[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. TISSUE=Lung; PubMed=2327978 [NCBI, ExPASy, EBI, Israel, Japan] Leung T.K.C., Rajendran M.Y., Monfries C., Hall C., Lim L.; "The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA."; Biochem. J. 267:125-132(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Ovary, and Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-250. DOI=10.1016/0888-7543(92)90409-L; PubMed=1346391 [NCBI, ExPASy, EBI, Israel, Japan] Leung T.K.C., Hall C., Rajendran M., Spurr N.K., Lim L.; "The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1."; Genomics 12:74-79(1992).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6. DOI=10.1016/0022-2836(88)90094-0; PubMed=3184191 [NCBI, ExPASy, EBI, Israel, Japan] Schiller P., Amin J., Ananthan J., Brown M.E., Scott W.A., Voellmy R.; "Cis-acting elements involved in the regulated expression of a human HSP70 gene."; J. Mol. Biol. 203:97-105(1988).
[5]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).
INDUCTION: Only at higher temperatures, and no basal expression.
SIMILARITY: Belongs to the heat shock protein 70 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X51757; CAA36061.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X51758; CAA36062.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004279; AAH04279.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC035665; AAH35665.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S78631; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

IPI00339269; -.

S09036; S09036.

NP_002146.2; -.

3D structure databases

PDB

3FE1; X-ray; 2.20 A; A/B/C=6-385.

[ExPASy / RCSB / EBI]

3FE1; -.

P17066; 8-556.

Protein-protein interaction databases

IntAct

P17066; 13.

PTM databases

PhosphoSite

P17066; -.

2D gel databases

HSC-2DPAGE

P17066; -.

Organism-specific databases

GeneCards

GC01P159760; -.
GC01P159761; -.

HGNC:5239; HSPA6.

CAB017452; -.

140555; gene. [NCBI / EBI]

PharmGKB

PA29505; -.

Gene expression databases

Bgee

P17066; -.

CleanEx

HS_HSPA6; -.

GermOnline

ENSG00000173110; Homo sapiens.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006986;	Biological process: response to unfolded protein (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR018181; Heat_shock_70_CS.
IPR001023; Hsp70.
IPR013126; Hsp_70.
Graphical view of domain structure.

PANTHER

PTHR19375; Hsp70; 1.

Pfam

PF00012; HSP70; 1.
Pfam graphical view of domain structure.

PRINTS

PR00301; HEATSHOCK70.

ProDom

PD000089; Hsp70; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00297; HSP70_1; 1.
PS00329; HSP70_2; 1.
PS01036; HSP70_3; 1.

Proteomic databases

PRIDE

P17066; -.

Genome annotation databases

Ensembl

ENSG00000173110; Homo sapiens. [Contig view]

GeneID

3310; -.

KEGG

hsa:3310; -.

Phylogenomic databases

HOGENOM

P17066; -.

HOVERGEN

P17066; -.

OMA

P17066; IQRNATI.

Other

13127; -.

HSPA6; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; Nucleotide-binding; Polymorphism; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 643`	`643`	`Heat shock 70 kDa protein 6.`	`PRO_0000078264`
`VARIANT`	`150 150`	`1`	`A -> T (in dbSNP:rs10919224 [NCBI]).`	`VAR_049605 [3D]`
`VARIANT`	`153 153`	`1`	`N -> S (in dbSNP:rs10919225 [NCBI]).`	`VAR_049606 [3D]`
`VARIANT`	`154 154`	`1`	`D -> N (in dbSNP:rs10919226 [NCBI]).`	`VAR_049607 [3D]`
`VARIANT`	`170 170`	`1`	`N -> K (in dbSNP:rs41297704 [NCBI]).`	`VAR_049608 [3D]`
`VARIANT`	`173 173`	`1`	`R -> P (in dbSNP:rs41297708 [NCBI]).`	`VAR_049609 [3D]`
`VARIANT`	`178 178`	`1`	`P -> A (in dbSNP:rs41297710 [NCBI]).`	`VAR_049610 [3D]`
`VARIANT`	`194 194`	`1`	`E -> K (in dbSNP:rs41297714 [NCBI]).`	`VAR_049611 [3D]`
`VARIANT`	`198 198`	`1`	`L -> F (in dbSNP:rs1079109 [NCBI]).`	`VAR_024182 [3D]`
`VARIANT`	`260 260`	`1`	`R -> H (in dbSNP:rs41299256 [NCBI]).`	`VAR_049612 [3D]`
`VARIANT`	`464 464`	`1`	`S -> I (in dbSNP:rs388218 [NCBI]).`	`VAR_049613`
`VARIANT`	`471 471`	`1`	`R -> H (in dbSNP:rs41299256 [NCBI]).`	`VAR_049614`
`VARIANT`	`528 528`	`1`	`K -> E (in dbSNP:rs570189 [NCBI]).`	`VAR_049615`
`VARIANT`	`562 562`	`1`	`D -> E (in dbSNP:rs753856 [NCBI]).`	`VAR_024183`
`VARIANT`	`572 572`	`1`	`M -> V (in dbSNP:rs452004 [NCBI]).`	`VAR_049616`
`VARIANT`	`577 577`	`1`	`R -> Q (in dbSNP:rs368844 [NCBI]).`	`VAR_049617`
`VARIANT`	`626 626`	`1`	`T -> A (in dbSNP:rs41299260 [NCBI]).`	`VAR_049618`
`CONFLICT`	`106 108`		`RVC -> PVS (in Ref. 1 and 3).`
`CONFLICT`	`263 263`		`R -> G (in Ref. 1; CAA36061).`

Sequence information

Length: 643 AA [This is the length of the unprocessed precursor]

Molecular weight: 71028 Da [This is the MW of the unprocessed precursor]

CRC64: BCE348F0226DB70B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ 

        70         80         90        100        110        120 
AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG GKPKVRVCYR GEDKTFYPEE 

       130        140        150        160        170        180 
ISSMVLSKMK ETAEAYLGQP VKHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA 

       190        200        210        220        230        240 
AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV 

       250        260        270        280        290        300 
NHFMEEFRRK HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT 

       310        320        330        340        350        360 
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK LLQDFFNGKE 

       370        380        390        400        410        420 
LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA 

       430        440        450        460        470        480 
TIPTKQTQTF TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF 

       490        500        510        520        530        540 
DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA 

       550        560        570        580        590        600 
KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE 

       610        620        630        640 
LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD

P17066 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools