EuRBPDB

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TCGA tumor abbreviations
  • ACCAdrenocortical carcinoma
  • BLCABladder Urothelial Carcinoma
  • BRCABreast invasive carcinoma
  • CESCCervical squamous cell carcinoma and endocervical adenocarcinoma
  • CHOLCholangio carcinoma
  • COADColon adenocarcinoma
  • DLBCLymphoid Neoplasm Diffuse Large B-cell Lymphoma
  • ESCAEsophageal carcinoma
  • GBMGlioblastoma multiforme
  • HNSCHead and Neck squamous cell carcinoma
  • KICHKidney Chromophobe
  • KIRCKidney renal clear cell carcinoma
  • KIRPKidney renal papillary cell carcinoma
  • LAMLAcute Myeloid Leukemia
  • LGGBrain Lower Grade Glioma
  • LIHCLiver hepatocellular carcinoma
  • LUADLung adenocarcinoma
  • LUSCLung squamous cell carcinoma
  • MESOMesothelioma
  • OVOvarian serous cystadenocarcinoma
  • PAADPancreatic adenocarcinoma
  • PCPGPheochromocytoma and Paraganglioma
  • PRADProstate adenocarcinoma
  • READRectum adenocarcinoma
  • SARCSarcoma
  • SKCMSkin Cutaneous Melanoma
  • STADStomach adenocarcinoma
  • TGCTThyroid carcinoma
  • THCAThyroid carcinoma
  • THYMThymoma
  • UCECUterine Corpus Endometrial Carcinoma
  • UCSUterine Carcinosarcoma
  • UVMUveal Melanoma

Note: Click here to get the extension of tumor abbreviations.


