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Protein

Heat shock 70 kDa protein

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.By similarity

GO - Molecular functioni

  • ATPase activity Source: AgBase
  • ATP binding Source: AgBase
  • C3HC4-type RING finger domain binding Source: AgBase
  • enzyme binding Source: AgBase
  • G-protein coupled receptor binding Source: AgBase
  • heat shock protein binding Source: AgBase
  • MHC class II protein complex binding Source: AgBase
  • progesterone receptor binding Source: AgBase
  • RNA binding Source: AgBase
  • ubiquitin protein ligase binding Source: AgBase
  • unfolded protein binding Source: AgBase

GO - Biological processi

  • ATP metabolic process Source: AgBase
  • negative regulation of supramolecular fiber organization Source: AgBase
  • negative regulation of transcription, DNA-templated Source: AgBase
  • protein refolding Source: AgBase
  • regulation of protein stability Source: AgBase
  • response to cold Source: AgBase
  • response to heat Source: AgBase
  • response to organic cyclic compound Source: AgBase
  • response to organonitrogen compound Source: AgBase
  • response to progesterone Source: AgBase

Keywordsi

Biological processStress response
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein
Short name:
HSP70
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: AgBase
  • cell Source: AgBase
  • cytoplasm Source: AgBase
  • cytosol Source: AgBase
  • extracellular exosome Source: AgBase
  • extracellular region Source: AgBase
  • extracellular space Source: AgBase
  • focal adhesion Source: AgBase
  • intracellular ribonucleoprotein complex Source: AgBase
  • membrane Source: AgBase
  • nucleus Source: AgBase
  • perikaryon Source: AgBase
  • Prp19 complex Source: AgBase
  • receptor complex Source: AgBase
  • ubiquitin ligase complex Source: AgBase

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000782791 – 634Heat shock 70 kDa proteinAdd BLAST634

Proteomic databases

PaxDbiP08106.
PRIDEiP08106.

Interactioni

Binary interactionsi

Show more details

GO - Molecular functioni

  • C3HC4-type RING finger domain binding Source: AgBase
  • enzyme binding Source: AgBase
  • G-protein coupled receptor binding Source: AgBase
  • heat shock protein binding Source: AgBase
  • MHC class II protein complex binding Source: AgBase
  • progesterone receptor binding Source: AgBase
  • ubiquitin protein ligase binding Source: AgBase
  • unfolded protein binding Source: AgBase

Protein-protein interaction databases

BioGridi684024. 6 interactors.
IntActiP08106. 2 interactors.
STRINGi9031.ENSGALP00000019120.

Structurei

3D structure databases

ProteinModelPortaliP08106.
SMRiP08106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 389Nucleotide-binding domain (NBD)By similarityAdd BLAST387
Regioni397 – 512Substrate-binding domain (SBD)By similarityAdd BLAST116

Domaini

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
KOiK03283.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiView protein in InterPro
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
PfamiView protein in Pfam
PF00012. HSP70. 1 hit.
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiView protein in PROSITE
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.

Sequencei

Sequence statusi: Complete.

P08106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER
60 70 80 90 100
LIGDAAKNQV AMNPTNTIFD AKRLIGRKYD DPTVQSDMKH WPFRVVNEGG
110 120 130 140 150
KPKVQVEYKG EMKTFFPEEI SSMVLTKMKE IAEAYLGKKV ETAVITVPAY
160 170 180 190 200
FNDSQRQATK DAGTITGLNV MRIINEPTAA AIAYGLDKKG TRAGEKNVLI
210 220 230 240 250
FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM VNRFVEEFKG
260 270 280 290 300
KHKRDNAGNK RAVRRLRTAC ERARRTLSSS TQASIEIDSL FEGIDFYTSI
310 320 330 340 350
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ
360 370 380 390 400
KLLQDFFNGK ELNKSINPDE AVAYGAAVQA AILMGDKSEN VQDLLLLDVT
410 420 430 440 450
PLSLGIETAG GVMTALIKRN TTIPTKQTQT FTTYSDNQSS VLVQVYEGER
460 470 480 490 500
AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT FDIDANGILN VSAVDKSTGK
510 520 530 540 550
ENKITITNDK GRLSKDDIDR MVQEAEKYKA EDEANRDRVG AKNSLESYTY
560 570 580 590 600
NMKQTVEDEK LKGKISDQDK QKVLDKCQEV ISSLDRNQMA EKEEYEHKQK
610 620 630
ELEKLCNPIV TKLYQGAGGA GAGGSGGPTI EEVD
Length:634
Mass (Da):69,751
Last modified:August 1, 1988 - v1
Checksum:i4270F7F08D365AEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02579 Genomic DNA. Translation: AAA48825.1.
PIRiA25646.
RefSeqiNP_001006686.1. NM_001006685.1.
UniGeneiGga.4942.

Genome annotation databases

GeneIDi423504.
KEGGigga:423504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02579 Genomic DNA. Translation: AAA48825.1.
PIRiA25646.
RefSeqiNP_001006686.1. NM_001006685.1.
UniGeneiGga.4942.

3D structure databases

ProteinModelPortaliP08106.
SMRiP08106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi684024. 6 interactors.
IntActiP08106. 2 interactors.
STRINGi9031.ENSGALP00000019120.

Proteomic databases

PaxDbiP08106.
PRIDEiP08106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi423504.
KEGGigga:423504.

Organism-specific databases

CTDi3306.

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
KOiK03283.

Miscellaneous databases

PROiP08106.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiView protein in InterPro
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
PfamiView protein in Pfam
PF00012. HSP70. 1 hit.
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiView protein in PROSITE
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHSP70_CHICK
AccessioniPrimary (citable) accession number: P08106
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: March 15, 2017
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.