Aliases for UBE2C Gene
- Ubiquitin Conjugating Enzyme E2 C 2 3 5
- UBCH10 2 3 4
- (E3-Independent) E2 Ubiquitin-Conjugating Enzyme C 3 4
- Ubiquitin-Conjugating Enzyme E2 C 3 4
- E2 Ubiquitin-Conjugating Enzyme C 3 4
- Ubiquitin-Protein Ligase C 3 4
- Mitotic-Specific Ubiquitin-Conjugating Enzyme 3
- Cyclin-Selective Ubiquitin Carrier Protein 3
External Ids for UBE2C Gene
Previous GeneCards Identifiers for UBE2C Gene
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin-protein ligases. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The encoded protein is required for the destruction of mitotic cyclins and for cell cycle progression, and may be involved in cancer progression. Multiple transcript variants encoding different isoforms have been found for this gene. Pseudogenes of this gene have been defined on chromosomes 4, 14, 15, 18, and 19. [provided by RefSeq, Aug 2013]
GeneCards Summary for UBE2C Gene
UBE2C (Ubiquitin Conjugating Enzyme E2 C) is a Protein Coding gene. Diseases associated with UBE2C include Methotrexate-Associated Lymphoproliferation and Complement Component 7 Deficiency. Among its related pathways are Cellular Senescence (REACTOME) and Class I MHC mediated antigen processing and presentation. Gene Ontology (GO) annotations related to this gene include ligase activity and ubiquitin protein ligase binding. An important paralog of this gene is UBE2B.
UniProtKB/Swiss-Prot Summary for UBE2C Gene
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.