P08107 (HSP71_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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
AND
Name:	HSPA1B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.17
Subunit structure	Component of a complex composed at least of CATSPER1, CATSPERB, CATSPERG and HSPA1B By similarity. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with TSC2. Interacts with IRAK1BP1. Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed. Interacts with DNAJC7. Interacts with CHCHD3. Ref.12 Ref.13 Ref.14 Ref.16 Ref.22 Ref.27
Subcellular location	Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.20
Tissue specificity	HSPA1B is testis-specific.
Induction	By heat shock.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone Host cell receptor for virus entry Receptor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB mRNA catabolic process Inferred from direct assay. Source: UniProtKB negative regulation of cell growth Inferred from mutant phenotype. Source: UniProtKB negative regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB negative regulation of inclusion body assembly Inferred from direct assay. Source: BHF-UCL protein refolding Inferred from direct assay. Source: BHF-UCL response to unfolded protein Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome endoplasmic reticulum Traceable author statement. Source: UniProtKB inclusion body Inferred from direct assay. Source: BHF-UCL mitochondrion Traceable author statement. Source: UniProtKB nuclear speck Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB ribonucleoprotein complex Inferred from direct assay Ref.20. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein N-terminus binding Inferred from physical interaction. Source: UniProtKB protein binding involved in protein folding Inferred from direct assay. Source: BHF-UCL receptor activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin protein ligase binding Inferred from physical interaction. Source: BHF-UCL unfolded protein binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGFR	P00533	4	EBI-629985,EBI-297353
GATA1	P15976	5	EBI-629985,EBI-3909284
MME	P08473	3	EBI-629985,EBI-353759
SSE1	P32589	2	EBI-629985,EBI-8648	From a different organism.
STUB1	Q9UNE7	3	EBI-629985,EBI-357085

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 641

640

Heat shock 70 kDa protein 1A/1B

PRO_0000078249

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.24

Modified residue

41

1

Phosphotyrosine Ref.19

Modified residue

106

1

Phosphoserine Ref.24

Modified residue

107

1

Phosphotyrosine Ref.24

Modified residue

108

1

N6-acetyllysine Ref.25

Modified residue

246

1

N6-acetyllysine Ref.25

Modified residue

348

1

N6-acetyllysine Ref.25

Modified residue

611

1

Phosphotyrosine Ref.21

Modified residue

631

1

Phosphoserine Ref.15 Ref.18 Ref.23

Natural variations

Natural variant

95

1

I → V. Ref.5

VAR_032152

Natural variant

110

1

E → D. Ref.3 Ref.5 Ref.6
Corresponds to variants rs17856061 [ dbSNP | Ensembl ] and rs562047 [ dbSNP | Ensembl ].

VAR_029053

Natural variant

467

1

A → V. Ref.5

VAR_032153

Natural variant

499

1

N → S. Ref.3 Ref.5
Corresponds to variants rs17855850 [ dbSNP | Ensembl ] and rs483638 [ dbSNP | Ensembl ].

VAR_029054

Experimental info

Sequence conflict

7

1

I → V in AAA52697. Ref.2

Sequence conflict

7

1

I → V in CAA28381. Ref.9

Sequence conflict

370

1

A → G in AAA52697. Ref.2

Sequence conflict

469

1

Missing in AAA52697. Ref.2

Secondary structure

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641

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Beta strand

13 – 22

10

Beta strand

25 – 28

4

Beta strand

36 – 39

4

Beta strand

42 – 44

3

Beta strand

49 – 51

3

Helix

53 – 57

5

Helix

58 – 61

4

Helix

63 – 65

3

Helix

70 – 73

4

Helix

81 – 87

7

Beta strand

91 – 97

7

Beta strand

100 – 107

8

Beta strand

110 – 114

5

Helix

116 – 135

20

Beta strand

141 – 146

6

Helix

152 – 164

13

Beta strand

168 – 174

7

Helix

175 – 182

8

Turn

183 – 186

4

Beta strand

190 – 200

11

Beta strand

205 – 213

9

Beta strand

219 – 225

7

Helix

230 – 248

19

Helix

257 – 273

17

Turn

274 – 276

3

Beta strand

277 – 288

12

Beta strand

291 – 298

8

Helix

299 – 312

14

Helix

314 – 323

10

Helix

328 – 330

3

Beta strand

332 – 338

7

Helix

339 – 342

4

Helix

344 – 353

10

Turn

354 – 356

3

Turn

365 – 367

3

Helix

368 – 380

13

Sequences

	Sequence		Length	Mass (Da)
	P08107 [UniParc]. Last modified May 15, 2007. Version 5. Checksum: 78F513118C96DE66	FASTA	641	70,052
	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

