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
15122791Reduction of double-stranded RNA-activated protein kinase in hepatocellular carcinoma associated with hepatitis B virus.J Med Virol2004 JunChen GG-
11991642The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR.RNA2002 AprBommer UA-
15607693A point mutation in the RNA-binding domain I results in decrease of PKR activation in acute lymphoblastic leukemia.Blood Cells Mol Dis2005 Jan-FebMurad JM-
16271080Expression of double-stranded RNA-activated protein kinase in small-size peripheral adenocarcinoma of the lung.Pathol Int2005 NovRoh MS-
19416861PKR, a p53 target gene, plays a crucial role in the tumor-suppressor function of p53.Proc Natl Acad Sci U S A2009 May 12Yoon CHdoi: 10.1073/pnas.0812148106
19106640Inhibition of RNA-dependent protein kinase (PKR) leads to cancer cell death and increases chemosensitivity.Cancer Biol Ther2009 FebPataer A-
18087277Increased expression of phosphorylated forms of RNA-dependent protein kinase and eukaryotic initiation factor 2alpha may signal skeletal muscle atrophy in weight-losing cancer patients.Br J Cancer2008 Jan 29Eley HL-
20930042Prognostic significance of RNA-dependent protein kinase on non-small cell lung cancer patients.Clin Cancer Res2010 Nov 15Pataer Adoi: 10.1158/1078-0432.CCR-10-0753
23682076Progesterone enhances calcitriol antitumor activity by upregulating vitamin D receptor expression and promoting apoptosis in endometrial cancer cells.Cancer Prev Res (Phila)2013 JulLee LRdoi: 10.1158/1940-6207.CAPR-12-0493
12483527Neoplastic progression in melanoma and colon cancer is associated with increased expression and activity of the interferon-inducible protein kinase, PKR.Oncogene2002 Dec 12Kim SH-
23370317Prognostic significance of combinations of RNA-dependent protein kinase and EphA2 biomarkers for NSCLC.J Thorac Oncol2013 MarGuo Cdoi: 10.1097/JTO.0b013e318282def7.
22102852The role of PKR/eIF2α signaling pathway in prognosis of non-small cell lung cancer.PLoS One2011He Ydoi: 10.1371/journal.pone.0024855
27203671Accumulation of RNA-dependent protein kinase (PKR) in the nuclei of lung cancer cells mediates radiation resistance.Oncotarget2016 Jun 21Hao Cdoi: 10.18632/oncotarget.9428.
29486283Musashi-1 promotes chemoresistant granule formation by PKR/eIF2α signalling cascade in refractory glioblastoma.Biochim Biophys Acta Mol Basis Dis2018 MayChen HYdoi: 10.1016/j.bbadis.2018.02.017
30275201Kisspeptin Inhibits Colorectal Cancer Cell Invasiveness by Activating PKR and PP2A.Anticancer Res2018 OctKim JNdoi: 10.21873/anticanres.12918.

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr237146920Missense_MutationnovelR58T0.11dsrm
BLCAchr237107333Missense_MutationnovelI532M0.31
BLCAchr237138346Missense_MutationnovelS204C0.16
BLCAchr237135513Missense_MutationnovelM252I0.13
BLCAchr237146876Missense_MutationNAE73Q0.28dsrm
BLCAchr237141680Missense_MutationnovelT88A0.29
BLCAchr237147773Missense_MutationNAE12Q0.11
BLCAchr237139657Nonsense_MutationnovelQ164*0.34
BLCAchr237139730SilentNAQ139Q0.19
BLCAchr237109198Nonsense_MutationnovelS492*0.24
BRCAchr237107321Missense_MutationNAL536F0.15
BRCAchr237114742Frame_Shift_DelnovelS456Afs*210.05
BRCAchr237122506Missense_MutationnovelR356M0.11
BRCAchr237146933Missense_MutationNAE54K0.24dsrm
CESCchr237135520In_Frame_InsnovelP250delinsQIFLT0.06
CESCchr237135521In_Frame_InsnovelL249_P250insI0.02
CESCchr237107353Nonsense_MutationnovelR526*0.05
CESCchr237138317Missense_MutationNAE214Q0.6
CESCchr2371071713'UTRnovel0.28
CESCchr237114775Nonsense_Mutationrs767957226R445*0.34
CESCchr237120057Missense_Mutationrs778283176E384K0.46
CESCchr237122568SilentnovelE335E0.05
CESCchr237149219Intronnovel0.44
CHOLchr237135510SilentnovelK253K0.12
COADchr237149050Intronnovel0.22
COADchr237137001Missense_MutationnovelN235I0.36
COADchr237109257Silentrs376530608Y472Y0.1
COADchr237120133Missense_MutationnovelK358N0.33
COADchr237146899Frame_Shift_DelNAN65Mfs*60.42dsrm
COADchr2371071563'UTRnovel0.4
COADchr237141573Silentrs140698756S123S0.36
COADchr2371478095'UTRnovel0.16
COADchr2371072713'UTRrs7580205870.14
COADchr237149050Intronnovel0.25
COADchr2371489765'UTRnovel0.19
GBMchr237146891Missense_MutationnovelA68S0.13dsrm
GBMchr237149257Intronnovel0.12
GBMchr237138536Missense_MutationnovelQ189L0.07
GBMchr237120084Missense_MutationnovelE375K0.23
GBMchr2371488845'UTRNA0.53
HNSCchr237120058Silentrs764479308G383G0.15
HNSCchr237141627Missense_MutationnovelI105M0.07
KIRCchr237139682Missense_MutationNAQ155H0.07
KIRCchr237120076Missense_MutationNAW377C0.4
KIRCchr237141569Frame_Shift_DelnovelV125Cfs*480.22
KIRCchr237135520In_Frame_InsnovelP250delinsQIFLT0.06
KIRCchr237135521In_Frame_InsnovelL249_P250insI0.05
KIRPchr237138568SilentNAS178S0.44
LIHCchr237122567Missense_MutationnovelT336A0.45
LIHCchr237122661Missense_MutationNAK304N0.55
LUADchr237141686Nonsense_MutationnovelL86Rfs*30.07
LUADchr237120137Missense_MutationNAS357L0.17
LUADchr237139635Missense_MutationnovelS171L0.09
LUADchr237122509Nonsense_MutationNAS355*0.12
LUADchr237138522Missense_MutationnovelV194L0.14
LUADchr2371489105'UTRnovel0.16
LUADchr237138309SilentnovelN216N0.1
LUSCchr237149163Intronnovel0.11
LUSCchr2371478155'UTRnovel0.15
LUSCchr2371489065'UTRnovel0.23
LUSCchr2371489995'UTRnovel0.26
LUSCchr237126318Silentrs757581996Y293Y0.2
LUSCchr237149096Intronnovel0.21
LUSCchr237147824Splice_Sitenovel0.07
OVchr2371069553'UTRnovel0.19
OVchr237126330Silentrs2302799D289D0.09
OVchr237147802Missense_MutationNAA2G0.41
OVchr237141581Nonsense_MutationnovelC121Kfs*30.03
OVchr237114826Missense_Mutationrs779693187V428I0.25
OVchr237126360Silentrs773100266G279G0.07
OVchr237120106Frame_Shift_InsnovelF368Pfs*120.04
PAADchr237138341Missense_MutationnovelG206C0.16
PAADchr237138280Missense_Mutationrs747731290S226L0.07
READchr237149178Intronnovel0.29
READchr237119982Missense_MutationnovelK409Q0.06
SKCMchr237107276SilentNAC551C0.39
SKCMchr237146895Silentrs180726204A66A0.26
SKCMchr237146896Missense_MutationnovelA66V0.24dsrm
SKCMchr237120043Frame_Shift_DelnovelK388Sfs*80.36
SKCMchr237138560Missense_MutationNAS181F0.22
SKCMchr237139677Missense_MutationNAA157V0.22
SKCMchr2371489965'UTRnovel0.19
SKCMchr237126360Silentrs773100266G279G0.14
SKCMchr237135535Missense_MutationNAP245L0.47
SKCMchr237147706Missense_MutationNAG34E0.21dsrm
SKCMchr237107493Frame_Shift_DelnovelD505Yfs*30.34
SKCMchr2371072073'UTRnovel0.44
SKCMchr237135528SilentnovelF247F0.49
SKCMchr237149048Intronnovel0.14
STADchr237149050Intronnovel0.22
STADchr237107287Nonsense_Mutationrs191011347R548*0.22
STADchr237149172Intronnovel0.17
STADchr237122658Silentrs771182529A305A0.23
STADchr2371489715'UTRnovel0.06
STADchr237149050Intronnovel0.38
STADchr237138285Missense_MutationNAS224R0.15
STADchr237136997SilentNAQ236Q0.26
STADchr237120117Missense_MutationNAI364V0.37
STADchr237135509Missense_Mutationrs758776026E254K0.23
STADchr237149050Intronnovel0.19
STADchr237149050Intronnovel0.36
STADchr237119993Missense_Mutationrs765483661I405T0.09
STADchr237149050Intronnovel0.38
STADchr237126409Missense_MutationNAF263S0.25
UCECchr237141667Missense_Mutationrs184007282S92Y0.22
UCECchr237126307Missense_Mutationrs746043207R297H0.48
UCECchr237146942Nonsense_MutationNAE51*0.38dsrm
UCECchr237149155Intronnovel0.36
UCECchr2371489325'UTRnovel0.31
UCECchr237107476Nonsense_MutationNAE511*0.4
UCECchr237139726Nonsense_MutationnovelE141*0.03
UCECchr237126307Missense_Mutationrs746043207R297H0.36
UCECchr237149049Intronnovel0.51
UCECchr237138307Missense_Mutationrs372927806S217Y0.32
UCECchr237109265Missense_MutationNAD470Y0.22
UCECchr2371489265'UTRnovel0.1
UCECchr237120133Missense_MutationNAK358N0.09
UCECchr237126307Missense_Mutationrs746043207R297H0.27
UCECchr237149105Intronnovel0.12
UCECchr237138533Missense_MutationnovelS190N0.15
UCECchr237149049Intronnovel0.35
UCECchr237114814Missense_MutationnovelD432Y0.26
UCECchr237146894Missense_Mutationrs367990775A67T0.36dsrm
UCECchr237141672Silentrs376000248T90T0.38
UCECchr2371490085'UTRnovel0.07
UCECchr237141672Silentrs376000248T90T0.53
UCECchr237149050Intronnovel0.21
UCECchr237120076Nonsense_MutationnovelW377*0.4
UCECchr237109257Silentrs376530608Y472Y0.35
UCECchr237141609Missense_MutationNAK111N0.37
UCECchr2371489855'UTRnovel0.4
UCECchr237139663Missense_MutationnovelY162H0.13
UCECchr237126392Nonsense_MutationnovelE269*0.48
UCECchr237107287Nonsense_Mutationrs191011347R548*0.34
UCECchr2371489855'UTRnovel0.34
UCECchr2371072713'UTRnovel0.24
UCECchr237138583Splice_RegionnovelK173K0.46
UCECchr237107506Missense_MutationNAG501C0.18
UCECchr237120124SilentNAC361C0.34
UCECchr237138549Missense_Mutationrs768969031T185A0.26
UCECchr237141672Silentrs376000248T90T0.51
UCECchr237139726Nonsense_MutationnovelE141*0.39
UCECchr237109250Missense_MutationnovelG475R0.15
UCECchr237114814Missense_MutationnovelD432Y0.49
UCECchr237114853Missense_MutationnovelN419H0.15
UCECchr237109256Missense_Mutationrs747429747A473T0.32
UCECchr237139722Missense_Mutationrs760178328Y142C0.44
UCECchr237147740Missense_MutationNAV23I0.32dsrm
UCECchr237149105Intronnovel0.38
UCECchr237107297Missense_MutationnovelE544D0.28
UCSchr237146942Nonsense_MutationNAE51*0.25dsrm
UVMchr237122654Missense_MutationNAR307C0.43

