Auxilin

Putative tyrosine-protein phosphatase auxilin is an enzyme that in humans is encoded by the DNAJC6 gene.[5][6][7]

DNAJC6
Identifiers
Aliases	DNAJC6, DJC6, PARK19, Auxilin, DnaJ heat shock protein family (Hsp40) member C6
External IDs	OMIM: 608375 MGI: 1919935 HomoloGene: 8865 GeneCards: DNAJC6
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p31.3 Start 65,248,219 bp[1] End 65,415,871 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 C6 Start 101,496,631 bp[2] End 101,642,799 bp[2]
Gene ontology Molecular function • protein tyrosine phosphatase activity • SH3 domain binding • phosphoprotein phosphatase activity • hydrolase activity • clathrin binding Cellular component • cytosol • synapse • vesicle • GO:0097483, GO:0097481 postsynaptic density • cytoplasm • intracellular membrane-bounded organelle • presynapse Biological process • peptidyl-tyrosine dephosphorylation • regulation of clathrin-dependent endocytosis • protein dephosphorylation • clathrin coat disassembly • receptor-mediated endocytosis • membrane organization • synaptic vesicle uncoating • clathrin-dependent endocytosis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9829	72685
Ensembl	ENSG00000116675	ENSMUSG00000028528
UniProt	O75061	Q80TZ3
RefSeq (mRNA)	NM_001256864 NM_001256865 NM_014787	NM_001164583 NM_001164584 NM_001164585 NM_198412 NM_001355179 NM_001355180
RefSeq (protein)	NP_001243793 NP_001243794 NP_055602	NP_001158055 NP_001158056 NP_001158057 NP_940804 NP_001342108 NP_001342109
Location (UCSC)	Chr 1: 65.25 – 65.42 Mb	Chr 4: 101.5 – 101.64 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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]

References

1. GRCh38: Ensembl release 89: ENSG00000116675 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028528 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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. PMC 312896. PMID 11147971.
7. "Entrez Gene: DNAJC6 DnaJ (Hsp40) homolog, subfamily C, member 6".
8. 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.
9. "Phosphatase Subfamily Auxilin - PhosphataseWiki". phosphatome.net.
10. 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.

External links

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

Further reading

• 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.