DNAJC6 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).
The protein tyrosine phosphatase domain and C2 domain pair of auxilin, located near the N-terminus of the polypeptide, constitute a superdomain, a tandem arrangement of two or more nominally unrelated domains that form a single heritable unit.
^Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O (Oct 1997). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Research4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID9455484.
Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E (Jul 2003). "Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin". The Journal of Biological Chemistry278 (28): 25357–68. doi:10.1074/jbc.M303738200. PMID12732633.
Scheele U, Kalthoff C, Ungewickell E (Sep 2001). "Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex". The Journal of Biological Chemistry276 (39): 36131–8. doi:10.1074/jbc.M106511200. PMID11470803.
Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Oct 1997). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro". DNA Research4 (5): 307–13. doi:10.1093/dnares/4.5.307. PMID9455477.