UBE2D2

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, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Two alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms. [provided by RefSeq]

ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection. Essential for viral activation of IRF3.

Biological Process protein autoubiquitination Source:ParkinsonsUK-UCL1 Publication
Biological Process protein K48-linked ubiquitination Source:UniProtKB1 Publication
Biological Process protein modification process Source:ProtInc1 Publication
Biological Process protein polyubiquitination Source:BHF-UCL1 Publication
Biological Process protein ubiquitination Source:ParkinsonsUK-UCL2 Publications
Biological Process ubiquitin-dependent protein catabolic process Source:ProtInc1 Publication

cytosol
extracellular exosome
nucleoplasm
nucleus
protein-containing complex
ubiquitin ligase complex