Heat shock protein family A member 6 (HSPA6)

Heat shock protein family A member 6 (HSPA6) is a protein coding gene encoding a strictly stress-inducible molecular chaperone of the HSP70 family, characterized by an N-terminal nucleotide-binding domain and a C-terminal substrate-binding domain[2]. HSPA6 enables ATP hydrolysis, heat shock protein binding, and unfolded protein binding activity, and is involved in protection against proteotoxic stress, refolding of misfolded proteins, and cellular response to stimuli[1]. It regulates the folding and transport of newly synthesized polypeptides and activates proteolysis of damaged proteins[1]. HSPA6 is implicated in various disease processes, such as cancer (with context-dependent effects on tumorigenesis), and infection, where it can facilitate translation of viral proteins through internal ribosome entry site (IRES) mechanisms[2][3]. It is located in cellular compartments such as the cytosol, centriole, and COP9 signalosome[1]. Recent work highlights HSPA6 as an emerging prognostic and therapeutic marker but not yet an established direct drug target[2][3][5].

Other names

Heat shock 70 kDa protein 6HSP70B'Heat shock 70 kDa protein B'Epididymis secretory sperm binding protein

For disease modulation or drug targeting: regulation of protein folding, stabilization of unfolded/misfolded proteins, proteostasis; manipulation of chaperone activity in cancer and infection[2][3].