Ubiquitin-conjugating enzyme E2 R1 (UBE2R1)

Ubiquitin-conjugating enzyme E2 R1 (UBE2R1, also known as CDC34) is an E2 class enzyme in the ubiquitin-proteasome pathway, responsible for transferring ubiquitin from E1 ubiquitin-activating enzyme onto substrates via E3 ubiquitin ligases. It is especially important for catalyzing polyubiquitination of proteins involved in cell cycle progression and proteasomal degradation, notably as a core component of the SCF (Skp, Cullin, F-box-containing) E3 ligase complexes. UBE2R1/CDC34 has a catalytic core typical of E2 enzymes and possesses C-terminal extensions that enable specific interaction with certain E3 ligases like the SCF complex. Its regulation is critical for cell cycle control, proliferation, and protein homeostasis, and aberrant activity or expression is associated with oncogenic phenotypes.

Other names

CDC34UBE2R1UBc3E2 ubiquitin-conjugating enzyme R1

Drugs targeting the ubiquitin-proteasome system typically inhibit proteasome-mediated degradation, leading to accumulation of ubiquitinated proteins and induction of apoptosis; E2-specific targeting would theoretically block ubiquitin transfer from E1 to E3 enzymes, but clinically relevant inhibitors for UBE2R1 are not established