Overview:

USP11 (ubiquitin carboxyl-terminal hydrolase 11) is a member of the ubiquitin specific proteases family (USPs) and is a protease that functions in the removal of conjugated ubiquitin from target proteins and polyubiquitin chains. The enzyme cleaves preferentially 'Lys-6' and 'Lys-63'-linked ubiquitin chains and is involved in regulating pathways that lead to NF-kappa-B activation by regulating IκB kinase α (1). USP11 also binds to p21, a cyclin-dependent kinase inhibitor and plays an important role in regulating cell-cycle progression and DNA damage responses.

Gene Aliases:

UHX1

Genbank Number:

NM_004651

References:

1. Yamaguchi, T. et al. The deubiquitinating enzyme USP11 controls an IkappaB kinase alpha (IKKalpha)-p53 signaling pathway in response to tumor necrosis factor alpha (TNFalpha). J Biol Chem. 282(47):33943-8, 2007.

2. Tanggang, D. et al: Deubiquitylation and stabilization of p21 by USP11 is critical for cell-cycle progression and DNA damage responses. Proceedings of the National Academy of Sciences 115(18): 4678-4683, 2018.