Putative tyrosine-protein phosphatase auxilin is an enzyme that in humans is encoded by the DNAJC6gene.
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).[supplied by OMIM]
^Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O (Feb 1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Res4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID9455484.
Scheele U, Alves J, Frank R, et al. (2003). "Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin.". J. Biol. Chem.278 (28): 25357–68. doi:10.1074/jbc.M303738200. PMID12732633.
Scheele U, Kalthoff C, Ungewickell E (2001). "Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex.". J. Biol. Chem.276 (39): 36131–8. doi:10.1074/jbc.M106511200. PMID11470803.
Ishikawa K, Nagase T, Nakajima D, et al. (1998). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro.". DNA Res.4 (5): 307–13. doi:10.1093/dnares/4.5.307. PMID9455477.