USP11

Description

The USP11 (ubiquitin specific peptidase 11) is a protein-coding gene located on chromosome X.

USP11, also known as Ubiquitin carboxyl-terminal hydrolase 11, is an enzyme encoded by the USP11 gene in humans. It belongs to the Ubiquitin specific proteases family (USPs), a sub-family of Deubiquitinating enzymes (DUBs). USPs are multi-domain proteases and belong to the C19 cysteine proteases subfamily. The catalytic domain is the largest and contains the catalytic triad, crucial for its function. The catalytic domain also has sequences with unknown roles. USP11 is a 963 amino acid protein with a molecular weight of approximately 109.8 kDa and a pI of ~5.28. It shares significant homology with USP15 and forms the DU subfamily with USP4. However, USP11 is the most distant member, with lower homology to USP15 compared to USP4.

USP11, also known as Ubiquitin carboxyl-terminal hydrolase 11, Deubiquitinating enzyme 11, Ubiquitin thioesterase 11, or Ubiquitin-specific-processing protease 11, is a protease that removes ubiquitin from target proteins and polyubiquitin chains. This action inhibits the degradation of target proteins by the proteasome. USP11 preferentially cleaves 'Lys-6' and 'Lys-63'-linked ubiquitin chains, with lower activity against 'Lys-11' and 'Lys-33'-linked chains and extremely low activity against 'Lys-27', 'Lys-29', and 'Lys-48'-linked chains. USP11 plays a role in regulating pathways leading to NF-kappa-B activation and DNA repair after double-stranded DNA breaks. It acts as a chromatin regulator through its association with the Polycomb group (PcG) multiprotein PRC1-like complex, potentially by deubiquitinating components of this complex. USP11 promotes cell proliferation by deubiquitinating phosphorylated E2F1.

USP11 is also known as UHX1.

Associated Diseases

WES Whole Exome Sequencing