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P08107 (HSP71_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 182. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock 70 kDa protein 1A/1B
Alternative name(s):
Heat shock 70 kDa protein 1/2
Short name=HSP70-1/HSP70-2
Short name=HSP70.1/HSP70.2
Gene names
Name:HSPA1A
Synonyms:HSPA1, HSX70
AND
Name:HSPA1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Ref.20

Subunit structure

Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2. Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed. Interacts with TRIM5 (via B30.2/SPRY domain). Interacts with METTL21A. Interacts with PARK2. Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.26 Ref.29 Ref.30 Ref.31

Subcellular location

Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.21

Tissue specificity

HSPA1B is testis-specific.

Induction

By heat shock.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
Host cell receptor for virus entry
Receptor
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.30. Source: BHF-UCL

RNA metabolic process

Traceable author statement. Source: Reactome

cellular heat acclimation

Inferred from mutant phenotype PubMed 21231916. Source: UniProt

cellular response to heat

Inferred from direct assay PubMed 24061851. Source: UniProt

gene expression

Traceable author statement. Source: Reactome

mRNA catabolic process

Inferred from direct assay PubMed 10205060. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17167422. Source: UniProtKB

negative regulation of cell death

Inferred from mutant phenotype PubMed 21231916. Source: UniProt

negative regulation of cell growth

Inferred from mutant phenotype PubMed 9553041. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 9553041. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 17167422. Source: BHF-UCL

negative regulation of inclusion body assembly

Inferred from direct assay PubMed 15603737. Source: BHF-UCL

positive regulation of erythrocyte differentiation

Inferred from mutant phenotype PubMed 17167422. Source: UniProtKB

protein refolding

Inferred from direct assay PubMed 15603737. Source: BHF-UCL

response to unfolded protein

Inferred from direct assay PubMed 10859165. Source: UniProtKB

   Cellular_componentaggresome

Inferred from direct assay PubMed 15885686. Source: UniProtKB

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

centriole

Inferred from direct assay PubMed 24061851. Source: UniProt

cytoplasm

Inferred from direct assay PubMed 10859165PubMed 9553041. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 21231916. Source: UniProt

endoplasmic reticulum

Traceable author statement PubMed 16130169. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 20458337. Source: UniProt

inclusion body

Inferred from direct assay PubMed 15603737. Source: BHF-UCL

mitochondrion

Traceable author statement PubMed 16130169. Source: UniProtKB

nuclear speck

Inferred from direct assay PubMed 9553041. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 10205060PubMed 17167422. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 10205060. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.21. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.30. Source: BHF-UCL

ATPase activity

Inferred from direct assay Ref.30. Source: BHF-UCL

ATPase activity, coupled

Inferred from direct assay PubMed 21231916. Source: UniProt

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

enzyme binding

Inferred from physical interaction Ref.30. Source: BHF-UCL

heat shock protein binding

Inferred from physical interaction Ref.30. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 9553041. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.15PubMed 15671022PubMed 18975920Ref.29. Source: UniProtKB

protein binding involved in protein folding

Inferred from direct assay PubMed 15603737. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 15603737. Source: BHF-UCL

unfolded protein binding

Traceable author statement PubMed 16130169. Source: UniProtKB

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08107-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P08107-2)

The sequence of this isoform differs from the canonical sequence as follows:
     96-150: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.24
Chain2 – 641640Heat shock 70 kDa protein 1A/1B
PRO_0000078249

Regions

Nucleotide binding12 – 154ATP
Nucleotide binding202 – 2043ATP
Nucleotide binding268 – 2758ATP
Nucleotide binding339 – 3424ATP

Sites

Binding site711ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.24
Modified residue1081N6-acetyllysine Ref.25
Modified residue2461N6-acetyllysine Ref.25
Modified residue3481N6-acetyllysine Ref.25
Modified residue5611N6,N6,N6-trimethyllysine; by METTL21A Ref.13 Ref.30
Modified residue6311Phosphoserine Ref.27
Modified residue6331Phosphoserine Ref.27
Modified residue6361Phosphothreonine Ref.27

Natural variations

Alternative sequence96 – 15055Missing in isoform 2.
VSP_044427
Natural variant951I → V. Ref.6
VAR_032152
Natural variant1101E → D. Ref.3 Ref.6 Ref.7
Corresponds to variant rs562047 [ dbSNP | Ensembl ].
VAR_029053
Natural variant4671A → V. Ref.6
VAR_032153
Natural variant4991N → S. Ref.3 Ref.6
Corresponds to variant rs483638 [ dbSNP | Ensembl ].
VAR_029054

Experimental info

Mutagenesis101D → A: Reduces affinity for ADP. Ref.36
Mutagenesis1991D → A: Reduces affinity for ADP. Ref.36
Mutagenesis5611K → R: Complete loss of in vitro methylation by METTL21A. Ref.13 Ref.30
Sequence conflict71I → V in AAA52697. Ref.2
Sequence conflict71I → V in CAA28381. Ref.10
Sequence conflict3551N → D in BAG65428. Ref.5
Sequence conflict3701A → G in AAA52697. Ref.2
Sequence conflict4691Missing in AAA52697. Ref.2
Sequence conflict4971K → N in BAG65428. Ref.5

