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
28291803Induction of Hsp70 in tumor cells treated with inhibitors of the Hsp90 activity: A predictive marker and promising target for radiosensitization.PLoS One2017 Mar 14Kudryavtsev VAdoi: 10.1371/journal.pone.0173640
18426646[Expression characteristics of heat shock protein 70 and pim-1 gene in bone marrow mononuclear cells from leukemia patients and their clinical significance].Zhongguo Shi Yan Xue Ye Xue Za Zhi2008 AprLi Y-
17616937Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis.Histol Histopathol2007 OctRamp Udoi: 10.14670/HH-22.1099.
18587674HBP21: a novel member of TPR motif family, as a potential chaperone of heat shock protein 70 in proliferative vitreoretinopathy (PVR) and breast cancer.Mol Biotechnol2008 NovLiu Qdoi: 10.1007/s12033-008-9080-5
22613557Identification of a potential tumor differentiation factor receptor candidate in prostate cancer cells.FEBS J2012 JulSokolowska Idoi: 10.1111/j.1742-4658.2012.08641.x
18790094cis-acting sequences and trans-acting factors in the localization of mRNA for mitochondrial ribosomal proteins.Biochim Biophys Acta2008 DecRusso Adoi: 10.1016/j.bbagrm.2008.08.006
22037021Extracellular HspBP1 inhibits formation of a cytotoxic Tag7-Hsp70 complex in vitro and in human serum.Biochimie2012 JanYashin DVdoi: 10.1016/j.biochi.2011.10.007
17278882Heat shock protein 70 and glycoprotein 96 are differentially expressed on the surface of malignant and nonmalignant breast cells.Cell Stress Chaperones2006 WinterMelendez K-
19069644[Synergistic effect of thermotherapy in combination with chemotherapy on lung tumor A549 cells growth through activation of c-Jun N-terminal kinase and inhibition of heat shock protein70 expression].Wei Sheng Yan Jiu2008 SepGao S-
17580361Patient survival by Hsp70 membrane phenotype: association with different routes of metastasis.Cancer2007 Aug 15Pfister K-
25347739Hsp70 in cancer: back to the future.Oncogene2015 Aug 6Sherman MYdoi: 10.1038/onc.2014.349
20714862Expression of Hsp27 and Hsp70 in lymphocytes and plasma in healthy workers and coal miners with lung cancer.J Huazhong Univ Sci Technolog Med Sci2010 AugWang Hdoi: 10.1007/s11596-010-0441-5
26559972A Novel Function of Molecular Chaperone HSP70: SUPPRESSION OF ONCOGENIC FOXM1 AFTER PROTEOTOXIC STRESS.J Biol Chem2016 Jan 1Halasi Mdoi: 10.1074/jbc.M115.678227
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-
15378924Content and synthesis of stress proteins in subcellular structures of cancer cells exposed to heat shock and cisplatin.Dokl Biochem Biophys2004 May-JunMavletova DA-
21725599ShRNA-mediated gene silencing of heat shock protein 70 inhibits human colon cancer growth.Mol Med Rep2011 Sep-OctZhong MAdoi: 10.3892/mmr.2011.528
25175595Heat shock proteins HSP70 and MRJ cooperatively regulate cell adhesion and migration through urokinase receptor.BMC Cancer2014 Aug 30Lin Ydoi: 10.1186/1471-2407-14-639.
22535481High HSP27 and HSP70 expression levels are independent adverse prognostic factors in primary resected colon cancer.Cell Oncol (Dordr)2012 JunBauer Kdoi: 10.1007/s13402-012-0079-3
26050647Quercetin Enhances Chemosensitivity to Gemcitabine in Lung Cancer Cells by Inhibiting Heat Shock Protein 70 Expression.Clin Lung Cancer2015 NovLee SHdoi: 10.1016/j.cllc.2015.05.006
24501795[Analysis of occurrence atypical proteins in the serum at smoking and non-smoking cigarettes patients with lung cancer].Przegl Lek2013Goda R-
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.
28192510Downregulation of Sp1 by Minnelide leads to decrease in HSP70 and decrease in tumor burden of gastric cancer.PLoS One2017 Feb 13Arora Ndoi: 10.1371/journal.pone.0171827
28848092Extracellular HSP70 Activates ERK1/2, NF-kB and Pro-Inflammatory Gene Transcription Through Binding with RAGE in A549 Human Lung Cancer Cells.Cell Physiol Biochem2017Somensi Ndoi: 10.1159/000480213
30245753Circulating Heat Shock Protein 70 Is a Novel Biomarker for Early Diagnosis of Lung Cancer.Dis Markers2018 Aug 29Tang Tdoi: 10.1155/2018/6184162
30337218Heat shock proteins 60 and 70 are associated with long-term outcome of T1-stage high-grade urothelial tumors of the bladder treated with intravesical Bacillus Calmette-Gu??rin immunotherapy.Urol Oncol2018 DecMano Rdoi: 10.1016/j.urolonc.2018.09.007

