HCSGD entry for HSP90AA1


1. General information

Official gene symbolHSP90AA1
Entrez ID3320
Gene full nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Other gene symbolsEL52 HSP86 HSP89A HSP90A HSP90N HSPC1 HSPCA HSPCAL1 HSPCAL4 HSPN Hsp89 Hsp90 LAP2
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0000086G2/M transition of mitotic cell cycleTASbiological_process
GO:0000166Nucleotide bindingTASmolecular_function
GO:0000278Mitotic cell cycleTASbiological_process
GO:0001764Neuron migrationIEAbiological_process
GO:0002134UTP bindingIEAmolecular_function
GO:0002135CTP bindingIEAmolecular_function
GO:0003009Skeletal muscle contractionIEAbiological_process
GO:0003729MRNA bindingIEAmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005524ATP bindingIEA TASmolecular_function
GO:0005525GTP bindingIEAmolecular_function
GO:0005576Extracellular regionTAScellular_component
GO:0005739MitochondrionIDAcellular_component
GO:0005829CytosolNAS TAScellular_component
GO:0005886Plasma membraneTAScellular_component
GO:0006200ATP catabolic processIDAbiological_process
GO:0006457Protein foldingIEAbiological_process
GO:0006839Mitochondrial transportTASbiological_process
GO:0006950Response to stressIEAbiological_process
GO:0006986Response to unfolded proteinNASbiological_process
GO:0007165Signal transductionNASbiological_process
GO:0007411Axon guidanceTASbiological_process
GO:0009408Response to heatIEAbiological_process
GO:0009651Response to salt stressIEAbiological_process
GO:0009986Cell surfaceIEAcellular_component
GO:0010592Positive regulation of lamellipodium assemblyIEAbiological_process
GO:0010659Cardiac muscle cell apoptotic processIEAbiological_process
GO:0016323Basolateral plasma membraneIEAcellular_component
GO:0016324Apical plasma membraneIEAcellular_component
GO:0016887ATPase activityIDAmolecular_function
GO:0017098Sulfonylurea receptor bindingIEAmolecular_function
GO:0019901Protein kinase bindingIEAmolecular_function
GO:0019903Protein phosphatase bindingIEAmolecular_function
GO:0030235Nitric-oxide synthase regulator activityIDAmolecular_function
GO:0030911TPR domain bindingIDA TASmolecular_function
GO:0031012Extracellular matrixIEAcellular_component
GO:0031526Brush border membraneIEAcellular_component
GO:0032564DATP bindingIEAmolecular_function
GO:0033160Positive regulation of protein import into nucleus, translocationIEAbiological_process
GO:0038096Fc-gamma receptor signaling pathway involved in phagocytosisTASbiological_process
GO:0042026Protein refoldingTASbiological_process
GO:0042470MelanosomeIEAcellular_component
GO:0042802Identical protein bindingIPImolecular_function
GO:0042803Protein homodimerization activityTASmolecular_function
GO:0043005Neuron projectionIEAcellular_component
GO:0043025Neuronal cell bodyIEAcellular_component
GO:0043234Protein complexIEAcellular_component
GO:0043627Response to estrogenIEAbiological_process
GO:0044281Small molecule metabolic processTASbiological_process
GO:0044325Ion channel bindingIEAmolecular_function
GO:0045040Protein import into mitochondrial outer membraneIDAbiological_process
GO:0045087Innate immune responseTASbiological_process
GO:0045429Positive regulation of nitric oxide biosynthetic processISSbiological_process
GO:0045793Positive regulation of cell sizeIEAbiological_process
GO:0046209Nitric oxide metabolic processTASbiological_process
GO:0048471Perinuclear region of cytoplasmIEAcellular_component
GO:0050999Regulation of nitric-oxide synthase activityTASbiological_process
GO:0051082Unfolded protein bindingIEAmolecular_function
GO:0051131Chaperone-mediated protein complex assemblyIDAbiological_process
GO:0060452Positive regulation of cardiac muscle contractionIEAbiological_process
GO:0071682Endocytic vesicle lumenTAScellular_component
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.37571784890.88836494430.99999024731.0000000000

  • Individual experiment result
    ( "-" represent NA in the specific microarray platform )

Data sourceUp or downLog fold change
GSE11954Up0.3440007757
GSE13712_SHEARUp0.3355159015
GSE13712_STATICUp0.4002201168
GSE19018Up0.1252753937
GSE19899_A1Up0.1013874025
GSE19899_A2Down-0.0441618433
PubMed_21979375_A1Down-0.1234191987
PubMed_21979375_A2Down-0.1465037037
GSE35957Down-0.2015534777
GSE36640Down-0.0722302229
GSE54402Up0.1027677881
GSE9593Down-0.2191586584
GSE43922Up0.0136686779
GSE24585Down-0.0370314234
GSE37065Up0.0655654164
GSE28863_A1Up0.1969744815
GSE28863_A2Up0.2515040987
GSE28863_A3Down-0.1326092642
GSE28863_A4Down-0.0194402322
GSE48662Up0.0222448569

