EuRBPDB

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  • Description
  • RBDs
  • RBPome
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • PPI
  • Paralogs
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000065978 (Gene tree)
Gene ID
4904
Gene Symbol
YBX1
Alias
YB-1|YB1|DBPB|NSEP-1|MDR-NF1|BP-8|CSDB|CSDA2|NSEP1
Full Name
Y-box binding protein 1
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Plus strand
Length
19,975 bases
Position
chr1:42,682,389-42,702,363
Accession
8014
RBP type
canonical RBP
Summary
This gene encodes a highly conserved cold shock domain protein that has broad nucleic acid binding properties. The encoded protein functions as both a DNA and RNA binding protein and has been implicated in numerous cellular processes including regulation of transcription and translation, pre-mRNA splicing, DNA reparation and mRNA packaging. This protein is also a component of messenger ribonucleoprotein (mRNP) complexes and may have a role in microRNA processing. This protein can be secreted through non-classical pathways and functions as an extracellular mitogen. Aberrant expression of the gene is associated with cancer proliferation in numerous tissues. This gene may be a prognostic marker for poor outcome and drug resistance in certain cancers. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene are found on multiple chromosomes. [provided by RefSeq, Sep 2015]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000361626CSDPF00313.221.7e-2511
ENSP00000389639CSDPF00313.225.2e-1311
ENSP00000405937CSDPF00313.226.6e-1211
RNA binding proteome (RBPome)
PIDTitleMethod TimeAuthorDoi
22681889The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts4SURIC & HEK2932012 MayBaltz AGDOI: 10.1016/j.molcel.2012.05.021
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & HEK2932019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & HEK2932018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
29431736Capturing the interactome of newly transcribed RNAPolyT-RICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNARIC & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNARICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
22658674Insights into RNA biology from an atlas of mammalian mRNA-binding proteinsRIC & Hela2012 May 31Castello ADOI: 10.1016/j.cell.2012.04.031
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & Hela2018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & MCF10A2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & MCF72018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & U2OS2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
27453046Comprehensive Identification of RNA-Binding Domains in Human CellsRIC & Hela2016 Aug 18Castello ADOI: 10.1016/j.molcel.2016.06.029
30352994Discovery of RNA-binding proteins and characterization of their dynamic responses by enhanced RNA interactome captureRIC & Jurkat2018 Oct 23Perez-Perri JIDOI:10.1038/s41467-018-06557-8

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
18753264Identification of cold-shock protein RBM3 as a possible regulator of skeletal muscle size through expression profiling.Am J Physiol Regul Integr Comp Physiol2008 OctDupont-Versteegden EEdoi: 10.1152/ajpregu.90455.2008
22801372Y-box binding protein 1 and RNase UK114 mediate monocyte chemoattractant protein 1 mRNA stability in vascular smooth muscle cells.Mol Cell Biol2012 SepDhawan Ldoi: 10.1128/MCB.00846-12
16887808The anti-HIV-1 editing enzyme APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules.J Biol Chem2006 Sep 29Kozak SL-
24107631The proteolytic YB-1 fragment interacts with DNA repair machinery and enhances survival during DNA damaging stress.Cell Cycle2013 Dec 15Kim ERdoi: 10.4161/cc.26670
18335541MBNL1 associates with YB-1 in cytoplasmic stress granules.J Neurosci Res2008 JulOnishi Hdoi: 10.1002/jnr.21655.
7711075cDNA encoding a chicken protein (CRP1) with homology to hnRNP type A/B.Biochim Biophys Acta1995 Apr 4Cvekl A-
16251272Regulation of RNA splicing by the methylation-dependent transcriptional repressor methyl-CpG binding protein 2.Proc Natl Acad Sci U S A2005 Dec 6Young JI-
18978732Y-Box-binding protein-1 is a promising predictive marker of radioresistance and chemoradioresistance in nasopharyngeal cancer.Mod Pathol2009 FebTay WLdoi: 10.1038/modpathol.2008.181
17704806Phosphorylation by Akt disables the anti-oncogenic activity of YB-1.Oncogene2008 Feb 14Bader AG-
22730292YB-1 binds to CAUC motifs and stimulates exon inclusion by enhancing the recruitment of U2AF to weak polypyrimidine tracts.Nucleic Acids Res2012 Sep 1Wei WJ-
22406259Localization of mRNAs encoding human mitochondrial oxidative phosphorylation proteins.Mitochondrion2012 MayMatsumoto Sdoi: 10.1016/j.mito.2012.02.004
26193840The value of cytoplasmic Y-box-binding protein 1 as a prognostic marker for breast cancer in Korean.Breast Cancer2016 SepLee Adoi: 10.1007/s12282-015-0625-8
27354655Nuclear Y-Box-binding Protein-1 Expression Predicts Poor Clinical Outcome in Stage III Colorectal Cancer.Anticancer Res2016 JulShiraiwa S-
26394155The Y-Box Binding Protein 1 Suppresses Alzheimer's Disease Progression in Two Animal Models.PLoS One2015 Sep 22Bobkova NVdoi: 10.1371/journal.pone.0138867
25980435YBX1/YB-1 induces partial EMT and tumourigenicity through secretion of angiogenic factors into the extracellular microenvironment.Oncotarget2015 May 30Gopal SK-
28515422Up regulation and nuclear translocation of Y-box binding protein 1 (YB-1) is linked to poor prognosis in ERG-negative prostate cancer.Sci Rep2017 May 17Heumann Adoi: 10.1038/s41598-017-02279-x.
