Putative 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] auxilin subfamily of lipid phosphatases and is predicted to be catalytically inactive.[ 9] [ 10]
^ a b c GRCh38: Ensembl release 89: ENSG00000116675 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028528 – Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O (October 1997). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain" . DNA Research . 4 (5): 345–9. doi :10.1093/dnares/4.5.345 PMID 9455484 . ^ Ohtsuka K, Hata M (April 2000). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature" . Cell Stress & Chaperones . 5 (2): 98–112. doi :10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 (inactive 2024-11-02). PMC 312896 PMID 11147971 . {{cite journal }}: CS1 maint: DOI inactive as of November 2024 (link )^ a b "Entrez Gene: DNAJC6 DnaJ (Hsp40) homolog, subfamily C, member 6" .^ Haynie DT, Xue B (May 2015). "Superdomains in the protein structure hierarchy: The case of PTP-C2" . Protein Science . 24 (5): 874–82. doi :10.1002/pro.2664 . PMC 4420535 PMID 25694109 . ^ "Phosphatase Subfamily Auxilin - PhosphataseWiki" . phosphatome.net .^ Chen MJ, Dixon JE, Manning G (April 2017). "Genomics and evolution of protein phosphatases". Science Signaling . 10 (474): eaag1796. doi :10.1126/scisignal.aag1796 . PMID 28400531 . S2CID 41041971 .
Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (September 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions" . Genome Research . 14 (9): 1711–8. doi :10.1101/gr.2435604 . PMC 515316 PMID 15342556 . Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E (July 2003). "Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin" . The Journal of Biological Chemistry . 278 (28): 25357–68. doi :10.1074/jbc.M303738200 PMID 12732633 . Scheele U, Kalthoff C, Ungewickell E (September 2001). "Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex" . The Journal of Biological Chemistry . 276 (39): 36131–8. doi :10.1074/jbc.M106511200 PMID 11470803 . Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (October 1997). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro" . DNA Research . 4 (5): 307–13. doi :10.1093/dnares/4.5.307 PMID 9455477 .