Secondary structure

............................................................................... 641
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 15, 2007. Version 5.
Checksum: 78F513118C96DE66

FASTA64170,052
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 6FBA863FEACE9DF1
Show »

FASTA58663,937

References

« Hide 'large scale' references
[1]"Structure and expression of the three MHC-linked HSP70 genes."
Milner C.M., Campbell R.D.
Immunogenetics 32:242-251(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70."
Hunt C., Morimoto R.I.
Proc. Natl. Acad. Sci. U.S.A. 82:6455-6459(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HSPA1A AND HSPA1B), VARIANTS ASP-110 AND SER-499.
[4]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HSPA1A AND HSPA1B).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterus.
[6]NIEHS SNPs program
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-95; ASP-110; VAL-467 AND SER-499.
[7]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-110.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain, Muscle, Pancreas, PNS and Skin.
[9]"Human major histocompatibility complex contains genes for the major heat shock protein HSP70."
Sargent C.A., Dunham I., Trowsdale J., Campbell R.D.
Proc. Natl. Acad. Sci. U.S.A. 86:1968-1972(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36 AND 360-424.
[10]"In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells."
Drabent B., Genthe A., Benecke B.-J.
Nucleic Acids Res. 14:8933-8948(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22 AND 617-641.
[11]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 77-155; 160-187; 221-247; 273-311; 326-342; 349-357; 362-416; 424-447; 459-469; 510-517; 540-550; 574-595 AND 598-641, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 37-49; 57-71; 78-88; 113-126; 160-187; 221-247; 302-311; 329-342; 349-357; 362-384; 540-550 AND 574-589, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[13]"A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, IDENTIFICATION BY MASS SPECTROMETRY.
[14]"Stable association of hsp90 and p23, but Not hsp70, with active human telomerase."
Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.
J. Biol. Chem. 276:15571-15574(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERT.
[15]"Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system."
Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M.
EMBO J. 22:3613-3623(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC7.
[16]"Phosphorylation and binding partner analysis of the TSC1-TSC2 complex."
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.
Biochem. Biophys. Res. Commun. 333:818-826(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole."
Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.
Biochem. J. 385:45-56(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP5C, IDENTIFICATION BY MASS SPECTROMETRY.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family."
Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.
DNA Cell Biol. 25:704-714(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRAK1BP1, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity."
Perez-Vargas J., Romero P., Lopez S., Arias C.F.
J. Virol. 80:3322-3331(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR ROTAVIRUS A.
[21]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[22]"Role of the cochaperone Tpr2 in Hsp90 chaperoning."
Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.
Biochemistry 47:8203-8213(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC7.
[23]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[25]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246 AND LYS-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha."
Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.
J. Biol. Chem. 285:7827-7837(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM5.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-633 AND THR-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function."
Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A., Perkins G.A., Ellisman M.H., Taylor S.S.
J. Biol. Chem. 286:2918-2932(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHCHD3.
[30]"Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, INTERACTION WITH METTL21A.
[31]"High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARK2.
[32]"Structure of a new crystal form of human hsp70 ATPase domain."
Osipiuk J., Walsh M.A., Freeman B.C., Morimoto R.I., Joachimiak A.
Acta Crystallogr. D 55:1105-1107(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382 IN COMPLEX WITH ADP, ATP-BINDING.
[33]"Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state."
Shida M., Arakawa A., Ishii R., Kishishita S., Takagi T., Kukimoto-Niino M., Sugano S., Tanaka A., Shirouzu M., Yokoyama S.
Acta Crystallogr. D 66:223-232(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 389-641 IN COMPLEX WITH ATP ANALOG, ATP-BINDING.
[34]"Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 1-387 IN COMPLEX WITH ADP, ATP-BINDING.
[35]"The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange."
Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F., Shirouzu M., Yokoyama S.
Structure 18:309-319(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-388 IN COMPLEX WITH BAG5.
[36]"Biochemical and structural studies on the high affinity of Hsp70 for ADP."
Arakawa A., Handa N., Shirouzu M., Yokoyama S.
Protein Sci. 20:1367-1379(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-388, ATP-BINDING, MUTAGENESIS OF ASP-10 AND ASP-199.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59828 Genomic DNA. Translation: AAA63226.1.
M59830 Genomic DNA. Translation: AAA63227.1.
M11717 Genomic DNA. Translation: AAA52697.1.
AF134726 Genomic DNA. Translation: AAD21815.1.
AF134726 Genomic DNA. Translation: AAD21816.1.
BA000025 Genomic DNA. Translation: BAB63299.1.
BA000025 Genomic DNA. Translation: BAB63300.1.
AK304652 mRNA. Translation: BAG65428.1.
DQ388429 Genomic DNA. Translation: ABD48956.1.
DQ451402 Genomic DNA. Translation: ABD96830.1.
AL662834 Genomic DNA. Translation: CAI17737.1.
AL662834 Genomic DNA. Translation: CAI17738.1.
AL671762 Genomic DNA. Translation: CAI18216.1.
AL671762 Genomic DNA. Translation: CAI18217.1.
AL929592 Genomic DNA. Translation: CAI18464.1.
AL929592 Genomic DNA. Translation: CAI18466.1.
BC002453 mRNA. Translation: AAH02453.1.
BC009322 mRNA. Translation: AAH09322.1.
BC018740 mRNA. Translation: AAH18740.1.
BC057397 mRNA. Translation: AAH57397.1.
BC063507 mRNA. Translation: AAH63507.1.
M24743 Genomic DNA. Translation: AAA59844.1.
M24744 Genomic DNA. Translation: AAA59845.1.
X04676 Genomic DNA. Translation: CAA28381.1.
X04677 Genomic DNA. Translation: CAA28382.1.
CCDSCCDS34414.1. [P08107-1]
CCDS34415.1. [P08107-1]
PIRA29160.
A45871.
I59139.
I79540.
RefSeqNP_005336.3. NM_005345.5. [P08107-1]
NP_005337.2. NM_005346.4. [P08107-1]
UniGeneHs.274402.
Hs.702139.
Hs.719966.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HJOX-ray2.30A3-382[»]
1S3XX-ray1.84A1-382[»]
1XQSX-ray2.90C/D184-371[»]
2E88X-ray1.80A1-388[»]
2E8AX-ray1.77A1-388[»]
2LMGNMR-A537-610[»]
3A8YX-ray2.30A/B1-388[»]
3ATUX-ray1.65A1-388[»]
3ATVX-ray1.58A1-388[»]
3AY9X-ray1.75A1-388[»]
3D2EX-ray2.35B/D1-382[»]
3D2FX-ray2.30B/D1-382[»]
3JXUX-ray2.14A1-387[»]
3LOFX-ray2.40A/B/C/D/E/F534-641[»]
4IO8X-ray2.58A1-382[»]
4J8FX-ray2.70A1-382[»]
ProteinModelPortalP08107.
SMRP08107. Positions 1-613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109535. 178 interactions.
109536. 84 interactions.
DIPDIP-211N.
IntActP08107. 109 interactions.
MINTMINT-96699.
STRING9606.ENSP00000364802.

