EuRBPDB

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  • Description
  • RBDs
  • RBPome
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • PPI
  • Paralogs
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000139546 (Gene tree)
Gene ID
6895
Gene Symbol
TARBP2
Alias
Trbp
Full Name
TARBP2 subunit of RISC loading complex
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Plus strand
Length
6,229 bases
Position
chr12:53,500,203-53,506,431
Accession
11569
RBP type
canonical RBP
Summary
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene binds between the bulge and the loop of the HIV-1 TAR RNA regulatory element and activates HIV-1 gene expression in synergy with the viral Tat protein. Alternative splicing results in multiple transcript variants encoding different isoforms. This gene also has a pseudogene. [provided by RefSeq, Jul 2008]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000377885dsrmPF00035.268.2e-3412
ENSP00000377885dsrmPF00035.268.2e-3422
ENSP00000416077dsrmPF00035.268.2e-3412
ENSP00000416077dsrmPF00035.268.2e-3422
ENSP00000266987dsrmPF00035.261.1e-3312
ENSP00000266987dsrmPF00035.261.1e-3322
ENSP00000447767dsrmPF00035.265.5e-2412
ENSP00000447767dsrmPF00035.265.5e-2422
ENSP00000458011dsrmPF00035.265.4e-1611
ENSP00000448199dsrmPF00035.269.5e-1611
ENSP00000449537dsrmPF00035.265.2e-0711
ENSP00000377885DND1_DSRMPF14709.71.1e-1011
ENSP00000416077DND1_DSRMPF14709.71.1e-1011
ENSP00000447767DND1_DSRMPF14709.71.1e-1011
ENSP00000266987DND1_DSRMPF14709.71.2e-1011
ENSP00000458011DND1_DSRMPF14709.71.9e-0611
ENSP00000448199DND1_DSRMPF14709.73.1e-0611
ENSP00000449537DND1_DSRMPF14709.72e-0511
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
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & MCF72018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
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-
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
24561616Interactions between the non-seed region of siRNA and RNA-binding RLC/RISC proteins, Ago and TRBP, in mammalian cells.Nucleic Acids Res2014 AprTakahashi Tdoi: 10.1093/nar/gku153
21368194Small molecule enoxacin is a cancer-specific growth inhibitor that acts by enhancing TAR RNA-binding protein 2-mediated microRNA processing.Proc Natl Acad Sci U S A2011 Mar 15Melo Sdoi: 10.1073/pnas.1014720108
23776147Processing of virus-derived cytoplasmic primary-microRNAs.Wiley Interdiscip Rev RNA2013 Jul-AugShapiro JSdoi: 10.1002/wrna.1169
16936726Argonaute-1 directs siRNA-mediated transcriptional gene silencing in human cells.Nat Struct Mol Biol2006 SepKim DH-
11725069Expression of TAR RNA-Binding Protein in Baculovirus and Co-Immunoprecipitation with Insect Cell Protein Kinase.J Biomed Sci1995 OctBlair ED-
11641396Organization of the human tarbp2 gene reveals two promoters that are repressed in an astrocytic cell line.J Biol Chem2001 Dec 28Bannwarth S-
16424907The role of PACT in the RNA silencing pathway.EMBO J2006 Feb 8Lee Y-
15918770Normal microRNA maturation and germ-line stem cell maintenance requires Loquacious, a double-stranded RNA-binding domain protein.PLoS Biol2005 JulForstemann K-
19219043A TARBP2 mutation in human cancer impairs microRNA processing and DICER1 function.Nat Genet2009 MarMelo SAdoi: 10.1038/ng.317
22279564TRBP and eIF6 homologue in Marsupenaeus japonicus play crucial roles in antiviral response.PLoS One2012Wang Sdoi: 10.1371/journal.pone.0030057
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
21711701A proteomic study of TAR-RNA binding protein (TRBP)-associated factors.Cell Biosci2011 Feb 25Chi YHdoi: 10.1186/2045-3701-1-9.
20932845Substrate-specific kinetics of Dicer-catalyzed RNA processing.J Mol Biol2010 Dec 3Chakravarthy Sdoi: 10.1016/j.jmb.2010.09.030
25544363Regulatory networks between neurotrophins and miRNAs in brain diseases and cancers.Acta Pharmacol Sin2015 FebShi Jdoi: 10.1038/aps.2014.135
24563327Up-regulation and worse prognostic marker of cytoplasmic TARBP2 expression in obstinate breast cancer.Med Oncol2014 AprLin Xdoi: 10.1007/s12032-014-0868-9
23690119Microsatellite instability and TARBP2 mutation study in upper urinary tract urothelial carcinoma.Am J Clin Pathol2013 JunBai Sdoi: 10.1309/AJCPBSLP8XHSWLOW.
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
28096385Correction for Melo et al., Small molecule enoxacin is a cancer-specific growth inhibitor that acts by enhancing TAR RNA-binding protein 2-mediated microRNA processing.Proc Natl Acad Sci U S A2017 Jan 24-doi: 10.1073/pnas.1621028114
26948382A designed recombinant fusion protein for targeted delivery of siRNA to the mouse brain.J Control Release2016 Apr 28Haroon MMdoi: 10.1016/j.jconrel.2016.03.007
27599909shRNAmediated silencing of TARBP2 inhibits NCIH1299 nonsmall cell lung cancer cell invasion and migration via the JNK/STAT3/AKT pathway.Mol Med Rep2016 OctShi Ydoi: 10.3892/mmr.2016.5723
294459101H, 13C and 15N resonance assignment of domain 1 of trans-activation response element (TAR) RNA binding protein isoform 1 (TRBP2) and its comparison with that of isoform 2 (TRBP1).Biomol NMR Assign2018 AprPaithankar Hdoi: 10.1007/s12104-018-9807-6
30759864TARBP2-Enhanced Resistance during Tamoxifen Treatment in Breast Cancer.Cancers (Basel)2019 Feb 12Wang MYdoi: 10.3390/cancers11020210.
30927622TARBP2 inhibits IRF7 activation by suppressing TRAF6-mediated K63-linked ubiquitination of IRF7.Mol Immunol2019 MayLing Tdoi: 10.1016/j.molimm.2019.02.019
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
19106622The NFAR's (nuclear factors associated with dsRNA): evolutionarily conserved members of the dsRNA binding protein family.RNA Biol2009 Jan-MarBarber GN-
18948111dsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi.J Mol Biol2008 Dec 26Parker GSdoi: 10.1016/j.jmb.2008.10.002
17452327Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA.J Biol Chem2007 Jun 15Kok KH-
25467938Double-stranded RNA in the biological control of grain aphid (Sitobion avenae F.).Funct Integr Genomics2015 MarWang Ddoi: 10.1007/s10142-014-0424-x
30347765Virus Sensor RIG-I Represses RNA Interference by Interacting with TRBP through LGP2 in Mammalian Cells.Genes (Basel)2018 Oct 19Takahashi Tdoi: 10.3390/genes9100511.
15123692Merlin, a tumor suppressor, interacts with transactivation-responsive RNA-binding protein and inhibits its oncogenic activity.J Biol Chem2004 Jul 16Lee JY-
25720988Conformation-dependent binding and tumor-targeted delivery of siRNA by a designed TRBP2: Affibody fusion protein.Nanomedicine2015 AugDar GHdoi: 10.1016/j.nano.2015.01.017
9230068Xlrbpa, a double-stranded RNA-binding protein associated with ribosomes and heterogeneous nuclear RNPs.J Cell Biol1997 Jul 28Eckmann CR-
16629595Are viral-encoded microRNAs mediating latent HIV-1 infection?DNA Cell Biol2006 AprWeinberg MS-
11438532Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression.J Biol Chem2001 Sep 7Daher A-
19820710Structural insights into RNA processing by the human RISC-loading complex.Nat Struct Mol Biol2009 NovWang HWdoi: 10.1038/nsmb.1673
19422693Characterization of the TRBP domain required for dicer interaction and function in RNA interference.BMC Mol Biol2009 May 7Daniels SMdoi: 10.1186/1471-2199-10-38.
23006623TRBP alters human precursor microRNA processing in vitro.RNA2012 NovLee HYdoi: 10.1261/rna.035501.112
22875687Backbone resonance assignments of the micro-RNA precursor binding region of human TRBP.Biomol NMR Assign2013 OctBenoit MPdoi: 10.1007/s12104-012-9416-8
17360756Small interfering RNAs against the TAR RNA binding protein, TRBP, a Dicer cofactor, inhibit human immunodeficiency virus type 1 long terminal repeat expression and viral production.J Virol2007 MayChristensen HS-
25668122HIV-1 RRE RNA acts as an RNA silencing suppressor by competing with TRBP-bound siRNAs.RNA Biol2015Daniels SMdoi: 10.1080/15476286.2015.1014759.
25064266HIV-1 translation and its regulation by cellular factors PKR and PACT.Virus Res2014 Nov 26Burugu Sdoi: 10.1016/j.virusres.2014.07.014
24352449Arabidopsis double-stranded RNA binding protein DRB3 participates in methylation-mediated defense against geminiviruses.J Virol2014 MarRaja Pdoi: 10.1128/JVI.02305-13
23658827Distinguishable in vitro binding mode of monomeric TRBP and dimeric PACT with siRNA.PLoS One2013 May 2Takahashi Tdoi: 10.1371/journal.pone.0063434
26221025Dengue NS3, an RNAi suppressor, modulates the human miRNA pathways through its interacting partner.Biochem J2015 Oct 1Kakumani PKdoi: 10.1042/BJ20150445
29540527A biosensor for MAPK-dependent Lin28 signaling.Mol Biol Cell2018 May 15Oldach LMdoi: 10.1091/mbc.E17-08-0500
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
31300274Nuclear TARBP2 Drives Oncogenic Dysregulation of RNA Splicing and Decay.Mol Cell2019 Jun 25Fish Ldoi: 10.1016/j.molcel.2019.06.001
12475984The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-containing RNAs in vitro and in vivo independently of its ability to inhibit the dsRNA-dependent kinase PKR.J Biol Chem2003 Feb 14Dorin D-
14585207Additive activity between the trans-activation response RNA-binding protein, TRBP2, and cyclin T1 on HIV type 1 expression and viral production in murine cells.AIDS Res Hum Retroviruses2003 SepBattisti PL-
25557550Dicer-TRBP complex formation ensures accurate mammalian microRNA biogenesis.Mol Cell2015 Feb 5Wilson RCdoi: 10.1016/j.molcel.2014.11.030
25043050Metastasis-suppressor transcript destabilization through TARBP2 binding of mRNA hairpins.Nature2014 Sep 11Goodarzi Hdoi: 10.1038/nature13466
23435228The RNA-binding region of human TRBP interacts with microRNA precursors through two independent domains.Nucleic Acids Res2013 AprBenoit MPdoi: 10.1093/nar/gkt086
29939295LGP2 virus sensor regulates gene expression network mediated by TRBP-bound microRNAs.Nucleic Acids Res2018 Sep 28Takahashi Tdoi: 10.1093/nar/gky575.
2011739Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR.Science1991 Mar 29Gatignol A-
9060615Specific repression of Tax trans-activation by TAR RNA-binding protein TRBP.J Virol1997 AprDonzeau M-
10369260A double-stranded RNA binding protein required for activation of repressed messages in mammalian germ cells.Nat Genet1999 JunZhong J-
16343534Cell-specific regulation of TRBP1 promoter by NF-Y transcription factor in lymphocytes and astrocytes.J Mol Biol2006 Feb 3Bannwarth S-
10849508Temporal control of protein synthesis during spermatogenesis.Int J Androl2000Braun RE-
16253139Dual role of TRBP in HIV replication and RNA interference: viral diversion of a cellular pathway or evasion from antiviral immunity?Retrovirology2005 Oct 27Gatignol A-
16271387Human RISC couples microRNA biogenesis and posttranscriptional gene silencing.Cell2005 Nov 18Gregory RI-
16188979Low TRBP levels support an innate human immunodeficiency virus type 1 resistance in astrocytes by enhancing the PKR antiviral response.J Virol2005 OctOng CL-
16142218TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing.EMBO Rep2005 OctHaase AD-
20184375Recognition of siRNA asymmetry by TAR RNA binding protein.Biochemistry2010 Apr 13Gredell JAdoi: 10.1021/bi902189s.
19605474ADAR1 interacts with PKR during human immunodeficiency virus infection of lymphocytes and contributes to viral replication.J Virol2009 OctClerzius Gdoi: 10.1128/JVI.02457-08
19301657Protein components of the microRNA pathway and human diseases.Methods Mol Biol2009Perron MPdoi: 10.1007/978-1-60327-547-7_18.
18936160TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.Mol Cell Biol2009 JanDaher Adoi: 10.1128/MCB.01030-08
18421256Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions.RNA Biol2008 Apr-JunLaraki G-
22933564The multiple functions of TRBP, at the hub of cell responses to viruses, stress, and cancer.Microbiol Mol Biol Rev2012 SepDaniels SMdoi: 10.1128/MMBR.00012-12.
22025453Expression levels of the microRNA maturing microprocessor complex component DGCR8 and the RNA-induced silencing complex (RISC) components argonaute-1, argonaute-2, PACT, TARBP1, and TARBP2 in epithelial skin cancer.Mol Carcinog2012 NovSand Mdoi: 10.1002/mc.20861
21294215Multiple levels of PKR inhibition during HIV-1 replication.Rev Med Virol2011 JanClerzius Gdoi: 10.1002/rmv.674
23207479Isolation and characterization of homologous TRBP cDNA for RNA interference in Penaeus monodon.Fish Shellfish Immunol2013 FebYang Ldoi: 10.1016/j.fsi.2012.11.022
