DNAJB1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''DnaJ homolog subfamily B member 1''' is a [[protein]] that in humans is encoded by the ''DNAJB1'' [[gene]].<ref name="pmid8975727">{{cite journal | vauthors = Hata M, Okumura K, Seto M, Ohtsuka K | title = Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2 | journal = Genomics | volume = 38 | issue = 3 | pages = 446–9 |date=Mar 1997 | pmid = 8975727 | pmc =  | doi = 10.1006/geno.1996.0653 }}</ref><ref name="pmid8250930">{{cite journal | author = Ohtsuka K | title = Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ | journal = Biochem Biophys Res Commun | volume = 197 | issue = 1 | pages = 235–40 |date=Jan 1994 | pmid = 8250930 | pmc = | doi =10.1006/bbrc.1993.2466  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3337| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
DNAJB1 has been shown to [[Protein-protein interaction|interact]] with:
| image = PBB_Protein_DNAJB1_image.jpg
* [[HSPA4]],<ref name = pmid14503850>{{cite journal | date = Aug 2003 | vauthors = Oh WK, Song J | title = Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation | journal = Mol. Cells | volume = 16 | issue = 1 | pages = 84–91 | pmid = 14503850 | doi = }}</ref> and
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hdj.
* [[STUB1]]<ref name = pmid10330192>{{cite journal | date = Jun 1999 | vauthors = Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C | title = Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions | journal = Mol. Cell. Biol. | volume = 19 | issue = 6 | pages = 4535–45 | pmid = 10330192 | pmc = 104411 | doi = 10.1128/mcb.19.6.4535}}</ref>
| PDB = {{PDB2|1hdj}}
| Name = DnaJ (Hsp40) homolog, subfamily B, member 1
| HGNCid = 5270
| Symbol = DNAJB1
| AltSymbols =; HSPF1; Hdj1; Hsp40
| OMIM = 604572
| ECnumber = 
| Homologene = 55957
| MGIid = 1931874
| GeneAtlas_image1 = PBB_GE_DNAJB1_200666_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DNAJB1_200664_s_at_tn.png
| Function = {{GNF_GO|id=GO:0031072 |text = heat shock protein binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}  
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}} {{GNF_GO|id=GO:0051085 |text = chaperone cofactor-dependent protein folding}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3337
    | Hs_Ensembl = ENSG00000132002
    | Hs_RefseqProtein = NP_006136
    | Hs_RefseqmRNA = NM_006145
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 14486582
    | Hs_GenLoc_end = 14490201
    | Hs_Uniprot = P25685
    | Mm_EntrezGene = 81489
    | Mm_Ensembl = ENSMUSG00000005483
    | Mm_RefseqmRNA = NM_018808
    | Mm_RefseqProtein = NP_061278
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 86498298
    | Mm_GenLoc_end = 86502008
    | Mm_Uniprot = Q3TIT6
  }}
}}
'''DnaJ (Hsp40) homolog, subfamily B, member 1''', also known as '''DNAJB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3337| accessdate = }}</ref>