  • Cancer Related Information
  • Basic Information

Cancer associated literatures
PIDTitleArticle TimeAuthorDoi
21129190Activating transcription factor-3 (ATF3) functions as a tumor suppressor in colon cancer and is up-regulated upon heat-shock protein 90 (Hsp90) inhibition.BMC Cancer2010 Dec 3Hackl Cdoi: 10.1186/1471-2407-10-668.
1882012790-kDa heat shock protein inhibition abrogates the topoisomerase I poison-induced G2/M checkpoint in p53-null tumor cells by depleting Chk1 and Wee1.Mol Pharmacol2009 JanTse ANdoi: 10.1124/mol.108.050807
14570880Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress.J Biol Chem2003 Dec 26Arlander SJ-
15009113Induction of Hsp90 protein expression in malignant melanomas and melanoma metastases.Exp Dermatol2004 JanBecker B-
22268041The role of heat shock protein 90 in the regulation of tumor cell apoptosis.Bull Exp Biol Med2011 FebKaigorodova EV-
15613472Hsp90 is essential for restoring cellular functions of temperature-sensitive p53 mutant protein but not for stabilization and activation of wild-type p53: implications for cancer therapy.J Biol Chem2005 Feb 25M??ller P-
23638161High expression of heat shock protein 90 is associated with tumor aggressiveness and poor prognosis in patients with advanced gastric cancer.PLoS One2013 Apr 26Wang Jdoi: 10.1371/journal.pone.0062876
22975376Control of tumor bioenergetics and survival stress signaling by mitochondrial HSP90s.Cancer Cell2012 Sep 11Chae YCdoi: 10.1016/j.ccr.2012.07.015.
26271675HSP90 Inhibitor-SN-38 Conjugate Strategy for Targeted Delivery of Topoisomerase I Inhibitor to Tumors.Mol Cancer Ther2015 NovProia DAdoi: 10.1158/1535-7163.MCT-15-0455
17083915Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin.Biochem Biophys Res Commun2006 Dec 22Noguchi M-
19965370The regulatory mechanism of Hsp90alpha secretion and its function in tumor malignancy.Proc Natl Acad Sci U S A2009 Dec 15Wang Xdoi: 10.1073/pnas.0908151106
24384723HER2/ErbB2 activates HSF1 and thereby controls HSP90 clients including MIF in HER2-overexpressing breast cancer.Cell Death Dis2014 Jan 2Schulz Rdoi: 10.1038/cddis.2013.508.
26334999Patient-derived heavy chain antibody targets cell surface HSP90 on breast tumors.BMC Cancer2015 Sep 3Devarakonda CVdoi: 10.1186/s12885-015-1608-z.
26782567Potential role of heat-shock proteins in giant cell tumors.Genet Mol Res2015 Dec 29Chen JTdoi: 10.4238/2015.December.29.24.
19855434Inhibitors of HSP90 block p95-HER2 signaling in Trastuzumab-resistant tumors and suppress their growth.Oncogene2010 Jan 21Chandarlapaty Sdoi: 10.1038/onc.2009.337
17299090Bortezomib enhances dendritic cell (DC)-mediated induction of immunity to human myeloma via exposure of cell surface heat shock protein 90 on dying tumor cells: therapeutic implications.Blood2007 Jun 1Spisek R-
24117238The regulatory mechanism of a client kinase controlling its own release from Hsp90 chaperone machinery through phosphorylation.Biochem J2014 Jan 1Lu XAdoi: 10.1042/BJ20130963.
20553606Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.BMC Cancer2010 Jun 16McCready Jdoi: 10.1186/1471-2407-10-294.
22510516Amplification and high-level expression of heat shock protein 90 marks aggressive phenotypes of human epidermal growth factor receptor 2 negative breast cancer.Breast Cancer Res2012 Apr 17Cheng Q-
27302312Value of serum human epididymis secretory protein 4 as a marker for differential diagnosis of malignant and benign gynecological diseases of patients in southern China.Clin Chim Acta2016 Aug 1Li Ldoi: 10.1016/j.cca.2016.06.010
25316816Plasma levels of heat shock protein 90 alpha associated with lung cancer development and treatment responses.Clin Cancer Res2014 Dec 1Shi Ydoi: 10.1158/1078-0432.CCR-14-0174
17088927Mechanisms of disease: the role of heat-shock protein 90 in genitourinary malignancy.Nat Clin Pract Urol2006 NovLattouf JB-
29178343PRDM14 directly interacts with heat shock proteins HSP90α and glucose-regulated protein 78.Cancer Sci2018 FebMoriya Cdoi: 10.1111/cas.13458
21369706Cell surface heat shock protein 90 modulates prostate cancer cell adhesion and invasion through the integrin-β1/focal adhesion kinase/c-Src signaling pathway.Oncol Rep2011 MayLiu Xdoi: 10.3892/or.2011.1202
22824801C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances.Oncogene2013 Jun 20Muller Pdoi: 10.1038/onc.2012.314
19569046Identification of novel hub genes associated with liver metastasis of gastric cancer.Int J Cancer2009 Dec 15Chang Wdoi: 10.1002/ijc.24699.
21875325Sulforaphane potentiates the efficacy of 17-allylamino 17-demethoxygeldanamycin against pancreatic cancer through enhanced abrogation of Hsp90 chaperone function.Nutr Cancer2011Li Ydoi: 10.1080/01635581.2011.596645
21478269Functional inactivation of endogenous MDM2 and CHIP by HSP90 causes aberrant stabilization of mutant p53 in human cancer cells.Mol Cancer Res2011 MayLi Ddoi: 10.1158/1541-7786.MCR-10-0534
