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Ubiquitin-conjugating enzyme E2 C (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme C) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme C) (UbcH10) (Ubiquitin carrier protein C) (Ubiquitin-protein ligase C)

 UBE2C_HUMAN             Reviewed;         179 AA.
O00762; A6NP33; E1P5N7; G3XAB7;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
12-SEP-2018, entry version 184.
RecName: Full=Ubiquitin-conjugating enzyme E2 C;
EC=2.3.2.23 {ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:20061386};
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme C;
EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
AltName: Full=E2 ubiquitin-conjugating enzyme C;
AltName: Full=UbcH10;
AltName: Full=Ubiquitin carrier protein C;
AltName: Full=Ubiquitin-protein ligase C;
Name=UBE2C; Synonyms=UBCH10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF CYS-114.
PubMed=9122200; DOI=10.1073/pnas.94.6.2362;
Townsley F.M., Aristarkhov A., Beck S., Hershko A., Ruderman J.V.;
"Dominant-negative cyclin-selective ubiquitin carrier protein E2-
C/UbcH10 blocks cells in metaphase.";
Proc. Natl. Acad. Sci. U.S.A. 94:2362-2367(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Lung adenocarcinoma, Lymph, Melanoma, Teratocarcinoma, and
Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF CYS-114.
PubMed=15558010; DOI=10.1038/nature03023;
Rape M., Kirschner M.W.;
"Autonomous regulation of the anaphase-promoting complex couples
mitosis to S-phase entry.";
Nature 432:588-595(2004).
[7]
CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME.
PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014;
Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.;
"E3-independent monoubiquitination of ubiquitin-binding proteins.";
Mol. Cell 26:891-898(2007).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
"Mechanism of ubiquitin-chain formation by the human anaphase-
promoting complex.";
Cell 133:653-665(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
FUNCTION.
PubMed=19820702; DOI=10.1038/ncb1983;
Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P.,
Pines J., Venkitaraman A.R.;
"UBE2S elongates ubiquitin chains on APC/C substrates to promote
mitotic exit.";
Nat. Cell Biol. 11:1363-1369(2009).
[11]
FUNCTION.
PubMed=19822757; DOI=10.1073/pnas.0907887106;
Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H.,
Rape M.;
"Identification of a physiological E2 module for the human anaphase-
promoting complex.";
Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009).
[12]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
PubMed=11927573; DOI=10.1074/jbc.M109398200;
Lin Y., Hwang W.C., Basavappa R.;
"Structural and functional analysis of the human mitotic-specific
ubiquitin-conjugating enzyme, UbcH10.";
J. Biol. Chem. 277:21913-21921(2002).
[17] {ECO:0000244|PDB:5L9U}
STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) IN COMPLEX WITH
APC/C, INTERACTION WITH ANAPC2, AND FUNCTION.
PubMed=27259151; DOI=10.1016/j.cell.2016.05.037;
Brown N.G., VanderLinden R., Watson E.R., Weissmann F., Ordureau A.,
Wu K.P., Zhang W., Yu S., Mercredi P.Y., Harrison J.S., Davidson I.F.,
Qiao R., Lu Y., Dube P., Brunner M.R., Grace C.R., Miller D.J.,
Haselbach D., Jarvis M.A., Yamaguchi M., Yanishevski D., Petzold G.,
Sidhu S.S., Kuhlman B., Kirschner M.W., Harper J.W., Peters J.M.,
Stark H., Schulman B.A.;
"Dual RING E3 architectures regulate multiubiquitination and ubiquitin
chain elongation by APC/C.";
Cell 165:1440-1453(2016).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In vitro catalyzes 'Lys-
11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential
factor of the anaphase promoting complex/cyclosome (APC/C), a cell
cycle-regulated ubiquitin ligase that controls progression through
mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains
on APC/C substrates, leading to the degradation of APC/C
substrates by the proteasome and promoting mitotic exit.
{ECO:0000269|PubMed:15558010, ECO:0000269|PubMed:18485873,
ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757,
ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:27259151}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:20061386}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-
activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:17588522}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000269|PubMed:18485873}.
-!- SUBUNIT: Component of the APC/C complex, composed of at least 14
distinct subunits that assemble into a complex of at least 19
chains with a combined molecular mass of around 1.2 MDa. Within
this complex, directly interacts with ANAPC2.
{ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:27259151}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O00762-1; Sequence=Displayed;
Name=2;
IsoId=O00762-2; Sequence=VSP_045647;
Note=No experimental confirmation available.;
Name=3;
IsoId=O00762-3; Sequence=VSP_045648;
Note=No experimental confirmation available.;
Name=4;
IsoId=O00762-4; Sequence=VSP_045649;
Note=No experimental confirmation available.;
-!- PTM: Autoubiquitinated by the APC/C complex, leading to its
degradation by the proteasome. Its degradation plays a central
role in APC/C regulation, allowing cyclin-A accumulation before S
phase entry. APC/C substrates inhibit the autoubiquitination of
UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active
until its substrates have been destroyed.
{ECO:0000269|PubMed:15558010}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/UBE2CID44079ch20q13.html";
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EMBL; U73379; AAB53362.1; -; mRNA.
EMBL; BT007300; AAP35964.1; -; mRNA.
EMBL; AL050348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75804.1; -; Genomic_DNA.
EMBL; CH471077; EAW75805.1; -; Genomic_DNA.
EMBL; CH471077; EAW75806.1; -; Genomic_DNA.
EMBL; CH471077; EAW75807.1; -; Genomic_DNA.
EMBL; BC007656; AAH07656.1; -; mRNA.
EMBL; BC016292; AAH16292.1; -; mRNA.
