Gene description for Hspa8
Gene name heat shock 70kDa protein 8
Gene symbol Hspa8
Other names/aliases Hsc70
Species Rattus norvegicus
 Database cross references - Hspa8
ExoCarta ExoCarta_24468
Vesiclepedia VP_24468
Entrez Gene 24468
UniProt P63018  
 Hspa8 identified in exosomes derived from the following tissue/cell type
Adipocytes 25998041    
Cortical neurones 16446100    
Hepatocytes 19367702    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
 Gene ontology annotations for Hspa8
Molecular Function
    G protein-coupled receptor binding GO:0001664 ISO
    phosphatidylserine binding GO:0001786 IEA
    phosphatidylserine binding GO:0001786 ISO
    RNA binding GO:0003723 IDA
    signaling receptor binding GO:0005102 IPI
    protein binding GO:0005515 IPI
    ATP binding GO:0005524 IDA
    ATP binding GO:0005524 IEA
    ATP binding GO:0005524 ISO
    ATP hydrolysis activity GO:0016887 IBA
    ATP hydrolysis activity GO:0016887 IDA
    ATP hydrolysis activity GO:0016887 ISO
    enzyme binding GO:0019899 IPI
    enzyme binding GO:0019899 ISO
    protein-macromolecule adaptor activity GO:0030674 ISO
    protein-macromolecule adaptor activity GO:0030674 ISS
    heat shock protein binding GO:0031072 IBA
    heat shock protein binding GO:0031072 ISO
    ubiquitin protein ligase binding GO:0031625 ISO
    A1 adenosine receptor binding GO:0031686 IPI
    peptide binding GO:0042277 IDA
    ADP binding GO:0043531 IDA
    protein folding chaperone GO:0044183 IBA
    receptor ligand activity GO:0048018 ISO
    unfolded protein binding GO:0051082 IEA
    unfolded protein binding GO:0051082 IMP
    unfolded protein binding GO:0051082 ISO
    protein-folding chaperone binding GO:0051087 ISO
    C3HC4-type RING finger domain binding GO:0055131 ISO
    ATP-dependent protein disaggregase activity GO:0140545 ISO
    ATP-dependent protein folding chaperone GO:0140662 IEA
    prostaglandin binding GO:1904593 IPI
    clathrin-uncoating ATPase activity GO:1990833 IDA
Biological Process
    G1/S transition of mitotic cell cycle GO:0000082 IEP
    kidney development GO:0001822 IEP
    positive regulation of T cell mediated cytotoxicity GO:0001916 IMP
    mRNA processing GO:0006397 IEA
    protein folding GO:0006457 IEA
    protein folding GO:0006457 ISO
    protein import into nucleus GO:0006606 IMP
    signal transduction GO:0007165 IEA
    skeletal muscle tissue development GO:0007519 IEP
    axo-dendritic transport GO:0008088 IEP
    RNA splicing GO:0008380 IEA
    response to xenobiotic stimulus GO:0009410 IEP
    response to nickel cation GO:0010045 IEP
    positive regulation of gene expression GO:0010628 IMP
    negative regulation of cardiac muscle cell apoptotic process GO:0010667 IMP
    response to activity GO:0014823 IEP
    cerebellum development GO:0021549 IEP
    positive regulation of cell migration GO:0030335 ISO
    forebrain development GO:0030900 IEP
    regulation of protein stability GO:0031647 ISO
    response to estradiol GO:0032355 IEP
    response to progesterone GO:0032570 IEP
    protein-containing complex disassembly GO:0032984 IMP
    cellular response to heat GO:0034605 IEP
    protein refolding GO:0042026 IBA
    protein refolding GO:0042026 ISO
    protein refolding GO:0042026 ISS
    response to starvation GO:0042594 IEP
    positive regulation of catalytic activity GO:0043085 IMP
    protein transmembrane import into intracellular organelle GO:0044743 IEP
    modulation by host of viral process GO:0044788 ISO
    positive regulation by host of viral genome replication GO:0044829 IEA
    positive regulation by host of viral genome replication GO:0044829 ISO
    estrous cycle GO:0044849 IEP
    response to ethanol GO:0045471 IEP
    positive regulation of proteolysis GO:0045862 IDA
    negative regulation of DNA-templated transcription GO:0045892 ISO
    negative regulation of DNA-templated transcription GO:0045892 ISS
    ATP metabolic process GO:0046034 ISO
    protein autophosphorylation GO:0046777 IDA
    positive regulation of mRNA splicing, via spliceosome GO:0048026 IEA
    positive regulation of mRNA splicing, via spliceosome GO:0048026 ISO
    positive regulation of phagocytosis GO:0050766 IMP
    chaperone cofactor-dependent protein refolding GO:0051085 IBA
    chaperone cofactor-dependent protein refolding GO:0051085 ISO
    regulation of cell cycle GO:0051726 IEA
    regulation of cell cycle GO:0051726 ISO
    chaperone-mediated protein folding GO:0061077 IDA
    chaperone-mediated protein folding GO:0061077 ISO
    regulation of protein complex stability GO:0061635 IDA
    chaperone-mediated autophagy GO:0061684 IDA
    chaperone-mediated autophagy GO:0061684 IGI
    late endosomal microautophagy GO:0061738 IEA
    late endosomal microautophagy GO:0061738 ISO
    protein targeting to lysosome involved in chaperone-mediated autophagy GO:0061740 ISO
    protein targeting to lysosome involved in chaperone-mediated autophagy GO:0061740 ISS
    cellular response to hydrogen peroxide GO:0070301 IEP
    cellular response to cadmium ion GO:0071276 IEP
    clathrin coat disassembly GO:0072318 IBA
    clathrin coat disassembly GO:0072318 IDA
    clathrin coat disassembly GO:0072318 IEA
    clathrin coat disassembly GO:0072318 ISO
    clathrin coat disassembly GO:0072318 ISO
    positive regulation of lysosomal membrane permeability GO:0097214 IMP
    maintenance of postsynaptic specialization structure GO:0098880 EXP
    maintenance of postsynaptic specialization structure GO:0098880 IDA
    maintenance of postsynaptic specialization structure GO:0098880 IMP
    regulation of postsynapse organization GO:0099175 IEA
    regulation of postsynapse organization GO:0099175 ISO
    negative regulation of NLRP3 inflammasome complex assembly GO:1900226 ISO
    negative regulation of supramolecular fiber organization GO:1902904 ISO
    positive regulation of protein refolding GO:1904592 IDA
    chaperone-mediated autophagy translocation complex disassembly GO:1904764 IDA
    slow axonal transport GO:1990832 IEP
    response to odorant GO:1990834 IEP
Subcellular Localization
    Prp19 complex GO:0000974 ISO
    Prp19 complex GO:0000974 ISS
    photoreceptor inner segment GO:0001917 IDA
    extracellular space GO:0005615 ISO
    nucleus GO:0005634 IBA
    nucleus GO:0005634 ISO
    nucleus GO:0005634 ISS
    spliceosomal complex GO:0005681 IEA
    spliceosomal complex GO:0005681 ISO
    nucleolus GO:0005730 IEA
    cytoplasm GO:0005737 IBA
    cytoplasm GO:0005737 ISO
    lysosomal membrane GO:0005765 IDA
    lysosomal membrane GO:0005765 ISO
    late endosome GO:0005770 IEA
    late endosome GO:0005770 ISO
    autophagosome GO:0005776 IDA
    cytosol GO:0005829 IBA
    cytosol GO:0005829 ISO
    cytosol GO:0005829 TAS
    microtubule GO:0005874 IDA
    intermediate filament GO:0005882 IDA
    plasma membrane GO:0005886 IBA
    synaptic vesicle GO:0008021 IDA
    cell surface GO:0009986 IDA
