Auxilin

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DnaJ (Hsp40) homolog, subfamily C, member 6
Protein DNAJC6 PDB 1n4c.png
PDB rendering based on 1n4c.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols DNAJC6 ; DJC6; PARK19
External IDs OMIM608375 MGI1919935 HomoloGene8865 GeneCards: DNAJC6 Gene
EC number 3.1.3.48
Orthologs
Species Human Mouse
Entrez 9829 72685
Ensembl ENSG00000116675 ENSMUSG00000028528
UniProt O75061 Q80TZ3
RefSeq (mRNA) NM_001256864 NM_001164583
RefSeq (protein) NP_001243793 NP_001158055
Location (UCSC) Chr 1:
65.25 – 65.42 Mb
Chr 4:
101.5 – 101.64 Mb
PubMed search [1] [2]

Putative tyrosine-protein phosphatase auxilin is an enzyme that in humans is encoded by the DNAJC6 gene.[1][2][3]

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).[3]

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.[4]

References

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Further reading

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