Ubiquitin-conjugating enzyme E2 variant 1 (UBE2V1)

Ubiquitin-conjugating enzyme E2 variant 1 (UBE2V1) is a member of the E2 family of ubiquitin-conjugating enzymes that is distinct in lacking the conserved catalytic cysteine required for canonical ubiquitin transfer activity[1][3][4]. Instead, UBE2V1 forms a heterodimer with UBE2N (also known as UBC13), enabling the synthesis of K63-linked polyubiquitin chains, which play critical roles in signaling rather than proteasomal degradation[3][4]. K63-linked polyubiquitination catalyzed by UBE2V1-containing complexes regulates diverse biological processes, including activation of NF-κB and MAPK pathways, DNA repair, and the cellular response to stress and protein aggregation[3][4][2]. UBE2V1 activity is linked to the pathogenesis of cancer, inflammatory responses, heart disease, age-related decline in oocyte quality, and developmental defects, with changes in its expression or function contributing to altered proteostasis, impaired DNA repair, and inappropriate immune activation[2][3][4]. UBE2V1 is considered a potential therapeutic target, particularly in conditions characterized by aberrant ubiquitination and protein aggregation[4].

Other names

UBE2V1UBE2VUEV1CROC1UEV-1UEV1ACROC-1CIR1P/OKcl.19TRAF6-regulated IKK activator 1 beta Uev1A

Drugs or small molecules that inhibit the UBE2V1-UBE2N complex can reduce K63-linked polyubiquitination, impacting NF-κB signaling, protein aggregate formation, and cell survival in cancers and heart disease[4][3].