28916481Identification of 2,4-dihydroxy-5-pyrimidinyl imidothiocarbomate as a novel inhibitor to Y box binding protein-1 (YB-1) and its therapeutic actions against breast cancer.Eur J Pharm Sci2018 Apr 30Gunasekaran VPdoi: 10.1016/j.ejps.2017.09.019
29059375Translational co-regulation of a ligand and inhibitor by a conserved RNA element.Nucleic Acids Res2018 Jan 9Zaucker Adoi: 10.1093/nar/gkx938.
29712925The RNA-binding protein YBX1 regulates epidermal progenitors at a posttranscriptional level.Nat Commun2018 Apr 30Kwon Edoi: 10.1038/s41467-018-04092-0.
29995936Y-box-binding protein 1 supports the early and late steps of HIV replication.PLoS One2018 Jul 11Weydert Cdoi: 10.1371/journal.pone.0200080
10906122Physical and functional interaction between two pluripotent proteins, the Y-box DNA/RNA-binding factor, YB-1, and the multivalent zinc finger factor, CTCF.J Biol Chem2000 Sep 22Chernukhin IV-
16193061Proteasome-mediated cleavage of the Y-box-binding protein 1 is linked to DNA-damage stress response.EMBO J2005 Oct 19Sorokin AV-
16782553The role of cytokine mRNA stability in the pathogenesis of autoimmune disease.Autoimmun Rev2006 MaySeko Y-
18078822U7 snRNA acts as a transcriptional regulator interacting with an inverted CCAAT sequence-binding transcription factor NF-Y.Biochim Biophys Acta2008 FebHiguchi T-
28341602Cytosolic YB-1 and NSUN2 are the only proteins recognizing specific motifs present in mRNAs enriched in exosomes.Biochim Biophys Acta Proteins Proteom2017 JunKossinova OAdoi: 10.1016/j.bbapap.2017.03.010
29028411Expanding the map of protein-RNA interaction sites via cell fusion followed by PAR-CLIP.RNA Biol2018 Mar 4Hinze Fdoi: 10.1080/15476286.2017.1384120
31160337Crystal structure of a Y-box binding protein 1 (YB-1)-RNA complex reveals key features and residues interacting with RNA.J Biol Chem2019 Jul 12Yang XJdoi: 10.1074/jbc.RA119.007545
10559330Physical and functional interaction between the Y-box binding protein YB-1 and human polyomavirus JC virus large T antigen.J Virol1999 DecSafak M-
16211256Expression of Y-Box binding protein-1 following hypericin-mediated photodynamic therapy in well-differentiated nasopharyngeal cancer in vivo.Int J Mol Med2005 NovDu HY-
19098458RNA-binding specificity of Y-box protein 1.RNA Biol2009 Jan-MarDong J-
20596676Y-box binding protein 1 is up-regulated in proliferative breast cancer and its inhibition deregulates the cell cycle.Int J Oncol2010 AugYu YN-
25354590HnRNP C, YB-1 and hnRNP L coordinately enhance skipping of human MUSK exon 10 to generate a Wnt-insensitive MuSK isoform.Sci Rep2014 Oct 30Nasrin Fdoi: 10.1038/srep06841.
24217978YB-1 protein: functions and regulation.Wiley Interdiscip Rev RNA2014 Jan-FebLyabin DNdoi: 10.1002/wrna.1200
26126888Thermodynamic characterization of the interaction between the human Y-box binding protein YB-1 and nucleic acids.Mol Biosyst2015 SepTanabe Ydoi: 10.1039/c5mb00184f.