25297628HSP90 supports tumor growth and angiogenesis through PRKD2 protein stabilization.Cancer Res2014 Dec 1Azoitei Ndoi: 10.1158/0008-5472.CAN-14-1017
16774932Sustained activation of protein kinase C downregulates nuclear factor-kappaB signaling by dissociation of IKK-gamma and Hsp90 complex in human colonic epithelial cells.Carcinogenesis2007 JanPark KA-
19635199[Expressions of heat shock protein (HSP) family HSP 60, 70 and 90alpha in colorectal cancer tissues and their correlations to pathohistological characteristics].Ai Zheng2009 JunZhang WL-
19576239Expression of Hsp90 chaperone [corrected] proteins in human tumor tissue.Int J Biol Macromol2009 Oct 1McDowell CLdoi: 10.1016/j.ijbiomac.2009.06.012
22989880Secreted Hsp90 is a novel regulator of the epithelial to mesenchymal transition (EMT) in prostate cancer.J Biol Chem2012 Nov 2Hance MWdoi: 10.1074/jbc.M112.389015
18800240Expression of heat shock protein 90 at the cell surface in human neuroblastoma cells.Cell Stress Chaperones2009 MayCid Cdoi: 10.1007/s12192-008-0076-7
22592212Hsp90 inhibition overcomes HGF-triggering resistance to EGFR-TKIs in EGFR-mutant lung cancer by decreasing client protein expression and angiogenesis.J Thorac Oncol2012 JulKoizumi Hdoi: 10.1097/JTO.0b013e3182519a2c.
22849407Hsp90 rescues PTK6 from proteasomal degradation in breast cancer cells.Biochem J2012 Oct 15Kang SA-
23065205HSP90, HSPA8, HIF-1 alpha and HSP70-2 polymorphisms in breast cancer: a case-control study.Mol Biol Rep2012 DecZagouri Fdoi: 10.1007/s11033-012-1984-2
24463348Heat shock protein 90 inhibitors in non-small-cell lung cancer.Curr Opin Oncol2014 MarPillai RNdoi: 10.1097/CCO.0000000000000047.
18497978Molecular characterization of hsp90 isoforms in colorectal cancer cells and its association with tumour progression.Int J Oncol2008 JunMilicevic Z-
23228483Leptin increases HER2 protein levels through a STAT3-mediated up-regulation of Hsp90 in breast cancer cells.Mol Oncol2013 JunGiordano Cdoi: 10.1016/j.molonc.2012.11.002
18820283Association of hsp90 to the hTERT promoter is necessary for hTERT expression in human oral cancer cells.Carcinogenesis2008 DecKim RHdoi: 10.1093/carcin/bgn225
24736948Ultrasound-targeted microbubble destruction combined with dual targeting of HSP72 and HSC70 inhibits HSP90 function and induces extensive tumor-specic apoptosis.Int J Oncol2014 JulWang Hdoi: 10.3892/ijo.2014.2388
22935698Combined inhibition of Wee1 and Hsp90 activates intrinsic apoptosis in cancer cells.Cell Cycle2012 Oct 1Iwai Adoi: 10.4161/cc.21926
24338924Extracellular Hsp90 mediates an NF-??B dependent inflammatory stromal program: implications for the prostate tumor microenvironment.Prostate2014 AprBohonowych JEdoi: 10.1002/pros.22761
21875461[FAK/c-Src signaling pathway mediates the expression of cell surface HSP90 in cultured human prostate cancer cells and its association with their invasive capability].Zhonghua Zhong Liu Za Zhi2011 MayLiu XG-
24952482Receptor ligand-triggered resistance to alectinib and its circumvention by Hsp90 inhibition in EML4-ALK lung cancer cells.Oncotarget2014 Jul 15Tanimoto A-
26556859Combined inhibition of heat shock proteins 90 and 70 leads to simultaneous degradation of the oncogenic signaling proteins involved in muscle invasive bladder cancer.Oncotarget2015 Nov 24Cavanaugh Adoi: 10.18632/oncotarget.5496.
20558745Secreted heat shock protein 90alpha induces colorectal cancer cell invasion through CD91/LRP-1 and NF-kappaB-mediated integrin alphaV expression.J Biol Chem2010 Aug 13Chen JSdoi: 10.1074/jbc.M110.139345
22912728Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion.PLoS One2012El Hamidieh Adoi: 10.1371/journal.pone.0042722
18320023Integration of gene dosage and gene expression in non-small cell lung cancer, identification of HSP90 as potential target.PLoS One2008 Mar 5Gallegos Ruiz MIdoi: 10.1371/journal.pone.0001722.
19142186Hsp90 is expressed and represents a therapeutic target in human oesophageal cancer using the inhibitor 17-allylamino-17-demethoxygeldanamycin.Br J Cancer2009 Jan 27Wu Xdoi: 10.1038/sj.bjc.6604855
17975158Targeting heat shock protein 90 in pancreatic cancer impairs insulin-like growth factor-I receptor signaling, disrupts an interleukin-6/signal-transducer and activator of transcription 3/hypoxia-inducible factor-1alpha autocrine loop, and reduces orthotopic tumor growth.Clin Cancer Res2007 Nov 1Lang SA-
28038472Secreted heat shock protein 90 promotes prostate cancer stem cell heterogeneity.Oncotarget2017 Mar 21Nolan KDdoi: 10.18632/oncotarget.14252.
28032595Prospective identification of resistance mechanisms to HSP90 inhibition in KRAS mutant cancer cells.Oncotarget2017 Jan 31Rouhi Adoi: 10.18632/oncotarget.13841.
29888262HSP90: A Novel Target Gene of miRNA-628-3p in A549 Cells.Biomed Res Int2018 May 20Pan Jdoi: 10.1155/2018/4149707

