USP17L2
Function
Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Regulates cell proliferation by deubiquitinating and inhibiting RCE1 thereby controlling the small GTPases NRAS and HRAS localization and activation. In parallel, mediates deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression. Also regulates cell proliferation and apoptosis through deubiquitination of SUDS3 a regulator of histone deacetylation. Through activation of the Rho family GTPases RAC1A, CDC42 and RHOA, regulates cell migration. Through the cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the cytoplasmic innate immune receptors RIGI and IFIH1 stimulates the cellular response to viral infection.
Sequence Similarities
Belongs to the peptidase C19 family. USP17 subfamily.
Tissue Specificity
Broadly expressed.
Cellular localization
- Nucleus
- Endoplasmic reticulum
Alternative names
DUB3, USP17, USP17H, USP17I, USP17J, USP17K, USP17L, USP17M, USP17L2, Ubiquitin carboxyl-terminal hydrolase 17, Deubiquitinating enzyme 17-like protein 2, Deubiquitinating protein 3, Ubiquitin carboxyl-terminal hydrolase 17-like protein 2, Ubiquitin thioesterase 17-like protein 2, Ubiquitin-specific-processing protease 17-like protein 2, DUB-3