HSPA6

Protein-coding gene in the species Homo sapiens
HSPA6
Available structures
PDBHuman UniProt search: PDBe RCSB
List of PDB id codes

3FE1

Identifiers
AliasesHSPA6, HSP70B', heat shock protein family A (Hsp70) member 6
External IDsOMIM: 140555; HomoloGene: 105648; GeneCards: HSPA6; OMA:HSPA6 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for HSPA6
Genomic location for HSPA6
Band1q23.3Start161,524,540 bp[1]
End161,526,894 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • blood

  • granulocyte

  • monocyte

  • spleen

  • upper lobe of left lung

  • C1 segment

  • placenta

  • testicle

  • left adrenal cortex

  • right adrenal cortex
    n/a
More reference expression data
BioGPS


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
SpeciesHumanMouse
Entrez

3310

n/a

Ensembl

ENSG00000173110

n/a

UniProt

P17066

n/a

RefSeq (mRNA)

NM_002155

n/a

RefSeq (protein)

NP_002146

n/a

Location (UCSC)Chr 1: 161.52 – 161.53 Mbn/a
PubMed search[2]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

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

Further reading

  • 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.
  • v
  • t
  • e
  • 1xqs: Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domain
    1xqs: Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domain

External links

  • v
  • t
  • e
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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