30139801Dynamic association of human mRNP proteins with mitochondrial tRNAs in the cytosol.RNA2018 DecJady BEdoi: 10.1261/rna.066738.118
30258867Role of post-translational modification of the Y box binding protein 1 in human cancers.Genes Dis2015 May 27Prabhu Ldoi: 10.1016/j.gendis.2015.05.001
30804514Gain-of-function mutation of microRNA-140 in human skeletal dysplasia.Nat Med2019 AprGrigelioniene Gdoi: 10.1038/s41591-019-0353-2
30905816tRNA-derived fragments and tRNA halves: The new players in cancers.Cancer Lett2019 Jun 28Zhu Ldoi: 10.1016/j.canlet.2019.03.012
10573156Interaction of YB-1 with human immunodeficiency virus type 1 Tat and TAR RNA modulates viral promoter activity.J Gen Virol1999 OctAnsari SA-
1398104A protein binding to CArG box motifs and to single-stranded DNA functions as a transcriptional repressor.Gene1992 Oct 1Kamada S-
7876087The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter.J Biol Chem1995 Feb 24MacDonald GH-
16913221[Nonspecific and specific interaction of Y-box binding protein 1 (YB-1) with mRNA and posttranscriptional regulation of protein synthesis in animal cells].Mol Biol (Mosk)2006 Jul-AugSkabkin MA-
12674497Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D).Biol Chem2003 JanMoraes KC-
12379116Binding capacity of human YB-1 protein for RNA containing 8-oxoguanine.Biochemistry2002 Oct 22Hayakawa H-
16489918Intracellular localization and content of YB-1 protein in multidrug resistant tumor cells.Biochemistry (Mosc)2006 FebVaiman AV-
11447123The RNA binding protein YB-1 binds A/C-rich exon enhancers and stimulates splicing of the CD44 alternative exon v4.EMBO J2001 Jul 16Stickeler E-
16354698Akt-mediated YB-1 phosphorylation activates translation of silent mRNA species.Mol Cell Biol2006 JanEvdokimova V-
10817758Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activation.Genes Dev2000 May 15Chen CY-
15743808Inhibition of protein synthesis by Y box-binding protein 1 blocks oncogenic cell transformation.Mol Cell Biol2005 MarBader AG-
15494450Structural organization of mRNA complexes with major core mRNP protein YB-1.Nucleic Acids Res2004 Oct 19Skabkin MA-
14662769Identification of RNA-binding proteins in RAW 264.7 cells that recognize a lipopolysaccharide-responsive element in the 3-untranslated region of the murine cyclooxygenase-2 mRNA.J Biol Chem2004 Feb 27Cok SJ-
14662883Hyaluronic acid or TNF-alpha plus fibronectin triggers granulocyte macrophage-colony-stimulating factor mRNA stabilization in eosinophils yet engages differential intracellular pathways and mRNA binding proteins.J Immunol2003 Dec 15Esnault S-
14530393Y box-binding protein 1 induces resistance to oncogenic transformation by the phosphatidylinositol 3-kinase pathway.Proc Natl Acad Sci U S A2003 Oct 14Bader AG-
19470374HSP60 interacts with YB-1 and affects its polysome association and subcellular localization.Biochem Biophys Res Commun2009 Aug 7Ohashi Sdoi: 10.1016/j.bbrc.2009.05.094
17339575.RNA2007 MayYang WH-
22590640Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.PLoS One2012Guryanov SGdoi: 10.1371/journal.pone.0036969
21788731Interplay between Y-box-binding protein 1 (YB-1) and poly(A) binding protein (PABP) in specific regulation of YB-1 mRNA translation.RNA Biol2011 Sep-OctLyabin DNdoi: 10.4161/rna.8.5.16022
20713358Post-transcriptional up-regulation of Tsc-22 by Ybx1, a target of miR-216a, mediates TGF-{beta}-induced collagen expression in kidney cells.J Biol Chem2010 Oct 29Kato Mdoi: 10.1074/jbc.M110.165027
28161363Molecular determinants of cytochrome C oxidase IV mRNA axonal trafficking.Mol Cell Neurosci2017 AprKar ANdoi: 10.1016/j.mcn.2017.01.008
25720531AUF-1 and YB-1 independently regulate β-globin mRNA in developing erythroid cells through interactions with poly(A)-binding protein.Mech Dev2015 Mayvan Zalen Sdoi: 10.1016/j.mod.2015.02.003
24926617p53-directed translational control can shape and expand the universe of p53 target genes.Cell Death Differ2014 OctZaccara Sdoi: 10.1038/cdd.2014.79
24832798Dynamic Interplay of Smooth Muscle α-Actin Gene-Regulatory Proteins Reflects the Biological Complexity of Myofibroblast Differentiation.Biology (Basel)2013 Mar 28Strauch ARdoi: 10.3390/biology2020555.
26289635Nanog RNA-binding proteins YBX1 and ILF3 affect pluripotency of embryonic stem cells.Cell Biol Int2016 AugGuo Cdoi: 10.1002/cbin.10539
27821766Epigenetic inactivation of the p53-induced long noncoding RNA TP53 target 1 in human cancer.Proc Natl Acad Sci U S A2016 Nov 22Diaz-Lagares A-
27559612Y-box protein 1 is required to sort microRNAs into exosomes in cells and in a cell-free reaction.Elife2016 Aug 25Shurtleff MJdoi: 10.7554/eLife.19276.
27565728Four nucleocytoplasmic-shuttling proteins and p53 interact specifically with the YB-NLS and are involved in anticancer reagent-induced nuclear localization of YB-1.Biochem Biophys Res Commun2016 Sep 23Tanaka Tdoi: 10.1016/j.bbrc.2016.08.129
25957686Endogenous tRNA-Derived Fragments Suppress Breast Cancer Progression via YBX1 Displacement.Cell2015 May 7Goodarzi Hdoi: 10.1016/j.cell.2015.02.053.
28740723At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair.Acta Naturae2017 Apr-JunAlemasova EE-
29073095Broad role for YBX1 in defining the small noncoding RNA composition of exosomes.Proc Natl Acad Sci U S A2017 Oct 24Shurtleff MJdoi: 10.1073/pnas.1712108114
29529249PERK/eIF2α signaling inhibits HIF-induced gene expression during the unfolded protein response via YB1-dependent regulation of HIF1α translation.Nucleic Acids Res2018 May 4Ivanova IGdoi: 10.1093/nar/gky127.
30637779Long-Read RNA Sequencing Identifies Alternative Splice Variants in Hepatocellular Carcinoma and Tumor-Specific Isoforms.Hepatology2019 Jan 13Chen Hdoi: 10.1002/hep.30500
17967896Identification of internal ribosome entry segment (IRES)-trans-acting factors for the Myc family of IRESs.Mol Cell Biol2008 JanCobbold LC-
24965446Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.J Virol2014 SepJefferson Mdoi: 10.1128/JVI.00984-14
29133115Structural features of the interaction of the 3'-untranslated region of mRNA containing exosomal RNA-specific motifs with YB-1, a potential mediator of mRNA sorting.Biochimie2018 JanYanshina DDdoi: 10.1016/j.biochi.2017.11.007
9488664Identification and molecular cloning of a human selenocysteine insertion sequence-binding protein. A bifunctional role for DNA-binding protein B.J Biol Chem1998 Mar 6Shen Q-
28382490Silencing of Y-box binding protein-1 by RNA interference inhibits proliferation, invasion, and metastasis, and enhances sensitivity to cisplatin through NF-kB signaling pathway in human neuroblastoma SH-SY5Y cells.Mol Cell Biochem2017 SepWang Hdoi: 10.1007/s11010-017-3011-3
29478751YBX1 at the crossroads of non-coding transcriptome, exosomal, and cytoplasmic granular signaling.Eur J Cell Biol2018 AprSuresh PSdoi: 10.1016/j.ejcb.2018.02.003
12168660RNA splicing mediated by YB-1 is inhibited by TLS/CHOP in human myxoid liposarcoma cells.J Orthop Res2002 JulRapp TB-
18395385Increased iron content and RNA oxidative damage in skeletal muscle with aging and disuse atrophy.Exp Gerontol2008 JunHofer Tdoi: 10.1016/j.exger.2008.02.007
18075498Y-box protein-1 controls transforming growth factor-beta1 translation in proximal tubular cells.Kidney Int2008 MarFraser DJ-
17888216Ribosomal P protein P0 as a candidate for the target antigen of anti-endothelial cell antibodies in mixed connective tissue disease.Clin Exp Rheumatol2007 Jul-AugNaniwa T-
21849455Y-box-binding protein 1 interacts with hepatitis C virus NS3/4A and influences the equilibrium between viral RNA replication and infectious particle production.J Virol2011 NovChatel-Chaix Ldoi: 10.1128/JVI.00719-11
23151846miR-137 inhibits the invasion of melanoma cells through downregulation of multiple oncogenic target genes.J Invest Dermatol2013 MarLuo Cdoi: 10.1038/jid.2012.357
27322209Long non-coding RNA stabilizes the Y-box-binding protein 1 and regulates the epidermal growth factor receptor to promote lung carcinogenesis.Oncotarget2016 Sep 13Wei MMdoi: 10.18632/oncotarget.10006.
23986595A host YB-1 ribonucleoprotein complex is hijacked by hepatitis C virus for the control of NS3-dependent particle production.J Virol2013 NovChatel-Chaix Ldoi: 10.1128/JVI.01474-13
27044807Y-box-binding protein 1 promotes tumor progression and inhibits cisplatin chemosensitivity in esophageal squamous cell carcinoma.Biomed Pharmacother2016 AprXu Jdoi: 10.1016/j.biopha.2016.01.037
26121257Pericentriolar Targeting of the Mouse Mammary Tumor Virus GAG Protein.PLoS One2015 Jun 29Zhang Gdoi: 10.1371/journal.pone.0131515
11325824Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein.Cancer Res2001 May 1Chansky HA-
19078965General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation.EMBO J2009 Jan 7Svitkin YVdoi: 10.1038/emboj.2008.259
20974626Nucleic acid sequence-based amplification in formalin-fixed and paraffin-embedded breast-cancer tissues.J Clin Pathol2010 DecRiehle Udoi: 10.1136/jcp.2010.078766
25605055Inhibition of abasic site cleavage in bubble DNA by multifunctional protein YB-1.J Mol Recognit2015 FebFomina EEdoi: 10.1002/jmr.2435
26498684The 5'-untranslated region of p16INK4a melanoma tumor suppressor acts as a cellular IRES, controlling mRNA translation under hypoxia through YBX1 binding.Oncotarget2015 Nov 24Bisio Adoi: 10.18632/oncotarget.5387.
26147853The Cold Shock Domain of YB-1 Segregates RNA from DNA by Non-Bonded Interactions.PLoS One2015 Jul 6Kljashtorny Vdoi: 10.1371/journal.pone.0130318
26102006Constitutive and functional expression of YB-1 in microglial cells.Neuroscience2015 Aug 20Keilhoff Gdoi: 10.1016/j.neuroscience.2015.06.023
29320405Effect of shRNA Mediated Silencing of YB-1 Protein on the Expression of Matrix Collagenases in Malignant Melanoma Cell In Vitro.Cells2018 Jan 10Ibrahim WNdoi: 10.3390/cells7010007.
30286788A novel long noncoding RNA HOXC-AS3 mediates tumorigenesis of gastric cancer by binding to YBX1.Genome Biol2018 Oct 4Zhang Edoi: 10.1186/s13059-018-1523-0.
30470227The long noncoding RNA LINC00312 induces lung adenocarcinoma migration and vasculogenic mimicry through directly binding YBX1.Mol Cancer2018 Nov 23Peng Zdoi: 10.1186/s12943-018-0920-z.
30605522YB-1, an abundant core mRNA-binding protein, has the capacity to form an RNA nucleoprotein filament: a structural analysis.Nucleic Acids Res2019 Apr 8Kretov DAdoi: 10.1093/nar/gky1303.
31106003Long non-coding RNA LINC01133 mediates nasopharyngeal carcinoma tumorigenesis by binding to YBX1.Am J Cancer Res2019 Apr 1Zhang W-
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000332220YBX1-202776-ENSP00000405937216 (aa)-C9J5V9
ENST00000436427YBX1-2031524-ENSP00000389639374 (aa)-H0Y449
ENST00000467957YBX1-204770--- (aa)--
ENST00000321358YBX1-2011514-ENSP00000361626324 (aa)-P67809
Gene Model
Click here to download ENSG00000065978's gene model file
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000065978's network

* RBP PPI network refers to all genes directly bind to RBP
Paralogs
Ensembl IDGene SymbolCoverageIdentiy ParalogGene SymbolCoverageIdentiy
ENSG00000065978YBX18555.034ENSG00000060138YBX37095.312
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000065978YBX110056.105ENSAPOG00000018321ybx110058.944Acanthochromis_polyacanthus
ENSG00000065978YBX18471.691ENSAMEG00000007421-9371.324Ailuropoda_melanoleuca
ENSG00000065978YBX18598.182ENSAMEG00000000494-8998.182Ailuropoda_melanoleuca
ENSG00000065978YBX15057.143ENSAMEG00000008087-6668.687Ailuropoda_melanoleuca
ENSG00000065978YBX19761.442ENSAMEG00000018423-9460.714Ailuropoda_melanoleuca
ENSG00000065978YBX17764.516ENSAMEG00000008685-8558.755Ailuropoda_melanoleuca
ENSG00000065978YBX110058.092ENSACIG00000022321ybx110061.272Amphilophus_citrinellus
ENSG00000065978YBX110058.501ENSAOCG00000009122ybx110058.213Amphiprion_ocellaris
ENSG00000065978YBX110055.233ENSAPEG00000014606ybx110057.771Amphiprion_percula
ENSG00000065978YBX110056.686ENSATEG00000012533ybx110058.430Anabas_testudineus
ENSG00000065978YBX18594.224ENSAPLG00000004899YBX19893.238Anas_platyrhynchos
ENSG00000065978YBX110085.232ENSANAG00000038455-10081.595Aotus_nancymaae
ENSG00000065978YBX110098.457ENSANAG00000022793YBX110098.457Aotus_nancymaae
ENSG00000065978YBX110075.309ENSANAG00000031055-10074.383Aotus_nancymaae
ENSG00000065978YBX110070.062ENSANAG00000035584-10068.519Aotus_nancymaae
ENSG00000065978YBX110058.092ENSACLG00000022705ybx110060.983Astatotilapia_calliptera
ENSG00000065978YBX110066.567ENSAMXG00000014478ybx19268.836Astyanax_mexicanus
ENSG00000065978YBX1100100.000ENSBTAG00000017368YBX1100100.000Bos_taurus
ENSG00000065978YBX1100100.000ENSCJAG00000003155YBX1100100.000Callithrix_jacchus
ENSG00000065978YBX18785.816ENSCAFG00000005471-8985.816Canis_familiaris
