DNAJC6

From Wikipedia, the free encyclopedia

DnaJ (Hsp40) homolog, subfamily C, member 6

PDB rendering based on 1n4c.

Available structures: 1n4c, 1nz6, 1xi5

Identifiers

Symbol(s)

DNAJC6; DJC6; KIAA0473; MGC129914; MGC129915; MGC48436

External IDs

OMIM: 608375 MGI: 1919935 HomoloGene: 8865

Gene ontology
Molecular Function:	• protein tyrosine phosphatase activity • hydrolase activity • heat shock protein binding
Biological Process:	• protein folding • protein amino acid dephosphorylation

Orthologs

Human

Mouse

Refseq

NM_014787 (mRNA)
NP_055602 (protein)

NM_198412 (mRNA)
NP_940804 (protein)

Location

Chr 1: 65.5 - 65.65 Mb

Chr 4: 101.01 - 101.14 Mb

Pubmed search

[1]

[2]

DnaJ (Hsp40) homolog, subfamily C, member 6, also known as DNAJC6, is a human gene.^[1]

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).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: DNAJC6 DnaJ (Hsp40) homolog, subfamily C, member 6.

[edit] Further reading

Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315-21. doi:10.1038/nature04727. PMID 16710414.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711-8. doi:10.1101/gr.2435604. PMID 15342556.
Scheele U, Alves J, Frank R, et al. (2003). "Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin.". J. Biol. Chem. 278 (28): 25357-68. doi:10.1074/jbc.M303738200. PMID 12732633.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Scheele U, Kalthoff C, Ungewickell E (2001). "Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex.". J. Biol. Chem. 276 (39): 36131-8. doi:10.1074/jbc.M106511200. PMID 11470803.
Ohtsuka K, Hata M (2001). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.". Cell Stress Chaperones 5 (2): 98-112. PMID 11147971.
Seki N, Ohira M, Nagase T, et al. (1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain.". DNA Res. 4 (5): 345-9. PMID 9455484.
Ishikawa K, Nagase T, Nakajima D, et al. (1998). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 4 (5): 307-13. PMID 9455477.