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UniProtKB/Swiss-Prot entry P08107


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HSP71_HUMAN
Primary accession number P08107
Secondary accession numbers P19790 Q5JQI4 Q5SP17 Q9UQL9 Q9UQM0
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on May 15, 2007 (Sequence version 5)
Annotations were last modified on    November 4, 2008 (Entry version 113)
Name and origin of the protein
Protein name Heat shock 70 kDa protein 1
Synonyms HSP70.1
HSP70-1/HSP70-2
Gene names
Name: HSPA1A
Synonyms: HSPA1
and
Name: HSPA1B
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00187095; PubMed=1700760 [NCBI, ExPASy, EBI, Israel, Japan]
Milner C.M., Campbell R.D.;
"Structure and expression of the three MHC-linked HSP70 genes.";
Immunogenetics 32:242-251(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3931075 [NCBI, ExPASy, EBI, Israel, Japan]
Hunt C., Morimoto R.I.;
"Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70.";
Proc. Natl. Acad. Sci. U.S.A. 82:6455-6459(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HSPA1A AND HSPA1B), AND VARIANTS ASP-110 AND SER-499.
DOI=10.1101/gr.1736803; PubMed=14656967 [NCBI, ExPASy, EBI, Israel, Japan]
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HSPA1A AND HSPA1B).
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-95; ASP-110; VAL-467 AND SER-499.
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-110.
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Muscle, Pancreas, PNS, 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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36 AND 360-424.
PubMed=2538825 [NCBI, ExPASy, EBI, Israel, Japan]
Sargent C.A., Dunham I., Trowsdale J., Campbell R.D.;
"Human major histocompatibility complex contains genes for the major heat shock protein HSP70.";
Proc. Natl. Acad. Sci. U.S.A. 86:1968-1972(1989).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22 AND 617-641.
DOI=10.1093/nar/14.22.8933; PubMed=3786141 [NCBI, ExPASy, EBI, Israel, Japan]
Drabent B., Genthe A., Benecke B.-J.;
"In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells.";
Nucleic Acids Res. 14:8933-8948(1986).
[10]
PROTEIN SEQUENCE OF 237-247; 329-342 AND 349-357, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[11]
INTERACTION WITH TSC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1016/j.bbrc.2005.05.175; PubMed=15963462 [NCBI, ExPASy, EBI, Israel, Japan]
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.;
"Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.";
Biochem. Biophys. Res. Commun. 333:818-826(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[13]
INTERACTION WITH IRAK1BP1, AND MASS SPECTROMETRY.
DOI=10.1089/dna.2006.25.704; PubMed=17233114 [NCBI, ExPASy, EBI, Israel, Japan]
Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.;
"The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family.";
DNA Cell Biol. 25:704-714(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-611, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382.
DOI=10.1107/S0907444999002103; PubMed=10216320 [NCBI, ExPASy, EBI, Israel, Japan]
Osipiuk J., Walsh M.A., Freeman B.C., Morimoto R.I., Joachimiak A.;
"Structure of a new crystal form of human hsp70 ATPase domain.";
Acta Crystallogr. D 55:1105-1107(1999).
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.
  • SUBUNIT: HSPA1B is found in a sperm-specific complex with CATSPER1 and CATSPERB (By similarity). Interacts with TSC2. Interacts with IRAK1BP1.
  • INTERACTION:
    P08473:MME; NbExp=1; IntAct=EBI-629985, EBI-353759;
  • TISSUE SPECIFICITY: HSPA1B is testis-specific.
  • INDUCTION: By heat shock.
  • 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
M59828; AAA63226.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M59830; AAA63227.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11717; AAA52697.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134726; AAD21815.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134726; AAD21816.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000025; BAB63299.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000025; BAB63300.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ388429; ABD48956.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ451402; ABD96830.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662834; CAI17737.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662834; CAI17738.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL671762; CAI18216.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL671762; CAI18217.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL929592; CAI18464.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL929592; CAI18466.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002453; AAH02453.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009322; AAH09322.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018740; AAH18740.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC057397; AAH57397.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063507; AAH63507.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24743; AAA59844.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24744; AAA59845.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04676; CAA28381.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04677; CAA28382.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29160; A29160.
A45871; A45871.
I59139; I59139.
I79540; I79540.
RefSeq NP_005336.3; -.
NP_005337.2; -.
UniGene Hs.274402
3D structure databases
PDB
1HJO; X-ray; 2.30 A; A=3-382.[ExPASy / RCSB / EBI]
