GenomeNet

Database: UniProt
Entry: O00762
LinkDB: O00762
Original site: O00762 
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   17-JUN-2020, entry version 199.
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:0000244|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; 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";
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   SMR; O00762; -.
DR   BioGRID; 116249; 74.
DR   DIP; DIP-52725N; -.
DR   IntAct; O00762; 11.
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   PaxDb; O00762; -.
DR   PeptideAtlas; O00762; -.
DR   PRIDE; O00762; -.
DR   ProteomicsDB; 12714; -. [O00762-1]
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; 452 antibodies.
DR   DNASU; 11065; -.
DR   Ensembl; ENST00000335046; ENSP00000335674; ENSG00000175063. [O00762-4]
DR   Ensembl; ENST00000352551; ENSP00000333975; ENSG00000175063. [O00762-3]
DR   Ensembl; ENST00000356455; ENSP00000348838; ENSG00000175063. [O00762-1]
DR   Ensembl; ENST00000372568; ENSP00000361649; ENSG00000175063. [O00762-2]
DR   GeneID; 11065; -.
DR   KEGG; hsa:11065; -.
DR   UCSC; uc002xpl.5; human. [O00762-1]
DR   CTD; 11065; -.
DR   DisGeNET; 11065; -.
DR   EuPathDB; HostDB:ENSG00000175063.16; -.
DR   GeneCards; UBE2C; -.
DR   HGNC; HGNC:15937; UBE2C.
DR   HPA; ENSG00000175063; Tissue enriched (lymphoid).
DR   MIM; 605574; gene.
DR   neXtProt; NX_O00762; -.
DR   OpenTargets; ENSG00000175063; -.
DR   PharmGKB; PA38057; -.
DR   eggNOG; KOG0421; Eukaryota.
DR   eggNOG; ENOG4111IGV; LUCA.
DR   GeneTree; ENSGT00930000150941; -.
DR   HOGENOM; CLU_030988_9_2_1; -.
DR   InParanoid; O00762; -.
DR   KO; K06688; -.
DR   OMA; HPNVDMS; -.
DR   PhylomeDB; O00762; -.
DR   TreeFam; TF101116; -.
DR   BRENDA; 2.3.2.B6; 2681.
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-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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; O00762; -.
DR   SIGNOR; O00762; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 11065; 388 hits in 798 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 oocyte and 178 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:0005623; C:cell; IEA:GOC.
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: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:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
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; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_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; Polymorphism;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:21406692"
FT   CHAIN           2..179
FT                   /note="Ubiquitin-conjugating enzyme E2 C"
FT                   /id="PRO_0000082560"
FT   ACT_SITE        114
FT                   /note="Glycyl thioester intermediate"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:21406692"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|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:0000244|PDB:4YII"
FT   STRAND          50..54
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   STRAND          61..68
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   STRAND          78..84
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   TURN            87..91
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   STRAND          95..100
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   STRAND          111..113
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   HELIX           116..118
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   TURN            119..121
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   HELIX           128..140
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   HELIX           150..155
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   HELIX           159..172
FT                   /evidence="ECO:0000244|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
//
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