Ubiquitin-conjugating enzyme E2 B (UBE2B)

Ubiquitin-conjugating enzyme E2 B (UBE2B) is an essential E2 ubiquitin-conjugating enzyme involved in the transfer of ubiquitin from E1 activating enzymes to target proteins via E3 ligases[1][3][4][5]. This enzyme is critical for post-replicative DNA damage repair, partnering with E3 ligases such as RAD18 and MDM2 to mediate histone and tumor suppressor protein (e.g., p53) ubiquitination, facilitating translesion synthesis and homologous recombination[1][3][4]. UBE2B plays a key role in maintaining genomic integrity, cellular stress responses, and normal sperm development. Aberrant expression or dysfunction of UBE2B contributes to oncogenesis, chemoresistance, and infertility. The enzyme is highly conserved across mammals and regulated by post-translational modifications and specific structural motifs. UBE2B is a potential therapeutic target, particularly in cancer, but clinical drug development is challenged by the risk of disrupting normal DNA repair and spermatogenesis[1][3][4].

Other names

RAD6BUBCH1HR6BhHR6BUBC2HHR6BE2 ubiquitin-conjugating enzyme BRAD6 homolog BUbiquitin carrier protein BUbiquitin-conjugating enzyme E2-17 kDaUbiquitin-protein ligase BE2-17kDaE2 ubiquitin-conjugating enzyme B (RAD6 homolog)

Inhibition of UBE2B or its complex with E3 ligases can impair ubiquitin-mediated protein degradation, sensitizing tumor cells to DNA-damaging agents and chemotherapeutics[1]. Targeting UBE2B can shift the balance of DNA repair from error-prone to error-free mechanisms, potentially limiting tumor cell survival under genotoxic stress.