20462493Structure of Arabidopsis HYPONASTIC LEAVES1 and its molecular implications for miRNA processing.Structure2010 May 12Yang SWdoi: 10.1016/j.str.2010.02.006.
25725290Early growth response gene 1, a TRBP binding protein, is involved in miRNA activity of miR-125a-3p in human cells.Cell Signal2015 JunWei Jdoi: 10.1016/j.cellsig.2015.02.016
25421511Stress-related alcohol consumption in heavy drinkers correlates with expression of miR-10a, miR-21, and components of the TAR-RNA-binding protein-associated complex.Alcohol Clin Exp Res2014 NovBeech RDdoi: 10.1111/acer.12549.
25110015Regulation of miRNA strand selection: follow the leader?Biochem Soc Trans2014 AugMeijer HAdoi: 10.1042/BST20140142.
27980417Clinicopathological Significance of TARBP2, APP, and ZNF395 in Breast Cancer.Breast Cancer (Auckl)2016 Dec 8Oi R-
24141778Ribosomal proteins L5 and L11 co-operatively inactivate c-Myc via RNA-induced silencing complex.Oncogene2014 Oct 9Liao JMdoi: 10.1038/onc.2013.430
24020926The PKR activator, PACT, becomes a PKR inhibitor during HIV-1 replication.Retrovirology2013 Sep 11Clerzius Gdoi: 10.1186/1742-4690-10-96.
23511973The rough endoplasmatic reticulum is a central nucleation site of siRNA-mediated RNA silencing.EMBO J2013 Apr 17Stalder Ldoi: 10.1038/emboj.2013.52
26486325The role of TARBP2 in the development and progression of cancers.Tumour Biol2016 JanYu Xdoi: 10.1007/s13277-015-4273-6
28174252TRBP maintains mammalian embryonic neural stem cell properties by acting as a novel transcriptional coactivator of the Notch signaling pathway.Development2017 Mar 1Byun SHdoi: 10.1242/dev.139493
26029872Trbp regulates heart function through microRNA-mediated Sox6 repression.Nat Genet2015 JulDing Jdoi: 10.1038/ng.3324
26012717Morphine Promotes Astrocyte-Preferential Differentiation of Mouse Hippocampal Progenitor Cells via PKC-epsilon-Dependent ERK Activation and TRBP Phosphorylation.Stem Cells2015 SepXu Cdoi: 10.1002/stem.2055
25843719A critical role for PKR complexes with TRBP in Immunometabolic regulation and eIF2-and-alpha; phosphorylation in obesity.Cell Rep2015 Apr 14Nakamura Tdoi: 10.1016/j.celrep.2015.03.021
28634830The microRNA effector RNA-induced silencing complex in hidradenitis suppurativa: a significant dysregulation within active inflammatory lesions.Arch Dermatol Res2017 SepHessam Sdoi: 10.1007/s00403-017-1752-1
29040648Molecular basis for asymmetry sensing of siRNAs by the Drosophila Loqs-PD/Dcr-2 complex in RNA interference.Nucleic Acids Res2017 Dec 1Tants JNdoi: 10.1093/nar/gkx886.
29045748Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins.Nucleic Acids Res2017 Dec 1Heyam Adoi: 10.1093/nar/gkx928.
29231267Contribution of the two dsRBM motifs to the double-stranded RNA binding and protein interactions of PACT.J Cell Biochem2018 AprChukwurah Edoi: 10.1002/jcb.26561
29348664Stress-induced TRBP phosphorylation enhances its interaction with PKR to regulate cellular survival.Sci Rep2018 Jan 18Chukwurah Edoi: 10.1038/s41598-018-19360-8.
29449323Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains.EMBO J2018 Mar 15Masliah Gdoi: 10.15252/embj.201797089
30390472TARBP2 negatively regulates IFN--and-beta; production and innate antiviral response by targeting MAVS.Mol Immunol2018 DecLing Tdoi: 10.1016/j.molimm.2018.10.017
30657254TARBP2-mediated destabilization of Nanog overcomes sorafenib resistance in hepatocellular carcinoma.Mol Oncol2019 AprLai HHdoi: 10.1002/1878-0261.12449
8723388Sequential steps in Tat trans-activation of HIV-1 mediated through cellular DNA, RNA, and protein binding factors.Gene Expr1996Gatignol A-
7568151Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo.Proc Natl Acad Sci U S A1995 Oct 10Cosentino GP-
11096080A Role of RNA Helicase A in cis-Acting Transactivation Response Element-mediated Transcriptional Regulation of Human Immunodeficiency Virus Type 1.J Biol Chem2001 Feb 23Fujii R-
18267968Functional dissection of siRNA sequence by systematic DNA substitution: modified siRNA with a DNA seed arm is a powerful tool for mammalian gene silencing with significantly reduced off-target effect.Nucleic Acids Res2008 AprUi-Tei Kdoi: 10.1093/nar/gkn042
21726814siRNA repositioning for guide strand selection by human Dicer complexes.Mol Cell2011 Jul 8Noland CLdoi: 10.1016/j.molcel.2011.05.028.
25608000Helical defects in microRNA influence protein binding by TAR RNA binding protein.PLoS One2015 Jan 21Acevedo Rdoi: 10.1371/journal.pone.0116749
25486461TARBP2 binding structured RNA elements drives metastasis.Cell Cycle2014Goodarzi Hdoi: 10.4161/15384101.2014.954453.
28369725RNA Polymerase I Inhibition with CX-5461 as a Novel Therapeutic Strategy to Target MYC in Multiple Myeloma.Br J Haematol2017 AprLee HCdoi: 10.1111/bjh.14525.
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000549572TARBP2-2111514-ENSP00000448948187 (aa)-F8VYK3
ENST00000456234TARBP2-2031368XM_005269114ENSP00000416077345 (aa)XP_005269171Q15633
ENST00000551741TARBP2-217992-ENSP0000044726292 (aa)-F8VZZ7
ENST00000549679TARBP2-2131466-ENSP0000044894388 (aa)-F8VYK6
ENST00000546889TARBP2-2051063--- (aa)--
ENST00000546763TARBP2-204846--- (aa)--
ENST00000548971TARBP2-2091493-ENSP0000044799394 (aa)-F8VTT7
ENST00000552650TARBP2-218954--- (aa)--
ENST00000394357TARBP2-2021402XM_005269115ENSP00000377885345 (aa)XP_005269172Q15633
ENST00000549028TARBP2-210557--- (aa)--
ENST00000266987TARBP2-2011867-ENSP00000266987366 (aa)-Q15633
ENST00000547541TARBP2-208430--- (aa)--
ENST00000547388TARBP2-207576--- (aa)--
ENST00000552817TARBP2-219668-ENSP00000458011160 (aa)-H3BV98
ENST00000547064TARBP2-206759XM_006719581ENSP00000448199196 (aa)XP_006719644F8VSA1
ENST00000551157TARBP2-2161008--- (aa)--
ENST00000549610TARBP2-2121116--- (aa)--
ENST00000550147TARBP2-2141855-ENSP00000450320113 (aa)-F8VP94
ENST00000550407TARBP2-2151132XM_005269117ENSP00000447767227 (aa)XP_005269174F8VZ57
ENST00000552857TARBP2-220916-ENSP00000449537165 (aa)-F8VW32
Gene Model
Click here to download ENSG00000139546's gene model file
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000139546's network

