982972685ENSG00000116675ENSMUSG00000028528O75061Q80TZ3NM_001256864NM_001256865NM_014787NM_001355180NP_001243793NP_001243794NP_055602NP_001342109Putative tyrosine-protein phosphatase auxilin is an enzyme that in humans is encoded by the DNAJC6 gene.

[5][6][7] 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).

[7] 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.

[8] The phosphatase domain belongs to the auxilin subfamily of lipid phosphatases and is predicted to be catalytically inactive.