DnaJ homolog subfamily C member 7

DNAJC7 (DnaJ homolog subfamily C member 7) is a molecular co-chaperone that regulates HSP70 and HSP90 chaperone activity during protein folding, particularly of steroid receptors including the glucocorticoid and progesterone receptors (UniProt: Q99615). The protein facilitates recycling of chaperone substrates and can induce ATP-independent dissociation of HSP90 from chaperone-substrate complexes, supporting protein homeostasis in the cytoplasm.

DNAJC7 is expressed broadly across tissues and is involved in cellular stress response and receptor trafficking pathways. No specific non-AD disease associations are documented in UniProt for this protein.

DNAJC7 is annotated for Alzheimer's Disease relevance in this dataset. Proteomics analysis of post-mortem AD brain versus age-matched controls using TMT-labeled mass spectrometry across four subcellular fractions (P2, P3, S2, S3) showed ambiguous directional change, with a mean log2 fold-change of −0.17 (Chaparral AD proteomics). The inconsistent directionality across fractions suggests differential subcellular localization or compartment-specific alterations in AD pathology.