ENSG00000065978YBX110099.383ENSCAFG00000002541YBX19099.383Canis_familiaris
ENSG00000065978YBX19366.445ENSCAFG00000030502-9355.305Canis_familiaris
ENSG00000065978YBX19894.937ENSCAFG00000017286-9497.697Canis_familiaris
ENSG00000065978YBX110079.012ENSCAFG00020014118-10078.086Canis_lupus_dingo
ENSG00000065978YBX110099.083ENSCAFG00020024089-10099.083Canis_lupus_dingo
ENSG00000065978YBX110092.593ENSCAFG00020002915YBX110092.593Canis_lupus_dingo
ENSG00000065978YBX18896.335ENSCAFG00020024987-9987.500Canis_lupus_dingo
ENSG00000065978YBX110095.370ENSCHIG00000002879-10095.370Capra_hircus
ENSG00000065978YBX110099.383ENSCHIG00000014169-10099.383Capra_hircus
ENSG00000065978YBX110087.423ENSTSYG00000006915-92100.000Carlito_syrichta
ENSG00000065978YBX18975.261ENSTSYG00000031930-9875.177Carlito_syrichta
ENSG00000065978YBX18389.179ENSCAPG00000006287YBX110089.179Cavia_aperea
ENSG00000065978YBX110099.383ENSCPOG00000010888Ybx110099.383Cavia_porcellus
ENSG00000065978YBX110075.617ENSCCAG00000020730-10075.617Cebus_capucinus
ENSG00000065978YBX19090.411ENSCCAG00000024658-8990.813Cebus_capucinus
ENSG00000065978YBX166100.000ENSCCAG00000025907-10074.691Cebus_capucinus
ENSG00000065978YBX18896.479ENSCCAG00000006015-9996.479Cebus_capucinus
ENSG00000065978YBX110086.992ENSCCAG00000033572-9099.170Cebus_capucinus
ENSG00000065978YBX18793.993ENSCCAG00000024381-10093.993Cebus_capucinus
ENSG00000065978YBX110083.642ENSCATG00000033345-10084.568Cercocebus_atys
ENSG00000065978YBX1100100.000ENSCATG00000016344-100100.000Cercocebus_atys
ENSG00000065978YBX18399.627ENSCLAG00000002253YBX110099.627Chinchilla_lanigera
ENSG00000065978YBX17699.595ENSCSAG00000001168YBX19999.209Chlorocebus_sabaeus
ENSG00000065978YBX18751.736ENSCPBG00000001655-9249.492Chrysemys_picta_bellii
ENSG00000065978YBX110089.231ENSCPBG00000009853-10089.231Chrysemys_picta_bellii
ENSG00000065978YBX18399.628ENSCANG00000035622-9899.628Colobus_angolensis_palliatus
ENSG00000065978YBX110079.321ENSCANG00000027745-9979.705Colobus_angolensis_palliatus
ENSG00000065978YBX19493.421ENSCANG00000032054-9893.310Colobus_angolensis_palliatus
ENSG00000065978YBX110098.765ENSCGRG00001002534Ybx110098.765Cricetulus_griseus_chok1gshd
ENSG00000065978YBX183100.000ENSCGRG00000001303-100100.000Cricetulus_griseus_crigri
ENSG00000065978YBX110054.678ENSCSEG00000019270ybx110061.357Cynoglossus_semilaevis
ENSG00000065978YBX110052.959ENSCVAG00000002318ybx110058.702Cyprinodon_variegatus
ENSG00000065978YBX110069.162ENSDARG00000004757ybx110064.478Danio_rerio
ENSG00000065978YBX19550.855ENSDNOG00000042304-10057.322Dasypus_novemcinctus
ENSG00000065978YBX18673.477ENSDNOG00000049716-8769.176Dasypus_novemcinctus
ENSG00000065978YBX19565.484ENSDNOG00000043057-8568.015Dasypus_novemcinctus
ENSG00000065978YBX110097.685ENSDNOG00000036760-10088.889Dasypus_novemcinctus
ENSG00000065978YBX19546.602ENSDNOG00000046107-9346.230Dasypus_novemcinctus
ENSG00000065978YBX19564.821ENSETEG00000014789-9062.500Echinops_telfairi
ENSG00000065978YBX17699.190ENSETEG00000004125-7699.190Echinops_telfairi
ENSG00000065978YBX17948.744ENSETEG00000002044-7958.152Echinops_telfairi
ENSG00000065978YBX110097.222ENSEASG00005007667-10088.580Equus_asinus_asinus
ENSG00000065978YBX18783.630ENSEASG00005007816-9785.409Equus_asinus_asinus
ENSG00000065978YBX18588.686ENSEASG00005006426-7388.686Equus_asinus_asinus
ENSG00000065978YBX110092.901ENSEASG00005001276-10092.901Equus_asinus_asinus