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr5133091354Nonsense_MutationnovelQ514*0.28
BLCAchr5133091333Missense_MutationnovelE507K0.24
BLCAchr51331045053'UTRnovel0.38
BLCAchr5133089084SilentnovelV389V0.17
BLCAchr5133067516Missense_MutationnovelY89H0.27
BRCAchr5133089111SilentNAV398V0.18
BRCAchr5133067505Missense_MutationNAS85C0.25
BRCAchr5133073255Missense_MutationnovelE152V0.39
BRCAchr5133076797Missense_MutationNAE269D0.4
BRCAchr5133101805Missense_MutationnovelR695L0.07
BRCAchr5133067519Missense_MutationNAD90Y0.24
BRCAchr5133089127SilentNAL404L0.28
BRCAchr5133076784Missense_MutationNAR265Q0.11
BRCAchr5133086837Missense_Mutationrs368924343R322C0.13
BRCAchr5133097214Silentrs142002805N619N0.1
BRCAchr5133104305In_Frame_DelnovelK798_Q802del0.32
CESCchr5133097214Silentrs142002805N619N0.38
CESCchr5133092699Splice_SitenovelX521_splice0.87
CESCchr5133096250Frame_Shift_InsnovelG602Sfs*30.18
CESCchr5133088556Splice_SitenovelX379_splice0.34
CESCchr5133103950Missense_MutationnovelK748R0.36
CESCchr5133092772Missense_MutationNAE545Q0.49
CESCchr5133074040Missense_MutationNAE193K0.14
COADchr5133076735Missense_MutationNAG249R0.49
COADchr5133088499Nonsense_MutationnovelE361*0.33
COADchr5133097250SilentnovelK631K0.23
COADchr5133089571SilentnovelE418E0.26
COADchr5133103911Frame_Shift_DelnovelS737Afs*90.18
COADchr5133076705Missense_MutationNAV239M0.08
COADchr5133086787Missense_MutationNAK305T0.29
COADchr5133089609Missense_MutationnovelV431A0.08
COADchr5133088499Nonsense_MutationnovelE361*0.32
COADchr5133065036Nonsense_MutationnovelQ55Hfs*40.05
GBMchr5133103951Missense_MutationnovelK748N0.06
GBMchr5133076886Missense_MutationnovelG299E0.31
GBMchr5133104419Frame_Shift_DelnovelE836Kfs*130.09
GBMchr5133067494SilentnovelE81E0.52
HNSCchr5133091353SilentnovelD513D0.33
HNSCchr5133091354Nonsense_MutationnovelQ514*0.46
HNSCchr5133104404Missense_Mutationrs144576995D831Y0.18
HNSCchr5133104264Nonsense_MutationnovelS784*0.18
HNSCchr5133104396Missense_Mutationrs377082440S828L0.28
HNSCchr5133065032Frame_Shift_InsnovelS54Mfs*60.09
HNSCchr5133076770SilentNAI260I0.54
HNSCchr5133064991Missense_MutationnovelS40C0.17
KIRCchr51330520865'UTRnovel0.39
KIRCchr5133103959Missense_MutationNAL751P0.22
KIRCchr5133088463Missense_MutationNAA349S0.27
KIRCchr5133104427SilentnovelD838D0.09
LGGchr5133070452Missense_MutationnovelA129T0.33
LGGchr5133088555Missense_MutationnovelQ379H0.24
LIHCchr5133065000Missense_MutationNAP43L0.15
LIHCchr51331045493'UTRnovel0.33
LIHCchr51331046733'UTRnovel0.57
LUADchr5133103865Nonsense_MutationnovelE720*0.14
LUADchr5133103963SilentnovelQ752Q0.08
LUADchr5133070479In_Frame_DelnovelD139_V142del0.14
LUADchr5133074095Missense_MutationNAS211F0.11
LUADchr5133067494Missense_MutationnovelE81D0.8
LUADchr5133101809Frame_Shift_DelnovelK697Nfs*60.33
LUADchr5133088466Missense_MutationNAV350L0.1
LUSCchr5133089118Missense_MutationNAP401S0.13
LUSCchr5133070388SilentNAE107E0.24
LUSCchr5133074014Missense_MutationNAY184C0.84
LUSCchr5133074058Missense_MutationnovelV199I0.5
LUSCchr51331044573'UTRnovel0.44
LUSCchr5133076772Missense_Mutationrs772742465R261H0.43
OVchr5133104246Missense_MutationnovelT778N0.2
PRADchr5133091295Missense_Mutationrs141758444S494N0.29
PRADchr5133089595Frame_Shift_DelnovelP427Lfs*20.31
PRADchr5133073279Missense_MutationnovelT160I0.48
PRADchr5133101878Missense_MutationnovelK719N0.18
READchr5133091262Missense_Mutationrs770551334R483Q0.2
