Heat shock 70 kDa protein 14

HSPA14 (Heat shock 70 kDa protein 14) is a molecular chaperone component of the ribosome-associated complex (RAC), which facilitates folding and stabilization of nascent polypeptide chains during translation (UniProt: Q0VDF9). The protein works in conjunction with DNAJC2 to stimulate ATPase activity and maintain newly synthesized proteins in a folding-competent state.

HSPA14 is expressed broadly across tissues and participates in fundamental protein biosynthesis quality control. No primary disease associations are documented in UniProt for this protein.

In Alzheimer's disease, HSPA14 shows reduced abundance in post-mortem AD brain tissue compared to age-matched controls (Chaparral AD proteomics). Quantitative proteomics analysis detected a mean log2 fold-change of −0.52 across subcellular fractions in human post-mortem AD brain versus control samples, indicating downregulation. This decreased expression may reflect alterations in translational capacity or protein quality control mechanisms associated with AD neurodegeneration.