Ubiquitin carboxyl-terminal hydrolase 17-like protein 5 (USP17L5)

Ubiquitin carboxyl-terminal hydrolase 17-like protein 5 (USP17L5) is a member of the deubiquitinating enzyme (DUB) family, specifically classified as a ubiquitin-specific protease. It functions as a cysteine protease that removes ubiquitin from substrate proteins, thereby regulating their stability, localization, and function. USP17 family members play essential roles in numerous cellular processes, including cell cycle progression (by stabilizing or deubiquitinating proteins such as CDC25A and SETD8), cell proliferation, cytoskeletal reorganization, and cell migration, as well as the differentiation of osteoblasts[1][2][3][4][5][6]. USP17 is induced by cytokines and chemokines, participates in signaling cascades (e.g., ERK pathway via Ras regulation), and is implicated in pathological processes such as tumorigenesis and metastatic cancer. The specific functional distinctions or tissue expression of the "like family member 5" subform (USP17L5), compared to other USP17 paralogs, are limited in the literature[5]. However, by homology and conserved domain structure, USP17L5 is inferred to share the key cellular and pathological functions attributed to USP17.

Other names

Ubiquitin-specific-processing protease 17-like protein 5Deubiquitinating enzyme 17-like protein 5Ubiquitin thioesterase 17-like protein 5Ubiquitin thiolesterase 17-like protein 5USP17L5

Inhibition or modulation of USP17L5 activity may disrupt deubiquitination of targets involved in cell cycle, migration, and proliferation, thereby potentially affecting tumor growth, invasion, or inflammatory responses