DnaJ heat shock protein family member A1 (DNAJA1)

DnaJ heat shock protein family member A1 (DNAJA1) is a human protein that functions as a co-chaperone within the Hsp70 system, helping to regulate ATP hydrolysis and client substrate transfer for proper protein folding, trafficking, prevention of aggregation, and protein degradation[1][3]. Structurally, it features a highly conserved N-terminal J domain responsible for Hsp70 interaction, a glycine/phenylalanine-rich region, zinc finger motifs, and a C-terminal substrate-binding domain[1][3]. DNAJA1 participates in diverse cellular functions, including protecting cells from stress-induced apoptosis, regulating protein import into mitochondria, and is implicated in responses to viral infection and certain neurodegenerative and oncological diseases[1][3][4]. It is considered a promising, though not yet clinically validated, therapeutic target in diseases such as cancer due to its regulatory role in proteostasis and cell death pathways[3].

Other names

DnaJ (Hsp40) homolog, subfamily A, member 1HSPF4Hdj-2NEDD7Dj-2HSJ2Neural precursor cell expressed, developmentally down-regulated 7DnaJ homolog subfamily A member 1Heat shock 40 kDa protein 4

For potential drugs: Inhibition or modulation of the Hsp40-Hsp70 (DNAJA1–HSPA1A/B) interaction; suppression of JNK pathway phosphorylation; alteration of apoptosis signaling; stabilization of misfolded protein handling[3].