UCH-L5
UCH-L5, commonly known as UCH37, is a ubiquitin C-terminal hydrolase distinguished by a C-terminal DEUBAD extension beyond its catalytic UCH domain. It is recruited to the 19S regulatory particle of the 26S proteasome through the receptor subunit ADRM1 (RPN13), where it trims ubiquitin chains from incoming substrates and can act as a checkpoint that delays or accelerates their proteasomal degradation. The enzyme also resides in the INO80 chromatin-remodeling complex, linking deubiquitination to genome maintenance. Elevated UCH-L5 expression has been documented in multiple cancers, and small-molecule inhibitors of this protease are being explored as anticancer agents.