References

	« Hide 'large scale' referencesShow '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: 1700760] [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: 3931075] [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: 14656967] [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]	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.
[6]	"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. , 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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-110.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Muscle, Pancreas, PNS and Skin.
[8]	"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: 2538825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36 AND 360-424.
[9]	"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: 3786141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22 AND 617-641.
[10]	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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	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, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[12]	"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: 11274138] [Abstract] Cited for: INTERACTION WITH TERT.
[13]	"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: 12853476] [Abstract] Cited for: INTERACTION WITH DNAJC7.
[14]	"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: 15963462] [Abstract] Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY.
[15]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 17233114] [Abstract] Cited for: INTERACTION WITH IRAK1BP1, MASS SPECTROMETRY.
[17]	"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: 16537599] [Abstract] Cited for: FUNCTION AS A RECEPTOR FOR ROTAVIRUS A.
[18]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[20]	"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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[21]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-611, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 18620420] [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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND TYR-107, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246 AND LYS-348, MASS SPECTROMETRY.
[26]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"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: 21081504] [Abstract] Cited for: INTERACTION WITH CHCHD3.
[28]	"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: 10216320] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382.
[29]	"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: 20223214] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-388 IN COMPLEX WITH BAG5.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
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.

IPI

IPI00304925.

PIR

A29160.
A45871.
I59139.
I79540.

RefSeq

NP_005336.3. NM_005345.5.
NP_005337.2. NM_005346.4.

UniGene

Hs.274402.
Hs.719966.
Hs.728810.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HJO	X-ray	2.30	A	3-382	[»]
1S3X	X-ray	1.84	A	1-382	[»]
1XQS	X-ray	2.90	C/D	184-371	[»]
2E88	X-ray	1.80	A	1-388	[»]
2E8A	X-ray	1.77	A	1-388	[»]
3A8Y	X-ray	2.30	A/B	1-388	[»]
3D2E	X-ray	2.35	B/D	1-382	[»]
3D2F	X-ray	2.30	B/D	1-382	[»]
3JXU	X-ray	2.14	A	1-387	[»]
3LOF	X-ray	2.40	A/B/C/D/E/F	534-641	[»]

ProteinModelPortal

P08107.

SMR

P08107. Positions 1-613.

ModBase

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Protein-protein interaction databases

DIP

DIP-211N.

IntAct

P08107. 60 interactions.

MINT

MINT-96699.

STRING

P08107.

Protein family/group databases

TCDB

1.A.33.1.3. cation channel-forming heat shock protein-70 (Hsp70) family.

PTM databases

PhosphoSite

P08107.

2D gel databases

SWISS-2DPAGE

P08107.

Cornea-2DPAGE

P08107.

DOSAC-COBS-2DPAGE

P08107.

OGP

P08107.

REPRODUCTION-2DPAGE

IPI00304925.

UCD-2DPAGE

P08107.

Proteomic databases

PRIDE

P08107.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000375650; ENSP00000364801; ENSG00000204388.
ENST00000375651; ENSP00000364802; ENSG00000204389.
ENST00000391548; ENSP00000375391; ENSG00000224501.
ENST00000391555; ENSP00000375399; ENSG00000212866.
ENST00000430065; ENSP00000404524; ENSG00000235941.
ENST00000433487; ENSP00000408907; ENSG00000234475.
ENST00000441618; ENSP00000406359; ENSG00000237724.
ENST00000445736; ENSP00000403530; ENSG00000231555.
ENST00000450744; ENSP00000393087; ENSG00000232804.

GeneID

3303.
3304.

KEGG

hsa:3303.
hsa:3304.

UCSC

uc003nxk.2. human.

Organism-specific databases

CTD

3303.
3304.

GeneCards

GC06P031796.
GC06P031797.

H-InvDB

HIX0005734.
HIX0057751.
HIX0058169.

HGNC

HGNC:5232. HSPA1A.
HGNC:5233. HSPA1B.

HPA

CAB008640.
CAB032815.

MIM

140550. gene.
603012. gene.

neXtProt

NX_P08107.

GenAtlas

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Phylogenomic databases

eggNOG

maNOG16200.

HOGENOM

HBG334976.

HOVERGEN

HBG051845.

InParanoid

P08107.

OMA

MAKSTAI.

OrthoDB

EOG4W6NVK.

PhylomeDB

P08107.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P08107.

CleanEx

HS_HSPA1A.

Genevestigator

P08107.

GermOnline

ENSG00000204388. Homo sapiens.
ENSG00000204389. Homo sapiens.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]

KO

K03283.

PANTHER

PTHR19375. Hsp70. 1 hit.

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

13107.

SOURCE

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Entry information

Entry name

HSP71_HUMAN

Accession

Primary (citable) accession number: P08107
Secondary accession number(s): P19790 , Q5JQI4, Q5SP17, Q9UQL9, Q9UQM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 15, 2007
Last modified:	January 25, 2012
This is version 153 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.