Ubiquitin specific protease 11 (USP11)

Ubiquitin specific protease 11 (USP11) is a cysteine protease enzyme that functions as a deubiquitinase, specifically removing ubiquitin from proteins to regulate their stability, localization, and activity[1][2][3][4]. USP11 is involved in key cellular processes including DNA damage repair, cell cycle control, and chromatin remodeling by deubiquitinating target proteins such as histone H2A, histone H2B, BRCA2, PALB2, p21, and XPC[3][4]. It plays a pivotal role in genomic stability, cell survival, and response to genotoxic stress. Dysregulation or overexpression of USP11 has been implicated in several cancers, where it may promote tumor progression or serve as a prognostic biomarker, especially in ERα-positive breast cancer[5]. USP11 is therefore considered a promising therapeutic target in oncology and potentially other diseases involving altered protein ubiquitination[4].

Other names

ubiquitin-specific protease 11ubiquitin specific peptidase 11

Inhibition of deubiquitinase activity leads to impaired DNA repair and altered cell proliferation