PSMA7 (proteasome 20S subunit alpha 7) is a core catalytic component of the 20S proteasome complex that mediates ubiquitin-dependent and -independent protein degradation. As part of the 26S proteasome, PSMA7 participates in ATP-dependent degradation of ubiquitinated proteins essential for maintaining protein homeostasis 1. Beyond canonical proteasomal function, PSMA7 serves specialized roles including modulation of HIF-1α stability, nuclear translocation of androgen receptors, hepatitis C virus translation, and regulation of innate immune responses through MAVS degradation. PSMA7 directly interacts with and mediates proteasome-dependent degradation of NOD1, a pattern recognition receptor involved in innate immunity 2. In disease contexts, PSMA7 shows contrasting roles: pan-cancer analysis reveals frequent 20q13.33 amplification of PSMA7 associated with adverse prognosis across multiple tumor types, where elevated expression promotes cancer growth 3. However, in cutaneous squamous cell carcinoma, higher PSMA7 expression correlates with favorable prognosis and suppresses progression by degrading NOD1 and MAVS, reducing cancer-associated cytokine production 4. PSMA7 elevation in NSCLC promotes metastasis through epithelial-mesenchymal transition, yet melittin-induced PSMA7 degradation suppresses lung cancer metastasis 5. PSMA7 emerged as a plasma biomarker for endometrial cancer detection 6, suggesting clinical diagnostic potential alongside its therapeutic relevance.