SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P08107

- HSP71_HUMAN

UniProt

P08107 - HSP71_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Heat shock 70 kDa protein 1A/1B
Gene
HSPA1A, HSPA1, HSX70
HSPA1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154ATP
Nucleotide bindingi202 – 2043ATP
Nucleotide bindingi268 – 2758ATP
Nucleotide bindingi339 – 3424ATP

GO - Molecular functioni

  1. ATP binding Source: BHF-UCL
  2. ATPase activity Source: BHF-UCL
  3. ATPase activity, coupled Source: UniProt
  4. double-stranded RNA binding Source: MGI
  5. enzyme binding Source: BHF-UCL
  6. heat shock protein binding Source: BHF-UCL
  7. poly(A) RNA binding Source: UniProtKB
  8. protein N-terminus binding Source: UniProtKB
  9. protein binding Source: UniProtKB
  10. protein binding involved in protein folding Source: BHF-UCL
  11. ubiquitin protein ligase binding Source: BHF-UCL
  12. unfolded protein binding Source: UniProtKB
  13. virus receptor activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: BHF-UCL
  2. RNA metabolic process Source: Reactome
  3. cellular heat acclimation Source: UniProt
  4. cellular response to heat Source: UniProt
  5. gene expression Source: Reactome
  6. mRNA catabolic process Source: UniProtKB
  7. mRNA metabolic process Source: Reactome
  8. negative regulation of apoptotic process Source: UniProtKB
  9. negative regulation of cell death Source: UniProt
  10. negative regulation of cell growth Source: UniProtKB
  11. negative regulation of cell proliferation Source: UniProtKB
  12. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  13. negative regulation of inclusion body assembly Source: BHF-UCL
  14. positive regulation of erythrocyte differentiation Source: UniProtKB
  15. protein refolding Source: BHF-UCL
  16. response to unfolded protein Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_200624. Attenuation phase.
REACT_200775. HSF1-dependent transactivation.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.

Protein family/group databases

TCDBi1.A.33.1.3. the cation channel-forming heat shock protein-70 (hsp70) family.

Names & Taxonomyi

Organism-specific databases

Protein namesi
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 namesi
Name:HSPA1A
Synonyms:HSPA1, HSX70
AND
Name:HSPA1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6
HGNCiHGNC:5232. HSPA1A.
HGNC:5233. HSPA1B.

Subcellular locationi

Cytoplasm
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.1 Publication

GO - Cellular componenti

  1. aggresome Source: UniProtKB
  2. blood microparticle Source: UniProt
  3. centriole Source: UniProt
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: UniProt
  6. endoplasmic reticulum Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProt
  8. inclusion body Source: BHF-UCL
  9. mitochondrion Source: UniProtKB
  10. nuclear speck Source: UniProtKB
  11. nucleus Source: UniProtKB
  12. perinuclear region of cytoplasm Source: UniProtKB
  13. ribonucleoprotein complex Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101D → A: Reduces affinity for ADP. 1 Publication
Mutagenesisi199 – 1991D → A: Reduces affinity for ADP. 1 Publication
Mutagenesisi561 – 5611K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications

Organism-specific databases

PharmGKBiPA29499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 641640Heat shock 70 kDa protein 1A/1B
PRO_0000078249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei108 – 1081N6-acetyllysine1 Publication
Modified residuei246 – 2461N6-acetyllysine1 Publication
Modified residuei348 – 3481N6-acetyllysine1 Publication
Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21A2 Publications
Modified residuei631 – 6311Phosphoserine1 Publication
Modified residuei633 – 6331Phosphoserine1 Publication
Modified residuei636 – 6361Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP08107.
PaxDbiP08107.
PRIDEiP08107.

2D gel databases

DOSAC-COBS-2DPAGEP08107.
OGPiP08107.
REPRODUCTION-2DPAGEIPI00304925.
SWISS-2DPAGEP08107.
UCD-2DPAGEP08107.

PTM databases

PhosphoSiteiP08107.

Expressioni

Tissue specificityi

HSPA1B is testis-specific.

Inductioni

By heat shock.

Gene expression databases

ArrayExpressiP08107.
BgeeiP08107.
CleanExiHS_HSPA1A.
GenevestigatoriP08107.

