Ubiquitin specific peptidase 7 (USP7)

Ubiquitin specific peptidase 7 (USP7) is a deubiquitinating enzyme that removes ubiquitin moieties from specific protein substrates, thereby regulating their stability and function. USP7 contains several structural domains, including a N-terminal TRAF-like domain for substrate recognition, a central catalytic domain, and multiple C-terminal ubiquitin-like domains that mediate interactions with various target proteins[1][3][5]. USP7 is essential for modulating pathways such as the p53 tumor suppressor axis, DNA damage response, and multiple epigenetic processes through histone deubiquitination[3][4][5]. Aberrant USP7 activity is linked to tumorigenesis (via p53/MDM2 regulation), immune modulation, and even behaviors associated with drug addiction[1][4][7]. Targeted inhibition of USP7 has emerged as a promising anticancer approach due to its central role in maintaining protein homeostasis and regulating cell fate decisions[1][3][7].

Other names

Ubiquitin-specific protease 7Herpes virus-associated ubiquitin-specific protease (HAUSP)

Inhibition of deubiquitinase activity, leading to accumulation of ubiquitinated target proteins and altered stability of substrates such as p53 and MDM2[1][3][7].