Gene description for Hspa5
Gene name heat shock protein 5
Gene symbol Hspa5
Other names/aliases BIP
GRP78
Species Rattus norvegicus
 Database cross references - Hspa5
ExoCarta ExoCarta_25617
Vesiclepedia VP_25617
Entrez Gene 25617
UniProt P06761  
 Hspa5 identified in exosomes derived from the following tissue/cell type
Adipocytes 25998041    
Hepatocytes 19367702    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
 Gene ontology annotations for Hspa5
Molecular Function
    DNA clamp loader activity GO:0003689 IEA
    protein binding GO:0005515 IPI
    ATP binding GO:0005524 IEA
    ATP binding GO:0005524 ISO
    ATP hydrolysis activity GO:0016887 IBA
    ATP hydrolysis activity GO:0016887 IEA
    ATP hydrolysis activity GO:0016887 ISO
    ATP hydrolysis activity GO:0016887 ISS
    enzyme binding GO:0019899 ISO
    protein domain specific binding GO:0019904 IEA
    protein domain specific binding GO:0019904 ISO
    protein serine/threonine kinase inhibitor activity GO:0030291 IEA
    protein serine/threonine kinase inhibitor activity GO:0030291 ISO
    heat shock protein binding GO:0031072 IBA
    ubiquitin protein ligase binding GO:0031625 IEA
    ubiquitin protein ligase binding GO:0031625 ISO
    ribosome binding GO:0043022 IEA
    ribosome binding GO:0043022 ISO
    protein folding chaperone GO:0044183 IBA
    protein folding chaperone GO:0044183 ISO
    unfolded protein binding GO:0051082 IPI
    misfolded protein binding GO:0051787 IDA
    misfolded protein binding GO:0051787 IEA
    misfolded protein binding GO:0051787 ISO
    cohesin loader activity GO:0061775 IEA
    chromatin extrusion motor activity GO:0140584 IEA
    ATP-dependent protein folding chaperone GO:0140662 IEA
    ATP-dependent H3-H4 histone complex chaperone activity GO:0140665 IEA
    ATP-dependent H2AZ histone chaperone activity GO:0140849 IEA
Biological Process
    luteolysis GO:0001554 IEP
    chromatin remodeling GO:0006338 IEA
    protein folding GO:0006457 IEA
    ER overload response GO:0006983 IEA
    ER overload response GO:0006983 ISO
    positive regulation of neuron projection development GO:0010976 IMP
    cerebellum structural organization GO:0021589 IEA
    cerebellum structural organization GO:0021589 ISO
    cerebellar Purkinje cell layer development GO:0021680 IEA
    cerebellar Purkinje cell layer development GO:0021680 ISO
    substantia nigra development GO:0021762 ISO
    neuron differentiation GO:0030182 IEP
    positive regulation of cell migration GO:0030335 IEA
    positive regulation of cell migration GO:0030335 ISO
    positive regulation of cell migration GO:0030335 ISS
    negative regulation of transforming growth factor beta receptor signaling pathway GO:0030512 IEA
    negative regulation of transforming growth factor beta receptor signaling pathway GO:0030512 ISO
    endoplasmic reticulum unfolded protein response GO:0030968 IBA
    endoplasmic reticulum unfolded protein response GO:0030968 IEA
    endoplasmic reticulum unfolded protein response GO:0030968 ISO
    post-translational protein targeting to membrane, translocation GO:0031204 IEA
    post-translational protein targeting to membrane, translocation GO:0031204 ISO
    post-translational protein targeting to membrane, translocation GO:0031204 ISS
    negative regulation of protein-containing complex assembly GO:0031333 ISS
    positive regulation of protein ubiquitination GO:0031398 IEA
    positive regulation of protein ubiquitination GO:0031398 ISO
    response to endoplasmic reticulum stress GO:0034976 IDA
    response to endoplasmic reticulum stress GO:0034976 IEP
    maintenance of protein localization in endoplasmic reticulum GO:0035437 IEA
    maintenance of protein localization in endoplasmic reticulum GO:0035437 ISO
    maintenance of protein localization in endoplasmic reticulum GO:0035437 ISS
    IRE1-mediated unfolded protein response GO:0036498 ISO
    ERAD pathway GO:0036503 IBA
    protein refolding GO:0042026 IBA
    cellular response to glucose starvation GO:0042149 IEA
    cellular response to glucose starvation GO:0042149 ISO