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
ACCchr14102085356Missense_MutationnovelR202I0.3
BLCAchr14102085885Silentrs577315542F134F0.38
BLCAchr14102081771Nonsense_MutationnovelE714*0.19
BLCAchr14102083982Missense_MutationnovelN383K0.39
BLCAchr14102085317Missense_MutationNAG215A0.1
BLCAchr14102086091Missense_MutationnovelD66Y0.28
BLCAchr14102085340SilentnovelV207V0.08
BLCAchr14102083039Missense_MutationNAE584K0.51
BLCAchr14102083963Missense_MutationNAD390N0.66
BLCAchr14102083240Missense_MutationnovelE517K0.09
BLCAchr14102084446Missense_MutationnovelR367T0.12
BLCAchr14102085346Missense_MutationNAE205D0.15
BLCAchr14102084953Missense_MutationNAE237Q0.7
BLCAchr14102084498Missense_MutationNAD350H0.18
BLCAchr14102083661SilentnovelK457K0.22
BLCAchr14102139278Missense_MutationnovelE43K0.6
BLCAchr14102084962Nonsense_MutationNAE234*0.29
BLCAchr14102086283Missense_MutationNAL32F0.27
BLCAchr14102085901Missense_MutationnovelS129F0.05
BLCAchr14102081734Missense_MutationnovelS726L0.6
BLCAchr14102139345SilentNAR20R0.64
BRCAchr14102139255SilentnovelL50L0.53
BRCAchr14102083536Splice_SitenovelX494_splice0.12
BRCAchr14102081777Frame_Shift_InsnovelV712Kfs*100.05
BRCAchr14102082243Missense_MutationNAD653N0.04
BRCAchr14102084939In_Frame_Delrs3832931K241del0.15
BRCAchr141020816053'UTRnovel0.32
BRCAchr14102084834Missense_MutationnovelK276N0.06
BRCAchr14102086312Missense_MutationnovelQ23E0.42
BRCAchr14102102042Missense_MutationNAL67I0.13
BRCAchr14102083292Missense_MutationNAK499N0.61
CESCchr14102085893Missense_MutationnovelG132R0.07
CESCchr14102086327Missense_MutationNAE18K0.23
CESCchr14102082118SilentnovelL694L0.28
CESCchr14102083874Frame_Shift_DelnovelK419Nfs*30.18
CESCchr14102086246Silentrs754536892L45L0.18
CESCchr14102085832Missense_MutationNAT152I0.42
CESCchr14102082278Missense_MutationNAS641C0.86
CESCchr14102084533Missense_MutationnovelR338T0.3
COADchr14102086034Frame_Shift_DelnovelQ85Kfs*140.05
COADchr14102084505SilentnovelA347A0.1
COADchr14102082294Missense_MutationnovelI636V0.08
COADchr14102085897Missense_MutationnovelM130I0.48
COADchr14102081783Missense_MutationNAA710S0.38
COADchr14102083874Frame_Shift_DelnovelK419Nfs*30.25
COADchr14102086309Missense_MutationnovelA24T0.11
COADchr14102082233Missense_MutationnovelD656G0.07
COADchr141020816113'UTRnovel0.17
COADchr14102081742Silentrs61999351D723D0.26
COADchr14102084558Frame_Shift_DelnovelS330Qfs*480.21
COADchr14102101980Silentrs768847708H87H0.23
ESCAchr14102084473Frame_Shift_DelnovelK358Rfs*200.38
ESCAchr141020816153'UTRnovel0.1
ESCAchr14102086362Missense_MutationnovelQ6L0.41
GBMchr14102084734Missense_MutationnovelG310R0.2
GBMchr14102082222Missense_MutationnovelK660E0.16
GBMchr14102085316SilentnovelG215G0.1
GBMchr14102086287Nonsense_MutationnovelS31*0.3
GBMchr14102086110Silentrs116285249I59I0.2
HNSCchr14102085793Missense_MutationnovelS165L0.13
HNSCchr14102085868Missense_MutationnovelS140F0.24
HNSCchr14102083086Nonsense_MutationnovelF568Sfs*20.08
HNSCchr14102083165Missense_MutationNAV542M0.21
HNSCchr14102082910Intronnovel0.33
KIRCchr14102086246Missense_MutationNAL45V0.24
KIRCchr14102085353Missense_MutationNAI203T0.61
KIRCchr14102083579Missense_Mutationrs201678802K485E0.18
KIRCchr14102085371Missense_MutationnovelY197C0.22
KIRCchr14102082149Missense_MutationNAH684R0.21
KIRCchr14102084721Frame_Shift_DelnovelK314Efs*50.28
KIRPchr14102084935Frame_Shift_InsnovelE243Rfs*160.21
KIRPchr14102082966Intronnovel0.48
KIRPchr14102085957Silentrs759018453I110I0.43
LGGchr14102085766Missense_MutationnovelT174I0.08
LGGchr14102085903SilentnovelI128I0.11
LIHCchr14102081731Missense_Mutationrs778338593R727H0.45
LIHCchr14102139400Missense_MutationnovelP2L0.35
LIHCchr14102086373SilentnovelP2P0.33
LIHCchr14102082329Frame_Shift_DelnovelS623Nfs*150.37
LIHCchr14102084819Frame_Shift_DelnovelK274Rfs*250.18
LIHCchr14102082971Intronnovel0.27
LIHCchr14102086063Missense_MutationnovelE75V0.14
LUADchr14102083023Intronnovel0.07
LUADchr14102082434Nonsense_MutationNAS589*0.53
LUADchr14102081749Missense_MutationNAG721V0.09
LUADchr14102082146Missense_MutationnovelA685G0.25
LUADchr14102083055Missense_Mutationrs756187710I578M0.25
LUADchr14102085329Missense_Mutationrs776320264S211F0.17
LUADchr14102086324Missense_MutationnovelT19S0.38
