O00762 (UBE2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 125.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 179 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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.5 Ref.6 Ref.8 Ref.9 Ref.10 |
| Catalytic activity | ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. Ref.6 |
| Pathway | |
| 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||||||||||||||||||||||||
| Chain | 2 – 179 | 178 | Ubiquitin-conjugating enzyme E2 C | PRO_0000082560 | ||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Active site | 114 | 1 | Glycyl thioester intermediate | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.7 | |||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||
| Natural variant | 25 | 1 | G → D. | VAR_007694 | ||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Mutagenesis | 114 | 1 | C → S: Loss of function; inhibition of cyclin-B degradation. Ref.1 Ref.5 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 31 – 45 | 15 | ||||||||||||||||||||||||||||
| Beta strand | 50 – 55 | 6 | ||||||||||||||||||||||||||||
| Beta strand | 58 – 68 | 11 | ||||||||||||||||||||||||||||
| Beta strand | 78 – 84 | 7 | ||||||||||||||||||||||||||||
| Turn | 87 – 91 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 95 – 100 | 6 | ||||||||||||||||||||||||||||
| Helix | 116 – 118 | 3 | ||||||||||||||||||||||||||||
| Turn | 119 – 121 | 3 | ||||||||||||||||||||||||||||
| Helix | 128 – 140 | 13 | ||||||||||||||||||||||||||||
| Helix | 150 – 155 | 6 | ||||||||||||||||||||||||||||
| Helix | 159 – 171 | 13 | ||||||||||||||||||||||||||||
Sequences
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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. 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] | "Autonomous regulation of the anaphase-promoting complex couples mitosis to S-phase entry." Rape M., Kirschner M.W. Nature 432:588-595(2004) [PubMed: 15558010] [Abstract] Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF CYS-114. |
| [6] | "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: 18485873] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. |
| [7] | "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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [8] | "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: 19820702] [Abstract] Cited for: FUNCTION. |
| [9] | "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: 19822757] [Abstract] Cited for: FUNCTION. |
| [10] | "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: 20061386] [Abstract] Cited for: FUNCTION. |
| [11] | "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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [12] | "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 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U73379 mRNA. Translation: AAB53362.1. BT007300 mRNA. Translation: AAP35964.1. AL050348 Genomic DNA. No translation available. BC007656 mRNA. Translation: AAH07656.1. BC016292 mRNA. Translation: AAH16292.1. BC050736 mRNA. Translation: AAH50736.1. | ||||||||||||
| IPI | IPI00013002. | ||||||||||||
| RefSeq | NP_008950.1. NM_007019.2. NP_861515.1. NM_181799.1. NP_861516.1. NM_181800.1. NP_861517.1. NM_181801.2. | ||||||||||||
| UniGene | Hs.93002. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | O00762. | ||||||||||||
| SMR | O00762. Positions 30-175. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | O00762. 7 interactions. | ||||||||||||
| STRING | O00762. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | O00762. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000356455; ENSP00000348838; ENSG00000175063. | ||||||||||||
| GeneID | 11065. | ||||||||||||
| KEGG | hsa:11065. | ||||||||||||
| UCSC | uc002xpm.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 11065. | ||||||||||||
| GeneCards | GC20P044442. | ||||||||||||
| H-InvDB | HIX0015862. | ||||||||||||
| HGNC | HGNC:15937. UBE2C. | ||||||||||||
| HPA | CAB011464. CAB035990. | ||||||||||||
| MIM | 605574. gene. | ||||||||||||
| neXtProt | NX_O00762. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG13072. | ||||||||||||
| HOGENOM | HBG756483. | ||||||||||||
| HOVERGEN | HBG063308. | ||||||||||||
| InParanoid | O00762. | ||||||||||||
| OMA | FHPNVDT. | ||||||||||||
| OrthoDB | EOG4FN4JS. | ||||||||||||
| PhylomeDB | O00762. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Reactome | REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_6900. Immune System. REACT_8017. APC-Cdc20 mediated degradation of Nek2A. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | O00762. | ||||||||||||
| Bgee | O00762. | ||||||||||||
| CleanEx | HS_UBE2C. | ||||||||||||
| Genevestigator | O00762. | ||||||||||||
| GermOnline | ENSG00000175063. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit. | ||||||||||||
| KO | K06688. | ||||||||||||
| Pfam | PF00179. UQ_con. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF54495. UBQ-conjugat/RWD-like. 1 hit. | ||||||||||||
| PROSITE | PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 42051. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | UBE2C_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O00762 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| 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 |

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