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Deubiquitinase DESI2 is an enzyme involved in the removal of ubiquitin from specific protein substrates, notably exhibiting activity against 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains and mediating deubiquitination of ribosomal protein S7 (RPS7), which leads to its stabilization. DESI2 also possesses S-depalmitoylase activity, meaning it can remove palmitoyl groups from proteins, and is involved in macromolecule depalmitoylation and proteolysis. By regulating protein ubiquitination and palmitoylation status, DESI2 plays an important role in maintaining cellular protein homeostasis and is potentially implicated in disease, including cancer. It is considered a prospective therapeutic target, but as of now, no approved drugs or specific inhibitors are noted in the literature. Notes on aliases and functional annotations: Many aliases derive from previous gene/protein nomenclature standards and protein domains but all refer to the same human protein product. No major sources list established drugs or highly specific biomarkers related to DESI2, and its status as a therapeutic target is emerging rather than established in clinical practice.
Inhibition of deubiquitination (hypothetical, no clinically approved inhibitors or specific reference drugs listed); Inhibition or modulation of S-depalmitoylase activity (hypothetical)
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