Ubiquitin carboxyl-terminal hydrolase 50 (USP50)

Ubiquitin carboxyl-terminal hydrolase 50 (USP50) is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes, though it is classified as a non-protease homolog in humans due to lack of catalytic acidic residues and little or no canonical deubiquitinating activity[1][3][5]. USP50 is a chromatin-associated protein that binds ubiquitin conjugates and is crucial for proper coordination of DNA replication, particularly by promoting correct selection and localization of helicases (notably WRN, RECQL4/5) and nucleases (FEN1, DNA2) at replication forks, supporting ongoing replication, maintaining telomere integrity, and aiding fork restart following genotoxic stress[1][2]. It also has regulatory roles in cell cycle progression (G2/M checkpoint), inflammasome assembly, and IL-1β production[3][5][7]. Loss or dysfunction of USP50 leads to replication stress, telomere instability, and has implications in cancer, premature aging, and hereditary genomic instability disorders[1][2][3]. No specific drugs are reported to directly target USP50 as of current knowledge.

Other names

Ubiquitin-specific peptidase 50USP50Ubiquitin carboxyl-terminal hydrolase 50Ubiquitin specific protease 50UBP50Inactive ubiquitin carboxyl-terminal hydrolase 50Inactive ubiquitin-specific peptidase 50