HSPA14: Difference between revisions

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{{for|GroEL/60 kDa heat shock protein with the same symbol|GroEL}}
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{{Infobox_gene}}
| update_page = yes
'''Heat shock 70 kDa protein 14''' also known as '''HSP70-like protein 1''' or '''heat shock protein HSP60''' is a [[protein]] that in humans is encoded by the ''HSPA14'' [[gene]].<ref name="pmid14592822">{{cite journal |vauthors=Wan T, Zhou X, Chen G, An H, Chen T, Zhang W, Liu S, Jiang Y, Yang F, Wu Y, Cao X | title = Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant | journal = Blood | volume = 103 | issue = 5 | pages = 1747–54 |date=March 2004 | pmid = 14592822 | doi = 10.1182/blood-2003-08-2828 | url = | issn = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSPA14 heat shock 70kDa protein 14| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51182| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Heat shock 70kDa protein 14
| HGNCid = 29526
| Symbol = HSPA14
| AltSymbols =; HSP70-4; HSP70L1; MGC131990
| OMIM = 610369
| ECnumber = 
| Homologene = 74307
| MGIid = 1354164
| GeneAtlas_image1 = PBB_GE_HSPA14_219212_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 = 51182
    | Hs_Ensembl = ENSG00000187522
    | Hs_RefseqProtein = NP_057383
    | Hs_RefseqmRNA = NM_016299
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 14920169
    | Hs_GenLoc_end = 14953746
    | Hs_Uniprot = 
    | Mm_EntrezGene = 50497
    | Mm_Ensembl = ENSMUSG00000051396
    | Mm_RefseqmRNA = NM_001037542
    | Mm_RefseqProtein = NP_001032631
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 3406126
    | Mm_GenLoc_end = 3430086
    | Mm_Uniprot = 
  }}
}}
'''Heat shock 70kDa protein 14''', also known as '''HSPA14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSPA14 heat shock 70kDa protein 14| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51182| 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=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=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=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=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=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=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=Scheufler C, Brinker A, Bourenkov G, ''et al.'' |title=Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. |journal=Cell |volume=101 |issue= 2 |pages= 199-210 |year= 2000 |pmid= 10786835 |doi= 10.1016/S0092-8674(00)80830-2 }}
*{{cite journal   |vauthors=Scheufler C, Brinker A, Bourenkov G, etal |title=Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. |journal=Cell |volume=101 |issue= 2 |pages= 199–210 |year= 2000 |pmid= 10786835 |doi= 10.1016/S0092-8674(00)80830-2 }}
*{{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=Wan T, Zhou X, Chen G, ''et al.'' |title=Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant. |journal=Blood |volume=103 |issue= 5 |pages= 1747-54 |year= 2004 |pmid= 14592822 |doi= 10.1182/blood-2003-08-2828 }}
*{{cite journal   |vauthors=Brandenberger R, Wei H, Zhang S, etal |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
*{{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 | author=Brandenberger R, Wei H, Zhang S, ''et al.'' |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707-16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{MeshName|HSPA14+protein,+human}}
 
{{Chaperones}}
 
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[[Category:Heat shock proteins]]
 
 
{{gene-10-stub}}

Latest revision as of 02:15, 27 October 2017

For GroEL/60 kDa heat shock protein with the same symbol, see GroEL.
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

Heat shock 70 kDa protein 14 also known as HSP70-like protein 1 or heat shock protein HSP60 is a protein that in humans is encoded by the HSPA14 gene.[1][2]


References

  1. ↑ Wan T, Zhou X, Chen G, An H, Chen T, Zhang W, Liu S, Jiang Y, Yang F, Wu Y, Cao X (March 2004). "Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant". Blood. 103 (5): 1747–54. doi:10.1182/blood-2003-08-2828. PMID 14592822.
  2. ↑ "Entrez Gene: HSPA14 heat shock 70kDa protein 14".

Further reading

  • Furlini G, Vignoli M, Re MC, et al. (1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein". J. Gen. Virol. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Scheufler C, Brinker A, Bourenkov G, et al. (2000). "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine". Cell. 101 (2): 199–210. doi:10.1016/S0092-8674(00)80830-2. PMID 10786835.
  • Lim MC, Brooke SM, Sapolsky RM (2003). "gp120 neurotoxicity fails to induce heat shock defenses, while the over expression of hsp70 protects against gp120". Brain Res. Bull. 61 (2): 183–8. doi:10.1016/S0361-9230(03)00113-8. PMID 12832005.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.

External links


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