UBE2R1/CDC34 Protein, Human (sf9, His, StrepII)

UBE2R1, a pivotal component in the ubiquitin-proteasome system, functions as an E2 ubiquitin-conjugating enzyme, adept at accepting ubiquitin from the E1 complex and catalyzing its covalent attachment to various protein substrates. In vitro, UBE2R1 demonstrates its catalytic prowess by efficiently mediating 'Lys-48'-linked polyubiquitination reactions. Collaborating with specific E3 ligase complexes, such as SCF(FBXW11) and SCF(SKP2), UBE2R1 plays a crucial role in orchestrating the ubiquitin-dependent degradation of key regulatory proteins. Notably, it participates in the polyubiquitination of NFKBIA, leading to its subsequent proteasomal degradation, thereby influencing processes related to cellular proliferation. UBE2R1's involvement extends to the regulation of cell cycle progression, targeting proteins like WEE1 kinase and beta-catenin for ubiquitination and degradation. Moreover, it becomes a target itself for the human herpes virus 1 protein ICP0, establishing dynamic interactions with proteasomes and contributing to the intricate landscape of cellular protein homeostasis.