Organism-specific databases

HPAiCAB008640.
CAB017451.
CAB032815.
HPA052504.

Interactioni

Subunit structurei

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 PARK2.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P298463EBI-629985,EBI-9303062From a different organism.
BCL2L12Q9HB09-22EBI-629985,EBI-6969019
EGFRP005334EBI-629985,EBI-297353
GATA1P159765EBI-629985,EBI-3909284
LoxP283016EBI-629985,EBI-642911From a different organism.
MMEP084733EBI-629985,EBI-353759
Phlda1Q623922EBI-629985,EBI-309727From a different organism.
PLK1P533505EBI-629985,EBI-476768
S100a1P354674EBI-629985,EBI-6477109From a different organism.
SNCAP378407EBI-629985,EBI-985879
SSE1P325892EBI-629985,EBI-8648From a different organism.
STUB1Q9UNE74EBI-629985,EBI-357085

Protein-protein interaction databases

BioGridi109535. 148 interactions.
109536. 52 interactions.
DIPiDIP-211N.
IntActiP08107. 112 interactions.
MINTiMINT-96699.
STRINGi9606.ENSP00000364802.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104
Beta strandi13 – 2210
Beta strandi25 – 284
Beta strandi36 – 394
Beta strandi42 – 443
Beta strandi49 – 513
Helixi53 – 564
Turni57 – 615
Helixi63 – 653
Helixi70 – 734
Helixi81 – 877
Beta strandi91 – 977
Beta strandi100 – 1078
Beta strandi110 – 1145
Helixi116 – 13520
Beta strandi141 – 1466
Helixi152 – 16413
Beta strandi168 – 1747
Helixi175 – 1828
Turni183 – 1864
Beta strandi190 – 20011
Beta strandi205 – 2139
Beta strandi216 – 22510
Helixi226 – 2283
Helixi230 – 24920
Helixi253 – 2553
Helixi257 – 27317
Turni274 – 2763
Beta strandi277 – 28812
Beta strandi291 – 2988
Helixi299 – 3057
Helixi307 – 3115
Helixi314 – 32310
Helixi328 – 3303
Beta strandi333 – 3386
Helixi339 – 3424
Helixi344 – 35310
Turni354 – 3563
Turni365 – 3673
Helixi368 – 38114
Helixi534 – 55320
Helixi556 – 5583
Helixi564 – 58320
Helixi589 – 61224

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP08107.
SMRiP08107. Positions 1-613.

Miscellaneous databases

EvolutionaryTraceiP08107.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP08107.
KOiK03283.
OMAiIRSSARC.
OrthoDBiEOG7PCJGF.
PhylomeDBiP08107.
TreeFamiTF105042.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P08107-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL    50
IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK 100
PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF 150
NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL 200
GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK 250
KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA 300
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL 350
QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS 400
LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT 450
KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK 500
ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK 550
SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE 600
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D 641
Length:641
Mass (Da):70,052
Last modified:May 15, 2007 - v5
Checksum:i78F513118C96DE66
GO
Isoform 2 (identifier: P08107-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:586
Mass (Da):63,937
Checksum:i6FBA863FEACE9DF1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951I → V.1 Publication
VAR_032152
Natural varianti110 – 1101E → D.3 Publications
Corresponds to variant rs562047 [ dbSNP | Ensembl ].
VAR_029053
Natural varianti467 – 4671A → V.1 Publication
VAR_032153
Natural varianti499 – 4991N → S.2 Publications
Corresponds to variant rs483638 [ dbSNP | Ensembl ].
VAR_029054

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei96 – 15055Missing in isoform 2.
VSP_044427Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71I → V in AAA52697. 1 Publication
Sequence conflicti7 – 71I → V in CAA28381. 1 Publication
Sequence conflicti355 – 3551N → D in BAG65428. 1 Publication
Sequence conflicti370 – 3701A → G in AAA52697. 1 Publication
Sequence conflicti469 – 4691Missing in AAA52697. 1 Publication
Sequence conflicti497 – 4971K → N in BAG65428. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34414.1. [P08107-1]
CCDS34415.1. [P08107-1]
PIRiA29160.
A45871.
I59139.
I79540.
RefSeqiNP_005336.3. NM_005345.5. [P08107-1]
NP_005337.2. NM_005346.4. [P08107-1]
UniGeneiHs.274402.
Hs.702139.
Hs.719966.