* RBP PPI network refers to all genes directly bind to RBP
Paralogs
Ensembl IDGene SymbolCoverageIdentiy ParalogGene SymbolCoverageIdentiy
ENSG00000139546TARBP29852.326ENSG00000180228PRKRA9751.087
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000139546TARBP210066.377ENSAPOG00000019892tarbp210065.301Acanthochromis_polyacanthus
ENSG00000139546TARBP299100.000ENSAMEG00000012601TARBP210096.448Ailuropoda_melanoleuca
ENSG00000139546TARBP210066.377ENSACIG00000016780tarbp210064.481Amphilophus_citrinellus
ENSG00000139546TARBP210066.667ENSAOCG00000005201tarbp210065.301Amphiprion_ocellaris
ENSG00000139546TARBP210066.667ENSAPEG00000008376tarbp210065.301Amphiprion_percula
ENSG00000139546TARBP210066.377ENSATEG00000025012tarbp210064.754Anabas_testudineus
ENSG00000139546TARBP29493.976ENSACAG00000001100TARBP210072.533Anolis_carolinensis
ENSG00000139546TARBP210099.180ENSANAG00000034453TARBP210099.180Aotus_nancymaae
ENSG00000139546TARBP210065.507ENSACLG00000018569tarbp29566.189Astatotilapia_calliptera
ENSG00000139546TARBP210066.954ENSAMXG00000016665tarbp29964.481Astyanax_mexicanus
ENSG00000139546TARBP299100.000ENSBTAG00000000435TARBP210097.541Bos_taurus
ENSG00000139546TARBP210099.180ENSCJAG00000018668TARBP210099.180Callithrix_jacchus
ENSG00000139546TARBP299100.000ENSCAFG00000006874TARBP210096.995Canis_familiaris
ENSG00000139546TARBP299100.000ENSCAFG00020020735TARBP210098.087Canis_lupus_dingo
ENSG00000139546TARBP29998.851ENSCHIG00000026017TARBP210094.070Capra_hircus
ENSG00000139546TARBP299100.000ENSTSYG00000035683TARBP210096.448Carlito_syrichta
ENSG00000139546TARBP27992.857ENSCAPG00000008981TARBP210093.778Cavia_aperea
ENSG00000139546TARBP29997.701ENSCPOG00000001009TARBP210093.443Cavia_porcellus
ENSG00000139546TARBP210099.130ENSCCAG00000033025TARBP210098.634Cebus_capucinus
ENSG00000139546TARBP210099.710ENSCATG00000026344TARBP210099.454Cercocebus_atys
ENSG00000139546TARBP29998.851ENSCLAG00000009175TARBP210094.262Chinchilla_lanigera
ENSG00000139546TARBP210099.420ENSCSAG00000005479TARBP210099.180Chlorocebus_sabaeus
ENSG00000139546TARBP29495.181ENSCPBG00000000654TARBP210075.072Chrysemys_picta_bellii
ENSG00000139546TARBP210099.490ENSCANG00000040415TARBP210098.634Colobus_angolensis_palliatus
ENSG00000139546TARBP299100.000ENSCGRG00001011856TARBP210094.809Cricetulus_griseus_chok1gshd
ENSG00000139546TARBP299100.000ENSCGRG00000009088TARBP210094.809Cricetulus_griseus_crigri
ENSG00000139546TARBP210067.919ENSCSEG00000010631tarbp210066.940Cynoglossus_semilaevis
ENSG00000139546TARBP28892.208ENSCVAG00000009832tarbp210066.125Cyprinodon_variegatus
ENSG00000139546TARBP210066.667ENSDARG00000070471tarbp210065.574Danio_rerio
ENSG00000139546TARBP299100.000ENSDNOG00000002144TARBP210096.175Dasypus_novemcinctus
ENSG00000139546TARBP28694.298ENSDORG00000001390Tarbp210094.298Dipodomys_ordii
ENSG00000139546TARBP2100100.000ENSDORG00000029983-100100.000Dipodomys_ordii
ENSG00000139546TARBP29996.552ENSETEG00000002458TARBP210080.601Echinops_telfairi
ENSG00000139546TARBP28485.135ENSEBUG00000002377tarbp29656.305Eptatretus_burgeri
ENSG00000139546TARBP299100.000ENSEASG00005010030TARBP210098.087Equus_asinus_asinus
ENSG00000139546TARBP299100.000ENSECAG00000011695TARBP210097.814Equus_caballus
ENSG00000139546TARBP29998.851ENSEEUG00000001128-9985.577Erinaceus_europaeus
ENSG00000139546TARBP210067.246ENSELUG00000010642tarbp29667.045Esox_lucius
ENSG00000139546TARBP299100.000ENSFCAG00000007757TARBP210097.268Felis_catus
ENSG00000139546TARBP299100.000ENSFDAG00000011932TARBP210095.082Fukomys_damarensis
ENSG00000139546TARBP28892.208ENSFHEG00000016118tarbp210066.957Fundulus_heteroclitus
ENSG00000139546TARBP210066.189ENSGMOG00000001290tarbp210065.135Gadus_morhua
ENSG00000139546TARBP210087.640ENSGALG00000048019-9587.778Gallus_gallus
ENSG00000139546TARBP27376.724ENSGALG00000038939-8373.094Gallus_gallus
ENSG00000139546TARBP28892.208ENSGAFG00000013341tarbp210065.301Gambusia_affinis
ENSG00000139546TARBP210065.230ENSGACG00000006645tarbp210063.369Gasterosteus_aculeatus
ENSG00000139546TARBP29495.181ENSGAGG00000021169TARBP210073.497Gopherus_agassizii
ENSG00000139546TARBP2100100.000ENSGGOG00000012637TARBP210099.727Gorilla_gorilla
ENSG00000139546TARBP210065.797ENSHBUG00000018639tarbp210064.208Haplochromis_burtoni
ENSG00000139546TARBP299100.000ENSHGLG00000001284TARBP210093.989Heterocephalus_glaber_female
ENSG00000139546TARBP299100.000ENSHGLG00100011274TARBP210093.989Heterocephalus_glaber_male
ENSG00000139546TARBP28892.208ENSHCOG00000001027tarbp210063.388Hippocampus_comes
ENSG00000139546TARBP29291.358ENSIPUG00000023701tarbp210066.125Ictalurus_punctatus
ENSG00000139546TARBP299100.000ENSSTOG00000003678TARBP210096.175Ictidomys_tridecemlineatus
