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O00762 (UBE2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 C

EC=6.3.2.19
Alternative name(s):
UbcH10
Ubiquitin carrier protein C
Ubiquitin-protein ligase C
Gene names
Name:UBE2C
Synonyms:UBCH10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. Ref.7

Pathway

Protein modification; protein ubiquitination. Ref.7

Subunit structure

Component of the APC/C complex.

Post-translational modification

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.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of anaphase-promoting complex activity

Traceable author statement PubMed 17443180. Source: UniProtKB

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

cell cycle

Non-traceable author statement PubMed 15504738. Source: UniProtKB

cyclin catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

exit from mitosis

Inferred from mutant phenotype Ref.10. Source: UniProtKB

free ubiquitin chain polymerization

Inferred from direct assay Ref.10. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic spindle assembly checkpoint

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Non-traceable author statement PubMed 15504738. Source: UniProtKB

positive regulation of exit from mitosis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein K11-linked ubiquitination

Inferred from direct assay Ref.7Ref.10Ref.11. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from direct assay Ref.11. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

spindle organization

Non-traceable author statement PubMed 15504738. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.7Ref.1. Source: UniProtKB

   Cellular_componentanaphase-promoting complex

Inferred from direct assay Ref.7Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.10. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00762-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00762-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O00762-3)

The sequence of this isoform differs from the canonical sequence as follows:
     44-72: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: O00762-4)

The sequence of this isoform differs from the canonical sequence as follows:
     73-140: VYEDLRYKLS...ILLSIQSLLG → AVGSIRTSST...LTLQLFLQMP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 179178Ubiquitin-conjugating enzyme E2 C
PRO_0000082560

Sites

Active site1141Glycyl thioester intermediate

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.13
Modified residue31Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 3939Missing in isoform 2.
VSP_045647
Alternative sequence44 – 7229Missing in isoform 3.
VSP_045648
Alternative sequence73 – 14068VYEDL…QSLLG → AVGSIRTSSTVCLLSGPRET QDSSKPLVWGLGWDMRLLLE LTLQLFLQMP in isoform 4.
VSP_045649
Natural variant251G → D.
VAR_007694

Experimental info

Mutagenesis1141C → S: Loss of function; inhibition of cyclin-B degradation. Ref.1 Ref.6

Secondary structure

...................... 179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 0B6F58A1F0665D9A

FASTA17919,652
        10         20         30         40         50         60 
MASQNRDPAA TSVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI SAFPESDNLF 

        70         80         90        100        110        120 
KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT PCYHPNVDTQ GNICLDILKE 

       130        140        150        160        170 
KWSALYDVRT ILLSIQSLLG EPNIDSPLNT HAAELWKNPT AFKKYLQETY SKQVTSQEP 

« Hide

Isoform 2 [UniParc].

Checksum: 194F276AD75D5168
Show »

FASTA14015,765
Isoform 3 [UniParc].

Checksum: 5410B7BA11DFC35E
Show »

FASTA15016,676
Isoform 4 [UniParc].

Checksum: D8F52001401888DA
Show »

FASTA16117,373

References

« Hide 'large scale' references
[1]"Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 blocks cells in metaphase."
Townsley F.M., Aristarkhov A., Beck S., Hershko A., Ruderman J.V.
Proc. Natl. Acad. Sci. U.S.A. 94:2362-2367(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-114.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
Tissue: Lung adenocarcinoma, Lymph, Melanoma, Teratocarcinoma and Uterus.
[6]"Autonomous regulation of the anaphase-promoting complex couples mitosis to S-phase entry."
Rape M., Kirschner M.W.
Nature 432:588-595(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF CYS-114.
[7]"Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit."
Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P., Pines J., Venkitaraman A.R.
Nat. Cell Biol. 11:1363-1369(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Identification of a physiological E2 module for the human anaphase-promoting complex."
Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M.
Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
David Y., Ziv T., Admon A., Navon A.
J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10."
Lin Y., Hwang W.C., Basavappa R.
J. Biol. Chem. 277:21913-21921(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73379 mRNA. Translation: AAB53362.1.
BT007300 mRNA. Translation: AAP35964.1.
AL050348 Genomic DNA. No translation available.
CH471077 Genomic DNA. Translation: EAW75804.1.
CH471077 Genomic DNA. Translation: EAW75805.1.
CH471077 Genomic DNA. Translation: EAW75806.1.
CH471077 Genomic DNA. Translation: EAW75807.1.
BC007656 mRNA. Translation: AAH07656.1.
BC016292 mRNA. Translation: AAH16292.1.
BC050736 mRNA. Translation: AAH50736.1.
BI858659 mRNA. No translation available.
BM556795 mRNA. No translation available.
BU844974 mRNA. No translation available.
CCDSCCDS13370.1. [O00762-1]
CCDS13371.1. [O00762-4]
CCDS13372.1. [O00762-3]
CCDS13374.1. [O00762-2]
RefSeqNP_001268670.1. NM_001281741.1.
NP_001268671.1. NM_001281742.1.
NP_008950.1. NM_007019.3. [O00762-1]
NP_861515.1. NM_181799.2. [O00762-4]
NP_861516.1. NM_181800.2. [O00762-3]
NP_861517.1. NM_181801.3. [O00762-2]
UniGeneHs.93002.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7KX-ray1.95A/B1-179[»]
ProteinModelPortalO00762.
SMRO00762. Positions 30-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116249. 65 interactions.
DIPDIP-52725N.
IntActO00762. 8 interactions.
STRING9606.ENSP00000348838.

PTM databases

PhosphoSiteO00762.

Proteomic databases

MaxQBO00762.
PaxDbO00762.
PRIDEO00762.

Protocols and materials databases

DNASU11065.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335046; ENSP00000335674; ENSG00000175063. [O00762-4]
ENST00000352551; ENSP00000333975; ENSG00000175063. [O00762-3]
ENST00000356455; ENSP00000348838; ENSG00000175063. [O00762-1]
ENST00000372568; ENSP00000361649; ENSG00000175063. [O00762-2]
ENST00000405520; ENSP00000385878; ENSG00000175063. [O00762-2]
GeneID11065.
KEGGhsa:11065.
UCSCuc002xpl.3. human.
uc002xpm.3. human. [O00762-1]

Organism-specific databases

CTD11065.
GeneCardsGC20P044442.
HGNCHGNC:15937. UBE2C.
HPACAB011464.
CAB035990.
HPA054975.
MIM605574. gene.
neXtProtNX_O00762.
PharmGKBPA38057.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233454.
HOVERGENHBG063308.
InParanoidO00762.
KOK06688.
OMAAELWDKD.
OrthoDBEOG7M0NTH.
PhylomeDBO00762.
TreeFamTF101116.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
SignaLinkO00762.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressO00762.
BgeeO00762.
CleanExHS_UBE2C.
GenevestigatorO00762.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO00762.
GeneWikiUBE2C.
GenomeRNAi11065.
NextBio42051.
PROO00762.
SOURCESearch...

Entry information

Entry nameUBE2C_HUMAN
AccessionPrimary (citable) accession number: O00762
Secondary accession number(s): A6NP33, E1P5N7, G3XAB7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM