DnaJ heat shock protein family (Hsp40) member C1 (DNAJC1)

DnaJ heat shock protein family (Hsp40) member C1 is a membrane-associated molecular chaperone that binds to the endoplasmic reticulum chaperone BiP and modulates protein synthesis. It contains two SANT domains that interact with serpin alpha 1-antichymotrypsin and inter-alpha trypsin inhibitor heavy chain 4. Its functions include chromatin binding and ATPase activator activity, supporting proper folding of proteins within the endoplasmic reticulum. DNAJC1 has been implicated in disease processes such as pyometritis and may facilitate glioblastoma progression by promoting extracellular matrix reorganization and macrophage infiltration. There are currently no known drugs directly targeting this molecule, nor established biomarker or safety concern data for therapeutic applications. Note: While DNAJC1 is a well-characterized molecular chaperone involved in cellular stress responses, it is not currently considered a direct therapeutic target such as an enzyme or receptor.

Other names

DnaJ homolog subfamily C member 1ERdj3J domain-containing protein 1