Ubiquitin-conjugating enzyme E2 U (UBE2U)

Ubiquitin-conjugating enzyme E2 U (UBE2U) is a member of the E2 family of enzymes, which are central to the ubiquitin-proteasome pathway responsible for tagging proteins for degradation or signaling through the covalent attachment of ubiquitin[4][3]. UBE2U consists of a typical UBC domain and a unique C-terminal extension[2]. Like other E2 enzymes, it acts as an intermediate, accepting activated ubiquitin from E1 enzymes and transferring it to substrate proteins, usually in conjunction with a ubiquitin E3 ligase[4][2]. UBE2U is predicted to participate in DNA repair and proteasome-mediated protein catabolic processes[3]. It is highly connected to multiple E3 ligases, suggesting a broad role in regulating ubiquitin-mediated processes, although detailed functional or disease links remain to be clarified[2]. UBE2U appears to be expressed with some tissue specificity, especially in the urogenital tract[2]. No drugs directly targeting UBE2U are currently known, and its biomarker or direct clinical safety relevance is not established.

Other names

UBE2UMGC35130E2 ubiquitin-conjugating enzyme UUbiquitin carrier protein UUbiquitin-protein ligase Utesticular tissue protein Li 216

Inhibitors or modulators would generally act by blocking the formation of E2~ubiquitin thioester intermediates or disrupting E2–E3 enzyme complexes