Ubiquitin carboxyl-terminal hydrolase 13 (USP13)

Ubiquitin carboxyl-terminal hydrolase 13 (USP13) is a deubiquitinating enzyme of the USP (ubiquitin-specific protease) family, functioning as a cysteine protease that removes ubiquitin moieties from target proteins, thereby regulating protein degradation, stability, and various signaling pathways[1][2][4][8]. It is ubiquitously expressed in human tissues, with enrichment in immune cells such as T cells[1]. USP13 plays critical roles in processes including cell cycle progression, apoptosis, autophagy, mitochondrial metabolism, and DNA damage response[2][3]. Its dysregulation is implicated in multiple human diseases, particularly cancer (e.g., ovarian, lung, colorectal cancers, glioblastoma, melanoma), where it may act as an oncogene by stabilizing substrates such as MCL1, ACLY, and MITF, or as a context-dependent regulator[1][2][3][4]. USP13 is actively investigated as a potential therapeutic target, although no specific drugs have yet been approved for its inhibition.

Other names

Isopeptidase T-3ubiquitin-specific protease 13deubiquitylating enzyme 13

Inhibition or modulation of deubiquitinase activity, leading to altered ubiquitin-mediated protein degradation and stabilization pathways