DnaJ/HSP40 Homolog Subfamily B, Member 12 (DNAJB12)

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.

By searching EST databases for J domain-containing proteins, Ohtsuka and Hata (2000) identified 10 mouse and human DNAJ homologs, including mouse Dnajb12. The predicted type-1b transmembrane protein contains 376 amino acids, with a J domain from residues 109 to 178. PSORT analysis suggested a nuclear localization.