Gene description for Hsp90ab1
Gene name heat shock protein 90 alpha (cytosolic), class B member 1
Gene symbol Hsp90ab1
Other names/aliases HSP90-BETA
HSP90B
HSPC2
Hspcb
Species Rattus norvegicus
 Database cross references - Hsp90ab1
ExoCarta ExoCarta_301252
Vesiclepedia VP_301252
Entrez Gene 301252
UniProt P34058  
 Hsp90ab1 identified in sEVs derived from the following tissue/cell type
Adipocytes 25998041    
Hepatocytes 19367702    
Mov neuroglial cells 15210972    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
 Gene ontology annotations for Hsp90ab1
Molecular Function
    UTP binding GO:0002134 IDA
    CTP binding GO:0002135 IDA
    double-stranded RNA binding GO:0003725 IEA
    double-stranded RNA binding GO:0003725 ISO
    protein binding GO:0005515 IPI
    ATP binding GO:0005524 IBA
    ATP binding GO:0005524 IDA
    ATP binding GO:0005524 IEA
    ATP binding GO:0005524 ISO
    ATP binding GO:0005524 TAS
    GTP binding GO:0005525 IDA
    ATP hydrolysis activity GO:0016887 IBA
    ATP hydrolysis activity GO:0016887 IEA
    sulfonylurea receptor binding GO:0017098 IPI
    protein kinase regulator activity GO:0019887 IEA
    protein kinase regulator activity GO:0019887 ISO
    kinase binding GO:0019900 ISO
    protein kinase binding GO:0019901 IEA
    protein kinase binding GO:0019901 ISO
    heat shock protein binding GO:0031072 IEA
    heat shock protein binding GO:0031072 ISO
    ubiquitin protein ligase binding GO:0031625 IEA
    ubiquitin protein ligase binding GO:0031625 ISO
    dATP binding GO:0032564 IDA
    peptide binding GO:0042277 IEA
    peptide binding GO:0042277 ISO
    identical protein binding GO:0042802 ISO
    protein homodimerization activity GO:0042803 IEA
    protein homodimerization activity GO:0042803 ISO
    histone deacetylase binding GO:0042826 IEA
    histone deacetylase binding GO:0042826 ISO
    ATP-dependent protein binding GO:0043008 IEA
    ATP-dependent protein binding GO:0043008 ISO
    protein folding chaperone GO:0044183 IMP
    protein folding chaperone GO:0044183 ISO
    transmembrane transporter binding GO:0044325 IPI
    protein dimerization activity GO:0046983 ISO
    protein dimerization activity GO:0046983 ISS
    tau protein binding GO:0048156 IEA
    tau protein binding GO:0048156 ISO
    unfolded protein binding GO:0051082 IBA
    unfolded protein binding GO:0051082 IEA
    DNA polymerase binding GO:0070182 IEA
    DNA polymerase binding GO:0070182 ISO
    protein phosphatase activator activity GO:0072542 IEA
    protein phosphatase activator activity GO:0072542 ISO
    disordered domain specific binding GO:0097718 IEA
    disordered domain specific binding GO:0097718 ISO
    protein carrier chaperone GO:0140597 NAS
    ATP-dependent protein folding chaperone GO:0140662 IEA
    receptor ligand inhibitor activity GO:0141069 IEA
    receptor ligand inhibitor activity GO:0141069 ISO
    receptor ligand inhibitor activity GO:0141069 ISS
    heterocyclic compound binding GO:1901363 IPI
    histone methyltransferase binding GO:1990226 IEA
    histone methyltransferase binding GO:1990226 ISO
Biological Process
    placenta development GO:0001890 IEA
    placenta development GO:0001890 ISO
    protein folding GO:0006457 IBA
    protein folding GO:0006457 IEA
    protein folding GO:0006457 ISO
    protein folding GO:0006457 TAS
    response to unfolded protein GO:0006986 TAS
    telomere maintenance via telomerase GO:0007004 IEA
    telomere maintenance via telomerase GO:0007004 ISO
    response to xenobiotic stimulus GO:0009410 IEP
    response to salt stress GO:0009651 IEP
    virion attachment to host cell GO:0019062 IEA
    virion attachment to host cell GO:0019062 ISO