LUADchr14102086272Frame_Shift_DelnovelI34Ffs*260.12
LUADchr14102082318Missense_MutationNAM628V0.13
LUSCchr14102082436SilentnovelV588V0.15
LUSCchr14102084509Missense_Mutationrs745418872R346H0.5
LUSCchr14102086221Nonsense_MutationnovelS53*0.09
LUSCchr14102082141Missense_MutationnovelR687G0.42
LUSCchr14102086325Missense_MutationNAE18D0.12
LUSCchr14102083213Missense_MutationnovelD526N0.2
OVchr14102083002Intronnovel0.07
OVchr14102085346Missense_MutationNAE205D0.25
OVchr14102082186SilentnovelL672L0.12
OVchr14102085433Splice_SitenovelX177_splice0.18
OVchr14102084929Frame_Shift_DelNAE244Kfs*720.42
PAADchr14102084826Missense_Mutationrs55793809K279M0.15
PAADchr14102086005SilentnovelT94T0.14
PAADchr14102081789Missense_MutationnovelT708A0.19
PAADchr14102083627Missense_MutationnovelA469T0.13
PCPGchr14102085900SilentnovelS129S0.43
PCPGchr14102085380Missense_MutationnovelQ194P0.38
PRADchr14102082206Nonsense_MutationnovelL665*0.27
READchr14102101914SilentNAL109L0.25
READchr14102083959Missense_MutationNAS391L0.44
READchr14102084926Nonsense_MutationNAE246*0.38
SARCchr14102082197Missense_MutationnovelE668A0.41
SARCchr14102083260Missense_MutationnovelR510L0.13
SKCMchr14102083255Missense_MutationNAR512W0.26
SKCMchr14102082958Intronnovel0.48
SKCMchr14102101967Missense_MutationnovelP92S0.04
SKCMchr14102101968SilentnovelF91F0.04
SKCMchr14102082283Silentrs113093780D639D0.3
SKCMchr14102082430SilentNAN590N0.88
SKCMchr14102084743Missense_MutationNAE307K0.4
SKCMchr14102082958Intronnovel0.28
SKCMchr14102083167Missense_Mutationrs144774653L541S0.24
SKCMchr141020816653'UTRnovel0.55
SKCMchr14102082889Intronnovel0.46
SKCMchr14102083846Nonsense_MutationNAE429*0.77
SKCMchr14102083644Missense_MutationnovelL463S0.37
SKCMchr14102086232SilentNAI49I0.22
SKCMchr14102086297Nonsense_MutationnovelQ28*0.41
SKCMchr14102083192Missense_MutationnovelL533V0.23
SKCMchr14102101967Missense_MutationnovelP92S0.42
SKCMchr14102085341Missense_MutationnovelV207A0.56
SKCMchr14102082207Missense_MutationnovelL665V0.27
STADchr14102085425Missense_MutationNAP179H0.22
STADchr14102084698Missense_MutationNAD322N0.07
STADchr14102086031Missense_MutationNAD86Y0.07
STADchr14102084814Missense_MutationNAK283T0.44
STADchr14102083972Missense_MutationNAG387W0.35
STADchr14102086021Missense_MutationNAL89P0.12
STADchr14102084425Missense_MutationnovelC374Y0.11
STADchr14102082232In_Frame_DelnovelD656del0.22
STADchr14102101980Silentrs768847708H87H0.19
STADchr14102085938Missense_MutationnovelA117S0.22
THCAchr14102083264Nonsense_MutationnovelE509*0.22
THCAchr14102083291Missense_Mutationrs752947562D500N0.07
UCECchr14102081779Missense_MutationnovelA711V0.45
UCECchr14102139319Missense_MutationNAY29C0.33
UCECchr14102083032Splice_SitenovelX585_splice0.13
UCECchr14102102023Missense_MutationNAS73Y0.35
UCECchr14102084482Missense_Mutationrs758715454R355K0.39
UCECchr14102082924Intronnovel0.52
UCECchr14102101935SilentnovelS102S0.37
UCECchr14102083889Missense_MutationNAK414N0.26
UCECchr141020815313'UTRnovel0.19
UCECchr14102083232SilentNAI519I0.12
UCECchr14102084790Missense_MutationNAN291S0.44
UCECchr14102101914SilentnovelL109L0.52
UCECchr14102084752Missense_MutationnovelI304V0.24
UCECchr14102084402SilentnovelL382L0.2
UCECchr14102083027Splice_Regionnovel0.51
UCECchr141020816373'UTRnovel0.5
UCECchr14102084823In_Frame_Insrs777317553K279dup0.51
UCECchr14102081762Missense_MutationNAP717S0.39
UCECchr14102082416Missense_MutationNAS595F0.3
UCECchr14102082245Missense_Mutationrs751002513A652V0.34
UCECchr14102083047Missense_MutationnovelK581T0.32
UCECchr141020815703'UTRnovel0.19
UCECchr14102082911Intronrs5779194330.64
UCECchr14102084453Missense_Mutationrs766449280V365I0.52
UCECchr14102086006Missense_MutationnovelT94N0.33
UCECchr14102101979Missense_Mutationrs749689152V88I0.25
UCECchr14102082268Missense_MutationnovelE644D0.45
UCECchr14102083808Missense_MutationnovelF441L0.38
UCECchr14102082402Missense_MutationNAV600I0.32
UCECchr14102082911Intronrs5779194330.22
UCECchr14102083936Missense_MutationNAS399T0.38
UCECchr14102082842Intronnovel0.13
UCECchr14102083546Missense_MutationnovelG496C0.2
UCECchr14102085849Missense_MutationnovelE146D0.09
UCECchr14102082972Intronnovel0.38
UCECchr14102081823Splice_SitenovelX697_splice0.15

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
BRCADEL0.23331.4717e-06
CESCDEL0.14240.00086239
CHOLDEL0.55560.00040262
COADDEL0.29050.050084
GBMDEL0.25135.7274e-07
HNSCDEL0.11690.0057325
KIRCDEL0.38260.0074281
KIRPDEL0.17010.085174
LIHCDEL0.32168.4799e-08
LUADDEL0.20540.0018747
LUSCAMP0.23350.064655
MESODEL0.41380.088547
PAADDEL0.08150.11332
READDEL0.38180.189
SKCMDEL0.28070.10277
STADDEL0.23130.0031145

Survival Analysis
CancerP-value Q-value
KIRC0.00049

Kaplan-Meier Survival Analysis

MESO0.032

Kaplan-Meier Survival Analysis

HNSC0.0012

Kaplan-Meier Survival Analysis

PRAD0.046

Kaplan-Meier Survival Analysis

BRCA0.00092

Kaplan-Meier Survival Analysis

KIRP0.028

Kaplan-Meier Survival Analysis

PAAD0.023

Kaplan-Meier Survival Analysis

LIHC0.00011

Kaplan-Meier Survival Analysis

LUAD0.0012

Kaplan-Meier Survival Analysis

UVM0.013

Kaplan-Meier Survival Analysis

OV0.042

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742

  • Description
  • RBPome
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • Pathways
  • Phenotypes
  • GWAS
  • PPI
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000080824 (Gene tree)
Gene ID
3320
Gene Symbol
HSP90AA1
Alias
Hsp89|Hsp90|FLJ31884|HSP90N|HSPC1|HSPCA
Full Name
heat shock protein 90 alpha family class A member 1
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
59,022 bases
Position
chr14:102,080,738-102,139,759
Accession
5253
RBP type
non-canonical RBP
Summary
The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]
RNA binding proteome (RBPome)
PIDTitleMethod TimeAuthorDoi
22681889The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts4SURIC & HEK2932012 MayBaltz AGDOI: 10.1016/j.molcel.2012.05.021
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & HEK2932019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & HEK2932018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
29431736Capturing the interactome of newly transcribed RNARICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
22658674Insights into RNA biology from an atlas of mammalian mRNA-binding proteinsRIC & Hela2012 May 31Castello ADOI: 10.1016/j.cell.2012.04.031
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & Hela2018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & MCF10A2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & MCF72018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & U2OS2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
27453046Comprehensive Identification of RNA-Binding Domains in Human CellsRIC & Hela2016 Aug 18Castello ADOI: 10.1016/j.molcel.2016.06.029
30352994Discovery of RNA-binding proteins and characterization of their dynamic responses by enhanced RNA interactome captureRIC & Jurkat2018 Oct 23Perez-Perri JIDOI:10.1038/s41467-018-06557-8

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
18801074Analysis of gene and protein expression of cytochrome P450 and stress-associated molecules in rat liver after spaceflight.Pathol Int2008 SepBaba Tdoi: 10.1111/j.1440-1827.2008.02275.x.
23575152Proteomic profiles of the embryonic chorioamnion and uterine caruncles in buffaloes (Bubalus bubalis) with normal and retarded embryonic development.Biol Reprod2013 May 16Balestrieri MLdoi: 10.1095/biolreprod.113.108696
20237157HSP90 protein stabilizes unloaded argonaute complexes and microscopic P-bodies in human cells.Mol Biol Cell2010 May 1Johnston Mdoi: 10.1091/mbc.E09-10-0885
30285465Sepiapterin alleviates impaired gastric nNOS function in spontaneous diabetic female rodents through NRF2 mRNA turnover and miRNA biogenesis pathway.Am J Physiol Gastrointest Liver Physiol2018 Dec 1Gangula PRdoi: 10.1152/ajpgi.00152.2018
11447118The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR.EMBO J2001 Jul 16Donze O-
11090140In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90.J Virol2000 DecHu J-
10694498Localization of HSP90 binding sites in the human hepatitis B virus polymerase.Biochem Biophys Res Commun2000 Mar 5Cho G-
15563614Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content.Plant Physiol2004 DecSjogren LL-
19467292SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein.Biochimie2009 AugOlieric Vdoi: 10.1016/j.biochi.2009.05.004