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Not regulated by compounds

  • Drugs

Not regulated by drugs

  • MicroRNAs

    • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-375MIMAT0000728MIRT020063MicroarrayFunctional MTI (Weak)20215506
hsa-miR-16-5pMIMAT0000069MIRT031959ProteomicsFunctional MTI (Weak)18668040
hsa-miR-1226-3pMIMAT0005577MIRT036428CLASHFunctional MTI (Weak)23622248
hsa-miR-760MIMAT0004957MIRT036729CLASHFunctional MTI (Weak)23622248
hsa-miR-425-5pMIMAT0003393MIRT039331CLASHFunctional MTI (Weak)23622248
hsa-miR-421MIMAT0003339MIRT039416CLASHFunctional MTI (Weak)23622248
hsa-miR-501-5pMIMAT0002872MIRT041140CLASHFunctional MTI (Weak)23622248
hsa-miR-484MIMAT0002174MIRT041642CLASHFunctional MTI (Weak)23622248
hsa-miR-324-3pMIMAT0000762MIRT042829CLASHFunctional MTI (Weak)23622248
hsa-miR-378a-3pMIMAT0000732MIRT043944CLASHFunctional MTI (Weak)23622248
hsa-miR-30e-5pMIMAT0000692MIRT044155CLASHFunctional MTI (Weak)23622248
hsa-miR-186-5pMIMAT0000456MIRT045178CLASHFunctional MTI (Weak)23622248
hsa-miR-185-5pMIMAT0000455MIRT045325CLASHFunctional MTI (Weak)23622248
hsa-miR-222-3pMIMAT0000279MIRT046648CLASHFunctional MTI (Weak)23622248
hsa-miR-204-5pMIMAT0000265MIRT047015CLASHFunctional MTI (Weak)23622248
hsa-miR-183-5pMIMAT0000261MIRT047124CLASHFunctional MTI (Weak)23622248
hsa-miR-10a-5pMIMAT0000253MIRT047507CLASHFunctional MTI (Weak)23622248
hsa-miR-30c-5pMIMAT0000244MIRT047953CLASHFunctional MTI (Weak)23622248
hsa-miR-25-3pMIMAT0000081MIRT050304CLASHFunctional MTI (Weak)23622248
hsa-miR-17-5pMIMAT0000070MIRT050979CLASHFunctional MTI (Weak)23622248
hsa-let-7b-5pMIMAT0000063MIRT052238CLASHFunctional MTI (Weak)23622248
hsa-miR-3943MIMAT0018359MIRT052896CLASHFunctional MTI (Weak)23622248
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    • mirRecord
No target information from mirRecord

6. Text-mining results about the gene

Gene occurances in abstracts of cellular senescence-associated articles: 6 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

24156782A novel Hsp90 inhibitor AT13387 induces senescence in EBV-positive nasopharyngeal carcinoma cells and suppresses tumor formation
24156782AT13387 is a novel heat shock protein 90 (Hsp90) inhibitor, which inhibits the chaperone function of Hsp90 and reduces expression of Hsp90-dependent client oncoproteins
2291583917AAG Treatment Accelerates Doxorubicin Induced Cellular Senescence: Hsp90 Interferes with Enforced Senescence of Tumor Cells
22915839Hsp90 chaperone has been identified as an attractive pharmacological target to combat cancer
22915839However, some metastatic tumors either fail to respond to Hsp90 inhibition or show recovery necessitating irreversible therapeutic strategies
22915839Doxorubicin induced senescence signaling was mediated by p53-p21(CIP/WAF-1) and was accelerated in the absence of functional Hsp90
22915839Our study discusses tumor selective functions of Hsp90 and discusses irrefutable strategies of Hsp90 inhibition in anticancer treatments
20974249Finally, we have observed an attenuation of the CHIP-associated molecular folding-refolding machinery during senescence, and supportively, inhibition of Hsp90 activity leads to rapid p53 degradation only in senescent cells
18325704To determine the mechanism of REMFS-induced effects, analysis of the cellular heat shock response revealed Hsp90 release from the heat shock transcription factor (HSF1)
18262743Furthermore, all three modulators tested in the present study bring about their effects by inducing stress response pathways in terms of an increase in the levels of stress proteins Hsp90, Hsp70 and heme-oxygenase-1 (HO-1), which is indicative of stress-induced hormesis bringing about the biologically beneficial effects
12470835In comparison, the amount of Hsp90 decreased both with aging and RMHS treatment in vitro
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