UBE2L3
Domain
In contrast to other ubiquitin-conjugating enzymes E2, residues essential for lysine reactivity are absent: Pro and a His residues are present instead of an Asp and an Asp residues in positions 88 and 119, respectively.
Function
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, RNF31 and ARIH1, that function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates ubiquitination by the CUL9-RBX1 complex (PubMed:38605244). 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.
Pathway
Protein modification; protein ubiquitination.
Post-translational modifications
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).
Sequence Similarities
Belongs to the ubiquitin-conjugating enzyme family.
Tissue Specificity
Ubiquitous, with highest expression in testis.
Cellular localization
- Nucleus
- Cytoplasm
Alternative names
UBCE7, UBCH7, UBE2L3, Ubiquitin-conjugating enzyme E2 L3, E2 ubiquitin-conjugating enzyme L3, L-UBC, UbcH7, Ubiquitin carrier protein L3, Ubiquitin-conjugating enzyme E2-F1, Ubiquitin-protein ligase L3