17804463Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system.Nucleic Acids Res2007Stahl M-
22016036The interaction between human initiation factor eIF3 subunit c and heat-shock protein 90: a necessary factor for translation mediated by the hepatitis C virus internal ribosome entry site.Virus Res2012 JanUjino Sdoi: 10.1016/j.virusres.2011.10.003
25855731Molecular chaperone Hsp90 is a therapeutic target for noroviruses.J Virol2015 JunVashist Sdoi: 10.1128/JVI.00315-15
30621721MOV10 binding circ-DICER1 regulates the angiogenesis of glioma via miR-103a-3p/miR-382-5p mediated ZIC4 expression change.J Exp Clin Cancer Res2019 Jan 8He Qdoi: 10.1186/s13046-018-0990-1.
22933272Differential roles of Hsp70 and Hsp90 in the assembly of the replicase complex of a positive-strand RNA plant virus.J Virol2012 NovMine Adoi: 10.1128/JVI.01659-12
22922937Sulforaphane synergistically enhances the cytotoxicity of arsenic trioxide in multiple myeloma cells via stress-mediated pathways.Oncol Rep2012 NovDoudican NAdoi: 10.3892/or.2012.1977
26828270A telomerase-derived peptide regulates reactive oxygen species and hepatitis C virus RNA replication in HCV-infected cells via heat shock protein 90.Biochem Biophys Res Commun2016 Feb 26Lee SAdoi: 10.1016/j.bbrc.2016.01.160
12054492Hsp90 makes the human HBV Pol competent for in vitro priming rather than maintaining the human HBV Pol/pregenomic RNA complex.Arch Biochem Biophys2002 May 1Gyoo Park S-
16087666Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone.J Biol Chem2005 Oct 7Murphy PJ-
22105779Inhibition of heat shock protein (molecular weight 90 kDa) attenuates proinflammatory cytokines and prevents lipopolysaccharide-induced liver injury in mice.Hepatology2012 MayAmbade Adoi: 10.1002/hep.24802
27115409Surface heat shock protein 90 serves as a potential receptor for calcium oxalate crystal on apical membrane of renal tubular epithelial cells.J Biol Inorg Chem2016 JulFong-Ngern Kdoi: 10.1007/s00775-016-1355-x
30541828Autophagy Promotes Replication of Influenza A Virus In Vitro.J Virol2019 Feb 5Wang Rdoi: 10.1128/JVI.01984-18
30508278Characterizations of HSP90-Interacting Complex in Renal Cells Using Tandem Affinity Purification and Its Potential Role in Kidney Stone Formation.Proteomics2018 DecManissorn Jdoi: 10.1002/pmic.201800004.
30982460HIF1A and NFAT5 coordinate Na+-boosted antibacterial defense via enhanced autophagy and autolysosomal targeting.Autophagy2019 Apr 14:1-18Neubert Pdoi: 10.1080/15548627.2019.1596483
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000216281HSP90AA1-2013379-ENSP00000216281732 (aa)-P07900
ENST00000334701HSP90AA1-2023510XM_011536718ENSP00000335153854 (aa)XP_011535020P07900
ENST00000553585HSP90AA1-203581-ENSP00000450712174 (aa)-G3V2J8
ENST00000557234HSP90AA1-208584-ENSP0000045224180 (aa)-G3V592
ENST00000554401HSP90AA1-2041710-ENSP0000045140052 (aa)-H0YJF5
ENST00000557089HSP90AA1-207694--- (aa)--
ENST00000560130HSP90AA1-210488--- (aa)--
ENST00000555662HSP90AA1-205429--- (aa)--
ENST00000556554HSP90AA1-206552--- (aa)--
ENST00000558600HSP90AA1-209595-ENSP00000489370100 (aa)-A0A0U1RR69
Gene Model
Click here to download ENSG00000080824's gene model file
Pathways
Pathway IDPathway NameSource
hsa04141Protein processing in endoplasmic reticulumKEGG
hsa04151PI3K-Akt signaling pathwayKEGG
hsa04217NecroptosisKEGG
hsa04612Antigen processing and presentationKEGG
hsa04621NOD-like receptor signaling pathwayKEGG
hsa04657IL-17 signaling pathwayKEGG
hsa04659Th17 cell differentiationKEGG
hsa04914Progesterone-mediated oocyte maturationKEGG
hsa04915Estrogen signaling pathwayKEGG
hsa05200Pathways in cancerKEGG
hsa05215Prostate cancerKEGG
hsa05418Fluid shear stress and atherosclerosisKEGG
Phenotypes
ensgIDTraitpValuePubmed ID
ENSG00000080824Tobacco Use Disorder4E-623942779
GWAS
ensgIDSNPChromosomePositionSNP-risk TraitPubmedID95% CIOr or BEAT EFO ID
ENSG00000080824rs119059614102129288ABehavioural disinhibition (generation interaction)23942779EFO_0005430|EFO_0008364|EFO_0005431|EFO_0005432|EFO_0004329|EFO_0003829
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000080824's network

