HSPA6

Heat shock 70kDa protein 6 (HSP70B')

PDB rendering based on 1xqs.

Available structures
PDB	1xqs

Identifiers

Symbols

HSPA6;

External IDs

OMIM: 140555 HomoloGene: 105648 GeneCards: HSPA6 Gene

Gene Ontology
Molecular function	• nucleotide binding • ATP binding
Cellular component	• signalosome
Biological process	• response to unfolded protein
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

XM_001134322

n/a

RefSeq (protein)

XP_001134322

n/a

Location (UCSC)

Chr 1:
161.49 – 161.5 Mb

n/a

PubMed search

[1]

n/a

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

References

^ 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')". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3310.

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. PMC 1131254. PMID 2327978. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1131254.
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. doi:10.1007/BF00178252. PMID 7545947.
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 ( Pt 1) (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): 2765–74. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=155079.
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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.

PDB gallery

1xqs: Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domain

External links

MeSH HSPA6+protein,+human

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES (Early pregnancy factor) · Hsp27 · Hsp47 · HSP60/GroEL Hsp40/DnaJ (A1, A2, A3, B1, B2, B11, B4, B6, B9, C1, C3, C5, C6, C7, C10, C11, C13, C14, C19) Hsp70 (1A, 1B, 1L, 2, 4, 4L, 5, 6, 7, 8, 9, 12A, 14) Hsp90 (α₁, α₂, β, ER, TRAP1)

Other	Alpha crystallin · Clusterin · Survival of motor neuron (SMN1, SMN2)

Protein targeting

Signal peptide

Ubiquitin

E1 Ubiquitin-activating enzyme (UBA1, UBA2, UBA3, UBA5, UBA6, UBA7, ATG7, NAE1, SAE1)

E2 Ubiquitin-conjugating enzyme (A • B • C • D1, D2, D3 • E1, E2, E3 • G1, G2 • H • I • J1, J2 • K • L1, L2, L3, L4, L6 • M • N • O • Q1, Q2 • R1 (CDC34), R2 • S • V1, V2 • Z)

E3 Ubiquitin ligase (VHL, Cullin, CBL, MDM2, FANCL, UBR1)

Deubiquitinating enzyme: Ataxin 3 • USP6 • CYLD

ATG3 • BIRC6 • UFC1

Other

SUMO protein

see also posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

HSPA6

References

Further reading

External links