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Heat shock protein 90kDa alpha (cytosolic), class B member 3, pseudogene (HSP90AB3P) is a pseudogene related to the HSP90 family of molecular chaperones and does not code for a functional protein[1][5]. It is predicted based on sequence similarity to the HSP90 chaperone proteins, which are involved in protein folding, stress response, and protein stabilization[1][2][5]. However, as a pseudogene, HSP90AB3P generally lacks the capacity to produce a functional protein product. Functional annotations reference possible ATP binding or unfolded protein binding activity based on homology rather than experimental evidence[1][5]. Like many pseudogenes, it may have a role in regulating gene expression of related functional genes, potentially by acting as a regulatory RNA or miRNA sponge, but it is not considered a receptor, enzyme, transporter, or other canonical drug target[4][5]. HSP90AB3P is not directly associated with disease or pharmacological intervention; it serves primarily as a genomic relic of the functional HSP90AB1 gene. Key rationale: - HSP90AB3P is a pseudogene according to multiple authoritative gene databases; no evidence supports protein or drug target function[1][5]. - The name and aliases clearly show it is a non-coding copy of a heat shock protein gene[1][5]. - Pseudogenes can sometimes play regulatory roles (e.g., as competitive endogenous RNA or affecting miRNA pathways), but these are not canonical target functions and are rarely characterized or actionable in therapeutic contexts[4]. - No known drugs target HSP90AB3P, nor is it considered a biomarker or source of safety concerns in therapy[5]. - The entry should be flagged as "is_incorrect: true" for drug discovery or pharmacological target purposes.
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