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
CESCAMP0.22370.099937
KIRPDEL0.02430.08832
PAADDEL0.08150.2014
PRADDEL0.05890.096106
TGCTAMP0.240.0050216

Survival Analysis
CancerP-value Q-value
KIRC0.011

Kaplan-Meier Survival Analysis

ACC0.00047

Kaplan-Meier Survival Analysis

SKCM0.00057

Kaplan-Meier Survival Analysis

BRCA0.038

Kaplan-Meier Survival Analysis

KIRP0.018

Kaplan-Meier Survival Analysis

PAAD0.0015

Kaplan-Meier Survival Analysis

KICH0.017

Kaplan-Meier Survival Analysis

UCEC0.0013

Kaplan-Meier Survival Analysis

LIHC0.017

Kaplan-Meier Survival Analysis

LGG0.00013

Kaplan-Meier Survival Analysis

OV0.037

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742

  • Description
  • RBDs
  • RBPome
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • Pathways
  • Phenotypes
  • GWAS
  • PPI
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000055332 (Gene tree)
Gene ID
5610
Gene Symbol
EIF2AK2
Alias
PKR|EIF2AK1|PPP1R83|PRKR
Full Name
eukaryotic translation initiation factor 2 alpha kinase 2
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
57,856 bases
Position
chr2:37,099,210-37,157,065
Accession
9437
RBP type
canonical RBP
Summary
The protein encoded by this gene is a serine/threonine protein kinase that is activated by autophosphorylation after binding to dsRNA. The activated form of the encoded protein can phosphorylate translation initiation factor EIF2S1, which in turn inhibits protein synthesis. This protein is also activated by manganese ions and heparin. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Oct 2011]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000385014dsrmPF00035.262.3e-2712
ENSP00000385014dsrmPF00035.262.3e-2722
ENSP00000233057dsrmPF00035.268.5e-2712
ENSP00000233057dsrmPF00035.268.5e-2722
ENSP00000378559dsrmPF00035.268.5e-2712
ENSP00000378559dsrmPF00035.268.5e-2722
ENSP00000393921dsrmPF00035.264.8e-1811
ENSP00000374663dsrmPF00035.268.5e-1511
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
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & HEK2932018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
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
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
8806538The RNA-binding and effector domains of the viral NS1 protein are conserved to different extents among influenza A and B viruses.Virology1996 Sep 1Wang W-
18366743The evolution of core proteins involved in microRNA biogenesis.BMC Evol Biol2008 Mar 25Murphy Ddoi: 10.1186/1471-2148-8-92.
9034343Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR.EMBO J1997 Feb 3Benkirane M-
8226967A cAMP-regulated RNA-binding protein that interacts with phosphoenolpyruvate carboxykinase (GTP) mRNA.J Biol Chem1993 Nov 15Nachaliel N-
7971266Structural features of adenovirus 2 virus-associated RNA required for binding to the protein kinase DAI.Nucleic Acids Res1994 Oct 25Clarke PA-
12210987Selection of small-molecule mediators of the RNA regulation of PKR, the RNA-dependent protein kinase.Chembiochem2002 Sep 2Carlson CB-
25630541Dissecting the roles of TRBP and PACT in double-stranded RNA recognition and processing of noncoding RNAs.Wiley Interdiscip Rev RNA2015 May-JunHeyam Adoi: 10.1002/wrna.1272
24954387'Black sheep' that don't leave the double-stranded RNA-binding domain fold.Trends Biochem Sci2014 JulGleghorn MLdoi: 10.1016/j.tibs.2014.05.003
7530396Mechanism of interferon action: RNA-binding activity of full-length and R-domain forms of the RNA-dependent protein kinase PKR--determination of KD values for VAI and TAR RNAs.Virology1995 Jan 10McCormack SJ-
9400613Interaction of the human protein kinase PKR with the mouse PKR homolog occurs via the N-terminal region of PKR and does not inactivate autophosphorylation activity of mouse PKR.Virology1997 Nov 24Rende-Fournier R-
23776147Processing of virus-derived cytoplasmic primary-microRNAs.Wiley Interdiscip Rev RNA2013 Jul-AugShapiro JSdoi: 10.1002/wrna.1169
9150867The regulation of the protein kinase PKR by RNA.Biochimie1996Robertson HD-
15070037Characterization of the chicken PKR: polymorphism of the gene and antiviral activity against vesicular stomatitis virus.Jpn J Vet Res2004 FebKo JH-
19232355Analysis of PKR structure by small-angle scattering.J Mol Biol2009 Apr 10VanOudenhove Jdoi: 10.1016/j.jmb.2009.02.019
23661684Differential roles of human Dicer-binding proteins TRBP and PACT in small RNA processing.Nucleic Acids Res2013 JulLee HYdoi: 10.1093/nar/gkt361
23531496Multiple sensors ensure guide strand selection in human RNAi pathways.RNA2013 MayNoland CLdoi: 10.1261/rna.037424.112
28611419Interaction of PKR with single-stranded RNA.Sci Rep2017 Jun 13Mayo CBdoi: 10.1038/s41598-017-03047-7.
1350676The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase.Proc Natl Acad Sci U S A1992 Jun 1Chang HW-
1364113Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI.Genes Dev1992 DecGreen SR-
9162083Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2.J Biol Chem1997 May 30Zhu S-
8756460Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR.Biochemistry1996 Aug 6Bevilacqua PC-
7776374Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR).J Mol Biol1995 May 26Schmedt C-
11967345RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA.J Virol2002 MayVende P-
11070079Chimeric double-stranded RNA-specific adenosine deaminase ADAR1 proteins reveal functional selectivity of double-stranded RNA-binding domains from ADAR1 and protein kinase PKR.Proc Natl Acad Sci U S A2000 Nov 7Liu Y-
16861808A new double-stranded RNA binding protein (DRBP-120) is associated with double-stranded RNA-activated protein kinase (PKR).Biosci Biotechnol Biochem2006 JulWatanabe S-
19569061Intracellular small interfering RNA delivery using genetically engineered double-stranded RNA binding protein domain.J Gene Med2009 SepKim Jdoi: 10.1002/jgm.1365.
19458189Hsp90 regulates the function of argonaute 2 and its recruitment to stress granules and P-bodies.Mol Biol Cell2009 JulPare JMdoi: 10.1091/mbc.E09-01-0082
18312693Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications.BMC Biol2008 Mar 3Rothenburg Sdoi: 10.1186/1741-7007-6-12.
20863128Minor-groove-modulating adenosine replacements control protein binding and RNAi activity in siRNAs.ACS Chem Biol2010 Dec 17Peacock Hdoi: 10.1021/cb100245u
23140277Specificity of the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR for double-stranded RNA: insights from thermodynamics and small-angle X-ray scattering.Biochemistry2012 Nov 20Patel Sdoi: 10.1021/bi300935p
30685091nc886, a non-coding RNA, inhibits UVB-induced MMP-9 and COX-2 expression via the PKR pathway in human keratinocytes.Biochem Biophys Res Commun2019 May 14Lee KSdoi: 10.1016/j.bbrc.2019.01.068
16466763Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA.Virology2006 May 25Li S-
7539103Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation.Mol Cell Biol1995 JunBarber GN-
7505074Mechanism of interferon action motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity.Virology1994 JanMcCormack SJ-
7514679Products of the porcine group C rotavirus NSP3 gene bind specifically to double-stranded RNA and inhibit activation of the interferon-induced protein kinase PKR.J Virol1994 JunLangland JO-
1351683Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase.Proc Natl Acad Sci U S A1992 Jun 15Feng GS-
9085850Surprising specificity of PKR binding to delta agent genomic RNA.RNA1997 AprCircle DA-
8810342Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties.J Biol Chem1996 Oct 11Patel RC-
8661426Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase.Virology1996 Jul 1George CX-
10320367Nuclear factor-90 of activated T-cells: A double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR.Biochemistry1999 May 11Langland JO-
7628456NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.EMBO J1995 Jul 17Bycroft M-
16580685Uncoupling of RNA binding and PKR kinase activation by viral inhibitor RNAs.J Mol Biol2006 May 19McKenna SA-
12414939Characterization of RNA determinants recognized by the arginine- and proline-rich region of Us11, a herpes simplex virus type 1-encoded double-stranded RNA binding protein that prevents PKR activation.J Virol2002 DecKhoo D-
11861913The 3'-untranslated regions of cytoskeletal muscle mRNAs inhibit translation by activating the double-stranded RNA-dependent protein kinase PKR.Nucleic Acids Res2002 Mar 1Nussbaum JM-
11447114Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.EMBO J2001 Jul 16Ung TL-
11468270Double-stranded RNA-dependent protein kinase, PKR, binds preferentially to Huntington's disease (HD) transcripts and is activated in HD tissue.Hum Mol Genet2001 Jul 15Peel AL-
11114159Straightening of bulged RNA by the double-stranded RNA-binding domain from the protein kinase PKR.Proc Natl Acad Sci U S A2000 Dec 19Zheng X-
10756189Site-specific modification and RNA crosslinking of the RNA-binding domain of PKR.Nucleic Acids Res2000 May 1Spanggord RJ-
16299777Methyl dynamics for understanding hydrophobic core packing of dynamically different motifs of double-stranded RNA binding domain of protein kinase R.Proteins2006 Feb 1Barnwal RP-
16250880Activation of the RNA-dependent protein kinase (PKR) of lymphocytes by regulatory RNAs: implications for immunomodulation in HIV infection.Curr HIV Res2005 OctWatanabe MA-