EMBL; BC050736; AAH50736.1; -; mRNA.
EMBL; BI858659; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BM556795; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BU844974; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS13370.1; -. [O00762-1]
CCDS; CCDS13371.1; -. [O00762-4]
CCDS; CCDS13372.1; -. [O00762-3]
CCDS; CCDS13374.1; -. [O00762-2]
RefSeq; NP_001268670.1; NM_001281741.1.
RefSeq; NP_001268671.1; NM_001281742.1.
RefSeq; NP_008950.1; NM_007019.3. [O00762-1]
RefSeq; NP_861515.1; NM_181799.2. [O00762-4]
RefSeq; NP_861516.1; NM_181800.2. [O00762-3]
RefSeq; NP_861517.1; NM_181801.3. [O00762-2]
UniGene; Hs.93002; -.
PDB; 1I7K; X-ray; 1.95 A; A/B=1-179.
PDB; 4YII; X-ray; 1.80 A; U=27-179.
PDB; 5A31; EM; 4.30 A; Q=29-173.
PDB; 5KHR; EM; 6.10 A; Q=1-179.
PDB; 5L9U; EM; 6.40 A; U=1-179.
PDBsum; 1I7K; -.
PDBsum; 4YII; -.
PDBsum; 5A31; -.
PDBsum; 5KHR; -.
PDBsum; 5L9U; -.
ProteinModelPortal; O00762; -.
SMR; O00762; -.
BioGrid; 116249; 68.
DIP; DIP-52725N; -.
IntAct; O00762; 10.
STRING; 9606.ENSP00000348838; -.
iPTMnet; O00762; -.
PhosphoSitePlus; O00762; -.
EPD; O00762; -.
PaxDb; O00762; -.
PeptideAtlas; O00762; -.
PRIDE; O00762; -.
ProteomicsDB; 12714; -.
ProteomicsDB; 48021; -.
TopDownProteomics; O00762-1; -. [O00762-1]
TopDownProteomics; O00762-3; -. [O00762-3]
DNASU; 11065; -.
Ensembl; ENST00000335046; ENSP00000335674; ENSG00000175063. [O00762-4]
Ensembl; ENST00000352551; ENSP00000333975; ENSG00000175063. [O00762-3]
Ensembl; ENST00000356455; ENSP00000348838; ENSG00000175063. [O00762-1]
Ensembl; ENST00000372568; ENSP00000361649; ENSG00000175063. [O00762-2]
GeneID; 11065; -.
KEGG; hsa:11065; -.
UCSC; uc002xpl.5; human. [O00762-1]
CTD; 11065; -.
DisGeNET; 11065; -.
EuPathDB; HostDB:ENSG00000175063.16; -.
GeneCards; UBE2C; -.
HGNC; HGNC:15937; UBE2C.
HPA; CAB011464; -.
HPA; CAB035990; -.
HPA; HPA034569; -.
HPA; HPA054975; -.
MIM; 605574; gene.
neXtProt; NX_O00762; -.
OpenTargets; ENSG00000175063; -.
PharmGKB; PA38057; -.
eggNOG; KOG0421; Eukaryota.
eggNOG; ENOG4111IGV; LUCA.
GeneTree; ENSGT00920000149047; -.
HOGENOM; HOG000233454; -.
HOVERGEN; HBG063308; -.
InParanoid; O00762; -.
KO; K06688; -.
OMA; AELWDKD; -.
OrthoDB; EOG091G0M7S; -.
PhylomeDB; O00762; -.
TreeFam; TF101116; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; O00762; -.
SIGNOR; O00762; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2C; human.
EvolutionaryTrace; O00762; -.
GeneWiki; UBE2C; -.
GenomeRNAi; 11065; -.
PRO; PR:O00762; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000175063; Expressed in 179 organ(s), highest expression level in oocyte.
CleanEx; HS_UBE2C; -.
ExpressionAtlas; O00762; baseline and differential.
Genevisible; O00762; HS.
GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; TAS:UniProtKB.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell cycle; Cell division; Complete proteome; Mitosis;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Transferase; Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692}.
CHAIN 2 179 Ubiquitin-conjugating enzyme E2 C.
/FTId=PRO_0000082560.
ACT_SITE 114 114 Glycyl thioester intermediate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 39 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045647.
VAR_SEQ 44 72 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045648.
VAR_SEQ 73 140 VYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNI
CLDILKEKWSALYDVRTILLSIQSLLG -> AVGSIRTSST
VCLLSGPRETQDSSKPLVWGLGWDMRLLLELTLQLFLQMP
(in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045649.
VARIANT 25 25 G -> D.
/FTId=VAR_007694.
MUTAGEN 114 114 C->S: Loss of function; inhibition of
cyclin-B degradation.
{ECO:0000269|PubMed:15558010,
ECO:0000269|PubMed:9122200}.
HELIX 30 45 {ECO:0000244|PDB:4YII}.
STRAND 50 54 {ECO:0000244|PDB:4YII}.
STRAND 61 68 {ECO:0000244|PDB:4YII}.
STRAND 78 84 {ECO:0000244|PDB:4YII}.
TURN 87 91 {ECO:0000244|PDB:4YII}.
STRAND 95 100 {ECO:0000244|PDB:4YII}.
STRAND 111 113 {ECO:0000244|PDB:4YII}.
HELIX 116 118 {ECO:0000244|PDB:4YII}.
TURN 119 121 {ECO:0000244|PDB:4YII}.
HELIX 128 140 {ECO:0000244|PDB:4YII}.
HELIX 150 155 {ECO:0000244|PDB:4YII}.
HELIX 159 172 {ECO:0000244|PDB:4YII}.
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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