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DNAJA1

{{Short description|Protein-coding gene in the species Homo sapiens}}

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DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the DNAJA1 gene.{{cite journal | vauthors = Chellaiah A, Davis A, Mohanakumar T | title = Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein | journal = Biochim Biophys Acta | volume = 1174 | issue = 1 | pages = 111–3 |date=August 1993 | pmid = 8334160 | doi = 10.1016/0167-4781(93)90103-k}}{{cite journal | vauthors = Ohtsuka K, Hata M | title = Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature | journal = Cell Stress & Chaperones | volume = 5 | issue = 2 | pages = 98–112 |date=January 2001 | doi = 10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 | doi-broken-date = 2024-11-02 | pmid = 11147971 | pmc = 312896 }}{{cite web | title = Entrez Gene: DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3301}}

Interactions

DNAJA1 has been shown to interact with PTTG1.{{cite journal |doi=10.1074/jbc.274.5.3151 |last=Pei |first=L |date=January 1999 |title=Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells |journal=J. Biol. Chem. |volume=274 |issue=5 |pages=3151–8 |location = UNITED STATES| issn = 0021-9258| pmid = 9915854 |doi-access=free }}

References

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Further reading

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  • {{cite journal | vauthors=Oh S, Iwahori A, Kato S |title=Human cDNA encoding DnaJ protein homologue. |journal=Biochim. Biophys. Acta |volume=1174 |issue= 1 |pages= 114–6 |year= 1993 |pmid= 8334161 |doi= 10.1016/0167-4781(93)90104-l}}
  • {{cite journal | vauthors=Kanazawa M, Terada K, Kato S, Mori M |title=HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria. |journal=J. Biochem. |volume=121 |issue= 5 |pages= 890–5 |year= 1997 |pmid= 9192730 |doi= 10.1093/oxfordjournals.jbchem.a021670}}
  • {{cite journal | vauthors=Davis AR, Alevy YG, Chellaiah A |title=Characterization of HDJ-2, a human 40 kD heat shock protein. |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 11 |pages= 1203–21 |year= 1998 |pmid= 9839446 |doi=10.1016/S1357-2725(98)00091-0 |display-authors=etal}}
  • {{cite journal | author=Pei L |title=Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells. |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 3151–8 |year= 1999 |pmid= 9915854 |doi=10.1074/jbc.274.5.3151 |doi-access=free }}
  • {{cite journal | vauthors=Meacham GC, Lu Z, King S |title=The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. |journal=EMBO J. |volume=18 |issue= 6 |pages= 1492–505 |year= 1999 |pmid= 10075921 |doi= 10.1093/emboj/18.6.1492 | pmc=1171238 |display-authors=etal}}
  • {{cite journal | vauthors=Terada K, Mori M |title=Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24728–34 |year= 2000 |pmid= 10816573 |doi= 10.1074/jbc.M002021200 |doi-access= free }}
  • {{cite journal | vauthors=Jana NR, Tanaka M, Wang G, Nukina N |title=Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. |journal=Hum. Mol. Genet. |volume=9 |issue= 13 |pages= 2009–18 |year= 2000 |pmid= 10942430 |doi=10.1093/hmg/9.13.2009 |doi-access=free }}
  • {{cite journal | vauthors=Bao YP, Cook LJ, O'Donovan D |title=Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12263–9 |year= 2002 |pmid= 11796717 |doi= 10.1074/jbc.M109633200 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Hernández MP, Chadli A, Toft DO |title=HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 11873–81 |year= 2002 |pmid= 11809754 |doi= 10.1074/jbc.M111445200 |doi-access= free }}
  • {{cite journal | vauthors=Imai Y, Soda M, Hatakeyama S |title=CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. |journal=Mol. Cell |volume=10 |issue= 1 |pages= 55–67 |year= 2002 |pmid= 12150907 |doi=10.1016/S1097-2765(02)00583-X |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal|bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal | vauthors=Hanai R, Mashima K |title=Characterization of two isoforms of a human DnaJ homologue, HSJ2. |journal=Mol. Biol. Rep. |volume=30 |issue= 3 |pages= 149–53 |year= 2004 |pmid= 12974469 |doi=10.1023/A:1024916223616 |s2cid=24105834 }}
  • {{cite journal | vauthors=Lehner B, Semple JI, Brown SE |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=10.1016/S0888-7543(03)00235-0 |display-authors=etal}}
  • {{cite journal | vauthors=Bouwmeester T, Bauch A, Ruffner H |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 |s2cid=11683986 |display-authors=etal}}
  • {{cite journal | vauthors=Marschang P, Brich J, Weeber EJ |title=Normal development and fertility of knockout mice lacking the tumor suppressor gene LRP1b suggest functional compensation by LRP1. |journal=Mol. Cell. Biol. |volume=24 |issue= 9 |pages= 3782–93 |year= 2004 |pmid= 15082773 |doi=10.1128/MCB.24.9.3782-3793.2004 | pmc=387731 |display-authors=etal}}
  • {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
  • {{cite journal | vauthors=Rush J, Moritz A, Lee KA |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94–101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046 |s2cid=7200157 |display-authors=etal}}
  • {{cite journal | vauthors=Hu Y, Zhou Z, Huang X |title=Expression of a novel DnaJA1 alternative splicing in human testis and sperm. |journal=Int. J. Androl. |volume=27 |issue= 6 |pages= 343–9 |year= 2005 |pmid= 15595953 |doi= 10.1111/j.1365-2605.2004.00492.x |display-authors=etal|doi-access=free }}

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{{Chaperones}}

Category:Heat shock proteins

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