16877044siRNA and isRNA: two edges of one sword.Mol Ther2006 OctSchlee M-
15043926Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium.Biophys Chem2004 Mar 1Ucci JW-
19467267Translational insensitivity to potent activation of PKR by HCV IRES RNA.Antiviral Res2009 SepShimoike Tdoi: 10.1016/j.antiviral.2009.05.004
17913645Biophysical and biochemical investigations of dsRNA-activated kinase PKR.Methods Enzymol2007McKenna SA-
23329698Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR.RNA2013 MarDzananovic Edoi: 10.1261/rna.035931.112
21937648The cellular TAR RNA binding protein, TRBP, promotes HIV-1 replication primarily by inhibiting the activation of double-stranded RNA-dependent kinase PKR.J Virol2011 DecSanghvi VRdoi: 10.1128/JVI.05240-11
23251028ATP-independent diffusion of double-stranded RNA binding proteins.Proc Natl Acad Sci U S A2013 Jan 2Koh HRdoi: 10.1073/pnas.1212917110
20478537Protein kinase R contributes to immunity against specific viruses by regulating interferon mRNA integrity.Cell Host Microbe2010 May 20Schulz Odoi: 10.1016/j.chom.2010.04.007.
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27011290Bacterial Riboswitches and Ribozymes Potently Activate the Human Innate Immune Sensor PKR.ACS Chem Biol2016 Apr 15Hull CMdoi: 10.1021/acschembio.6b00081
27826097Oxidative stress drives CD8+ T-cell skin trafficking in patients with vitiligo through CXCL16 upregulation by activating the unfolded protein response in keratinocytes.J Allergy Clin Immunol2017 JulLi Sdoi: 10.1016/j.jaci.2016.10.013
26335380Endoplasmic reticulum (ER) stress protein responses in relation to spatio-temporal dynamics of astroglial responses to status epilepticus in rats.Neuroscience2015 Oct 29Ko ARdoi: 10.1016/j.neuroscience.2015.08.061
26061044The Tumor Suppressive Effects of HPP1 Are Mediated Through JAK-STAT-Interferon Signaling Pathways.DNA Cell Biol2015 AugHernandez JMdoi: 10.1089/dna.2014.2730
26083833COPII-Dependent ER Export: A Critical Component of Insulin Biogenesis and β-Cell ER Homeostasis.Mol Endocrinol2015 AugFang Jdoi: 10.1210/me.2015-1012
28445962PSMA-homing dsRNA chimeric protein vector kills prostate cancer cells and activates anti-tumor bystander responses.Oncotarget2017 Apr 11Langut Ydoi: 10.18632/oncotarget.15733.
28882789Litopenaeus vannamei activating transcription factor 6 alpha gene involvement in ER-stress response and white spot symptom virus infection.Fish Shellfish Immunol2017 NovYuan Kdoi: 10.1016/j.fsi.2017.09.013
29395325Human ADAR1 Prevents Endogenous RNA from Triggering Translational Shutdown.Cell2018 Feb 8Chung Hdoi: 10.1016/j.cell.2017.12.038
30209174Human Host Range Restriction of the Vaccinia Virus C7/K1 Double Deletion Mutant Is Mediated by an Atypical Mode of Translation Inhibition.J Virol2018 Nov 12Sivan Gdoi: 10.1128/JVI.01329-18
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30981813The metastasis suppressor, NDRG1, differentially modulates the endoplasmic reticulum stress response.Biochim Biophys Acta Mol Basis Dis2019 Sep 1Merlot AMdoi: 10.1016/j.bbadis.2019.04.007
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000390013EIF2AK2-202564-ENSP00000374663102 (aa)-F8WBH4
ENST00000395127EIF2AK2-2034343-ENSP00000378559551 (aa)-P19525
ENST00000411537EIF2AK2-205623-ENSP00000393921141 (aa)-C9JZT2
ENST00000233057EIF2AK2-20110042XM_011532987ENSP00000233057551 (aa)XP_011531289P19525
ENST00000647926EIF2AK2-2082235-ENSP00000497534551 (aa)-UPI000000D925
ENST00000405334EIF2AK2-2041533-ENSP00000385014510 (aa)-P19525
ENST00000462861EIF2AK2-206411--- (aa)--
ENST00000496059EIF2AK2-207845--- (aa)--
Gene Model
Click here to download ENSG00000055332's gene model file
Pathways
Pathway IDPathway NameSource
hsa04141Protein processing in endoplasmic reticulumKEGG
hsa04217NecroptosisKEGG
hsa05160Hepatitis CKEGG
hsa05162MeaslesKEGG
hsa05164Influenza AKEGG
hsa05165Human papillomavirus infectionKEGG
hsa05167Kaposi sarcoma-associated herpesvirus infectionKEGG
hsa05168Herpes simplex virus 1 infectionKEGG
hsa05169Epstein-Barr virus infectionKEGG
hsa05203Viral carcinogenesisKEGG
Phenotypes
ensgIDTraitpValuePubmed ID
ENSG00000055332Nutritional and Metabolic Diseases9.1250000E-005-
ENSG00000055332Smoking9.5400000E-006-
ENSG00000055332Glucose2E-625524916
ENSG00000055332Insulin Resistance2E-625524916
GWAS
ensgIDSNPChromosomePositionSNP-risk TraitPubmedID95% CIOr or BEAT EFO ID
ENSG00000055332rs4233921237127006?Glucose homeostasis traits25524916[-0.0172-0.2572] unit decrease0.12EFO_0004471|EFO_0006896
ENSG00000055332rs2254958237149148?Adolescent idiopathic scoliosis30019117EFO_0005423
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000055332's network