Chemistry

BindingDBP08107.
ChEMBLCHEMBL5460.

Protein family/group databases

TCDB1.A.33.1.3. the cation channel-forming heat shock protein-70 (hsp70) family.

PTM databases

PhosphoSiteP08107.

Polymorphism databases

DMDM147744565.

2D gel databases

DOSAC-COBS-2DPAGEP08107.
OGPP08107.
REPRODUCTION-2DPAGEIPI00304925.
SWISS-2DPAGEP08107.
UCD-2DPAGEP08107.

Proteomic databases

MaxQBP08107.
PaxDbP08107.
PRIDEP08107.

Protocols and materials databases

DNASU3303.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375650; ENSP00000364801; ENSG00000204388. [P08107-1]
ENST00000375651; ENSP00000364802; ENSG00000204389. [P08107-1]
ENST00000391548; ENSP00000375391; ENSG00000224501. [P08107-1]
ENST00000391555; ENSP00000375399; ENSG00000212866. [P08107-1]
ENST00000400040; ENSP00000382915; ENSG00000215328.
ENST00000430065; ENSP00000404524; ENSG00000235941. [P08107-1]
ENST00000433487; ENSP00000408907; ENSG00000234475. [P08107-1]
ENST00000441618; ENSP00000406359; ENSG00000237724. [P08107-1]
ENST00000445736; ENSP00000403530; ENSG00000231555. [P08107-1]
ENST00000450744; ENSP00000393087; ENSG00000232804. [P08107-1]
GeneID3303.
3304.
KEGGhsa:3303.
hsa:3304.
UCSCuc003nxj.3. human. [P08107-1]

Organism-specific databases

CTD3303.
3304.
GeneCardsGC06P031823.
GC06P031824.
GC06Pi31794.
GC06Pi31806.
GC06Pj31770.
GC06Pj31782.
GC06Pk31765.
GC06Pk31777.
GC06Pn31773.
GC06Pn31785.
H-InvDBHIX0058169.
HIX0058187.
HIX0166160.
HGNCHGNC:5232. HSPA1A.
HGNC:5233. HSPA1B.
HPACAB008640.
CAB017451.
CAB032815.
HPA052504.
MIM140550. gene.
603012. gene.
neXtProtNX_P08107.
PharmGKBPA29499.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP08107.
KOK03283.
OMAIRSSARC.
OrthoDBEOG7PCJGF.
PhylomeDBP08107.
TreeFamTF105042.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP08107.
BgeeP08107.
CleanExHS_HSPA1A.
GenevestigatorP08107.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA1A. human.
EvolutionaryTraceP08107.
GeneWikiHSPA1A.
NextBio13103.
PROP08107.
SOURCESearch...

Entry information

Entry nameHSP71_HUMAN
AccessionPrimary (citable) accession number: P08107
Secondary accession number(s): B4E3B6 expand/collapse secondary AC list , P19790, Q5JQI4, Q5SP17, Q9UQL9, Q9UQM0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 182 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM