UBE2W Activators

UBE2W, or ubiquitin-conjugating enzyme E2 W, is a member of the E2 ubiquitin-conjugating enzyme family and plays a unique role in the ubiquitination process, whereby ubiquitin, a small regulatory protein, is attached to substrates. This post-translational modification can signal for protein degradation, alter protein function, or affect protein localization.The UBE2W gene encodes the UBE2W enzyme in humans. Unlike other E2 enzymes that typically attach ubiquitin to the ε-amino group of lysine residues on substrate proteins, UBE2W is known to have the distinctive capability to attach ubiquitin to the N-terminus of substrate proteins, a process known as N-terminal ubiquitination. This form of ubiquitination can mark proteins for degradation by the proteasome, a protein complex responsible for degrading unneeded or damaged proteins by proteolysis, which is a significant cellular mechanism for regulating protein levels and function.

N-terminal ubiquitination by UBE2W is particularly important because it widens the diversity of ubiquitination's impact on cellular processes. UBE2W's activity is implicated in the regulation of various cellular processes, including the DNA damage response, signal transduction pathways, and the cell cycle.Altered function or dysregulation of UBE2W has been associated with several human diseases, including cancer. The enzyme's role in modulating protein stability and function makes it a potential target for intervention, and understanding its activity is important for the development of drugs that can manipulate ubiquitination pathways.