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Reviewed, UniProtKB/Swiss-Prot O00762 (UBE2C_HUMAN)

Last modified June 16, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin-conjugating enzyme E2 C
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase C
    Ubiquitin carrier protein C
    UbcH10
Gene names
Name: UBE2C
Synonyms: UBCH10
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Required for the destruction of mitotic cyclins.

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from Experiment. Source: Reactome

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin catabolic process Ref.1

Inferred from direct assay. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle

Inferred from Experiment. Source: Reactome

phosphoinositide-mediated signaling

Non-traceable author statement. Source: UniProtKB

positive regulation of exit from mitosis Ref.1

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle

Inferred from Experiment. Source: Reactome

protein ubiquitination Ref.1

Inferred from direct assay. Source: UniProtKB

regulation of protein metabolic process

Inferred from electronic annotation. Source: InterPro

spindle organization

Non-traceable author statement. Source: UniProtKB

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

nucleoplasm

Inferred from Experiment. Source: Reactome

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity Ref.1

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179Ubiquitin-conjugating enzyme E2 C
PRO_0000082560

Sites

Active site1141Glycyl thioester intermediate

Natural variations

Natural variant251G → D
VAR_007694

Experimental info

Mutagenesis1141C → S: Inhibition of cyclin B degradation. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O00762-1 [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

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: 9122200] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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].
[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: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph and Uterus.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"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: 11927573] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

U73379 mRNA. Translation: AAB53362.1.
BT007300 mRNA. Translation: AAP35964.1.
AL050348 Genomic DNA. Translation: CAB66118.1.
BC007656 mRNA. Translation: AAH07656.1.
BC016292 mRNA. Translation: AAH16292.1.
BC050736 mRNA. Translation: AAH50736.1.
IPIIPI00013002.
RefSeqNP_008950.1.
NP_861515.1.
NP_861516.1.
NP_861517.1.
UniGeneHs.93002

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1I7KX-ray1.95A/B1-179[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO00762. 1 interaction.

Proteomic databases

PRIDEO00762.

Genome annotation databases

EnsemblENSG00000175063. Homo sapiens. [Contig view]
GeneID11065.
KEGGhsa:11065.

Organism-specific databases

GeneCardsGC20P043874.
H-InvDBHIX0015862.
HGNCHGNC:15937. UBE2C.
HPACAB011464.
MIM605574. gene.
PharmGKBPA38057.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO00762.
HOVERGENO00762.
OMAO00762. KEKWSAV.

Enzyme and pathway databases

BRENDA6.3.2.19. 247.
ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.

Gene expression databases

ArrayExpressO00762.
BgeeO00762.
CleanExHS_UBE2C.
GermOnlineENSG00000175063. Homo sapiens.

Family and domain databases

InterProIPR015582. Ubiquitin-conj_enz_E2_H10.
IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]
Gene3DG3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
PANTHERPTHR11621:SF26. UbcH10. 1 hit.
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
ProDomPD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00212. UBCc. 1 hit.
[Graphical view]
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio42051.
SOURCESearch...

Entry information

Entry nameUBE2C_HUMAN
AccessionPrimary (citable) accession number: O00762
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 20

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents