Protein information
  Protein summary    Phosphorylation site    Dephosphorylation site    Mutation site
  Differential expressed protein    Hyperphosphorylation site    Direct interaction pair    Function Annotation

Protein Summary
UniProt/SwissProt ID:HS90A_HUMAN
Description:heat shock protein 90kDa alpha (cytosolic), class A member 1 [Source:HGNC Symbol;Acc:5253]
Location:chr14 q32.31
Node attribute:substrate

Phosphorylation site
PositionPhosphoPeptideCatalytic kinaseSource
S63KIRYEsLTDPSHATPase_cPhosphoSitePlus
S641INPDHsIIETLHPRD
Y438NYKKFyEQFSKHSP90PhosphoSitePlus
T195LKEDQtEYLEECDC45; ZipPhosphoSitePlus
T566QEEKKtKFENLHSP90PhosphoSitePlus
T847EGDDDtSRMEEHPRD
Y492NQKHIyYITGERegPhos
S831TADDTsAAVTEHPRD
T7PEETQtQDQPMDNAPKRegPhos
S385IEDVGsDEEEECSNK2A1HPRD
S263IEDVGsDEEEECK2_alphaphosphoELM; SysPTM
S505DQVANsAFVERHSP90PhosphoSitePlus
T109INNLGtIAKSGHATPase_cPhosphoSitePlus
T293EELNKtKPIWTCDC45; Zip; HSP90PhosphoSitePlus
S315GEFYKsLTNDWHPRD
Y604IVTSTyGWTANHSP90PhosphoSitePlus
T65RYESLtDPSKLHATPase_cPhosphoSitePlus
T210NKQDRtLTIVDHPRD
T830PTADDtSAAVTHPRD
T99TGIGMtKADLIHATPase_cPhosphoSitePlus
S763INPDHsIIETLHPRD
T607STYGWtANMERHSP90PhosphoSitePlus
T683LEDPQtHANRIHPRD
T725EGDDDtSRMEEHPRD; phosphoELM
S437GEFYKsLTNDWHPRD
S460NRKKLsELLRYHSP90PhosphoSitePlus
S353RDKEVsDDEAECSNK2A1HPRD
S353RDKEVsDDEAEHPRD
S726GDDDTsRMEEHPRD; phosphoELM
S231RDKEVsDDEAECK2a1RegPhos; SysPTM
S602CCIVTsTYGWTHSP90PhosphoSitePlus
T826DEDDPtADDTSHPRD
S231RDKEVsDDEAECDC45; Zip; HSP90PhosphoSitePlus; SysPTM
S263IEDVGsDEEEECK2a1(CK2 alphaRegPhos; SysPTM
S674TALLSsGFSLEHPRD
S589EKVVVsNRLVTHSP90PhosphoSitePlus
S442FYEQFsKNIKLHSP90PhosphoSitePlus
S711EKVVVsNRLVTHPRD
Y627NSTMGyMAAKKHSP90PhosphoSitePlus
S263IEDVGsDEEEECSNK2A1HPRD; SysPTM
T127LMPEEtQTQDQPRKDCHPRD
S374KEEKEsEDKPEHPRD
T624LRDNStMGYMAHSP90PhosphoSitePlus
T88NKQDRtLTIVDHATPase_cPhosphoSitePlus
S252KEEKEsEDKPEHPRD; phosphoELM; RegPhos; SysPTM
S795ETALLsSGFSLHPRD
T94LTIVDtGIGMTHATPase_cPhosphoSitePlus
S263IEDVGsDEEEEHPRD; phosphoELM; RegPhos; SysPTM
Y789LVILLyETALLHPRD
S113GTIAKsGTKAFHATPase_cPhosphoSitePlus
T708PTADDtSAAVTHPRD
S72PSKLDsGKELHHATPase_cPhosphoSitePlus
T805LEDPQtHANRIHPRD
T7PEETQtQDQPMPhosphoSitePlus
Y313EYGEFyKSLTNCDC45; HSP90PhosphoSitePlus
T5TQDQphosphoELM
S252KEEKEsEDKPECDC45; Zip; HSP90PhosphoSitePlus; SysPTM
Y492NQKHIyYITGEHSP90PhosphoSitePlus
S231RDKEVsDDEAECK2_groupphosphoELM; RegPhos; SysPTM
S391RGVVDsEDLPLHSP90PhosphoSitePlus
T467LLRYYtSASGDHSP90PhosphoSitePlus
T129PEETQtQDQPMPRKDCHPRD
S848GDDDTsRMEEHPRD
S709TADDTsAAVTEHPRD
S476GDEMVsLKDYCHSP90PhosphoSitePlus
T704DEDDPtADDTSHPRD
S231RDKEVsDDEAECSNK2A1HPRD; SysPTM
Y493QKHIYyITGETHSP90PhosphoSitePlus
Y528EPIDEyCVQQLHSP90PhosphoSitePlus
Y284KIKEKyIDQEECDC45; Zip; HSP90PhosphoSitePlus
S263IEDVGsDEEEECK2a1RegPhos; SysPTM
S796TALLSsGFSLEHPRD
S673ETALLsSGFSLHPRD
S231RDKEVsDDEAECK2a1-rsRegPhos; SysPTM
S263IEDVGsDEEEECK2_groupphosphoELM; RegPhos; SysPTM
Y434EDKENyKKFYEHSP90PhosphoSitePlus
T498YITGEtKDQVAHSP90PhosphoSitePlus
Y309ITNEEyGEFYKCDC45; HSP90PhosphoSitePlus
T669ILLYEtALLSSHSP90PhosphoSitePlus
T5MPEETqTQDQRegPhos
S623ALRDNsTMGYMHSP90PhosphoSitePlus
S315GEFYKsLTNDWCDC45; HSP90PhosphoSitePlus
S263IEDVGsDEEEECDC45; Zip; HSP90PhosphoSitePlus; SysPTM
T7DQPMDNA-PKphosphoELM
Y38IINTFySNKEIPhosphoSitePlus
T90QDRTLtIVDTGHATPase_cPhosphoSitePlus
T5MPEETqTQDQDNAPKRegPhos
S799LSSGFsLEDPQHPRD
S589EKVVVsNRLVTHPRD
T5_MPEEtQTQDQPhosphoSitePlus
T7DQPMPRKDCHPRD
S453GIHEDsQNRKKHSP90PhosphoSitePlus
T603CIVTStYGWTAHSP90PhosphoSitePlus
S263IEDVGsDEEEECK2a1-rsRegPhos; SysPTM
Y689HANRIyRMIKLHSP90PhosphoSitePlus
S385IEDVGsDEEEEHPRD
T5TQDQPRKDCHPRD
S406EMLQQsKILKVHSP90PhosphoSitePlus
Y466ELLRYyTSASGHSP90PhosphoSitePlus
Y61LDKIRyESLTDHATPase_cPhosphoSitePlus
Y667LVILLyETALLHPRD
T212QDRTLtIVDTGHPRD
Y197EDQTEyLEERRCDC45; Zip; HSP90PhosphoSitePlus
S399LPLNIsREMLQHSP90PhosphoSitePlus
T219IGYPItLFVEKCDC45; Zip; HSP90PhosphoSitePlus
T88NKQDRtLTIVDHPRD
S677LSSGFsLEDPQHPRD
S543GKTLVsVTKEGHSP90PhosphoSitePlus
T317FYKSLtNDWEDCDC45; HSP90PhosphoSitePlus
T540EFEGKtLVSVTHSP90PhosphoSitePlus
S231RDKEVsDDEAEHPRD; phosphoELM; RegPhos; SysPTM
Y313EYGEFyKSLTNRegPhos
T482LKDYCtRMKENHSP90PhosphoSitePlus
T90QDRTLtIVDTGHPRD