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== References ==
{{PBB_Summary
{{reflist}}
| section_title =
| summary_text =
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Hattori H, Liu YC, Tohnai I |title=Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells. |journal=Cell Struct. Funct. |volume=17 |issue= 1 |pages= 77–86 |year= 1992 |pmid= 1586970 |doi=10.1247/csf.17.77 |display-authors=etal}}
| citations =
*{{cite journal  | vauthors=Raabe T, Manley JL |title=A human homologue of the Escherichia coli DnaJ heat-shock protein. |journal=Nucleic Acids Res. |volume=19 |issue= 23 |pages= 6645 |year= 1992 |pmid= 1754405 |doi=10.1093/nar/19.23.6645  | pmc=329243  }}
*{{cite journal  | author=Hattori H, Liu YC, Tohnai I, ''et al.'' |title=Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells. |journal=Cell Struct. Funct. |volume=17 |issue= 1 |pages= 77-86 |year= 1992 |pmid= 1586970 |doi=  }}
*{{cite journal  | vauthors=Freeman BC, Morimoto RI |title=The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. |journal=EMBO J. |volume=15 |issue= 12 |pages= 2969–79 |year= 1996 |pmid= 8670798 |doi= | pmc=450238 }}
*{{cite journal  | author=Raabe T, Manley JL |title=A human homologue of the Escherichia coli DnaJ heat-shock protein. |journal=Nucleic Acids Res. |volume=19 |issue= 23 |pages= 6645 |year= 1992 |pmid= 1754405 |doi= }}
*{{cite journal  | vauthors=Qian YQ, Patel D, Hartl FU, McColl DJ |title=Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. |journal=J. Mol. Biol. |volume=260 |issue= 2 |pages= 224–35 |year= 1996 |pmid= 8764402 |doi= 10.1006/jmbi.1996.0394 }}
*{{cite journal  | author=Ohtsuka K |title=Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 1 |pages= 235-40 |year= 1994 |pmid= 8250930 |doi=  }}
*{{cite journal  | vauthors=Shi Y, Mosser DD, Morimoto RI |title=Molecular chaperones as HSF1-specific transcriptional repressors. |journal=Genes Dev. |volume=12 |issue= 5 |pages= 654–66 |year= 1998 |pmid= 9499401 |doi= 10.1101/gad.12.5.654| pmc=316571  }}
*{{cite journal  | author=Freeman BC, Morimoto RI |title=The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. |journal=EMBO J. |volume=15 |issue= 12 |pages= 2969-79 |year= 1996 |pmid= 8670798 |doi= }}
*{{cite journal  | vauthors=Hata M, Ohtsuka K |title=Characterization of HSE sequences in human Hsp40 gene: structural and promoter analysis. |journal=Biochim. Biophys. Acta |volume=1397 |issue= 1 |pages= 43–55 |year= 1998 |pmid= 9545528 |doi= 10.1016/S0167-4781(97)00208-X}}
*{{cite journal  | author=Qian YQ, Patel D, Hartl FU, McColl DJ |title=Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. |journal=J. Mol. Biol. |volume=260 |issue= 2 |pages= 224-35 |year= 1996 |pmid= 8764402 |doi= 10.1006/jmbi.1996.0394 }}
*{{cite journal  | vauthors=Zou J, Guo Y, Guettouche T |title=Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. |journal=Cell |volume=94 |issue= 4 |pages= 471–80 |year= 1998 |pmid= 9727490 |doi=10.1016/S0092-8674(00)81588-3  |display-authors=etal}}
*{{cite journal  | author=Hata M, Okumura K, Seto M, Ohtsuka K |title=Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2. |journal=Genomics |volume=38 |issue= 3 |pages= 446-9 |year= 1997 |pmid= 8975727 |doi= 10.1006/geno.1996.0653 }}
*{{cite journal  | vauthors=Melville MW, Tan SL, Wambach M |title=The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity. |journal=J. Biol. Chem. |volume=274 |issue= 6 |pages= 3797–803 |year= 1999 |pmid= 9920933 |doi=10.1074/jbc.274.6.3797 |display-authors=etal}}
*{{cite journal  | author=Shi Y, Mosser DD, Morimoto RI |title=Molecular chaperones as HSF1-specific transcriptional repressors. |journal=Genes Dev. |volume=12 |issue= 5 |pages= 654-66 |year= 1998 |pmid= 9499401 |doi= }}
*{{cite journal  | vauthors=Ballinger CA, Connell P, Wu Y |title=Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4535–45 |year= 1999 |pmid= 10330192 |doi=  10.1128/mcb.19.6.4535| pmc=104411  |display-authors=etal}}
*{{cite journal  | author=Hata M, Ohtsuka K |title=Characterization of HSE sequences in human Hsp40 gene: structural and promoter analysis. |journal=Biochim. Biophys. Acta |volume=1397 |issue= 1 |pages= 43-55 |year= 1998 |pmid= 9545528 |doi=  }}
*{{cite journal  | vauthors=Michels AA, Kanon B, Bensaude O, Kampinga HH |title=Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36757–63 |year= 2000 |pmid= 10593983 |doi=10.1074/jbc.274.51.36757  }}
*{{cite journal  | author=Zou J, Guo Y, Guettouche T, ''et al.'' |title=Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. |journal=Cell |volume=94 |issue= 4 |pages= 471-80 |year= 1998 |pmid= 9727490 |doi=  }}