    positive regulation of transforming growth factor beta receptor signaling pathway GO:0030511 IEA
    positive regulation of transforming growth factor beta receptor signaling pathway GO:0030511 ISO
    positive regulation of transforming growth factor beta receptor signaling pathway GO:0030511 ISS
    regulation of protein ubiquitination GO:0031396 IEA
    regulation of protein ubiquitination GO:0031396 ISO
    negative regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0032435 IEA
    negative regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0032435 ISO
    negative regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0032435 ISS
    regulation of protein localization GO:0032880 ISO
    cellular response to heat GO:0034605 IBA
    cellular response to heat GO:0034605 IEA
    cellular response to heat GO:0034605 ISO
    response to cocaine GO:0042220 IEP
    positive regulation of protein import into nucleus GO:0042307 IMP
    negative regulation of apoptotic process GO:0043066 IEA
    negative regulation of apoptotic process GO:0043066 ISO
    negative regulation of neuron apoptotic process GO:0043524 IMP
    positive regulation of cell differentiation GO:0045597 IEA
    positive regulation of cell differentiation GO:0045597 ISO
    positive regulation of cell size GO:0045793 IMP
    protein stabilization GO:0050821 IBA
    chaperone-mediated protein complex assembly GO:0051131 IEA
    chaperone-mediated protein complex assembly GO:0051131 ISO
    regulation of cell cycle GO:0051726 IEA
    regulation of cell cycle GO:0051726 ISO
    regulation of cell cycle GO:0051726 ISS
    chaperone-mediated protein folding GO:0061077 IEA
    chaperone-mediated protein folding GO:0061077 IMP
    chaperone-mediated protein folding GO:0061077 ISO
    regulation of protein complex stability GO:0061635 NAS
    chaperone-mediated autophagy GO:0061684 NAS
    cellular response to interleukin-4 GO:0071353 IEA
    cellular response to interleukin-4 GO:0071353 ISO
    cellular response to organic cyclic compound GO:0071407 IEP
    positive regulation of protein serine/threonine kinase activity GO:0071902 IMP
    supramolecular fiber organization GO:0097435 IEA
    supramolecular fiber organization GO:0097435 ISO
    negative regulation of proteasomal protein catabolic process GO:1901799 IMP
    negative regulation of proteasomal protein catabolic process GO:1901799 ISO
    negative regulation of complement-dependent cytotoxicity GO:1903660 IMP
    telomerase holoenzyme complex assembly GO:1905323 IEA
    telomerase holoenzyme complex assembly GO:1905323 ISO
    positive regulation of protein localization to cell surface GO:2000010 IEA
    positive regulation of protein localization to cell surface GO:2000010 ISO
Subcellular Localization
    extracellular region GO:0005576 IEA
    extracellular region GO:0005576 ISO
    extracellular region GO:0005576 ISS
    nucleus GO:0005634 ISO
    nucleus GO:0005634 ISS
    cytoplasm GO:0005737 IEA
    cytoplasm GO:0005737 ISO
    lysosomal membrane GO:0005765 IDA
    cytosol GO:0005829 IBA
    cytosol GO:0005829 IEA
    cytosol GO:0005829 ISO
    plasma membrane GO:0005886 IBA
    COP9 signalosome GO:0008180 IEA
    COP9 signalosome GO:0008180 ISO
    cell surface GO:0009986 IDA
    inclusion body GO:0016234 IDA
    basolateral plasma membrane GO:0016323 IDA
    apical plasma membrane GO:0016324 IDA
    brush border membrane GO:0031526 IDA
    protein-containing complex GO:0032991 IBA
    protein-containing complex GO:0032991 ISO
    aryl hydrocarbon receptor complex GO:0034751 IEA
    aryl hydrocarbon receptor complex GO:0034751 ISO
    aryl hydrocarbon receptor complex GO:0034751 ISS
    melanosome GO:0042470 IEA
    neuronal cell body GO:0043025 IEA
    neuronal cell body GO:0043025 ISO
