HSPA6

HSPA6
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	3FE1
Identifiers
Aliases	HSPA6, HSP70B', heat shock protein family A (Hsp70) member 6
External IDs	OMIM: 140555 HomoloGene: 105648 GeneCards: HSPA6
Gene location (Human)
Chr.	Chromosome 1 (human)
End	161,526,894 bp
RNA expression pattern
	Top expressed in
	blood; ; monocyte; ; spleen; ; upper lobe of left lung; ; placenta; ; appendix; ; gallbladder; ; ascending aorta; ; right coronary artery; ; anterior pituitary;
	n/a
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	enzyme binding; unfolded protein binding; nucleotide binding; protein binding; ATP binding; heat shock protein binding; ATPase activity; protein folding chaperone activity; misfolded protein binding;
Cellular component	cytoplasm; centriole; COP9 signalosome; cytosol; extracellular exosome; blood microparticle; extracellular region; secretory granule lumen; ficolin-1-rich granule lumen; nucleus; protein-containing complex;
Biological process	cellular heat acclimation; response to unfolded protein; cellular response to heat; protein refolding; neutrophil degranulation; Unfolded Protein Response; chaperone cofactor-dependent protein refolding;
	Sources:Amigo / QuickGO
Orthologs
	3310
	n/a
	ENSG00000173110
	n/a
	P17066
	n/a
	NM_002155
	n/a
	NP_002146
	n/a
	Wikidata
View/Edit Human

Heat shock 70 kDa protein 6 is a protein that in humans is encoded by the HSPA6 gene.^[3]^[4]

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000173110 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ "Entrez Gene: HSPA6 heat shock 70kDa protein 6 (HSP70B')".

Further reading[edit]

Leung TK, Rajendran MY, Monfries C, et al. (1990). "The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA". Biochem. J. 267 (1): 125–32. doi:10.1042/bj2670125. PMC 1131254. PMID 2327978.
Schiller P, Amin J, Ananthan J, et al. (1988). "Cis-acting elements involved in the regulated expression of a human HSP70 gene". J. Mol. Biol. 203 (1): 97–105. doi:10.1016/0022-2836(88)90094-0. PMID 3184191.
Rensing SA, Maier UG (1994). "Phylogenetic analysis of the stress-70 protein family". J. Mol. Evol. 39 (1): 80–6. Bibcode:1994JMolE..39...80R. doi:10.1007/BF00178252. PMID 7545947. S2CID 37505045.
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.
Mercier PA, Winegarden NA, Westwood JT (1999). "Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress". J. Cell Sci. 112. ( Pt 16) (16): 2765–74. doi:10.1242/jcs.112.16.2765. PMID 10413683.
O'Keeffe B, Fong Y, Chen D, et al. (2000). "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". J. Biol. Chem. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616.
Agostini I, Popov S, Li J, et al. (2000). "Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex". Exp. Cell Res. 259 (2): 398–403. doi:10.1006/excr.2000.4992. PMID 10964507.
Gurer C, Cimarelli A, Luban J (2002). "Specific incorporation of heat shock protein 70 family members into primate lentiviral virions". J. Virol. 76 (9): 4666–70. doi:10.1128/JVI.76.9.4666-4670.2002. PMC 155079. PMID 11932435.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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. S2CID 35451084.
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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

External links[edit]

HSPA6+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000173110 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1346391-3] 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.

[entrez-4] "Entrez Gene: HSPA6 heat shock 70kDa protein 6 (HSP70B')".

[1]

[2]

[3]

[4]

HSPA6

References[edit]

Further reading[edit]

External links[edit]

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