UBE2L3

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 (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro. Several alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Sep 2009]

Ubiquitin Conjugating Enzyme E2 L3

Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.

Biological Process cell cycle phase transition Source:UniProtKB1 Publication
Biological Process cell population proliferation Source:UniProtKB1 Publication
Biological Process cellular response to glucocorticoid stimulus Source:UniProtKB1 Publication
Biological Process cellular response to steroid hormone stimulus Source:UniProtKB1 Publication
Biological Process positive regulation of protein targeting to mitochondrion Source:ParkinsonsUK-UCL1 Publication
Biological Process positive regulation of protein ubiquitination Source:ParkinsonsUK-UCL1 Publication
Biological Process positive regulation of ubiquitin-protein transferase activity Source:ParkinsonsUK-UCL1 Publication
Biological Process protein K11-linked ubiquitination Source:UniProtKB1 Publication
Biological Process protein modification process Source:UniProtKB1 Publication
Biological Process protein polyubiquitination Source:UniProtKB2 Publications
Biological Process protein ubiquitination Source:UniProtKB1 Publication
Biological Process regulation of DNA-templated transcription Source:UniProtKB1 Publication
Biological Process ubiquitin-dependent protein catabolic process Source:GO_Central1 Publication

Nucleus
Cytoplasm

Ubiquitinated. The alteration of UBE2L3 protein levels during the S-phase of the cell cycle is due to ubiquitin-dependent proteasomal degradation. Autoubiquitinated in vitro (PubMed:22496338).