ENSG00000139546TARBP2100100.000ENSJJAG00000007198-100100.000Jaculus_jaculus
ENSG00000139546TARBP29790.588ENSJJAG00000014366-9581.633Jaculus_jaculus
ENSG00000139546TARBP28892.208ENSKMAG00000012142tarbp210064.754Kryptolebias_marmoratus
ENSG00000139546TARBP28892.208ENSLBEG00000015027tarbp210065.847Labrus_bergylta
ENSG00000139546TARBP27494.340ENSLACG00000007087TARBP29660.282Latimeria_chalumnae
ENSG00000139546TARBP29292.593ENSLOCG00000005711tarbp210067.486Lepisosteus_oculatus
ENSG00000139546TARBP29494.040ENSLAFG00000002620TARBP210085.211Loxodonta_africana
ENSG00000139546TARBP210099.710ENSMFAG00000013567TARBP210099.454Macaca_fascicularis
ENSG00000139546TARBP210099.490ENSMMUG00000018492TARBP210099.180Macaca_mulatta
ENSG00000139546TARBP210099.710ENSMNEG00000036477TARBP210099.454Macaca_nemestrina
ENSG00000139546TARBP210099.710ENSMLEG00000029583TARBP210099.454Mandrillus_leucophaeus
ENSG00000139546TARBP210065.507ENSMAMG00000010272tarbp29766.189Mastacembelus_armatus
ENSG00000139546TARBP210065.797ENSMZEG00005006895tarbp210064.208Maylandia_zebra
ENSG00000139546TARBP299100.000ENSMAUG00000019805Tarbp210094.809Mesocricetus_auratus
ENSG00000139546TARBP2100100.000ENSMICG00000027441TARBP2100100.000Microcebus_murinus
ENSG00000139546TARBP29996.552ENSMOCG00000003691Tarbp210092.896Microtus_ochrogaster
ENSG00000139546TARBP210067.536ENSMMOG00000010374tarbp210066.667Mola_mola
ENSG00000139546TARBP210065.994ENSMALG00000009773tarbp210065.217Monopterus_albus
ENSG00000139546TARBP299100.000MGP_CAROLIEiJ_G0020356Tarbp210095.133Mus_caroli
ENSG00000139546TARBP2100100.000ENSMUSG00000023051Tarbp29999.091Mus_musculus
ENSG00000139546TARBP299100.000MGP_PahariEiJ_G0020355Tarbp210093.989Mus_pahari
ENSG00000139546TARBP299100.000MGP_SPRETEiJ_G0021249Tarbp210095.133Mus_spretus
ENSG00000139546TARBP299100.000ENSMPUG00000005944TARBP210096.995Mustela_putorius_furo
ENSG00000139546TARBP299100.000ENSMLUG00000010035TARBP210097.268Myotis_lucifugus
ENSG00000139546TARBP2100100.000ENSNGAG00000017769-100100.000Nannospalax_galili
ENSG00000139546TARBP28692.105ENSNBRG00000011845-7583.696Neolamprologus_brichardi
ENSG00000139546TARBP28892.208ENSNBRG00000003967TARBP29255.789Neolamprologus_brichardi
ENSG00000139546TARBP2100100.000ENSNLEG00000017690TARBP2100100.000Nomascus_leucogenys
ENSG00000139546TARBP210095.455ENSMEUG00000001916TARBP210082.787Notamacropus_eugenii
ENSG00000139546TARBP27992.857ENSOPRG00000011397TARBP210093.778Ochotona_princeps
ENSG00000139546TARBP299100.000ENSODEG00000013413TARBP210095.133Octodon_degus
ENSG00000139546TARBP28892.208ENSONIG00000005115tarbp29767.705Oreochromis_niloticus
ENSG00000139546TARBP29898.837ENSOCUG00000005700TARBP210093.443Oryctolagus_cuniculus
ENSG00000139546TARBP28692.105ENSORLG00000005209tarbp210065.847Oryzias_latipes
ENSG00000139546TARBP28692.105ENSORLG00020017755tarbp210064.481Oryzias_latipes_hni
ENSG00000139546TARBP28692.105ENSORLG00015013237tarbp210064.754Oryzias_latipes_hsok
ENSG00000139546TARBP28892.208ENSOMEG00000018860tarbp210065.027Oryzias_melastigma
ENSG00000139546TARBP299100.000ENSOGAG00000001744TARBP210097.268Otolemur_garnettii
ENSG00000139546TARBP299100.000ENSOARG00000016437TARBP210096.995Ovis_aries
ENSG00000139546TARBP2100100.000ENSPPAG00000030429TARBP2100100.000Pan_paniscus
ENSG00000139546TARBP299100.000ENSPPRG00000000189TARBP210097.268Panthera_pardus
ENSG00000139546TARBP299100.000ENSPTIG00000007859TARBP210089.757Panthera_tigris_altaica
ENSG00000139546TARBP2100100.000ENSPTRG00000005020TARBP2100100.000Pan_troglodytes
ENSG00000139546TARBP210099.710ENSPANG00000010689TARBP210099.454Papio_anubis
ENSG00000139546TARBP28893.506ENSPKIG00000002455tarbp210065.940Paramormyrops_kingsleyae
ENSG00000139546TARBP28892.208ENSPMGG00000006497tarbp29965.289Periophthalmus_magnuspinnatus
ENSG00000139546TARBP29997.701ENSPEMG00000014285Tarbp210093.169Peromyscus_maniculatus_bairdii
ENSG00000139546TARBP29069.663ENSPMAG00000000105tarbp210058.382Petromyzon_marinus
ENSG00000139546TARBP210094.318ENSPCIG00000006672TARBP29282.787Phascolarctos_cinereus
ENSG00000139546TARBP28892.208ENSPFOG00000007586tarbp210065.847Poecilia_formosa
ENSG00000139546TARBP28892.208ENSPLAG00000017659tarbp210065.574Poecilia_latipinna
ENSG00000139546TARBP28892.208ENSPMEG00000007775tarbp210065.847Poecilia_mexicana
ENSG00000139546TARBP28892.208ENSPREG00000007815tarbp210065.574Poecilia_reticulata
ENSG00000139546TARBP299100.000ENSPPYG00000004583TARBP210092.623Pongo_abelii
ENSG00000139546TARBP210094.388ENSPCAG00000005352TARBP210080.328Procavia_capensis
ENSG00000139546TARBP299100.000ENSPCOG00000013102TARBP210098.087Propithecus_coquereli
ENSG00000139546TARBP299100.000ENSPVAG00000012286TARBP210091.530Pteropus_vampyrus
ENSG00000139546TARBP210065.797ENSPNYG00000014125tarbp210064.208Pundamilia_nyererei
