DNAJB12 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 (Ohtsuka and Hata, 2000 [PubMed 11147971]).[supplied by
OMIM].
