DnaJ/HSP40 Homolog Subfamily B, Member 11 (DNAJB11)

DNAJB11 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 C-terminal cysteine-rich region.The deduced 358-amino acid protein has a calculated molecular mass of 40.5 kD and shares 99% sequence identity with the mouse protein. DNAJB11 contains a conserved J domain, a weak G/F region, and a region that contains 4 cysteines but lacks the zinc finger domain found in some DNAJ proteins. The secondary and tertiary structures of DNAJB11 closely resemble those of HDJ1 (DNAJB1). Northern blot analysis detected transcripts of 1.5 and 2.0 kb in all tissues examined.