Gene description for Hsp90aa1
Gene name heat shock protein 90, alpha (cytosolic), class A member 1
Gene symbol Hsp90aa1
Other names/aliases Hsp86
Hsp90
Hspca
Species Rattus norvegicus
 Database cross references - Hsp90aa1
ExoCarta ExoCarta_299331
Vesiclepedia VP_299331
Entrez Gene 299331
UniProt P82995  
 Hsp90aa1 identified in sEVs 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    
 Gene ontology annotations for Hsp90aa1
Molecular Function
    UTP binding GO:0002134 IDA
    CTP binding GO:0002135 IDA
    mRNA binding GO:0003729 IDA
    protein binding GO:0005515 IPI
    ATP binding GO:0005524 IBA
    ATP binding GO:0005524 IDA
    ATP binding GO:0005524 ISO
    GTP binding GO:0005525 IDA
    ATP hydrolysis activity GO:0016887 IBA
    ATP hydrolysis activity GO:0016887 ISO
    sulfonylurea receptor binding GO:0017098 IPI
    protein phosphatase binding GO:0019903 IPI
    nitric-oxide synthase regulator activity GO:0030235 ISO
    nitric-oxide synthase regulator activity GO:0030235 ISS
    TPR domain binding GO:0030911 ISO
    TPR domain binding GO:0030911 ISS
    ubiquitin protein ligase binding GO:0031625 ISO
    dATP binding GO:0032564 IDA
    identical protein binding GO:0042802 ISO
    protein homodimerization activity GO:0042803 ISO
    histone deacetylase binding GO:0042826 ISO
    protein folding chaperone GO:0044183 ISO
    transmembrane transporter binding GO:0044325 IPI
    tau protein binding GO:0048156 IPI
    tau protein binding GO:0048156 ISO
    GTPase binding GO:0051020 ISO
    Rho GDP-dissociation inhibitor binding GO:0051022 IDA
    unfolded protein binding GO:0051082 IBA
    unfolded protein binding GO:0051082 TAS
    DNA polymerase binding GO:0070182 ISO
    scaffold protein binding GO:0097110 ISO
    disordered domain specific binding GO:0097718 ISO
    protein carrier chaperone GO:0140597 NAS
    ATP-dependent protein folding chaperone GO:0140662 IEA
    protein tyrosine kinase binding GO:1990782 ISO
Biological Process
    neuron migration GO:0001764 IMP
    activation of innate immune response GO:0002218 ISO
    activation of innate immune response GO:0002218 ISS
    positive regulation of defense response to virus by host GO:0002230 ISO
    positive regulation of defense response to virus by host GO:0002230 ISS
    skeletal muscle contraction GO:0003009 IEP
    protein folding GO:0006457 IBA
    protein folding GO:0006457 ISO
    protein folding GO:0006457 TAS
    telomere maintenance via telomerase GO:0007004 ISO
    response to heat GO:0009408 ISS
    response to cold GO:0009409 ISS
    response to xenobiotic stimulus GO:0009410 IEP
    response to salt stress GO:0009651 IEP
    positive regulation of lamellipodium assembly GO:0010592 IMP
    cardiac muscle cell apoptotic process GO:0010659 IEP
    regulation of protein ubiquitination GO:0031396 ISO
    positive regulation of protein polymerization GO:0032273 ISO
    positive regulation of interferon-beta production GO:0032728 ISO
    positive regulation of interferon-beta production GO:0032728 ISS
    regulation of protein localization GO:0032880 ISO
    cellular response to heat GO:0034605 IBA
    cellular response to heat GO:0034605 ISO
    response to cocaine GO:0042220 IEP
    positive regulation of protein import into nucleus GO:0042307 IMP
    regulation of apoptotic process GO:0042981 ISO
    regulation of apoptotic process GO:0042981 ISS
    response to estrogen GO:0043627 IEP
    protein insertion into mitochondrial outer membrane GO:0045040 ISO
    positive regulation of nitric oxide biosynthetic process GO:0045429 ISO
    positive regulation of nitric oxide biosynthetic process GO:0045429 ISS
    positive regulation of protein catabolic process GO:0045732 ISO
    positive regulation of cell size GO:0045793 IMP
    response to antibiotic GO:0046677 ISS
    protein stabilization GO:0050821 IBA
    protein stabilization GO:0050821 ISO
    chaperone-mediated protein complex assembly GO:0051131 ISO
    positive regulation of cardiac muscle contraction GO:0060452 IEP
    regulation of protein complex stability GO:0061635 NAS
    chaperone-mediated autophagy GO:0061684 NAS
    cellular response to virus GO:0098586 ISO
    cellular response to virus GO:0098586 ISS
    regulation of postsynaptic membrane neurotransmitter receptor levels GO:0099072 EXP
    regulation of postsynaptic membrane neurotransmitter receptor levels GO:0099072 IDA
    neurofibrillary tangle assembly GO:1902988 IEA
    neurofibrillary tangle assembly GO:1902988 ISO
    telomerase holoenzyme complex assembly GO:1905323 ISO
Subcellular Localization
    nucleus GO:0005634 IBA
    nucleus GO:0005634 ISS
    nucleoplasm GO:0005654 IEA
    nucleoplasm GO:0005654 ISO
    cytoplasm GO:0005737 ISO
    cytoplasm GO:0005737 ISS
    mitochondrion GO:0005739 ISO
    mitochondrion GO:0005739 ISS