ENSG00000065978YBX110092.901ENSECAG00000023592YBX110092.901Equus_caballus
ENSG00000065978YBX110068.519ENSECAG00000014432-9858.631Equus_caballus
ENSG00000065978YBX19987.926ENSEEUG00000007494-9187.926Erinaceus_europaeus
ENSG00000065978YBX110064.228ENSEEUG00000005657-9875.934Erinaceus_europaeus
ENSG00000065978YBX1100100.000ENSFCAG00000022604-100100.000Felis_catus
ENSG00000065978YBX18287.594ENSFALG00000010305YBX19488.679Ficedula_albicollis
ENSG00000065978YBX110086.420ENSFDAG00000006047-9198.141Fukomys_damarensis
ENSG00000065978YBX18399.627ENSFDAG00000003679YBX110099.627Fukomys_damarensis
ENSG00000065978YBX110053.116ENSFHEG00000002081ybx110061.357Fundulus_heteroclitus
ENSG00000065978YBX19644.922ENSGMOG00000015216ybx110059.593Gadus_morhua
ENSG00000065978YBX110089.571ENSGALG00000004848YBX110089.877Gallus_gallus
ENSG00000065978YBX110053.709ENSGAFG00000019142ybx110062.537Gambusia_affinis
ENSG00000065978YBX110055.331ENSGACG00000006447ybx110060.641Gasterosteus_aculeatus
ENSG00000065978YBX18849.135ENSGAGG00000002880-8547.482Gopherus_agassizii
ENSG00000065978YBX18795.730ENSGAGG00000022893-7895.730Gopherus_agassizii
ENSG00000065978YBX19792.038ENSGGOG00000023581-9792.459Gorilla_gorilla
ENSG00000065978YBX1100100.000ENSGGOG00000004758YBX1100100.000Gorilla_gorilla
ENSG00000065978YBX110055.102ENSHBUG00000010038ybx110061.765Haplochromis_burtoni
ENSG00000065978YBX110086.769ENSHGLG00000007474-10088.000Heterocephalus_glaber_female
ENSG00000065978YBX110099.691ENSHGLG00000019595YBX110099.691Heterocephalus_glaber_female
ENSG00000065978YBX19379.070ENSHGLG00000010998-9479.016Heterocephalus_glaber_female
ENSG00000065978YBX110081.790ENSHGLG00000017026-10083.951Heterocephalus_glaber_female
ENSG00000065978YBX110074.691ENSHGLG00100015192-10074.074Heterocephalus_glaber_male
ENSG00000065978YBX19976.471ENSHGLG00100015095-9975.232Heterocephalus_glaber_male
ENSG00000065978YBX18398.507ENSHGLG00100013939-10098.507Heterocephalus_glaber_male
ENSG00000065978YBX18656.291ENSHCOG00000017322ybx19259.736Hippocampus_comes
ENSG00000065978YBX160100.000ENSIPUG00000021584ybx110066.667Ictalurus_punctatus
ENSG00000065978YBX18399.628ENSSTOG00000000116YBX19399.628Ictidomys_tridecemlineatus
ENSG00000065978YBX18580.364ENSJJAG00000002819-9178.909Jaculus_jaculus
ENSG00000065978YBX110071.914ENSJJAG00000019196-10070.988Jaculus_jaculus
ENSG00000065978YBX19976.923ENSJJAG00000019501-8174.679Jaculus_jaculus
ENSG00000065978YBX110056.560ENSKMAG00000013012ybx110059.184Kryptolebias_marmoratus
ENSG00000065978YBX110053.314ENSLBEG00000005509ybx110059.312Labrus_bergylta
ENSG00000065978YBX110076.453ENSLACG00000018135YBX110075.841Latimeria_chalumnae
ENSG00000065978YBX18578.246ENSLOCG00000002530ybx19376.632Lepisosteus_oculatus
ENSG00000065978YBX110099.383ENSLAFG00000007597YBX110099.383Loxodonta_africana
ENSG00000065978YBX17490.041ENSLAFG00000031170-10092.116Loxodonta_africana
ENSG00000065978YBX1100100.000ENSMFAG00000040529-100100.000Macaca_fascicularis
ENSG00000065978YBX18774.021ENSMMUG00000043132-9477.857Macaca_mulatta
ENSG00000065978YBX110082.716ENSMMUG00000041539-10081.173Macaca_mulatta
ENSG00000065978YBX110092.284ENSMMUG00000013136-9999.656Macaca_mulatta
ENSG00000065978YBX110099.691ENSMNEG00000044209-10099.691Macaca_nemestrina
ENSG00000065978YBX19485.197ENSMNEG00000029948-9889.753Macaca_nemestrina
ENSG00000065978YBX19481.311ENSMNEG00000041744-9980.212Macaca_nemestrina
