Heat shock protein family A (Hsp70) member 7 (HSPA7)

Heat shock protein family A (Hsp70) member 7 (HSPA7) is annotated in the human genome as a member of the Hsp70 family of molecular chaperones, typically involved in protein folding, protection from proteotoxic stress, and maintenance of cellular proteostasis[1][3][6]. However, HSPA7 in humans is characterized as a pseudogene—it is not believed to encode a functional protein[1][5][6]. Predictions based on sequence analysis suggest HSPA7 could potentially enable ATP hydrolysis, heat shock protein binding, and protein folding chaperone activities, but there is no robust evidence of physiological function or protein expression in humans[1][3][6]. Notably, while the broader Hsp70 family is involved in protein folding and stress responses with established roles in health and disease (such as cancer and neurodegeneration), the specific HSPA7 gene does not have confirmed roles as a drug target, nor are there any known interacting drugs or therapeutic mechanisms associated with it[1][5][6]. HSPA7 has been reported as a poor prognostic biomarker in kidney renal clear cell carcinoma, but not as a direct therapeutic target[5]. Key points: - HSPA7 is a pseudogene in humans and does not code for an active protein product[1][5][6]. - It is not considered a therapeutic target and lacks evidence of receptor, enzyme, or transporter activity[1][5][6]. - Aliases (where used) are primarily based on nomenclature and do not reflect genuine protein products in humans. Any reference to HSPA7 as a target (receptor, enzyme, etc.) is likely erroneous or based on incomplete information regarding its pseudogene status.

Other names

HSP70BHeat shock 70kDa protein 7 (HSP70B)Heat shock 70kD protein 7 (HSP70B)Heat shock protein family A member 7Putative heat shock 70 kDa protein 7Heat shock 70 kDa protein B