HSPA6: Difference between revisions

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{{Infobox_gene}}
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'''Heat shock 70 kDa protein 6''' is a [[protein]] that in humans is encoded by the ''HSPA6'' [[gene]].<ref name="pmid1346391">{{cite journal |vauthors=Leung TK, Hall C, Rajendran M, Spurr NK, Lim L | title = The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1 | journal = Genomics | volume = 12 | issue = 1 | pages = 74–9 |date=Mar 1992 | pmid = 1346391 | pmc =  | doi =10.1016/0888-7543(92)90409-L }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSPA6 heat shock 70kDa protein 6 (HSP70B')| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3310| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_HSPA6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xqs.
| PDB = {{PDB2|1xqs}}
| Name = Heat shock 70kDa protein 6 (HSP70B')
| HGNCid = 5239
| Symbol = HSPA6
| AltSymbols =;
| OMIM = 140555
| ECnumber = 
| Homologene = 
| MGIid = 
| GeneAtlas_image1 = PBB_GE_HSPA6_117_at_tn.png
| GeneAtlas_image2 = PBB_GE_HSPA6_213418_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP 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 = 3310
    | Hs_Ensembl = ENSG00000173110
    | Hs_RefseqProtein = XP_001134322
    | Hs_RefseqmRNA = XM_001134322
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 159760392
    | Hs_GenLoc_end = 159763324
    | Hs_Uniprot = P17066
    | Mm_EntrezGene =   
    | Mm_Ensembl = 
    | Mm_RefseqmRNA =   
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Heat shock 70kDa protein 6 (HSP70B')''', also known as '''HSPA6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSPA6 heat shock 70kDa protein 6 (HSP70B')| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3310| accessdate = }}</ref>


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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Leung TK, Hall C, Rajendran M, ''et al.'' |title=The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1. |journal=Genomics |volume=12 |issue= 1 |pages= 74-9 |year= 1992 |pmid= 1346391 |doi=  }}
*{{cite journal   |vauthors=Leung TK, Rajendran MY, Monfries C, etal |title=The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA. |journal=Biochem. J. |volume=267 |issue= 1 |pages= 125–32 |year= 1990 |pmid= 2327978 |doi= | pmc=1131254 }}
*{{cite journal  | author=Leung TK, Rajendran MY, Monfries C, ''et al.'' |title=The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA. |journal=Biochem. J. |volume=267 |issue= 1 |pages= 125-32 |year= 1990 |pmid= 2327978 |doi=  }}
*{{cite journal   |vauthors=Schiller P, Amin J, Ananthan J, etal |title=Cis-acting elements involved in the regulated expression of a human HSP70 gene. |journal=J. Mol. Biol. |volume=203 |issue= 1 |pages= 97–105 |year= 1988 |pmid= 3184191 |doi=10.1016/0022-2836(88)90094-0 }}
*{{cite journal | author=Schiller P, Amin J, Ananthan J, ''et al.'' |title=Cis-acting elements involved in the regulated expression of a human HSP70 gene. |journal=J. Mol. Biol. |volume=203 |issue= 1 |pages= 97-105 |year= 1988 |pmid= 3184191 |doi=  }}
*{{cite journal  |vauthors=Rensing SA, Maier UG |title=Phylogenetic analysis of the stress-70 protein family. |journal=J. Mol. Evol. |volume=39 |issue= 1 |pages= 80–6 |year= 1994 |pmid= 7545947 |doi=10.1007/BF00178252 }}
*{{cite journal  | author=Rensing SA, Maier UG |title=Phylogenetic analysis of the stress-70 protein family. |journal=J. Mol. Evol. |volume=39 |issue= 1 |pages= 80-6 |year= 1994 |pmid= 7545947 |doi=  }}
*{{cite journal   |vauthors=Furlini G, Vignoli M, Re MC, etal |title=Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein. |journal=J. Gen. Virol. |volume=75 |issue=  1|pages= 193–9 |year= 1994 |pmid= 7906708 |doi=10.1099/0022-1317-75-1-193 }}
*{{cite journal | author=Furlini G, Vignoli M, Re MC, ''et al.'' |title=Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein. |journal=J. Gen. Virol. |volume=75 ( Pt 1) |issue=  |pages= 193-9 |year= 1994 |pmid= 7906708 |doi=  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  |vauthors=Mercier PA, Winegarden NA, Westwood JT |title=Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress. | series=112 |journal=J. Cell Sci. |volume=( Pt 16) |issue=  |pages= 2765–74 |year= 1999 |pmid= 10413683 |doi=  }}
*{{cite journal  | author=Mercier PA, Winegarden NA, Westwood JT |title=Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress. |journal=J. Cell. Sci. |volume=112 ( Pt 16) |issue=  |pages= 2765-74 |year= 1999 |pmid= 10413683 |doi=  }}
*{{cite journal   |vauthors=O'Keeffe B, Fong Y, Chen D, etal |title=Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 279–87 |year= 2000 |pmid= 10617616 |doi=10.1074/jbc.275.1.279 }}
*{{cite journal | author=O'Keeffe B, Fong Y, Chen D, ''et al.'' |title=Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 279-87 |year= 2000 |pmid= 10617616 |doi=  }}
*{{cite journal   |vauthors=Agostini I, Popov S, Li J, etal |title=Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 398–403 |year= 2000 |pmid= 10964507 |doi= 10.1006/excr.2000.4992 }}
*{{cite journal | author=Agostini I, Popov S, Li J, ''et al.'' |title=Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 398-403 |year= 2000 |pmid= 10964507 |doi= 10.1006/excr.2000.4992 }}
*{{cite journal  |vauthors=Gurer C, Cimarelli A, Luban J |title=Specific incorporation of heat shock protein 70 family members into primate lentiviral virions. |journal=J. Virol. |volume=76 |issue= 9 |pages= 4666–70 |year= 2002 |pmid= 11932435 |doi=10.1128/JVI.76.9.4666-4670.2002  | pmc=155079 }}
*{{cite journal  | author=Gurer C, Cimarelli A, Luban J |title=Specific incorporation of heat shock protein 70 family members into primate lentiviral virions. |journal=J. Virol. |volume=76 |issue= 9 |pages= 4666-70 |year= 2002 |pmid= 11932435 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }}
*{{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=Lim MC, Brooke SM, Sapolsky RM |title=gp120 neurotoxicity fails to induce heat shock defenses, while the over expression of hsp70 protects against gp120. |journal=Brain Res. Bull. |volume=61 |issue= 2 |pages= 183–8 |year= 2003 |pmid= 12832005 |doi=10.1016/S0361-9230(03)00113-8 }}
*{{cite journal  | author=Lim MC, Brooke SM, Sapolsky RM |title=gp120 neurotoxicity fails to induce heat shock defenses, while the over expression of hsp70 protects against gp120. |journal=Brain Res. Bull. |volume=61 |issue= 2 |pages= 183-8 |year= 2003 |pmid= 12832005 |doi=  }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 }}
*{{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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3310}}
== External links ==
* {{MeshName|HSPA6+protein,+human}}
{{Chaperones}}
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[[Category:Heat shock proteins]]


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Latest revision as of 20:04, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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

Heat shock 70 kDa protein 6 is a protein that in humans is encoded by the HSPA6 gene.[1][2]


References

  1. Leung TK, Hall C, Rajendran M, Spurr NK, Lim L (Mar 1992). "The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1". Genomics. 12 (1): 74–9. doi:10.1016/0888-7543(92)90409-L. PMID 1346391.
  2. "Entrez Gene: HSPA6 heat shock 70kDa protein 6 (HSP70B')".

Further reading

External links