsoncology.org/Genes/UBE2CID44079ch20q13.html";
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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 PDBsum; 1I7K; -.
DR PDBsum; 4YII; -.
DR PDBsum; 5A31; -.
DR PDBsum; 5KHR; -.
DR PDBsum; 5L9U; -.
DR AlphaFoldDB; O00762; -.
DR SMR; O00762; -.
DR BioGRID; 116249; 79.
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; O00762; -.
DR PeptideAtlas; O00762; -.
DR PRIDE; O00762; -.
DR ProteomicsDB; 15210; -.
DR ProteomicsDB; 1657; -.
DR ProteomicsDB; 33704; -.
DR ProteomicsDB; 48021; -. [O00762-1]
DR TopDownProteomics; O00762-1; -. [O00762-1]
DR TopDownProteomics; O00762-3; -. [O00762-3]
DR ABCD; O00762; 2 sequenced antibodies.
DR Antibodypedia; 27753; 490 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 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; HPNVDMS; -.
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; 429 hits in 1095 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 158 other tissues.
DR ExpressionAtlas; O00762; baseline and differential.
DR Genevisible; O00762; HS.
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: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; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
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