Dephosphorylation site
HS90A_HUMAN do not have dephosphorylation site.

Mutation site
Ensembl IDVariationSourceCancer namePubmed
ENSP00000335153N566TCOSMICHepatocellular Carcinoma21822264
ENSP00000335153P48SCOSMICCentral Nervous System Neoplasms18772890
ENSP00000335153D854GCOSMICCentral Nervous System Neoplasms18772890
ENSP00000335153R323GCOSMICProstate Cancer20668451
ENSP00000335153E327DCOSMICOvarian Cancer21720365
ENSP00000335153E351QCOSMICBreast Cancer20668451

Differential expressed protein
Ensembl IDCancer nameDesignSampleChangeRatioPubmed
ENSP00000335153Uterine CancerNormal vs. CancertissueUp17902640
ENSP00000335153Hepatocellular CarcinomaNormal vs. CancertissueUp2.111866469
ENSP00000335153hepatitis B virusNormal vs. CancertissueUp2.914654528
ENSP00000335153hepatitis C virusNormal vs. CancertissueUp2.914654528
ENSP00000335153Hepatocellular CarcinomaNormal vs. CancertissueUp2.914654528
ENSP00000335153Hepatocellular CarcinomaCancer vs. Cancer (HCC vs. HuCCA)cell lineUp20069059
ENSP00000335153Lung CancerTreatment(none vs betulin-treatment)cell lineDown0.1419085751
ENSP00000335153Gastric CancerNormal vs. CancertissueDown0.3519330469
ENSP00000335153Neoplasms by Histologic TypeTreatment (none vs. SB203580 treatment 21 hour)cell lineDown0.5815169874
ENSP00000335153Neoplasms by Histologic TypeCancer vs. Cancer (subtype)tissueUp1.416807943
ENSP00000335153Gastric CancerTreatment (none vs. drug-resistant)cell lineDown0.6920625496
ENSP00000335153Uterine CancerNormal vs. Cancercell lineUp1.615838902
ENSP00000335153Hepatocellular CarcinomaNormal vs. CancertissueUp2.811866469

Hyperphosphorylation site
HS90A_HUMAN do not have hyperphosphorylation site.

