DnaJ heat shock protein family (Hsp40) member B5 (DNAJB5)

DnaJ heat shock protein family (Hsp40) member B5 (DNAJB5) is a molecular chaperone and co-chaperone belonging to the Hsp40 (DnaJ) family, characterized by an N-terminal DNAJ domain and a C-terminal substrate-binding domain, though lacking the cysteine-rich domain seen in some other family members[3][7][8]. It is primarily involved in recognizing and binding to unfolded proteins, facilitating correct protein refolding and cellular protein quality control, thereby protecting cells from protein misfolding stress[1][2][3][7][8]. The protein is typically upregulated during cell stress, such as heat shock, and acts in concert with Hsp70 chaperones[1][8]. In mouse models, its interaction in multi-protein complexes can contribute to the regulation of cardiac hypertrophy[3]. DNAJB5 is not currently recognized as a direct therapeutic target or drug receptor, and no drugs or clinical biomarkers are specifically listed for it[3][7][8].

Other names

HSC40Hsc40Heat shock protein Hsp40-2Heat shock protein Hsp40-3Heat shock protein cognate 40dnaJ homolog subfamily B member 5DnaJ (Hsp40) homolog, subfamily B, member 5heat shock cognate 40