    lysosomal lumen GO:0043202 TAS
    dendritic growth cone GO:0044294 IEA
    dendritic growth cone GO:0044294 ISO
    axonal growth cone GO:0044295 IEA
    axonal growth cone GO:0044295 ISO
    perinuclear region of cytoplasm GO:0048471 IBA
    perinuclear region of cytoplasm GO:0048471 IEA
    perinuclear region of cytoplasm GO:0048471 ISO
    protein folding chaperone complex GO:0101031 IMP
    protein folding chaperone complex GO:0101031 ISO
    dynein axonemal particle GO:0120293 IEA
    dynein axonemal particle GO:0120293 ISS
    HSP90-CDC37 chaperone complex GO:1990565 IEA
    HSP90-CDC37 chaperone complex GO:1990565 ISO
    sperm head plasma membrane GO:1990913 IDA
    ooplasm GO:1990917 IDA
 Experiment description of studies that identified Hsp90ab1 in sEVs
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 39
MISEV standards
✔
IEM
Biophysical techniques
✔
TSG101|HSC70|FLOT1
Enriched markers
✘ Negative markers
✘ Particle analysis
Identified molecule protein
Identification method Mass spectrometry
PubMed ID 15210972    
Organism Mus musculus
Experiment description Cells release prions in association with exosomes.
Authors "Fevrier B, Vilette D, Archer F, Loew D, Faigle W, Vidal M, Laude H, Raposo G"
Journal name PNAS
Publication year 2004
Sample Mov neuroglial cells
Sample name Mov neuroglial cell
Isolation/purification methods Differential centrifugation
Sucrose density gradient
Flotation density 1.14 g/mL
Molecules identified in the study Protein
Methods used in the study Mass spectrometry [QSTAR]
Western blotting
Immunoelectron Microscopy
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 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 Hsp90ab1
  Protein Interactor ExoCarta ID Identification method PubMed Species
1 Katna1  
Affinity Capture-MS Rattus norvegicus
2 Snca  
Affinity Capture-MS Rattus norvegicus
3 Sumo3  
Affinity Capture-MS Rattus norvegicus
4 Gja1  
Affinity Capture-MS Rattus norvegicus
5 Itm2b 290364
Affinity Capture-MS Rattus norvegicus
View the network image/svg+xml
 Pathways in which Hsp90ab1 is involved
PathwayEvidenceSource
Aryl hydrocarbon receptor signalling IEA Reactome
Attenuation phase IEA Reactome
Axon guidance IEA Reactome
Biological oxidations IEA Reactome
Cell Cycle IEA Reactome
Cell Cycle, Mitotic IEA Reactome
Cellular response to heat stress IEA Reactome
Cellular responses to stimuli IEA Reactome
Cellular responses to stress IEA Reactome
DDX58/IFIH1-mediated induction of interferon-alpha/beta IEA Reactome
Developmental Biology IEA Reactome
ESR-mediated signaling IEA Reactome
Estrogen-dependent gene expression IEA Reactome
Fcgamma receptor (FCGR) dependent phagocytosis IEA Reactome
G2/M Transition IEA Reactome
HSF1 activation 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
Inflammasomes IEA Reactome
Innate Immune System IEA Reactome
Metabolism IEA Reactome
Mitotic G2-G2/M phases IEA Reactome
Nervous system development IEA Reactome
Neutrophil degranulation IEA Reactome
Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signaling pathways IEA Reactome
Phase I - Functionalization of compounds IEA Reactome
Regulation of actin dynamics for phagocytic cup formation IEA Reactome
RHO GTPase cycle IEA Reactome
RHOBTB GTPase Cycle IEA Reactome
RHOBTB2 GTPase cycle IEA Reactome
Sema3A PAK dependent Axon repulsion IEA Reactome
Semaphorin interactions IEA Reactome
Signal Transduction IEA Reactome
Signaling by Nuclear Receptors IEA Reactome
Signaling by Rho GTPases IEA Reactome
Signaling by Rho GTPases, Miro GTPases and RHOBTB3 IEA Reactome
The NLRP3 inflammasome IEA Reactome
The role of GTSE1 in G2/M progression after G2 checkpoint IEA Reactome





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