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Ubiquitin specific peptidase 17 like family member 20 (USP17L20) is a protein-coding gene located on chromosome 4 that encodes a **deubiquitinating enzyme** of the USP family[3][10]. USP17L20 catalyzes the removal of ubiquitin moieties from substrate proteins, modulating their stability, localization, and activity. Through its enzymatic action, it regulates key cellular processes, including cell cycle progression, proliferation, apoptosis, migration, and cellular responses to viral infections[1][10][11]. Genetic studies have associated variation in USP17L20 with a spectrum of immunodeficiency disorders, certain types of obesity, spermatogenic failure, and possibly neurodegenerative conditions such as Alzheimer disease[1]. Despite its functional importance, no drugs are currently documented to specifically target USP17L20.
For hypothetical inhibitors: inhibition of deubiquitinase activity leading to altered protein ubiquitination status. No specific drugs currently documented.
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