Genome annotation databases

EnsembliENST00000375650; 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]
GeneIDi3303.
3304.
KEGGihsa:3303.
hsa:3304.
UCSCiuc003nxj.3. human. [P08107-1]

Polymorphism databases

DMDMi147744565.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34414.1. [P08107-1 ]
CCDS34415.1. [P08107-1 ]
PIRi A29160.
A45871.
I59139.
I79540.
RefSeqi NP_005336.3. NM_005345.5. [P08107-1 ]
NP_005337.2. NM_005346.4. [P08107-1 ]
UniGenei Hs.274402.
Hs.702139.
Hs.719966.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2LMG NMR - A 537-610 [» ]
3A8Y X-ray 2.30 A/B 1-388 [» ]
3ATU X-ray 1.65 A 1-388 [» ]
3ATV X-ray 1.58 A 1-388 [» ]
3AY9 X-ray 1.75 A 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 [» ]
4IO8 X-ray 2.58 A 1-382 [» ]
4J8F X-ray 2.70 A 1-382 [» ]
ProteinModelPortali P08107.
SMRi P08107. Positions 1-613.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109535. 148 interactions.
109536. 52 interactions.
DIPi DIP-211N.
IntActi P08107. 112 interactions.
MINTi MINT-96699.
STRINGi 9606.ENSP00000364802.

Chemistry

BindingDBi P08107.
ChEMBLi CHEMBL5460.

Protein family/group databases

TCDBi 1.A.33.1.3. the cation channel-forming heat shock protein-70 (hsp70) family.

PTM databases

PhosphoSitei P08107.

Polymorphism databases

DMDMi 147744565.

2D gel databases

DOSAC-COBS-2DPAGE P08107.
OGPi P08107.
REPRODUCTION-2DPAGE IPI00304925.
SWISS-2DPAGE P08107.
UCD-2DPAGE P08107.

Proteomic databases

MaxQBi P08107.
PaxDbi P08107.
PRIDEi P08107.

Protocols and materials databases

DNASUi 3303.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375650 ; 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 ]
GeneIDi 3303.
3304.
KEGGi hsa:3303.
hsa:3304.
UCSCi uc003nxj.3. human. [P08107-1 ]

Organism-specific databases

CTDi 3303.
3304.
GeneCardsi GC06P031823.
GC06P031824.
GC06Pi31794.
GC06Pi31806.
GC06Pj31770.
GC06Pj31782.
GC06Pk31765.
GC06Pk31777.
GC06Pn31773.
GC06Pn31785.
H-InvDB HIX0058169.
HIX0058187.
HIX0166160.
HGNCi HGNC:5232. HSPA1A.
HGNC:5233. HSPA1B.
HPAi CAB008640.
CAB017451.
CAB032815.
HPA052504.
MIMi 140550. gene.
603012. gene.
neXtProti NX_P08107.
PharmGKBi PA29499.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
HOGENOMi HOG000228135.
HOVERGENi HBG051845.
InParanoidi P08107.
KOi K03283.
OMAi IRSSARC.
OrthoDBi EOG7PCJGF.
PhylomeDBi P08107.
TreeFami TF105042.

Enzyme and pathway databases

Reactomei REACT_200624. Attenuation phase.
REACT_200775. HSF1-dependent transactivation.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.

Miscellaneous databases

ChiTaRSi HSPA1A. human.
EvolutionaryTracei P08107.
GeneWikii HSPA1A.
NextBioi 13103.
PROi P08107.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08107.
Bgeei P08107.
CleanExi HS_HSPA1A.
Genevestigatori P08107.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  22. 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. 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.

Entry informationi

Entry nameiHSP71_HUMAN
AccessioniPrimary (citable) accession number: P08107
Secondary accession number(s): B4E3B6
, P19790, Q5JQI4, Q5SP17, Q9UQL9, Q9UQM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 15, 2007
Last modified: September 3, 2014
This is version 183 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi