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HSP90AA6P is a human pseudogene that shares homology with the active heat shock protein 90kDa alpha (Hsp90α), a stress-inducible molecular chaperone involved in protein folding, stabilization, and degradation. Unlike its ancestral gene (HSP90AA1), HSP90AA6P does not encode a functional chaperone protein and thus does not participate directly in cellular stress response or protein homeostasis. Pseudogenes may have a coding-independent role at the RNA level, such as acting as a microRNA decoy, thereby modulating the expression of the parental gene and potentially influencing disease processes indirectly[6]. However, there is no experimental or clinical evidence indicating therapeutic target status, drug interaction, or established disease relevance for HSP90AA6P itself.
None for HSP90AA6P (noncoding pseudogene). For parental HSP90AA1 protein: inhibition of ATPase activity disrupts chaperone function, leading to cell death in tumor cells[3].
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