DnaJ heat shock protein family member A2 (DNAJA2)

DnaJ heat shock protein family member A2 (DNAJA2) is a molecular chaperone belonging to the heat shock protein 40 (Hsp40) family. It acts as a co-chaperone of Hsp70/Hsc70 proteins, critical for protein folding and maintaining proteostasis within the cell. DNAJA2 contains several distinct domains, notably a conserved N-terminal J domain, a glycine/phenylalanine-rich region, and a cysteine-rich, zinc finger-like domain. Structurally, DNAJA2 can form oligomers and higher-order tubular assemblies, regulated by hydrophobic and electrostatic interactions, which influence its chaperone activity. Functionally, DNAJA2 is essential for ATP hydrolysis stimulation in Hsp70, binding to and remodeling unfolded client proteins, and facilitating mitochondrial protein import. Recent findings highlight a specific role for DNAJA2 in genome stability and DNA repair processes, particularly in transcription-coupled nucleotide excision repair (TC-NER), where it promotes the removal and autophagic degradation of CSB protein in response to UV-induced DNA damage. DNAJA2's activity is implicated in the cellular response to stress and is associated with several diseases, including renal carcinoma (as NY-REN-14 antigen), subacute bacterial endocarditis, and autoimmune vasculitis. No drugs are currently known to specifically target DNAJA2 for therapeutic intervention, nor are safety concerns or mechanisms of action for drug targeting established as of current literature.

Other names

DnaJ homolog subfamily A member 2CPR3HIRIP4DJ3DNJ3cell cycle progression restoration gene 3 proteinHIRA-interacting protein 4Renal carcinoma antigen NY-REN-14PRO3015RDJ2