Direct Interaction Pair
SourceTargetRelationshipResource
PRKDC_HUMANHS90A_HUMANkinase -> substrateHPRD
CSK21_HUMANHS90A_HUMANkinase -> substrateHPRD; Robert H Newman (2013)
ZAGL2_HUMANHS90A_HUMANkinase -> substrateRegPhos

Function Annotation
KEGG Pathway
KEGG IDPathway
hsa04141Protein processing in endoplasmic reticulum
hsa05215Prostate cancer
hsa04914Progesterone-mediated oocyte maturation
hsa04612Antigen processing and presentation
hsa04621NOD-like receptor signaling pathway
hsa05200Pathways in cancer

Gene Ontology
GO IDGO_TermEvidenceOntology
GO:0006839mitochondrial transportTASbiological_process
GO:0033160positive regulation of protein import into nucleusIEAbiological_process
GO:0002135CTP bindingIEAmolecular_function
GO:0006986response to unfolded proteinNASbiological_process
GO:0000166nucleotide bindingTASmolecular_function
GO:0042470melanosomeIEAcellular_component
GO:0005525GTP bindingIEAmolecular_function
GO:0043005neuron projectionIEAcellular_component
GO:0009408response to heatIEAbiological_process
GO:0007411axon guidanceTASbiological_process
GO:0000086G2/M transition of mitotic cell cycleTASbiological_process
GO:0005829cytosolIEAcellular_component
GO:0030911TPR domain bindingTASmolecular_function
GO:0005524ATP bindingTASmolecular_function
GO:0051082unfolded protein bindingIEAmolecular_function
GO:0044325ion channel bindingIEAmolecular_function
GO:0005737cytoplasmIEAcellular_component
GO:0044281small molecule metabolic processTASbiological_process
GO:0010659cardiac muscle cell apoptotic processIEAbiological_process
GO:0043627response to estrogen stimulusIEAbiological_process
GO:0003729mRNA bindingIEAmolecular_function
GO:0048471perinuclear region of cytoplasmIEAcellular_component
GO:0010592positive regulation of lamellipodium assemblyIEAbiological_process
GO:0017098sulfonylurea receptor bindingIEAmolecular_function
GO:0019903protein phosphatase bindingIEAmolecular_function
GO:0009986cell surfaceIEAcellular_component
GO:0000278mitotic cell cycleTASbiological_process
GO:0032564dATP bindingIEAmolecular_function
GO:0050999regulation of nitric-oxide synthase activityTASbiological_process
GO:0016323basolateral plasma membraneIEAcellular_component
GO:0043025neuronal cell bodyIEAcellular_component
GO:0045429positive regulation of nitric oxide biosynthetic pIEAbiological_process
GO:0003009skeletal muscle contractionIEAbiological_process
GO:0016887ATPase activityIDAmolecular_function
GO:0019901protein kinase bindingIEAmolecular_function
GO:0030235nitric-oxide synthase regulator activityIDAmolecular_function
GO:0031526brush border membraneIEAcellular_component
GO:0042026protein refoldingTASbiological_process
GO:0016324apical plasma membraneIEAcellular_component
GO:0031012extracellular matrixIEAcellular_component
GO:0005886plasma membraneTAScellular_component
GO:0005622intracellularIEAcellular_component
GO:0006200ATP catabolic processIDAbiological_process
GO:0009651response to salt stressIEAbiological_process
GO:0005515protein bindingIPImolecular_function
GO:0042803protein homodimerization activityTASmolecular_function
GO:0006457protein foldingIEAbiological_process
GO:0060452positive regulation of cardiac muscle contractionIEAbiological_process
GO:0046209nitric oxide metabolic processTASbiological_process
GO:0042803protein homodimerization activityIEAmolecular_function
GO:0043234protein complexIEAcellular_component
GO:0007165signal transductionNASbiological_process
GO:0045429positive regulation of nitric oxide biosynthetic pISSbiological_process
GO:0005829cytosolNAScellular_component
GO:0006950response to stressIEAbiological_process
GO:0001764neuron migrationIEAbiological_process
GO:0051131chaperone-mediated protein complex assemblyIDAbiological_process
GO:0045793positive regulation of cell sizeIEAbiological_process
GO:0042802identical protein bindingIPImolecular_function
GO:0002134UTP bindingIEAmolecular_function
GO:0045040protein import into mitochondrial outer membraneIDAbiological_process
GO:0005515protein bindingIEAmolecular_function
GO:0005524ATP bindingIEAmolecular_function