DNAJB8 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus; a glycine/phenylalanine (G/F)-rich region; and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain.
DnaJ (Hsp40) homolog, subfamily B, member 8; DnaJ homolog 6; DnaJ homolog subfamily B member 8; mDj6; testicular tissue protein Li 56
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