    lysosomal membrane GO:0005765 NAS
    cytosol GO:0005829 IBA
    cytosol GO:0005829 ISO
    plasma membrane GO:0005886 IBA
    cell surface GO:0009986 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 IDA
    protein-containing complex GO:0032991 ISO
    sperm flagellum GO:0036126 IDA
    melanosome GO:0042470 IEA
    neuronal cell body GO:0043025 IBA
    neuronal cell body GO:0043025 IDA
    neuronal cell body GO:0043025 ISO
    lysosomal lumen GO:0043202 TAS
    myelin sheath GO:0043209 IBA
    myelin sheath GO:0043209 IDA
    dendritic growth cone GO:0044294 ISO
    axonal growth cone GO:0044295 ISO
    perinuclear region of cytoplasm GO:0048471 IBA
    perinuclear region of cytoplasm GO:0048471 IDA
    perinuclear region of cytoplasm GO:0048471 ISO
    collagen-containing extracellular matrix GO:0062023 IDA
    sperm mitochondrial sheath GO:0097226 IDA
    sperm plasma membrane GO:0097524 IDA
 Experiment description of studies that identified Hsp90aa1 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 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]
Western blotting
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]
Western blotting
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 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 Hsp90aa1
  Protein Interactor ExoCarta ID Identification method PubMed Species
1 Grb7  
Affinity Capture-MS Rattus norvegicus
2 Gja1  
Affinity Capture-MS Rattus norvegicus
3 Ahr 25690
Affinity Capture-Western Rattus norvegicus
4 Cyp1a1  
Reconstituted Complex Rattus norvegicus
5 Snca  
Affinity Capture-MS Rattus norvegicus
6 Stk11  
Affinity Capture-Western Rattus norvegicus
7 Nr3c1  
Reconstituted Complex Rattus norvegicus
8 Katna1  
Affinity Capture-MS Rattus norvegicus
9 Ksr1  
Affinity Capture-Western Rattus norvegicus
10 Itm2b 290364
Affinity Capture-MS Rattus norvegicus
11 Cyp2b1  
Reconstituted Complex Rattus norvegicus
12 Tp53  
Affinity Capture-Western Rattus norvegicus
13 TGFBR2 7048
Affinity Capture-Western Homo sapiens
14 Sumo3  
Affinity Capture-MS Rattus norvegicus
15 Cyp2e1  
Reconstituted Complex Rattus norvegicus
16 Wasl  
Affinity Capture-Western Rattus norvegicus
Affinity Capture-Western Rattus norvegicus
Reconstituted Complex Rattus norvegicus
17 Brdt  
Affinity Capture-MS Rattus norvegicus
View the network image/svg+xml
 Pathways in which Hsp90aa1 is involved
PathwayEvidenceSource
Anchoring of the basal body to the plasma membrane IEA Reactome
Attenuation phase IEA Reactome
AURKA Activation by TPX2 IEA Reactome
Axon guidance 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
Centrosome maturation IEA Reactome
Cilium Assembly IEA Reactome
DDX58/IFIH1-mediated induction of interferon-alpha/beta IEA Reactome
Developmental Biology IEA Reactome
Downregulation of ERBB2 signaling IEA Reactome
Drug-mediated inhibition of ERBB2 signaling IEA Reactome
eNOS activation IEA Reactome
ESR-mediated signaling IEA Reactome
Estrogen-dependent gene expression IEA Reactome
Extra-nuclear estrogen signaling 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
Innate Immune System IEA Reactome
Loss of Nlp from mitotic centrosomes IEA Reactome
Loss of proteins required for interphase microtubule organization from the centrosome IEA Reactome
M Phase IEA Reactome
Metabolism IEA Reactome
Metabolism of cofactors IEA Reactome
Metabolism of nitric oxide: NOS3 activation and regulation IEA Reactome
Metabolism of vitamins and cofactors IEA Reactome
Mitotic G2-G2/M phases IEA Reactome
Mitotic Prometaphase IEA Reactome
Nervous system development IEA Reactome
Neutrophil degranulation IEA Reactome
Organelle biogenesis and maintenance IEA Reactome
Programmed Cell Death IEA Reactome
Recruitment of mitotic centrosome proteins and complexes IEA Reactome
Recruitment of NuMA to mitotic centrosomes IEA Reactome
Regulated Necrosis IEA Reactome
Regulation of actin dynamics for phagocytic cup formation IEA Reactome
Regulation of necroptotic cell death IEA Reactome
Regulation of PLK1 Activity at G2/M Transition IEA Reactome
RHO GTPase cycle IEA Reactome
RHOBTB GTPase Cycle IEA Reactome
RHOBTB2 GTPase cycle IEA Reactome
RIPK1-mediated regulated necrosis IEA Reactome
Sema3A PAK dependent Axon repulsion IEA Reactome
Semaphorin interactions IEA Reactome
Signal Transduction IEA Reactome
Signaling by ERBB2 IEA Reactome
Signaling by Nuclear Receptors IEA Reactome
Signaling by Receptor Tyrosine Kinases IEA Reactome
Signaling by Rho GTPases IEA Reactome
Signaling by Rho GTPases, Miro GTPases and RHOBTB3 IEA Reactome
Signaling by VEGF IEA Reactome
Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation IEA Reactome
The role of GTSE1 in G2/M progression after G2 checkpoint IEA Reactome
VEGFA-VEGFR2 Pathway IEA Reactome
VEGFR2 mediated vascular permeability IEA Reactome





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