READchr5133088418Missense_MutationNAD334N0.08
READchr5133076812Missense_MutationNAK274N0.42
READchr5133088485Missense_MutationnovelK356T0.37
READchr5133103967Missense_Mutationrs771075745K754E0.27
READchr5133076792Missense_Mutationrs199586152Q268E0.59
SKCMchr5133073232In_Frame_DelnovelP145_D150del0.07
SKCMchr5133065027Missense_MutationNAA52V0.1
SKCMchr5133074123SilentnovelL220L0.6
SKCMchr5133099572Missense_MutationNAE653K0.22
SKCMchr5133089611Missense_MutationNAL432F0.32
SKCMchr5133076770SilentNAI260I0.62
SKCMchr5133103980Missense_Mutationrs769795778T758I0.16
SKCMchr5133089611Missense_MutationNAL432F0.38
STADchr5133076796Missense_MutationnovelE269V0.13
STADchr5133104303Frame_Shift_DelNAN799Mfs*500.2
STADchr5133096203Missense_MutationNAL586V0.18
STADchr5133104303Frame_Shift_DelNAN799Mfs*500.27
STADchr5133096156Missense_MutationnovelA570E0.5
STADchr5133088455Missense_MutationNAR346Q0.25
STADchr5133092723Silentrs759663275E528E0.18
THCAchr5133065008Missense_MutationNAR46C0.04
THCAchr5133091368Nonsense_MutationnovelE518_E519ins*0.07
THCAchr5133074038In_Frame_DelnovelE193_K194del0.08
THYMchr5133096243Missense_MutationnovelE599A0.41
UCECchr5133074118Nonsense_MutationNAK219*0.29
UCECchr5133065012Missense_MutationNAS47L0.26
UCECchr5133088547Missense_MutationNAA377T0.25
UCECchr5133089069Silentrs764891442S384S0.32
UCECchr5133052269Missense_MutationNAD7Y0.31
UCECchr5133097212Missense_MutationnovelN619H0.3
UCECchr5133088455Missense_MutationNAR346Q0.43
UCECchr5133067434Missense_MutationnovelK61N0.44
UCECchr5133101761Splice_RegionnovelN680N0.33
UCECchr5133099653Splice_SitenovelX679_splice0.57
UCECchr5133088485Missense_MutationnovelK356T0.04
UCECchr5133076655Missense_MutationNAV222A0.3
UCECchr5133104310SilentNAN799N0.3
UCECchr5133104361Missense_MutationnovelQ816H0.16
UCECchr5133104396Missense_Mutationrs377082440S828L0.46
UCECchr5133052322SilentnovelE24E0.41
UCECchr5133089088Nonsense_MutationnovelE391*0.5
UCECchr5133074109Missense_MutationNAN216D0.37
UCECchr5133096221Nonsense_MutationNAE592*0.4
UCECchr51331111983'Flanknovel0.38
UCECchr5133091319Missense_MutationnovelK502T0.51
UCECchr5133073291Missense_MutationnovelG164D0.28
UCECchr5133104435Silentnovel*841*0.32
UCECchr5133096126Missense_MutationnovelK560T0.48
UCECchr5133096212Missense_MutationnovelI589V0.23
UCECchr51331112793'Flanknovel0.35
UCECchr5133096133SilentnovelD562D0.34
UCECchr5133070459Missense_MutationnovelS131I0.3
UCECchr5133104280Missense_MutationnovelK789N0.7
UCECchr5133104311Missense_MutationNAA800T0.32
UCECchr5133070396Missense_Mutationrs773711727R110Q0.43
UCECchr5133103895Missense_MutationnovelD730N0.32
UCECchr5133076677Silentrs751904979T229T0.24
UCECchr5133089574SilentnovelV419V0.32
UCECchr5133088455Missense_MutationNAR346Q0.47
UCECchr5133103906Missense_MutationnovelK733N0.45
UCECchr5133089593Missense_MutationNAA426S0.23
UCECchr5133076657Missense_MutationnovelL223M0.39
UCECchr5133088538Nonsense_MutationnovelR374*0.44
UCECchr5133091356SilentNAQ514Q0.5
UCECchr5133065032Missense_MutationNAS54R0.15
UCECchr5133074052Missense_MutationNAN197Y0.37
UCECchr5133076812Missense_MutationNAK274N0.24
UCECchr5133103934Missense_MutationnovelE743K0.34
UCECchr5133104344Missense_MutationNAD811Y0.11
UCECchr5133104396Missense_Mutationrs377082440S828L0.29
UCECchr5133067540Nonsense_MutationNAG97*0.3
UCECchr5133104303Frame_Shift_DelNAN799Mfs*500.27
UCECchr51330520155'UTRnovel0.54
UCSchr5133088415Nonsense_MutationnovelE333*0.46

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
KIRPDEL0.03820.11554
LAMLDEL0.0891.2971e-07
LUADDEL0.30817.4776e-05
LUSCDEL0.64470.002071
MESODEL0.14940.20184
PRADAMP0.02640.16448
STADDEL0.27892.8835e-08
THCAAMP0.03610.075436
THCADEL00.23456

Survival Analysis
CancerP-value Q-value
KIRC0.0058

Kaplan-Meier Survival Analysis

UCS0.007

Kaplan-Meier Survival Analysis

HNSC0.026

Kaplan-Meier Survival Analysis

SKCM0.0074

Kaplan-Meier Survival Analysis

KIRP0.0082

Kaplan-Meier Survival Analysis

LAML0.0097

Kaplan-Meier Survival Analysis

KICH0.012

Kaplan-Meier Survival Analysis

GBM0.029

Kaplan-Meier Survival Analysis

LIHC0.00055

Kaplan-Meier Survival Analysis

LGG0.0052

Kaplan-Meier Survival Analysis

LUAD0.0003

Kaplan-Meier Survival Analysis

UVM0.0074

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
  • Gene Ontology
Description
Ensembl ID
ENSG00000170606 (Gene tree)
Gene ID
3308
Gene Symbol
HSPA4
Alias
HS24/P52|HSPH2
Full Name
heat shock protein family A (Hsp70) member 4
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Plus strand
Length
54,488 bases
Position
chr5:133,051,962-133,106,449
Accession
5237
RBP type
non-canonical RBP
Summary
(Heat Shock Protein Family A (Hsp70) Member 4) is a Protein Coding gene. Diseases associated with HSPA4 include Ischemia and Transient Cerebral Ischemia. Among its related pathways are Mechanisms of CFTR activation by S-nitrosoglutathione (normal and CF) and Regulation of degradation of deltaF508 CFTR in CF. An important paralog of this gene is HSPA4L.
RNA binding proteome (RBPome)
PIDTitleMethod TimeAuthorDoi
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 RNAPolyT-RICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNARICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
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

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
11720291Analysis of sequence-specific binding of RNA to Hsp70 and its various homologs indicates the involvement of N- and C-terminal interactions.RNA2001 NovZimmer C-
7511613RNA/protein interactions in the 5'-untranslated leader of HSP70 mRNA in Drosophila lysates. Lack of evidence for specific protein binding.J Biol Chem1994 Apr 8Hess MA-
11581272Thermodynamics and kinetics of Hsp70 association with A + U-rich mRNA-destabilizing sequences.J Biol Chem2001 Nov 30Wilson GM-
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.
28679534Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions.J Biol Chem2017 Aug 25Kishor Adoi: 10.1074/jbc.M117.785394
31293389Combined Cyclosporin A and Hypothermia Treatment Inhibits Activation of BV-2 Microglia but Induces an Inflammatory Response in an Ischemia/Reperfusion Hippocampal Slice Culture Model.Front Cell Neurosci2019 Jun 25Wowro SJdoi: 10.3389/fncel.2019.00273
21732077Differential expression of the transcripts of Spartina alterniflora Loisel (smooth cordgrass) induced in response to petroleum hydrocarbon.Mol Biotechnol2012 MayRamanaRao MVdoi: 10.1007/s12033-011-9436-0.
26386576Expression of hsrOmega-RNAi transgene prior to heat shock specifically compromises accumulation of heat shock-induced Hsp70 in Drosophila melanogaster.Cell Stress Chaperones2016 JanSingh AKdoi: 10.1007/s12192-015-0644-6
10358092Mammalian Hsp70 and Hsp110 proteins bind to RNA motifs involved in mRNA stability.J Biol Chem1999 Jun 11Henics T-
25498946Leishmania braziliensis replication protein A subunit 1: molecular modelling, protein expression and analysis of its affinity for both DNA and RNA.Parasit Vectors2014 Dec 12Nocua PAdoi: 10.1186/s13071-014-0573-8.
9722628Specific binding of Drosophila nuclear protein PEP (protein on ecdysone puffs) to hsp70 DNA and RNA.Nucleic Acids Res1998 Sep 15Hamann S-
16563814RNA delivery by heat shock protein-70 into mammalian cells: a preliminary study.Cell Biol Int2006 MayHenics T-
16474124Proteomics analysis of the tombusvirus replicase: Hsp70 molecular chaperone is associated with the replicase and enhances viral RNA replication.J Virol2006 MarServa S-
11359930Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation.Mol Biol Cell2001 MayWaelter S-
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-
19165146Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA.EMBO J2009 Mar 4Katahira Jdoi: 10.1038/emboj.2009.5
18991684Post-transcriptional regulation of HSP70 expression following oxidative stress in SH-SY5Y cells: the potential involvement of the RNA-binding protein HuR.Curr Pharm Des2008Amadio M-
17913810Chaperones activate hepadnavirus reverse transcriptase by transiently exposing a C-proximal region in the terminal protein domain that contributes to epsilon RNA binding.J Virol2007 DecStahl M-
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-
22058113Ribosomal deficiencies in Diamond-Blackfan anemia impair translation of transcripts essential for differentiation of murine and human erythroblasts.Blood2012 Jan 5Horos Rdoi: 10.1182/blood-2011-06-358200
20965275Characterization of Hsp70 gene in Chironomus riparius: expression in response to endocrine disrupting pollutants as a marker of ecotoxicological stress.Comp Biochem Physiol C Toxicol Pharmacol2011 JanMorales Mdoi: 10.1016/j.cbpc.2010.10.003
11599570Characterization and regulation of the major histocompatibility complex-encoded proteins Hsp70-Hom and Hsp70-1/2.Cell Stress Chaperones2001 JulFourie AM-
24324328Estrogen receptor modulatory effects of germinated brown rice bioactives in the uterus of rats through the regulation of estrogen-induced genes.Drug Des Devel Ther2013 Dec 2Muhammad SIdoi: 10.2147/DDDT.S50861