    postsynaptic density GO:0014069 IDA
    postsynaptic density GO:0014069 IDA
    axon GO:0030424 IDA
    dendrite GO:0030425 IDA
    asymmetric synapse GO:0032279 IDA
    protein-containing complex GO:0032991 IDA
    melanosome GO:0042470 IEA
    neuronal cell body GO:0043025 IDA
    terminal bouton GO:0043195 HDA
    terminal bouton GO:0043195 IDA
    dendritic spine GO:0043197 IDA
    dendritic shaft GO:0043198 IDA
    lysosomal lumen GO:0043202 TAS
    perikaryon GO:0043204 IDA
    neuron spine GO:0044309 IDA
    perinuclear region of cytoplasm GO:0048471 IDA
    perinuclear region of cytoplasm GO:0048471 IEA
    perinuclear region of cytoplasm GO:0048471 ISO
    extracellular exosome GO:0070062 IEA
    extracellular exosome GO:0070062 ISO
    photoreceptor ribbon synapse GO:0098684 IEA
    photoreceptor ribbon synapse GO:0098684 ISO
    glycinergic synapse GO:0098690 EXP
    glycinergic synapse GO:0098690 IDA
    glycinergic synapse GO:0098690 IEA
    glycinergic synapse GO:0098690 IMP
    glycinergic synapse GO:0098690 ISO
    presynapse GO:0098793 IDA
    presynapse GO:0098793 IEA
    presynapse GO:0098793 ISO
    postsynapse GO:0098794 IDA
    glutamatergic synapse GO:0098978 IDA
    glutamatergic synapse GO:0098978 IEA
    glutamatergic synapse GO:0098978 ISO
    postsynaptic specialization membrane GO:0099634 IEA
    postsynaptic specialization membrane GO:0099634 ISO
    protein folding chaperone complex GO:0101031 ISO
    lysosomal matrix GO:1990836 IDA
    ribonucleoprotein complex GO:1990904 ISO
    ribonucleoprotein complex GO:1990904 ISS
 Experiment description of studies that identified Hspa8 in exosomes
1
Experiment ID 225
MISEV standards
EM
Biophysical techniques
GAPDH|CD63
Enriched markers
Negative markers
NTA
Particle analysis
Identified molecule protein
Identification method Mass spectrometry
PubMed ID 25998041    
Organism Rattus norvegicus
Experiment description Proteomic Analysis of Extracellular Vesicles Released by Adipocytes of Otsuka Long-Evans Tokushima Fatty (OLETF) Rats.
Authors Lee JE, Moon PG, Lee IK, Baek MC
Journal name Protein J
Publication year 2015
Sample Adipocytes
Sample name Adipocytes
Isolation/purification methods Differential centrifugation
Filtration
Ultracentrifugation
Flotation density -
Molecules identified in the study Protein
Methods used in the study Mass spectrometry
Western blotting
2
Experiment ID 30
MISEV standards
EM
Biophysical techniques
Alix|TSG101|FLOT
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry
PubMed ID 16446100    
Organism Rattus norvegicus
Experiment description Exosomes are released by cultured cortical neurones.
Authors Faure J, Lachenal G, Court M, Hirrlinger J, Chatellard-Causse C, Blot B, Grange J, Schoehn G, Goldberg Y, Boyer V, Kirchhoff F, Raposo G, Garin J, Sadoul R
Journal name MCN
Publication year 2006
Sample Cortical neurones
Sample name Cortical neurones
Isolation/purification methods Differential centrifugation
Sucrose density gradient
Flotation density 1.13 g/mL
Molecules identified in the study Protein
Methods used in the study Mass spectrometry [QTOF]
Western blotting
3
Experiment ID 35
MISEV standards
CEM
Biophysical techniques
TSG101|Alix|CD81|CD63
Enriched markers
HSPA5
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry
PubMed ID 19367702    
Organism Rattus norvegicus
Experiment description Characterization and Comprehensive Proteome Profiling of Exosomes Secreted by Hepatocytes.