    response to cocaine GO:0042220 IEP
    negative regulation of apoptotic process GO:0043066 IEA
    negative regulation of apoptotic process GO:0043066 ISO
    chaperone cofactor-dependent protein refolding GO:0051085 IBA
    neuron apoptotic process GO:0051402 IEP
    proteolysis involved in protein catabolic process GO:0051603 IEA
    proteolysis involved in protein catabolic process GO:0051603 ISO
    cellular response to antibiotic GO:0071236 IEP
    cellular response to calcium ion GO:0071277 IEP
    cellular response to manganese ion GO:0071287 IEP
    cellular response to cAMP GO:0071320 IEP
    cellular response to interleukin-4 GO:0071353 IEA
    cellular response to interleukin-4 GO:0071353 ISO
    cellular response to xenobiotic stimulus GO:0071466 IEP
    cellular response to gamma radiation GO:0071480 IEP
    stress response to metal ion GO:0097501 IEP
    chromatin looping GO:0140588 IEA
    negative regulation of IRE1-mediated unfolded protein response GO:1903895 ISS
    negative regulation of PERK-mediated unfolded protein response GO:1903898 IEA
    negative regulation of PERK-mediated unfolded protein response GO:1903898 ISO
    response to methamphetamine hydrochloride GO:1904313 IEP
    cellular response to nerve growth factor stimulus GO:1990090 IEP
Subcellular Localization
    nucleus GO:0005634 IBA
    nucleus GO:0005634 ISO
    cytoplasm GO:0005737 IBA
    cytoplasm GO:0005737 ISO
    mitochondrion GO:0005739 IEA
    mitochondrion GO:0005739 ISO
    endoplasmic reticulum GO:0005783 IDA
    endoplasmic reticulum GO:0005783 ISO
    endoplasmic reticulum lumen GO:0005788 IBA
    endoplasmic reticulum lumen GO:0005788 IEA
    endoplasmic reticulum lumen GO:0005788 ISO
    endoplasmic reticulum membrane GO:0005789 IEA
    endoplasmic reticulum membrane GO:0005789 ISO
    smooth endoplasmic reticulum GO:0005790 IDA
    endoplasmic reticulum-Golgi intermediate compartment GO:0005793 IEA
    endoplasmic reticulum-Golgi intermediate compartment GO:0005793 ISO
    cytosol GO:0005829 IEA
    cytosol GO:0005829 ISO
    cytosol GO:0005829 ISS
    plasma membrane GO:0005886 IEA
    plasma membrane GO:0005886 ISO
    COP9 signalosome GO:0008180 IEA
    COP9 signalosome GO:0008180 ISO
    cell surface GO:0009986 IEA
    cell surface GO:0009986 ISO
    membrane GO:0016020 IBA
    membrane GO:0016020 IDA
    midbody GO:0030496 IEA
    midbody GO:0030496 ISO
    protein-containing complex GO:0032991 ISO
    endoplasmic reticulum chaperone complex GO:0034663 IBA
    endoplasmic reticulum chaperone complex GO:0034663 IEA
    endoplasmic reticulum chaperone complex GO:0034663 ISO
    melanosome GO:0042470 IEA
    neuronal cell body GO:0043025 IDA
    dendritic shaft GO:0043198 IDA
    intracellular membrane-bounded organelle GO:0043231 ISO
 Experiment description of studies that identified Hspa5 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 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
3
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
4
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
5
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
6
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
7
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
8
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
9
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
10
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
 Protein-protein interactions for Hspa5
  Protein Interactor ExoCarta ID Identification method PubMed Species
1 Gja1  
Affinity Capture-MS Rattus norvegicus
2 Thbs1 445442
Affinity Capture-Western Rattus norvegicus
3 Hyou1 192235
Affinity Capture-Western Rattus norvegicus
4 Pdia4 116598
Affinity Capture-Western Rattus norvegicus
Affinity Capture-Western Rattus norvegicus
5 Itm2b 290364
Affinity Capture-MS Rattus norvegicus
6 Hsp90b1 362862
Affinity Capture-Western Rattus norvegicus
7 Tg  
Affinity Capture-Western Rattus norvegicus
Affinity Capture-Western Rattus norvegicus
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