Ubiquitin specific peptidase 17 like family member 3 (USP17L3)

Ubiquitin specific peptidase 17 like family member 3 (USP17L3) is a cysteine-type deubiquitinating enzyme that removes conjugated ubiquitin from substrate proteins to regulate diverse cell processes, including protein stability, cell proliferation, apoptosis, cell cycle progression, cell migration, and response to cytokines and chemokines. Induction of USP17L3 has been observed in response to inflammatory and migratory cues (e.g., chemokines like CXCL12 and IL-8) in immune and cancer cells, where it is required for both directional and random migration by regulating cytoskeletal rearrangements and the localization of small GTPases such as Ras, RhoA, Rac1, and Cdc42. It has been identified as a regulator downstream of cytokine and chemokine signaling and is implicated in processes relevant to inflammation and metastatic cancer[1][3][8]. Genetic associations with developmental disorders have also been reported[3].

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 3USP17BUSP17FDeubiquitinating enzyme 17-like protein 3Ubiquitin thioesterase 17-like protein 3Ubiquitin-specific-processing protease 17-like protein 3ubiquitin specific peptidase 17-like 3ubiquitin thioesterase 17-like protein 3USP17L3

Removal of conjugated ubiquitin from substrate proteins to regulate their stability and function, affecting cell cycle, migration, and signaling pathways[3][8][1].