Ubiquitin-conjugating enzyme E2 V2 (UBE2V2)

Ubiquitin-conjugating enzyme E2 V2 (UBE2V2) is a member of the E2 family of ubiquitin-conjugating enzymes, also known as ubiquitin-carrier enzymes. UBE2V2 operates as part of the ubiquitination cascade, specifically catalyzing the transfer of ubiquitin from the E1 activating enzyme to various substrates, often in cooperation with an E3 ubiquitin ligase. UBE2V2, while lacking a catalytic cysteine, forms a heterodimer with another E2 enzyme (like UBE2N/UBE2V1) to catalyze Lys63-linked polyubiquitin chain formation—a process important in DNA repair and cell signaling. Dysfunction or dysregulation of UBE2V2 has been associated with human diseases such as cancer and neurodegenerative disorders. Ubiquitin-conjugating enzyme E2 V2 and its E2 enzyme partners are emerging as potential drug targets in the ubiquitin–proteasome system, but currently, no clinically approved drugs specifically target UBE2V2. Therapeutic targeting faces the challenge of selectivity since the active site and “backside” pockets of E2 enzymes are relatively shallow and similar across family members, complicating the design of specific, potent inhibitors.

Other names

Ubiquitin-conjugating enzyme E2 variant 2UBE2V2UEV-2CROC1

Inhibitors of E2 enzymes can block protein ubiquitination, interfering with proteasomal degradation or modulating signaling cascades