E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (  ). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets . The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 . E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes (, ). Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear . According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest . According to another report EIF4E2 ubiquitination leads to its subsequent degradation . Acts as the ligase involved in ISGylation of EIF4E2 . In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology .
Subcellular locations: Cytoplasm, Nucleus, Nucleus, Cajal body
Mainly cytoplasmic . Present in Lewy body .
Widely expressed.