1S3X; X-ray; 1.84 A; A=1-382.[ExPASy / RCSB / EBI]
1XQS; X-ray; 2.90 A; C/D=182-371.[ExPASy / RCSB / EBI]
2E88; X-ray; 1.80 A; A=1-388.[ExPASy / RCSB / EBI]
2E8A; X-ray; 1.77 A; A=1-388.[ExPASy / RCSB / EBI]
3D2E; X-ray; 2.35 A; B/D=1-382.[ExPASy / RCSB / EBI]
3D2F; X-ray; 2.30 A; B/D=1-382.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HJO; -.
1S3X; -.
1XQS; -.
2E88; -.
2E8A; -.
3D2E; -.
3D2F; -.
SMR P08107; 1-554.
ModBase P08107.
Protein-protein interaction databases
DIP DIP:211N; -.
IntAct P08107; -.
PTM databases
PhosphoSite P08107; -.
Polymorphism databases
NIEHS-SNPs HSPA1A.
2D gel databases
SWISS-2DPAGE P08107; -.
Cornea-2DPAGE P08107; -.
DOSAC-COBS-2DPAGE P08107; -.
OGP P08107; -.
REPRODUCTION-2DPAGE IPI00304925; -.
Organism-specific databases
H-InvDB HIX0005734; -.
HIX0057728; -.
HGNC HGNC:5232; HSPA1A.
HGNC:5233; HSPA1B.
GenAtlas HSPA1A.
HPA CAB008640; -.
MIM 140550; gene. [NCBI / EBI]
603012; gene. [NCBI / EBI]
PharmGKB PA29498; -.
GeneCards P08107.
Gene expression databases
ArrayExpress P08107; -.
CleanEx HS_HSPA1A; -.
HS_HSPA1B; -.
GermOnline ENSG00000204388; Homo sapiens.
ENSG00000204389; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (traceable author statement from UniProtKB).
GO:0005739; Cellular component: mitochondrion (traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0051082; Molecular function: unfolded protein binding (traceable author statement from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0006402; Biological process: mRNA catabolic process (traceable author statement from ProtInc).
GO:0006986; Biological process: response to unfolded protein (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro 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.
BLOCKS P08107.
ProtoNet P08107.
Genome annotation databases
Ensembl ENSG00000204388; Homo sapiens. [Contig view]
ENSG00000204389; Homo sapiens. [Contig view]
ENSG00000212860; Homo sapiens. [Contig view]
ENSG00000212866; Homo sapiens. [Contig view]
ENSG00000215292; Homo sapiens. [Contig view]
GeneID 3303; -.
3304; -.
KEGG hsa:3304; -.
Phylogenomic databases
HOVERGEN P08107; -.
Other
NextBio 13107; -.
SOURCE HSPA1A; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Chaperone; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Polymorphism; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   641  641     Heat shock 70 kDa protein 1. PRO_0000078249
MOD_RES   611   611        Phosphotyrosine. 
MOD_RES   631   631        Phosphoserine. 
VARIANT   95    95  1     I -> V. VAR_032152 [3D]
VARIANT   110   110  1     E -> D (in dbSNP:rs17856061 [NCBI] and dbSNP:rs562047 [NCBI]). VAR_029053 [3D]
VARIANT   467   467  1     A -> V. VAR_032153 
VARIANT   499   499  1     N -> S (in dbSNP:rs17855850 [NCBI] and dbSNP:rs483638 [NCBI]). VAR_029054 
CONFLICT   7     7        I -> V (in Ref. 2; AAA52697 and 9; CAA28381). 
CONFLICT   370   370        A -> G (in Ref. 2; AAA52697). 
CONFLICT   469   469        Missing (in Ref. 2; AAA52697). 
STRAND   7    11  5      
STRAND   13    22  10      
STRAND   25    28  4      
STRAND   36    39  4      
STRAND   42    44  3      
STRAND   49    51  3      
HELIX   53    57  5      
HELIX   58    61  4      
HELIX   63    65  3      
HELIX   70    73  4      
HELIX   81    87  7      
STRAND   91    97  7      
STRAND   100   107  8      
STRAND   110   114  5      
HELIX   116   135  20      
STRAND   141   146  6      
HELIX   152   164  13      
STRAND   168   174  7      
HELIX   175   182  8      
TURN   183   186  4      
STRAND   190   200  11      
STRAND   205   213  9      
STRAND   219   225  7      
HELIX   230   248  19      
HELIX   257   273  17      
TURN   274   276  3      
STRAND   277   288  12      
STRAND   291   298  8      
HELIX   299   312  14      
HELIX   314   323  10      
HELIX   328   330  3      
STRAND   332   338  7      
HELIX   339   342  4      
HELIX   344   353  10      
TURN   354   356  3      
TURN   365   367  3      
HELIX   368   380  13      
Sequence information
Length: 641 AA [This is the length of the unprocessed precursor] Molecular weight: 70052 Da [This is the MW of the unprocessed precursor] CRC64: 78F513118C96DE66 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 

        70         80         90        100        110        120 
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS 

       130        140        150        160        170        180 
SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA 

       190        200        210        220        230        240 
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH 

       250        260        270        280        290        300 
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA 

       310        320        330        340        350        360 
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN 

       370        380        390        400        410        420 
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI 

       430        440        450        460        470        480 
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI 

       490        500        510        520        530        540 
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN 

       550        560        570        580        590        600 
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE 

       610        620        630        640 
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D 

P08107 in FASTA format

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View entry in raw text format (no links)
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