*{{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=Melville MW, Tan SL, Wambach M, ''et al.'' |title=The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity. |journal=J. Biol. Chem. |volume=274 |issue= 6 |pages= 3797-803 |year= 1999 |pmid= 9920933 |doi= }}
*{{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 |year= 2001 |pmid= 11147971 |doi=10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2  | pmc=312896 }}
*{{cite journal  | author=Ballinger CA, Connell P, Wu Y, ''et al.'' |title=Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4535-45 |year= 1999 |pmid= 10330192 |doi= }}
*{{cite journal  | vauthors=Kuncewicz T, Balakrishnan P, Snuggs MB, Kone BC |title=Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages. |journal=Am. J. Physiol. Renal Physiol. |volume=281 |issue= 2 |pages= F326–36 |year= 2001 |pmid= 11457725 |doi= }}
*{{cite journal  | author=Michels AA, Kanon B, Bensaude O, Kampinga HH |title=Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36757-63 |year= 2000 |pmid= 10593983 |doi=  }}
*{{cite journal  | vauthors=Pang Q, Keeble W, Christianson TA |title=FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity. |journal=EMBO J. |volume=20 |issue= 16 |pages= 4478–89 |year= 2001 |pmid= 11500375 |doi= 10.1093/emboj/20.16.4478  | pmc=125562 |display-authors=etal}}
*{{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=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=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=Anwar A, Siegel D, Kepa JK, Ross D |title=Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14060–7 |year= 2002 |pmid= 11821413 |doi= 10.1074/jbc.M111576200 }}
*{{cite journal  | author=Kuncewicz T, Balakrishnan P, Snuggs MB, Kone BC |title=Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages. |journal=Am. J. Physiol. Renal Physiol. |volume=281 |issue= 2 |pages= F326-36 |year= 2001 |pmid= 11457725 |doi= }}
*{{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}}
*{{cite journal  | author=Pang Q, Keeble W, Christianson TA, ''et al.'' |title=FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity. |journal=EMBO J. |volume=20 |issue= 16 |pages= 4478-89 |year= 2001 |pmid= 11500375 |doi= 10.1093/emboj/20.16.4478 }}
*{{cite journal  | vauthors=Reuter TY, Medhurst AL, Waisfisz Q |title=Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport. |journal=Exp. Cell Res. |volume=289 |issue= 2 |pages= 211–21 |year= 2003 |pmid= 14499622 |doi=10.1016/S0014-4827(03)00261-1  |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  |author1=Honeyman, Joshua N |author2=Simon E |author3=Robine N |title=Detection of a Recurrent DNAJB1-PRKACA Chimeric Transcript in Fibrolamellar Hepatocellular Carcinoma. |journal=Science|volume=343  |pages= 1010–1014 |year= 2014 | doi= 10.1126/science.1249484 | pmid= 24578576|display-authors=etal | pmc=4286414}}
*{{cite journal  | author=Anwar A, Siegel D, Kepa JK, Ross D |title=Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14060-7 |year= 2002 |pmid= 11821413 |doi= 10.1074/jbc.M111576200 }}
*{{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  | author=Reuter TY, Medhurst AL, Waisfisz Q, ''et al.'' |title=Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport. |journal=Exp. Cell Res. |volume=289 |issue= 2 |pages= 211-21 |year= 2003 |pmid= 14499622 |doi=  }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3337}}


{{protein-stub}}
{{Chaperones}}
{{WikiDoc Sources}}
 
[[Category:Heat shock proteins]]
 
 
{{gene-19-stub}}

Latest revision as of 18:37, 30 August 2017

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

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.[1][2][3]

Interactions

DNAJB1 has been shown to interact with:

References

  1. ↑ Hata M, Okumura K, Seto M, Ohtsuka K (Mar 1997). "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2". Genomics. 38 (3): 446–9. doi:10.1006/geno.1996.0653. PMID 8975727.
  2. ↑ Ohtsuka K (Jan 1994). "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ". Biochem Biophys Res Commun. 197 (1): 235–40. doi:10.1006/bbrc.1993.2466. PMID 8250930.
  3. ↑ "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1".
  4. ↑ Oh WK, Song J (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells. 16 (1): 84–91. PMID 14503850.
  5. ↑ Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C (Jun 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Mol. Cell. Biol. 19 (6): 4535–45. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192.

Further reading


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