Ubiquitin-conjugating enzyme E2 L3 (UBE2L3)

Ubiquitin-conjugating enzyme E2 L3 (UBE2L3) is a member of the E2 family of ubiquitin-conjugating enzymes, which function in the cellular ubiquitination cascade responsible for tagging proteins for proteasomal degradation. UBE2L3 acts as a central mediator in this process, specifically transferring ubiquitin from E1-activating enzymes to substrate-targeting E3 ligases, with a particular preference for working with HECT-type and RBR family E3 ligases. It regulates protein homeostasis, cell cycle progression (notably during the G1/S transition), NF-κB precursor ubiquitination, and DNA double-strand break repair pathway choice. Genomic studies have implicated UBE2L3 in several autoimmune disorders and its activity is crucial for proper immune function and viral clearance. Alteration in UBE2L3 expression or function has been linked to disease, including cancer susceptibility through its impact on DNA repair, and autoimmune predisposition through changes in protein ubiquitination pathways. While no specific approved drugs directly target UBE2L3, its role in cancer biology and autoimmunity makes it a promising candidate for future therapeutic intervention[1][2][3].

Other names

UBCE7UBCH7E2 ubiquitin-conjugating enzyme L3L-UBCUbcH7Ubiquitin carrier protein L3Ubiquitin-conjugating enzyme E2-F1Ubiquitin-protein ligase L3E2-F1UbcM4

Small molecules may inhibit UBE2L3-mediated ubiquitin transfer, disrupting downstream protein degradation and cell regulatory processes. Targeted depletion or inhibition can sensitize cancer cells by promoting error-prone DNA repair and apoptosis[1].