The USP17L1 gene (USP17L1 stands for: Ubiquitin Specific Peptidase 17 Like Family Member 1) is a protein coding gene located on chromosome 8p23.1. Biochemical activities associated with this gene include cysteine-type peptidase activity and cysteine-type deubiquitinase activity. An important paralog of this gene is USP17L3.
The encoded protein, a deubiquitinating enzyme(protease), is localized in the endoplasmic reticulum and is probably active in the cytosol and nucleus. The enzyme removes conjugated ubiquitin from certain proteins in order to regulate various cellular processes. These include cell proliferation, cell cycle progression, apoptosis, cell migration and the cellular response to viral infections.
Ubiquitin-specific proteases (USPs) play a key role in numerous cellular processes and make up the majority of human deubiquitinating enzymes (DUBs). It is assumed that their modular structure determines substrate recognition and subcellular localization. They are characterized by the presence of ubiquitin-like (UBL) domains. The UBL domain thus appears to be the most abundant domain in the human USP family, after the characteristic catalytic domain.