DnaJ/HSP40 Homolog Subfamily B, Member 8 (DNAJB8)

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 .

By searching EST databases for J domain-containing proteins, Ohtsuka and Hata (2000) identified 10 mouse and human DNAJ homologs, including mouse Dnajb8. The predicted type II transmembrane protein contains 227 amino acids with an N-terminal J domain.