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Heat shock protein family A (Hsp70) member 14 (HSPA14) is a molecular chaperone belonging to the HSP70 family, encoded by the HSPA14 gene in humans[1][5]. HSPA14 is involved in protein folding and maintenance of newly synthesized polypeptides as part of the ribosome-associated complex (RAC), contributing critically to cellular stress response and proteostasis[2][6][8][10]. It is predicted to have ATP-binding, protein folding chaperone activity, and interacts with misfolded or unfolded proteins[3][7][9]. HSPA14 may be implicated in cancer and other diseases involving disrupted protein homeostasis, and is being explored as a potential drug target, though no specific therapeutics are currently approved[6][11].
Chaperone modulation (theoretical; drugs would modulate folding activity or protein-protein interactions in the ribosome-associated complex[6].)
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