ENSG00000139546TARBP210067.435ENSPNAG00000011128tarbp210065.301Pygocentrus_nattereri
ENSG00000139546TARBP299100.000ENSRNOG00000042355Tarbp210092.896Rattus_norvegicus
ENSG00000139546TARBP210099.710ENSRBIG00000027150TARBP210099.454Rhinopithecus_bieti
ENSG00000139546TARBP210099.710ENSRROG00000044783TARBP210099.710Rhinopithecus_roxellana
ENSG00000139546TARBP299100.000ENSSBOG00000027305TARBP210098.907Saimiri_boliviensis_boliviensis
ENSG00000139546TARBP210076.136ENSSBOG00000034049-9575.248Saimiri_boliviensis_boliviensis
ENSG00000139546TARBP210094.318ENSSHAG00000007064TARBP210084.890Sarcophilus_harrisii
ENSG00000139546TARBP28892.208ENSSFOG00015010784tarbp29667.139Scleropages_formosus
ENSG00000139546TARBP210066.763ENSSMAG00000012769tarbp210065.027Scophthalmus_maximus
ENSG00000139546TARBP210065.797ENSSDUG00000018818tarbp210064.481Seriola_dumerili
ENSG00000139546TARBP210065.797ENSSLDG00000001835tarbp210064.481Seriola_lalandi_dorsalis
ENSG00000139546TARBP27288.060ENSSARG00000001010TARBP27388.060Sorex_araneus
ENSG00000139546TARBP26096.226ENSSPUG00000005895TARBP210052.674Sphenodon_punctatus
ENSG00000139546TARBP28892.208ENSSPAG00000022797tarbp210064.754Stegastes_partitus
ENSG00000139546TARBP299100.000ENSSSCG00000000276TARBP210097.268Sus_scrofa
ENSG00000139546TARBP28890.909ENSTRUG00000014379tarbp210064.481Takifugu_rubripes
ENSG00000139546TARBP28890.909ENSTNIG00000007065tarbp210064.208Tetraodon_nigroviridis
ENSG00000139546TARBP27998.052ENSTBEG00000012751-5597.688Tupaia_belangeri
ENSG00000139546TARBP299100.000ENSTTRG00000017177TARBP210095.902Tursiops_truncatus
ENSG00000139546TARBP299100.000ENSUAMG00000009011TARBP210096.995Ursus_americanus
ENSG00000139546TARBP299100.000ENSUMAG00000010461TARBP210096.448Ursus_maritimus
ENSG00000139546TARBP299100.000ENSVVUG00000028150TARBP210098.087Vulpes_vulpes
ENSG00000139546TARBP29981.609ENSXETG00000012644tarbp29770.391Xenopus_tropicalis
ENSG00000139546TARBP28892.208ENSXMAG00000017836tarbp210065.847Xiphophorus_maculatus
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0003725double-stranded RNA binding23661684.25608000.IDAFunction
GO:0005515protein binding15973356.16142218.16424907.17452327.17507929.17531811.17932509.18178619.19668211.19716330.19804757.19820710.19836333.21858095.21900206.21903422.23361462.23622242.23636329.23661684.25416956.25446899.25910212.IPIFunction
GO:0005654nucleoplasm-IDAComponent
GO:0005737cytoplasm17452327.IDAComponent
GO:0005829cytosol-TASComponent
GO:0006469negative regulation of protein kinase activity11641396.TASProcess
GO:0007286spermatid development-IEAProcess
GO:0007338single fertilization-IEAProcess
GO:0010586miRNA metabolic process-TASProcess
GO:0016442RISC complex-IEAComponent
GO:0016604nuclear body-IDAComponent
GO:0019899enzyme binding25557550.IPIFunction
GO:0030422production of siRNA involved in RNA interference15973356.17452327.IDAProcess
GO:0030422production of siRNA involved in RNA interference-TASProcess
GO:0030423targeting of mRNA for destruction involved in RNA interference15973356.IMPProcess
GO:0031054pre-miRNA processing15973356.16357216.16424907.18178619.23661684.IDAProcess
GO:0035068micro-ribonucleoprotein complex17531811.IDAComponent
GO:0035087siRNA loading onto RISC involved in RNA interference15973356.IDAProcess
GO:0035196production of miRNAs involved in gene silencing by miRNA15973356.23661684.IDAProcess
GO:0035197siRNA binding15973356.IDAFunction
GO:0035198miRNA binding-IEAFunction
GO:0035264multicellular organism growth-IEAProcess
GO:0035280miRNA loading onto RISC involved in gene silencing by miRNA18178619.IDAProcess
GO:0036002pre-mRNA binding19820710.TASFunction
GO:0042802identical protein binding25416956.IPIFunction
GO:0042803protein homodimerization activity17452327.IPIFunction
GO:0043403skeletal muscle tissue regeneration-IEAProcess
GO:0045070positive regulation of viral genome replication11641396.IDAProcess
GO:0045727positive regulation of translation-IEAProcess
GO:0046782regulation of viral transcription11641396.IDAProcess
GO:0047485protein N-terminus binding19820710.IPIFunction
GO:0048471perinuclear region of cytoplasm-IEAComponent
GO:0050689negative regulation of defense response to virus by host11641396.IDAProcess
GO:0051149positive regulation of muscle cell differentiation-IEAProcess
GO:0061351neural precursor cell proliferation-IEAProcess
GO:0070578RISC-loading complex15973356.16357216.17531811.18178619.19820710.23661684.IDAComponent
GO:0070883pre-miRNA binding23435228.23661684.IDAFunction
GO:0070883pre-miRNA binding18178619.IDAFunction
GO:0090065regulation of production of siRNA involved in RNA interference-IEAProcess
GO:1903798regulation of production of miRNAs involved in gene silencing by miRNA-IEAProcess

Cancer associated literatures
PIDTitleArticle TimeAuthorDoi
22698405A TARBP2-dependent miRNA expression profile underlies cancer stem cell properties and provides candidate therapeutic reagents in Ewing sarcoma.Cancer Cell2012 Jun 12De Vito Cdoi: 10.1016/j.ccr.2012.04.023.
15123692Merlin, a tumor suppressor, interacts with transactivation-responsive RNA-binding protein and inhibits its oncogenic activity.J Biol Chem2004 Jul 16Lee JY-
26486325The role of TARBP2 in the development and progression of cancers.Tumour Biol2016 JanYu Xdoi: 10.1007/s13277-015-4273-6
24563327Up-regulation and worse prognostic marker of cytoplasmic TARBP2 expression in obstinate breast cancer.Med Oncol2014 AprLin Xdoi: 10.1007/s12032-014-0868-9
22933564The multiple functions of TRBP, at the hub of cell responses to viruses, stress, and cancer.Microbiol Mol Biol Rev2012 SepDaniels SMdoi: 10.1128/MMBR.00012-12.
20877318Reassessing the TARBP2 mutation rate in hereditary nonpolyposis colorectal cancer.Nat Genet2010 OctGarre Pdoi: 10.1038/ng1010-817.
22025453Expression levels of the microRNA maturing microprocessor complex component DGCR8 and the RNA-induced silencing complex (RISC) components argonaute-1, argonaute-2, PACT, TARBP1, and TARBP2 in epithelial skin cancer.Mol Carcinog2012 NovSand Mdoi: 10.1002/mc.20861
27599909shRNAmediated silencing of TARBP2 inhibits NCIH1299 nonsmall cell lung cancer cell invasion and migration via the JNK/STAT3/AKT pathway.Mol Med Rep2016 OctShi Ydoi: 10.3892/mmr.2016.5723

