Ubiquitin carboxyl-terminal hydrolase 25 (USP25)

Ubiquitin carboxyl-terminal hydrolase 25 (USP25) is a member of the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin moieties conjugated to substrate proteins, thus regulating their stability and function[6][7][8]. As a thiol-dependent hydrolase, it removes ubiquitin from proteins marked for degradation, thereby controlling protein turnover and numerous cellular processes such as inflammation and signal transduction[6][7][8]. USP25 is implicated in various disease states, notably cancer and inflammatory conditions, due to its regulatory role in key proteostasis and cell signaling pathways[7]. Currently, while USP25 is considered a therapeutic target and is under investigation for drug development, no standard clinical inhibitors are established.

Other names

USP25UBP25

Inhibition of deubiquitinating activity (by small molecules or experimental agents; not standard clinical drugs in current references)