Ubiquitin specific peptidase 17-like family member 12 (USP17L12)

Ubiquitin specific peptidase 17-like family member 12 (USP17L12) is a member of the USP17 family of deubiquitinating enzymes, characterized by cysteine-type protease activity that removes ubiquitin from conjugated proteins. This enzyme is active in the cytosol and nucleus, and is predicted to be involved in regulating protein stability, cell cycle progression (especially at G1/S and G2/M phases), apoptosis, and cell migration. The USP17 family is rapidly induced in response to inflammatory chemokines and cytokines, facilitating cytoskeletal rearrangements crucial for chemotaxis and cellular motility. USP17L12 is a therapeutic target candidate in cancer, immune, and infectious diseases because of its regulatory roles; its inhibition may impact cell proliferation, migration, and apoptosis, all central to tumorigenesis and inflammation. While multiple USP17 family paralogs exist, USP17L12 is specifically encoded on human chromosome 4, and shares structural features with other deubiquitinating enzymes but with unique sequence identifiers and regulatory characteristics. No specific drugs or biomarkers for USP17L12 are currently in clinical use or described in the literature.

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 12USP17L12UL17C (protein)

Drugs targeting USP17 proteins would likely act as enzyme inhibitors, blocking deubiquitinase activity to modulate cell cycle, migration, or apoptosis