Authors Conde-Vancells J, Rodriguez-Suarez E, Embade N, Gil D, Matthiesen R, Valle M, Elortza F, Lu SC, Mato JM, Falcon-Perez JM
Journal name JPR
Publication year 2008
Sample Hepatocytes
Sample name Hepatocytes
Isolation/purification methods Differential centrifugation
Filtration
Sucrose density gradient
Flotation density -
Molecules identified in the study Protein
Methods used in the study Mass spectrometry [QTOF]
Western blotting
4
Experiment ID 90
MISEV standards
EM
Biophysical techniques
HSC70|HSP90|TSG101|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D2 Rep 1
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
5
Experiment ID 94
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D4 Rep 1
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
6
Experiment ID 95
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D7 Rep 1
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.13-1.25 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
7
Experiment ID 96
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D2 Rep 2
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
8
Experiment ID 97
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D4 Rep 2
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
9
Experiment ID 98
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D7 Rep 2
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.13-1.25 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
10
Experiment ID 99
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [QSTAR]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D2 Rep 3
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
11
Experiment ID 100
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [QSTAR]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D4 Rep 3
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
12
Experiment ID 101
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [QSTAR]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E.
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D7 Rep 3
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.13-1.25 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
 Protein-protein interactions for Hspa8
  Protein Interactor ExoCarta ID Identification method PubMed Species
1 DNAJC7 7266
Two-hybrid Homo sapiens
2 HSPBP1 23640
Affinity Capture-Western Homo sapiens
3 BAG3 9531
Affinity Capture-Western Homo sapiens
4 Gja1  
Affinity Capture-MS Rattus norvegicus
5 Bag1  
Affinity Capture-Western Rattus norvegicus
6 Ap2a1  
Affinity Capture-MS Rattus norvegicus
7 Snca  
Affinity Capture-MS Rattus norvegicus
8 DNAJC3  
Reconstituted Complex Bos taurus
Two-hybrid Bos taurus
9 TTC1 7265
Two-hybrid Homo sapiens
10 SGTA 6449
Two-hybrid Homo sapiens
11 DNAJB1 3337
Reconstituted Complex Homo sapiens
Two-hybrid Homo sapiens
12 Grb7  
Affinity Capture-MS Rattus norvegicus
Affinity Capture-Western Rattus norvegicus
13 Itm2b 290364
Affinity Capture-MS Rattus norvegicus
14 STIP1 10963
Two-hybrid Homo sapiens
15 Katna1  
Affinity Capture-MS Rattus norvegicus
16 Sumo3  
Affinity Capture-MS Rattus norvegicus
17 PRDX1 5052
Affinity Capture-MS Homo sapiens
18 Ap2b1 140670
Affinity Capture-MS Rattus norvegicus
View the network image/svg+xml
 Pathways in which Hspa8 is involved
PathwayEvidenceSource
Antiviral mechanism by IFN-stimulated genes IEA Reactome
Attenuation phase IEA Reactome
AUF1 (hnRNP D0) binds and destabilizes mRNA IEA Reactome
Cellular response to heat stress IEA Reactome
Cellular responses to stimuli IEA Reactome
Cellular responses to stress IEA Reactome
Clathrin-mediated endocytosis IEA Reactome
Cytokine Signaling in Immune system IEA Reactome
GABA synthesis, release, reuptake and degradation IEA Reactome
Golgi Associated Vesicle Biogenesis IEA Reactome
HSF1-dependent transactivation IEA Reactome
HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand IEA Reactome
Immune System IEA Reactome
Innate Immune System IEA Reactome
Interferon Signaling IEA Reactome
Lysosome Vesicle Biogenesis IEA Reactome
Membrane Trafficking IEA Reactome
Metabolism of proteins IEA Reactome
Metabolism of RNA IEA Reactome
mRNA Splicing IEA Reactome
mRNA Splicing - Major Pathway IEA Reactome
Neuronal System IEA Reactome
Neurotransmitter release cycle IEA Reactome
Neutrophil degranulation IEA Reactome
PKR-mediated signaling IEA Reactome
Post-translational protein modification IEA Reactome
Processing of Capped Intron-Containing Pre-mRNA IEA Reactome
Protein methylation IEA Reactome
Regulation of HSF1-mediated heat shock response IEA Reactome
Regulation of mRNA stability by proteins that bind AU-rich elements IEA Reactome
trans-Golgi Network Vesicle Budding IEA Reactome
Transmission across Chemical Synapses IEA Reactome
Vesicle-mediated transport IEA Reactome





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