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr1253505764Missense_MutationNAS286C0.22
BLCAchr1253505744SilentnovelL279L0.26
BLCAchr1253505816SilentnovelE303E0.07
BLCAchr1253503721Missense_MutationNAS112F0.09
BLCAchr1253506147Silentnovel*367*0.46
BRCAchr1253505698Missense_MutationnovelT264N0.1
BRCAchr1253502159SilentNAV66V0.23
BRCAchr1253501435SilentnovelG9G0.31
BRCAchr1253501424Nonsense_MutationNAQ6*0.17
BRCAchr1253503765Missense_MutationnovelA127T0.12
BRCAchr1253502121Missense_MutationNAE54K0.35
BRCAchr1253506021Frame_Shift_DelnovelL326Hfs*160.45
CESCchr12535063893'UTRnovel0.38
CESCchr1253504767Missense_MutationNAR189C0.22
CESCchr1253505712Nonsense_Mutationrs769325580R269*0.44
CESCchr1253503024Splice_Regionnovel0.29
COADchr1253503725SilentNAP113P0.34
COADchr1253504730Silentrs200766710P176P0.32
COADchr1253504758Missense_MutationnovelP186T0.13
COADchr1253506089Missense_Mutationrs747821228R348C0.28
COADchr1253504404Missense_Mutationrs139126157P144A0.19
COADchr1253503131Splice_SitenovelX109_splice0.38
COADchr1253504792Missense_MutationnovelR197Q0.29
COADchr1253504723Missense_MutationNAR174Q0.4
COADchr1253502168SilentnovelG69G0.16
COADchr1253505174Missense_MutationnovelA218V0.56
COADchr1253504773Nonsense_MutationNAE191*0.21
COADchr1253505676Nonsense_Mutationrs758198296R257*0.16
COADchr1253504773Nonsense_MutationNAE191*0.55
COADchr1253504656Intronnovel0.31
COADchr1253505194Missense_MutationnovelV225M0.37
ESCAchr12535013195'UTRnovel0.21
GBMchr1253502095Missense_MutationnovelT45M0.2
GBMchr12535062243'UTRnovel0.58
GBMchr1253503752Missense_MutationNAI122M0.03
GBMchr1253504800Missense_Mutationrs771112623R200C0.37
HNSCchr1253502114SilentnovelL51L0.29
HNSCchr1253506130SilentnovelI361I0.26
HNSCchr1253502106Missense_MutationnovelD49N0.2
HNSCchr1253503946Intronnovel0.29
HNSCchr1253504443Frame_Shift_InsnovelC158Vfs*460.23
KICHchr1253502095Missense_MutationnovelT45M0.2
KIRCchr1253504379Intronnovel0.1
KIRCchr12535061713'UTRnovel0.14
KIRPchr1253505766SilentnovelL287L0.24
KIRPchr1253501617Intronnovel0.57
KIRPchr1253506056Missense_MutationNAC337R0.3
KIRPchr1253502140Frame_Shift_InsnovelN61*0.5
LAMLchr1253503788SilentnovelV134V0.05
LGGchr1253505713Missense_Mutationrs759508001R269Q0.32
LGGchr1253502133Frame_Shift_InsnovelQ59Tfs*570.03
LIHCchr1253502135Missense_MutationnovelH58Q0.21
LIHCchr1253504695Splice_Regionnovel0.33
LIHCchr1253505762SilentnovelG285G0.84
LUADchr1253505230Missense_MutationNAE237K0.07
LUSCchr1253506108Missense_Mutationrs140535249R354H0.19
OVchr1253504741Missense_MutationnovelV180G0.13
PAADchr1253506082SilentnovelE345E0.17
READchr1253505677Missense_MutationNAR257Q0.33
READchr1253505158Missense_MutationNAA213T0.11
READchr1253504784Missense_MutationNAM194I0.13
SKCMchr1253502109Missense_MutationnovelL50F0.09
SKCMchr1253504390Splice_Regionnovel0.34
SKCMchr1253505145SilentNAT208T0.1
SKCMchr1253502162Silentrs542850740T67T0.38
SKCMchr1253504775SilentNAE191E0.17
SKCMchr1253502128Missense_MutationnovelQ56R0.29
SKCMchr1253502129Missense_MutationnovelQ56H0.29
STADchr1253504758Missense_MutationnovelP186S0.32
STADchr1253506130SilentnovelI361I0.28
STADchr1253503908Intronnovel0.18
STADchr1253505661Missense_MutationNAR252C0.21
STADchr1253506040SilentNAT331T0.11
STADchr1253505852Splice_SitenovelX315_splice0.29
STADchr1253503776SilentNAA130A0.41
STADchr1253503830Intronnovel0.32
THCAchr1253504617Intronnovel0.08
UCECchr1253504773Nonsense_MutationNAE191*0.36
UCECchr1253505797Missense_MutationNAV297A0.33
UCECchr1253503109SilentNAE102E0.25
UCECchr1253505175Silentrs190258088A218A0.31
UCECchr1253505192Missense_Mutationrs562284475R224Q0.44
UCECchr12535062453'UTRnovel0.33
UCECchr1253504399Frame_Shift_Insrs765100595M145Hfs*130.36
UCECchr12535061503'UTRnovel0.3
UCECchr1253504274Intronnovel0.29
UCECchr1253504455Missense_Mutationrs569814780V161I0.13
UCECchr12535012115'UTRnovel0.5
UCECchr1253504773Nonsense_MutationNAE191*0.27
UCECchr1253505691Missense_MutationNAG262C0.23
UCECchr1253502093SilentNAK44K0.14
UCECchr1253505794Missense_Mutationrs769254353R296H0.22
UCECchr1253501669Intronnovel0.33
UCECchr1253504767Missense_MutationNAR189C0.43
UCECchr1253505201Missense_Mutationrs765847634T227M0.79
UCECchr1253503950Intronnovel0.24
UCECchr1253505207Missense_MutationNAP229H0.08
UCECchr1253506090Missense_Mutationrs771785979R348H0.39
UCECchr1253503966Intronnovel0.44
UCECchr1253504773Nonsense_MutationNAE191*0.38
UCECchr1253504239Intronnovel0.33
UCECchr1253502125Missense_MutationnovelG55D0.13
UCECchr1253504445Missense_MutationnovelE157D0.26
UCECchr1253505682Missense_Mutationrs746965828R259W0.36
UCECchr1253503176Intronnovel0.5
UCECchr1253504238Intronnovel0.14
UCECchr1253504404Missense_Mutationrs139126157P144S0.37
UCECchr1253506105Missense_Mutationrs573462744R353H0.42
UCECchr12535013715'UTRnovel0.58
UCECchr1253502130Missense_MutationNAA57T0.37

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
DLBCAMP0.18750.085003
READDEL0.06060.064633
STADDEL0.08840.22179

Survival Analysis
CancerP-value Q-value
STAD0.042

Kaplan-Meier Survival Analysis

MESO0.026

Kaplan-Meier Survival Analysis

ACC0.0091

Kaplan-Meier Survival Analysis

UCS0.0015

Kaplan-Meier Survival Analysis

HNSC0.033

Kaplan-Meier Survival Analysis

SKCM0.0012

Kaplan-Meier Survival Analysis

PAAD0.014

Kaplan-Meier Survival Analysis

KICH0.007

Kaplan-Meier Survival Analysis

LIHC0.0016

Kaplan-Meier Survival Analysis

LGG0.0045

Kaplan-Meier Survival Analysis

UVM0.0093

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742


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