* RBP PPI network refers to all genes directly bind to RBP
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000055332EIF2AK29936.471ENSAPOG00000010686-9835.260Acanthochromis_polyacanthus
ENSG00000055332EIF2AK210059.857ENSAMEG00000017552EIF2AK210060.036Ailuropoda_melanoleuca
ENSG00000055332EIF2AK29742.857ENSAOCG00000003368-9636.932Amphiprion_ocellaris
ENSG00000055332EIF2AK29939.130ENSAOCG00000003388-9138.086Amphiprion_ocellaris
ENSG00000055332EIF2AK29640.580ENSAPEG00000023903-9933.333Amphiprion_percula
ENSG00000055332EIF2AK29740.449ENSAPEG00000023919-9737.640Amphiprion_percula
ENSG00000055332EIF2AK29840.541ENSACAG00000008379EIF2AK29840.541Anolis_carolinensis
ENSG00000055332EIF2AK29971.532ENSANAG00000035319EIF2AK210071.532Aotus_nancymaae
ENSG00000055332EIF2AK29635.220ENSACLG00000023699-9538.699Astatotilapia_calliptera
ENSG00000055332EIF2AK29543.478ENSACLG00000023938-9634.161Astatotilapia_calliptera
ENSG00000055332EIF2AK210062.162ENSBTAG00000008703EIF2AK210061.441Bos_taurus
ENSG00000055332EIF2AK210088.652ENSCJAG00000003819EIF2AK29984.574Callithrix_jacchus
ENSG00000055332EIF2AK210061.905ENSCAFG00000006051EIF2AK29961.483Canis_familiaris
ENSG00000055332EIF2AK210061.905ENSCAFG00020022842EIF2AK29961.483Canis_lupus_dingo
ENSG00000055332EIF2AK210061.151ENSCHIG00000016319EIF2AK210060.612Capra_hircus
ENSG00000055332EIF2AK210066.667ENSTSYG00000013328EIF2AK29961.444Carlito_syrichta
ENSG00000055332EIF2AK29948.288ENSCAPG00000016388-9948.649Cavia_aperea
ENSG00000055332EIF2AK210054.902ENSCPOG00000012198EIF2AK29953.273Cavia_porcellus
ENSG00000055332EIF2AK210084.397ENSCCAG00000037822EIF2AK29979.348Cebus_capucinus
ENSG00000055332EIF2AK210082.979ENSCATG00000036727EIF2AK210082.033Cercocebus_atys
ENSG00000055332EIF2AK28360.000ENSCLAG00000008409-9959.348Chinchilla_lanigera
ENSG00000055332EIF2AK210083.122ENSCSAG00000012135EIF2AK29983.122Chlorocebus_sabaeus
ENSG00000055332EIF2AK210067.647ENSCHOG00000004388-8862.222Choloepus_hoffmanni
ENSG00000055332EIF2AK210061.765ENSCGRG00001021739eIF2aK29959.420Cricetulus_griseus_chok1gshd
ENSG00000055332EIF2AK210061.765ENSCGRG00000015847Eif2ak29961.047Cricetulus_griseus_crigri
ENSG00000055332EIF2AK210065.714ENSDNOG00000010498EIF2AK210059.503Dasypus_novemcinctus
ENSG00000055332EIF2AK210064.706ENSDORG00000009488Eif2ak29464.014Dipodomys_ordii
ENSG00000055332EIF2AK29766.667ENSETEG00000009782-8859.701Echinops_telfairi
ENSG00000055332EIF2AK210065.686ENSEASG00005007360EIF2AK29760.108Equus_asinus_asinus
ENSG00000055332EIF2AK210066.667ENSECAG00000011726EIF2AK29761.636Equus_caballus
ENSG00000055332EIF2AK25849.843ENSEEUG00000005539-6049.843Erinaceus_europaeus
ENSG00000055332EIF2AK210065.972ENSFCAG00000006339EIF2AK210063.964Felis_catus
ENSG00000055332EIF2AK29337.687ENSFALG00000011889EIF2AK29436.313Ficedula_albicollis
ENSG00000055332EIF2AK28457.940ENSFDAG00000006052-9957.759Fukomys_damarensis
ENSG00000055332EIF2AK29836.519ENSGALG00000010560EIF2AK29837.696Gallus_gallus
ENSG00000055332EIF2AK29542.857ENSGAFG00000005269-9345.833Gambusia_affinis
ENSG00000055332EIF2AK29840.598ENSGAGG00000002104EIF2AK29840.105Gopherus_agassizii
ENSG00000055332EIF2AK210098.582ENSGGOG00000005556EIF2AK210098.548Gorilla_gorilla
ENSG00000055332EIF2AK210058.696ENSHGLG00000013093EIF2AK210058.333Heterocephalus_glaber_female
ENSG00000055332EIF2AK210058.514ENSHGLG00100005051EIF2AK210058.152Heterocephalus_glaber_male
ENSG00000055332EIF2AK210072.549ENSSTOG00000013886EIF2AK29962.319Ictidomys_tridecemlineatus
ENSG00000055332EIF2AK29663.265ENSJJAG00000015000-9947.740Jaculus_jaculus
ENSG00000055332EIF2AK29837.681ENSKMAG00000008407-9835.754Kryptolebias_marmoratus
ENSG00000055332EIF2AK29532.215ENSLOCG00000015909-9834.466Lepisosteus_oculatus
ENSG00000055332EIF2AK210067.647ENSLAFG00000018604EIF2AK210061.290Loxodonta_africana
ENSG00000055332EIF2AK210081.560ENSMFAG00000030576EIF2AK29980.747Macaca_fascicularis
ENSG00000055332EIF2AK210081.560ENSMMUG00000037522EIF2AK210079.533Macaca_mulatta
ENSG00000055332EIF2AK210082.270ENSMNEG00000040090EIF2AK210071.143Macaca_nemestrina
ENSG00000055332EIF2AK210082.979ENSMLEG00000033494EIF2AK210079.317Mandrillus_leucophaeus