* RBP PPI network refers to all genes directly bind to RBP
Orthologs identified by RBPome
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000080824HSP90AA19875.627WBGene00000915daf-219974.095Caenorhabditis_elegans
ENSG00000080824HSP90AA19878.412FBgn0001233Hsp839978.134Drosophila_melanogaster
ENSG00000080824HSP90AA17855.263FBgn0026761Trap18945.540Drosophila_melanogaster
ENSG00000080824HSP90AA19886.134ENSG00000096384HSP90AB110085.246Homo_sapiens
ENSG00000080824HSP90AA17371.053ENSG00000166598HSP90B110068.750Homo_sapiens
ENSG00000080824HSP90AA18741.564ENSG00000126602TRAP110054.286Homo_sapiens
ENSG00000080824HSP90AA110099.045ENSMUSG00000021270Hsp90aa110099.502Mus_musculus
ENSG00000080824HSP90AA19886.555ENSMUSG00000023944Hsp90ab110085.656Mus_musculus
ENSG00000080824HSP90AA17371.053ENSMUSG00000020048Hsp90b18950.301Mus_musculus
ENSG00000080824HSP90AA18345.813ENSMUSG00000005981Trap18645.813Mus_musculus
ENSG00000080824HSP90AA17386.842YPL240CHSP829960.139Saccharomyces_cerevisiae
ENSG00000080824HSP90AA17386.842YMR186WHSC829960.251Saccharomyces_cerevisiae
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0000086G2/M transition of mitotic cell cycle-TASProcess
GO:0000166nucleotide binding11470816.TASFunction
GO:0001934positive regulation of protein phosphorylation19363271.IDAProcess
GO:0003723RNA binding22658674.22681889.HDAFunction
GO:0005515protein binding21873635.IBAFunction
GO:0005515protein binding9660753.9817749.12176997.12526792.12604615.12853476.12855682.14638689.14676191.14743216.15708368.16169070.16275660.16307917.17024179.18195352.19026643.19740745.19875381.20029029.20133715.20188096.20195357.20353823.20374249.20558745.20864032.20936779.21360678.21871133.21988832.22022502.22843495.23349634.23414517.23431407.23455922.23995768.24189400.24658140.24794838.24949977.25036637.25416956.25486457.25609649.25738358.26496610.26517842.26754925.27086506.27353360.28330616.29127155.IPIFunction
GO:0005524ATP binding21873635.IBAFunction
GO:0005524ATP binding27353360.IDAFunction
GO:0005524ATP binding11470816.TASFunction
GO:0005576extracellular region-TASComponent
GO:0005634nucleus21630459.HDAComponent
GO:0005634nucleus21873635.IBAComponent
GO:0005634nucleus-ISSComponent
GO:0005654nucleoplasm-TASComponent
GO:0005737cytoplasm21873635.IBAComponent
GO:0005737cytoplasm10791971.IDAComponent
GO:0005737cytoplasm-ISSComponent
GO:0005829cytosol21873635.IBAComponent
GO:0005829cytosol12526792.NASComponent
GO:0005829cytosol-TASComponent
GO:0005886plasma membrane21873635.IBAComponent
GO:0005886plasma membrane-TASComponent
GO:0006839mitochondrial transport12526792.TASProcess
GO:0006898receptor-mediated endocytosis-TASProcess
GO:0006986response to unfolded protein2527334.NASProcess
GO:0007004telomere maintenance via telomerase10197982.IDAProcess
GO:0007165signal transduction11470816.NASProcess
GO:0009408response to heat21873635.IBAProcess
GO:0009408response to heat-ISSProcess
GO:0009409response to cold-ISSProcess
GO:0009986cell surface21873635.IBAComponent
GO:0010389regulation of G2/M transition of mitotic cell cycle-TASProcess
GO:0016020membrane19946888.HDAComponent
GO:0016887ATPase activity15937123.27353360.29127155.IDAFunction
GO:0019221cytokine-mediated signaling pathway-TASProcess
GO:0021955central nervous system neuron axonogenesis-ISSProcess
GO:0023026MHC class II protein complex binding20458337.HDAFunction
GO:0030010establishment of cell polarity-ISSProcess
GO:0030235nitric-oxide synthase regulator activity21873635.IBAFunction
GO:0030235nitric-oxide synthase regulator activity15937123.IDAFunction
GO:0030911TPR domain binding9660753.IDAFunction
GO:0030911TPR domain binding12526792.TASFunction
GO:0031396regulation of protein ubiquitination16809764.IDAProcess
GO:0031625ubiquitin protein ligase binding16207813.IPIFunction
GO:0032273positive regulation of protein polymerization19363271.IDAProcess
GO:0032991protein-containing complex21873635.IBAComponent
GO:0032991protein-containing complex23349634.IDAComponent
GO:0033138positive regulation of peptidyl-serine phosphorylation-ISSProcess
GO:0034605cellular response to heat21873635.IBAProcess
GO:0034774secretory granule lumen-TASComponent
GO:0038096Fc-gamma receptor signaling pathway involved in phagocytosis-TASProcess
GO:0038128ERBB2 signaling pathway-TASProcess
GO:0042026protein refolding9660753.TASProcess
GO:0042470melanosome-IEAComponent
GO:0042623ATPase activity, coupled-TASFunction
GO:0042802identical protein binding29127155.IDAFunction
GO:0042802identical protein binding8289821.16169070.21360678.21460846.25036637.IPIFunction
GO:0042803protein homodimerization activity21873635.IBAFunction
GO:0042803protein homodimerization activity29127155.IDAFunction
GO:0042803protein homodimerization activity11470816.TASFunction
GO:0042826histone deacetylase binding16809764.IPIFunction
GO:0043025neuronal cell body21873635.IBAComponent
GO:0043025neuronal cell body-ISSComponent
GO:0043202lysosomal lumen25719862.TASComponent
GO:0043209myelin sheath21873635.IBAComponent
GO:0043254regulation of protein complex assembly20176123.NASProcess
GO:0043312neutrophil degranulation-TASProcess
GO:0043335protein unfolding20176123.NASProcess
GO:0044294dendritic growth cone-ISSComponent
GO:0044295axonal growth cone-ISSComponent
GO:0045040protein import into mitochondrial outer membrane15644312.IDAProcess
GO:0045429positive regulation of nitric oxide biosynthetic process-ISSProcess
GO:0046677response to antibiotic-ISSProcess
GO:0048010vascular endothelial growth factor receptor signaling pathway-TASProcess
GO:0048156tau protein binding19363271.IPIFunction
GO:0048471perinuclear region of cytoplasm21873635.IBAComponent
GO:0048471perinuclear region of cytoplasm-ISSComponent
GO:0048675axon extension-ISSProcess
GO:0050821protein stabilization21873635.IBAProcess
GO:0050821protein stabilization27353360.IMPProcess
GO:0050821protein stabilization-TASProcess
GO:0050999regulation of nitric-oxide synthase activity-TASProcess
GO:0051020GTPase binding24337748.IPIFunction
GO:0051082unfolded protein binding21873635.IBAFunction
GO:0051131chaperone-mediated protein complex assembly15644312.IDAProcess
GO:0051186cofactor metabolic process-TASProcess
GO:0051897positive regulation of protein kinase B signaling-ISSProcess
GO:0051973positive regulation of telomerase activity10197982.IDAProcess
GO:0061684chaperone-mediated autophagy25719862.TASProcess
GO:0070062extracellular exosome11487543.12519789.19199708.20458337.23533145.HDAComponent
GO:0070182DNA polymerase binding10197982.19751963.IPIFunction
GO:0071682endocytic vesicle lumen-TASComponent
GO:0097110scaffold protein binding10409742.IPIFunction
GO:0097711ciliary basal body-plasma membrane docking-TASProcess
GO:0097718disordered domain specific binding21873635.IBAFunction
GO:0097718disordered domain specific binding15713458.IPIFunction
GO:1900034regulation of cellular response to heat-TASProcess
GO:1902949positive regulation of tau-protein kinase activity19363271.IDAProcess
GO:1903364positive regulation of cellular protein catabolic process18292230.IGIProcess
GO:1903827regulation of cellular protein localization-ISSProcess
GO:1904813ficolin-1-rich granule lumen-TASComponent
GO:1905323telomerase holoenzyme complex assembly10197982.IDAProcess
GO:1990782protein tyrosine kinase binding20353823.IPIFunction
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