15479789Nuclear heat shock response and novel nuclear domain 10 reorganization in respiratory syncytial virus-infected a549 cells identified by high-resolution two-dimensional gel electrophoresis.J Virol2004 NovBrasier AR-
2498651Cortisol alters gene expression during involution of the rat ventral prostate.Mol Endocrinol1989 AprRennie PS-
9015264Distinct stress-inducible and developmentally regulated heat shock transcription factors in Xenopus oocytes.Dev Biol1997 Jan 1Gordon S-
15735003p53CSV, a novel p53-inducible gene involved in the p53-dependent cell-survival pathway.Cancer Res2005 Feb 15Park WR-
19083193The role of HSP70 on ENPP1 expression and insulin-receptor activation.J Mol Med (Berl)2009 FebMarucci Adoi: 10.1007/s00109-008-0429-9
21763498Reciprocal regulation of human immunodeficiency virus-1 gene expression and replication by heat shock proteins 40 and 70.J Mol Biol2011 Jul 29Kumar Mdoi: 10.1016/j.jmb.2011.04.005.
21739554Label-free nondestructive discrimination of colon carcinoma sublines and biomolecular insights into their differential Hsp70 expression: DNA/RNA nucleobase specific changes.Chembiochem2011 Aug 16Donfack Pdoi: 10.1002/cbic.201000653
21390211Heat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo.PLoS One2011 Feb 24Li Gdoi: 10.1371/journal.pone.0016546.
25253355DnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activity.J Virol2014 DecCao Mdoi: 10.1128/JVI.02475-14
23667540N,N'-dinitrosopiperazine--mediated heat-shock protein 70-2 expression is involved in metastasis of nasopharyngeal carcinoma.PLoS One2013 May 7Peng Zdoi: 10.1371/journal.pone.0062908
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.
30975014Autophagy in Xenopus laevis rod photoreceptors is independently regulated by phototransduction and misfolded RHOP23H.Autophagy2019 Apr 12:1-20Wen RHdoi: 10.1080/15548627.2019.1596487
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000504328HSPA4-202552--- (aa)--
ENST00000514825HSPA4-203690--- (aa)--
ENST00000617074HSPA4-2052358-ENSP00000481686699 (aa)-A0A087WYC1
ENST00000304858HSPA4-2014825-ENSP00000302961840 (aa)-P34932
ENST00000615899HSPA4-2042204-ENSP00000478102475 (aa)-A0A087WTS8
Gene Model
Click here to download ENSG00000170606's gene model file
Pathways
Pathway IDPathway NameSource
hsa04530Tight junctionKEGG
hsa04612Antigen processing and presentationKEGG
Phenotypes
ensgIDTraitpValuePubmed ID
ENSG00000170606Blood Pressure3.2952171E-005-
GWAS
ensgIDSNPChromosomePositionSNP-risk TraitPubmedID95% CIOr or BEAT EFO ID
ENSG00000170606rs1471339675133091160GReticulocyte fraction of red cells27863252[0.024-0.048] unit increase0.03596435EFO_0007986
ENSG00000170606rs5711733995133106107?Heel bone mineral density30048462[0.019-0.029] unit decrease0.0242276EFO_0009270
ENSG00000170606rs728014455133053267CHeel bone mineral density30598549[0.015-0.024] unit decrease0.0196744EFO_0009270
ENSG00000170606rs557477515133061659ADiastolic blood pressure30224653[0.16-0.27] mmHg decrease0.2159EFO_0006336
ENSG00000170606rs1407672845133090504?Eosinophil counts30595370EFO_0004842
ENSG00000170606rs65961005133071366CBreast cancer29059683[1.04-1.09] (Oncoarray)1.0638298EFO_0000305
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000170606's network

* RBP PPI network refers to all genes directly bind to RBP
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0005515protein binding22990239.25416956.29568061.30021884.IPIFunction
GO:0005524ATP binding8335910.NASFunction
GO:0005634nucleus21873635.IBAComponent
GO:0005829cytosol21873635.IBAComponent
GO:0005829cytosol21231916.IDAComponent
GO:0006986response to unfolded protein8335910.NASProcess
GO:0045040protein import into mitochondrial outer membrane15644312.IDAProcess
GO:0051131chaperone-mediated protein complex assembly15644312.IDAProcess
GO:0070062extracellular exosome20458337.HDAComponent
GO:0070062extracellular exosome21276792.IDAComponent
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