Ubiquitin-conjugating enzyme E2 R2 (UBE2R2)

Ubiquitin-conjugating enzyme E2 R2 (UBE2R2) is a member of the E2 ubiquitin-conjugating enzyme family, functioning in the ubiquitin-proteasome system for targeted protein degradation[1][3][4]. UBE2R2 receives ubiquitin from an E1 ubiquitin-activating enzyme and catalyzes its covalent attachment to target proteins, typically in cooperation with E3 ubiquitin ligases[1][3][4]. In vitro, UBE2R2 can facilitate both monoubiquitination and lysine 48 (K48)-linked polyubiquitination, contributing to proteasomal degradation pathways[1][4]. CK2-dependent phosphorylation of UBE2R2 regulates its interaction with β-TrCP and enhances β-catenin degradation, implicating it in Wnt signaling and cell growth regulation[1][3][4]. Diseases associated with UBE2R2 dysregulation include various cancers and spinal muscular atrophy, and it may also play a role in viral infections such as herpes simplex[4]. No drugs are currently known to directly target UBE2R2 in clinical use.

Other names

UBE2R2CDC34BUBC3BFLJ20419MGC10481E2 ubiquitin-conjugating enzyme R2Ubiquitin carrier protein R2Ubiquitin-conjugating enzyme E2-CDC34BUbiquitin-protein ligase R2ubiquitin conjugating enzyme E2R 2ubiquitin-conjugating enzyme UBC3B

Inhibitors or modulators would affect protein ubiquitination processes; no clinically approved drugs identified as directly targeting this enzyme