• Source: Auxilin

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




Function


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).




Structure


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




References






External links


Human DNAJC6 genome location and DNAJC6 gene details page in the UCSC Genome Browser.




Further reading

Kata Kunci Pencarian:

• Auxilin
• GAK (protein)
• Vesicular transport protein
• Tensin
• Protein domain
• PTEN (gene)
• Clathrin adaptor protein
• Co-chaperone
• HSPA8
• Beta2-adaptin C-terminal domain