Ubiquitin-conjugating enzyme E2 G1 (UBE2G1)

Ubiquitin-conjugating enzyme E2 G1 (UBE2G1) is an E2 class enzyme that catalyzes the covalent attachment of ubiquitin to substrate proteins, a crucial step in ubiquitin-mediated proteasomal degradation[2][4]. It acts downstream of ubiquitin-activating enzyme E1 and collaborates with E3 ubiquitin ligases, being specifically involved in catalyzing Lys-48 and Lys-63 linked polyubiquitin chains, which typically target proteins for degradation[2]. UBE2G1 plays an essential role in the turnover of regulatory proteins involved in cell cycle, apoptosis, immune response, and protein quality control processes[1][2][3]. In cancer biology and therapeutic protein degradation, UBE2G1 is critical for the action of cereblon modulating agents (e.g., lenalidomide, pomalidomide) by promoting degradation of neomorphic substrates via K48-linked polyubiquitination, and its deficiency confers drug resistance in targeted degradation therapies[1]. UBE2G1 is also highly conserved across eukaryotes and interacts with proteins such as NEDD8, suggesting broader regulatory roles in cellular homeostasis and immune responses[3].

Other names

E2 ubiquitin-conjugating enzyme G1UBE2GUBC7E217Kubiquitin carrier protein G1ubiquitin-protein ligase G1ubiquitin-conjugating enzyme E2G 1

Drugs induce target protein degradation via ubiquitination and subsequent proteasomal elimination (as mediated by cereblon modulating agents and the CRL4^CRBN^ E3 ligase complex with UBE2G1)