ENSG00000055332EIF2AK29643.478ENSMZEG00005009747-7334.553Maylandia_zebra
ENSG00000055332EIF2AK29837.961ENSMGAG00000011175EIF2AK29838.772Meleagris_gallopavo
ENSG00000055332EIF2AK29958.770ENSMAUG00000000309Eif2ak29958.770Mesocricetus_auratus
ENSG00000055332EIF2AK210067.647ENSMICG00000003317EIF2AK29267.904Microcebus_murinus
ENSG00000055332EIF2AK210054.902ENSMOCG00000021613-9952.907Microtus_ochrogaster
ENSG00000055332EIF2AK29944.615ENSMMOG00000000659-9536.219Mola_mola
ENSG00000055332EIF2AK210045.098ENSMODG00000015286-9845.902Monodelphis_domestica
ENSG00000055332EIF2AK210062.136MGP_CAROLIEiJ_G0021889Eif2ak210051.268Mus_caroli
ENSG00000055332EIF2AK210059.804ENSMUSG00000024079Eif2ak210057.866Mus_musculus
ENSG00000055332EIF2AK210060.784MGP_PahariEiJ_G0020877Eif2ak210057.451Mus_pahari
ENSG00000055332EIF2AK210059.804MGP_SPRETEiJ_G0022803Eif2ak210057.324Mus_spretus
ENSG00000055332EIF2AK29465.714ENSMPUG00000009893EIF2AK29960.348Mustela_putorius_furo
ENSG00000055332EIF2AK210058.451ENSMLUG00000003513-9957.014Myotis_lucifugus
ENSG00000055332EIF2AK28548.941ENSMLUG00000030615-10050.212Myotis_lucifugus
ENSG00000055332EIF2AK210067.647ENSNGAG00000017501Eif2ak210061.302Nannospalax_galili
ENSG00000055332EIF2AK29437.662ENSNBRG00000019369-9635.227Neolamprologus_brichardi
ENSG00000055332EIF2AK210091.489ENSNLEG00000016201EIF2AK29991.552Nomascus_leucogenys
ENSG00000055332EIF2AK29364.211ENSOPRG00000008168-8754.094Ochotona_princeps
ENSG00000055332EIF2AK29545.387ENSOANG00000003939-9744.946Ornithorhynchus_anatinus
ENSG00000055332EIF2AK210074.510ENSOCUG00000007223EIF2AK29966.546Oryctolagus_cuniculus
ENSG00000055332EIF2AK210071.034ENSOGAG00000002562EIF2AK210069.065Otolemur_garnettii
ENSG00000055332EIF2AK210060.179ENSOARG00000009740EIF2AK210059.643Ovis_aries
ENSG00000055332EIF2AK210098.582ENSPPAG00000034727EIF2AK210098.551Pan_paniscus
ENSG00000055332EIF2AK210065.278ENSPPRG00000003287EIF2AK210063.964Panthera_pardus
ENSG00000055332EIF2AK210065.972ENSPTIG00000018329EIF2AK210063.964Panthera_tigris_altaica
ENSG00000055332EIF2AK210098.582ENSPTRG00000011834EIF2AK210098.551Pan_troglodytes
ENSG00000055332EIF2AK210082.979ENSPANG00000004770EIF2AK210082.157Papio_anubis
ENSG00000055332EIF2AK29642.315ENSPSIG00000018049EIF2AK29742.780Pelodiscus_sinensis
ENSG00000055332EIF2AK210061.765ENSPEMG00000010269Eif2ak210054.130Peromyscus_maniculatus_bairdii
ENSG00000055332EIF2AK29946.004ENSPCIG00000010984-9946.004Phascolarctos_cinereus
ENSG00000055332EIF2AK29739.130ENSPLAG00000023907-9634.043Poecilia_latipinna
ENSG00000055332EIF2AK29541.935ENSPREG00000007871-9641.935Poecilia_reticulata
ENSG00000055332EIF2AK210095.745ENSPPYG00000012493EIF2AK210091.016Pongo_abelii
ENSG00000055332EIF2AK29565.992ENSPCAG00000013068EIF2AK28865.992Procavia_capensis
ENSG00000055332EIF2AK210071.631ENSPCOG00000014117EIF2AK29968.603Propithecus_coquereli
ENSG00000055332EIF2AK210066.667ENSPVAG00000013831EIF2AK210061.844Pteropus_vampyrus
ENSG00000055332EIF2AK210059.804ENSRNOG00000048315Eif2ak210057.554Rattus_norvegicus
ENSG00000055332EIF2AK210084.397ENSRBIG00000034494EIF2AK29985.193Rhinopithecus_bieti
ENSG00000055332EIF2AK210085.481ENSRROG00000040152EIF2AK210085.481Rhinopithecus_roxellana
ENSG00000055332EIF2AK210082.270ENSSBOG00000026743EIF2AK210080.978Saimiri_boliviensis_boliviensis
ENSG00000055332EIF2AK29947.143ENSSHAG00000001447-9947.857Sarcophilus_harrisii
ENSG00000055332EIF2AK29936.932ENSSFOG00015008993-9836.932Scleropages_formosus
ENSG00000055332EIF2AK29636.864ENSSMAG00000010248-9136.730Scophthalmus_maximus
ENSG00000055332EIF2AK29736.872ENSSDUG00000002941-9436.872Seriola_dumerili
ENSG00000055332EIF2AK29634.104ENSSPAG00000007546-9634.104Stegastes_partitus
ENSG00000055332EIF2AK28642.925ENSSPAG00000007673-8335.811Stegastes_partitus
ENSG00000055332EIF2AK210061.413ENSSSCG00000008496-10061.483Sus_scrofa
ENSG00000055332EIF2AK210058.824ENSSSCG00000039055-7556.693Sus_scrofa
ENSG00000055332EIF2AK29637.251ENSTGUG00000008788EIF2AK29736.661Taeniopygia_guttata
ENSG00000055332EIF2AK29633.153ENSTRUG00000002791-9733.153Takifugu_rubripes
ENSG00000055332EIF2AK28939.231ENSTNIG00000000327-10037.219Tetraodon_nigroviridis
