Auxilin
Protein-coding gene in the species Homo sapiens
From Wikipedia, the free encyclopedia
Putative tyrosine-protein phosphatase auxilin is an enzyme that in humans is encoded by the DNAJC6 gene.[5][6][7]
| DNAJC6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | DNAJC6, DJC6, PARK19, Auxilin, DnaJ heat shock protein family (Hsp40) member C6 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 608375; MGI: 1919935; HomoloGene: 8865; GeneCards: DNAJC6; OMA:DNAJC6 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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).[7]
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.[8] The phosphatase domain belongs to the auxilin subfamily of lipid phosphatases and is predicted to be catalytically inactive.[9][10]