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{{Infobox_gene}}
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'''DnaJ homolog subfamily A member 1''' is a [[protein]] that in humans is encoded by the ''DNAJA1'' [[gene]].<ref name="pmid8334160">{{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 | pmc =  | doi = 10.1016/0167-4781(93)90103-k}}</ref><ref name="pmid11147971">{{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 | pmid = 11147971 | pmc = 312896 | doi =10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2 | year = }}</ref><ref name="entrez">{{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| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = DnaJ (Hsp40) homolog, subfamily A, member 1
| HGNCid = 5229
| Symbol = DNAJA1
| AltSymbols =; DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; hDJ-2
| OMIM = 602837
| ECnumber = 
| Homologene = 55588
| MGIid = 1270129
| GeneAtlas_image1 = PBB_GE_DNAJA1_200880_at_tn.png
| GeneAtlas_image2 = PBB_GE_DNAJA1_200881_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0031072 |text = heat shock protein binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050750 |text = low-density lipoprotein receptor binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component =  
  | Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3301
    | Hs_Ensembl = ENSG00000086061
    | Hs_RefseqProtein = NP_001530
    | Hs_RefseqmRNA = NM_001539
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 33015209
    | Hs_GenLoc_end = 33029905
    | Hs_Uniprot = P31689
    | Mm_EntrezGene = 15502
    | Mm_Ensembl = ENSMUSG00000028410
    | Mm_RefseqmRNA = NM_008298
    | Mm_RefseqProtein = NP_032324
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 40911204
    | Mm_GenLoc_end = 40923635
    | Mm_Uniprot = Q3TK61
  }}
}}
'''DnaJ (Hsp40) homolog, subfamily A, member 1''', also known as '''DNAJA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3301| accessdate = }}</ref>


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==Interactions==
DNAJA1 has been shown to [[Protein-protein interaction|interact]] with [[PTTG1]].<ref name=pmid9915854>{{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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9915854 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=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 |year= 1993 |pmid= 8334160 |doi=  }}
*{{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  | author=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=  }}
*{{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  | author=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=  }}
*{{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=Davis AR, Alevy YG, Chellaiah A, ''et al.'' |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=  }}
*{{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 }}
*{{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=  }}
*{{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  | author=Meacham GC, Lu Z, King S, ''et al.'' |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 }}
*{{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 }}
*{{cite journal  | author=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 }}
*{{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  }}
*{{cite journal  | author=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= }}
*{{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}}
*{{cite journal  | author=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 |year= 2001 |pmid= 11147971 |doi= }}
*{{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 }}
*{{cite journal  | author=Bao YP, Cook LJ, O'Donovan D, ''et al.'' |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 }}
*{{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}}
*{{cite journal  | author=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 }}
*{{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 }}
*{{cite journal  | author=Imai Y, Soda M, Hatakeyama S, ''et al.'' |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=  }}
*{{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 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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  | author=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= }}
*{{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 |display-authors=etal}}
*{{cite journal  | author=Lehner B, Semple JI, Brown SE, ''et al.'' |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=  }}
*{{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  | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |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 }}
*{{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  | author=Marschang P, Brich J, Weeber EJ, ''et al.'' |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= }}
*{{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 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{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}}
*{{cite journal  | author=Rush J, Moritz A, Lee KA, ''et al.'' |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 }}
*{{cite journal  | author=Hu Y, Zhou Z, Huang X, ''et al.'' |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 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Chaperones}}
{{WikiDoc Sources}}
 
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[[Category:Heat shock proteins]]
 
 
{{gene-9-stub}}

Latest revision as of 07:35, 10 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the DNAJA1 gene.[1][2][3]


Interactions

DNAJA1 has been shown to interact with PTTG1.[4]

References

  1. ↑ Chellaiah A, Davis A, Mohanakumar T (August 1993). "Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein". Biochim Biophys Acta. 1174 (1): 111–3. doi:10.1016/0167-4781(93)90103-k. PMID 8334160.
  2. ↑ Ohtsuka K, Hata M (January 2001). "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.
  3. ↑ "Entrez Gene: DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1".
  4. ↑ Pei, L (January 1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". J. Biol. Chem. UNITED STATES. 274 (5): 3151–8. doi:10.1074/jbc.274.5.3151. ISSN 0021-9258. PMID 9915854.

Further reading


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