ENSG00000055332EIF2AK210060.284ENSTBEG00000014601-8263.402Tupaia_belangeri
ENSG00000055332EIF2AK210064.324ENSTTRG00000006882EIF2AK210064.324Tursiops_truncatus
ENSG00000055332EIF2AK28555.368ENSUAMG00000015141-9955.368Ursus_americanus
ENSG00000055332EIF2AK210059.712ENSUMAG00000014765EIF2AK210059.712Ursus_maritimus
ENSG00000055332EIF2AK29962.681ENSVPAG00000003303EIF2AK29962.749Vicugna_pacos
ENSG00000055332EIF2AK210063.107ENSVVUG00000018911EIF2AK210061.011Vulpes_vulpes
ENSG00000055332EIF2AK29133.455ENSXETG00000025302eif2ak29833.635Xenopus_tropicalis
ENSG00000055332EIF2AK29544.737ENSXCOG00000006974-9444.737Xiphophorus_couchianus
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0000186activation of MAPKK activity15229216.IMPProcess
GO:0001819positive regulation of cytokine production-ISSProcess
GO:0003723RNA binding22681889.HDAFunction
GO:0003725double-stranded RNA binding21266579.IDAFunction
GO:0004672protein kinase activity21873635.IBAFunction
GO:0004672protein kinase activity12882984.15229216.18835251.IDAFunction
GO:0004672protein kinase activity21123651.IMPFunction
GO:0004674protein serine/threonine kinase activity1695551.TASFunction
GO:0004694eukaryotic translation initiation factor 2alpha kinase activity21873635.IBAFunction
GO:0004694eukaryotic translation initiation factor 2alpha kinase activity25329545.IMPFunction
GO:0004715non-membrane spanning protein tyrosine kinase activity-IEAFunction
GO:0005515protein binding8576172.9143277.9431994.10390359.10488152.11160738.11773402.11836380.12610133.12882984.15121867.15229216.16288713.16785445.16957780.18096616.18362360.18835251.18971339.20395957.21903422.22801494.23455922.IPIFunction
GO:0005524ATP binding-IEAFunction
GO:0005634nucleus-IEAComponent
GO:0005737cytoplasm15121867.IDAComponent
GO:0005829cytosol-IDAComponent
GO:0005829cytosol-TASComponent
GO:0005840ribosome10390359.TASComponent
GO:0006412translation-IEAProcess
GO:0006468protein phosphorylation19189853.IDAProcess
GO:0008285negative regulation of cell proliferation1351683.TASProcess
GO:0009615response to virus19189853.IMPProcess
GO:0009636response to toxic substance-IEAProcess
GO:0010998regulation of translational initiation by eIF2 alpha phosphorylation-IEAProcess
GO:0016020membrane19946888.HDAComponent
GO:0017148negative regulation of translation12882984.IDAProcess
GO:0017148negative regulation of translation12610133.19189853.IMPProcess
GO:0018108peptidyl-tyrosine phosphorylation-IEAProcess
GO:0019888protein phosphatase regulator activity10866685.TASFunction
GO:0022626cytosolic ribosome21873635.IBAComponent
GO:0030683evasion or tolerance by virus of host immune response-TASProcess
GO:0030968endoplasmic reticulum unfolded protein response-IEAProcess
GO:0032722positive regulation of chemokine production-ISSProcess
GO:0032874positive regulation of stress-activated MAPK cascade-ISSProcess
GO:0033689negative regulation of osteoblast proliferation16216244.IMPProcess
GO:0034198cellular response to amino acid starvation25329545.IMPProcess
GO:0035455response to interferon-alpha19840259.IDAProcess
GO:0042802identical protein binding16373505.IPIFunction
GO:0043066negative regulation of apoptotic process-IEAProcess
GO:0043666regulation of phosphoprotein phosphatase activity-IEAProcess
GO:0045071negative regulation of viral genome replication19189853.19840259.IMPProcess
GO:0045087innate immune response-IEAProcess
GO:0046777protein autophosphorylation22801494.IDAProcess
GO:0046777protein autophosphorylation16216244.IMPProcess
GO:0048471perinuclear region of cytoplasm15121867.IDAComponent
GO:0051092positive regulation of NF-kappaB transcription factor activity15121867.IDAProcess
GO:0051607defense response to virus-IEAProcess
GO:1900225regulation of NLRP3 inflammasome complex assembly-ISSProcess
GO:1901224positive regulation of NIK/NF-kappaB signaling-ISSProcess
GO:1901532regulation of hematopoietic progenitor cell differentiation-ISSProcess
GO:1902033regulation of hematopoietic stem cell proliferation-ISSProcess
GO:1902036regulation of hematopoietic stem cell differentiation-ISSProcess
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