ENSG00000065978YBX19976.398ENSMNEG00000034201-9678.882Macaca_nemestrina
ENSG00000065978YBX19971.118ENSMLEG00000040651-9477.143Mandrillus_leucophaeus
ENSG00000065978YBX183100.000ENSMLEG00000012973YBX1100100.000Mandrillus_leucophaeus
ENSG00000065978YBX110059.366ENSMAMG00000018242ybx19860.678Mastacembelus_armatus
ENSG00000065978YBX110054.810ENSMZEG00005020438ybx110060.588Maylandia_zebra
ENSG00000065978YBX18393.309ENSMGAG00000006879YBX110092.937Meleagris_gallopavo
ENSG00000065978YBX110098.769ENSMICG00000014984-10098.769Microcebus_murinus
ENSG00000065978YBX110085.276ENSMICG00000038133-10084.000Microcebus_murinus
ENSG00000065978YBX110087.915ENSMICG00000046432-10088.218Microcebus_murinus
ENSG00000065978YBX19678.846ENSMOCG00000002864-9382.394Microtus_ochrogaster
ENSG00000065978YBX19374.503ENSMOCG00000004348-9471.197Microtus_ochrogaster
ENSG00000065978YBX18686.786ENSMOCG00000010734-9087.410Microtus_ochrogaster
ENSG00000065978YBX18567.119ENSMMOG00000014235ybx19368.439Mola_mola
ENSG00000065978YBX110088.889ENSMODG00000017214YBX110088.889Monodelphis_domestica
ENSG00000065978YBX18951.987ENSMODG00000022963-8154.511Monodelphis_domestica
ENSG00000065978YBX110055.425ENSMALG00000001192ybx19260.738Monopterus_albus
ENSG00000065978YBX110098.148MGP_CAROLIEiJ_G0026396Ybx110098.148Mus_caroli
ENSG00000065978YBX110098.457ENSMUSG00000028639Ybx110098.457Mus_musculus
ENSG00000065978YBX110098.148MGP_PahariEiJ_G0028725Ybx110098.148Mus_pahari
ENSG00000065978YBX110098.457MGP_SPRETEiJ_G0027373Ybx110098.457Mus_spretus
ENSG00000065978YBX110084.685ENSMPUG00000013922-10086.186Mustela_putorius_furo
ENSG00000065978YBX110087.346ENSMLUG00000029452-10087.346Myotis_lucifugus
ENSG00000065978YBX110081.040ENSMLUG00000024638-10081.040Myotis_lucifugus
ENSG00000065978YBX110069.136ENSNGAG00000001099-10066.667Nannospalax_galili
ENSG00000065978YBX110054.227ENSNBRG00000003194ybx110060.588Neolamprologus_brichardi
ENSG00000065978YBX1100100.000ENSNLEG00000012324YBX1100100.000Nomascus_leucogenys
ENSG00000065978YBX19984.211ENSNLEG00000006575-9684.161Nomascus_leucogenys
ENSG00000065978YBX18384.133ENSNLEG00000028962-10084.133Nomascus_leucogenys
ENSG00000065978YBX18395.522ENSOPRG00000008050YBX19995.522Ochotona_princeps
ENSG00000065978YBX110082.407ENSODEG00000004098-10082.099Octodon_degus
ENSG00000065978YBX19886.792ENSODEG00000007841-9585.849Octodon_degus
ENSG00000065978YBX15998.230ENSODEG00000001592-9798.230Octodon_degus
ENSG00000065978YBX110081.173ENSODEG00000001517-10080.864Octodon_degus
ENSG00000065978YBX110071.166ENSODEG00000005696-10070.370Octodon_degus
ENSG00000065978YBX110085.802ENSODEG00000005030-10085.494Octodon_degus
ENSG00000065978YBX19686.859ENSODEG00000003847-9686.885Octodon_degus
ENSG00000065978YBX19983.125ENSODEG00000006802-9684.868Octodon_degus
ENSG00000065978YBX110054.519ENSONIG00000002062ybx110060.882Oreochromis_niloticus
ENSG00000065978YBX18489.420ENSOANG00000011725YBX19889.420Ornithorhynchus_anatinus
ENSG00000065978YBX19785.032ENSOCUG00000021258-9785.032Oryctolagus_cuniculus
ENSG00000065978YBX19945.690ENSOCUG00000000147-7953.695Oryctolagus_cuniculus
ENSG00000065978YBX17799.597ENSOCUG00000028047-10099.597Oryctolagus_cuniculus
ENSG00000065978YBX19969.255ENSOCUG00000022716-9968.944Oryctolagus_cuniculus
ENSG00000065978YBX17658.333ENSOCUG00000021653-10054.902Oryctolagus_cuniculus
ENSG00000065978YBX110085.185ENSOCUG00000026608-10085.185Oryctolagus_cuniculus
ENSG00000065978YBX110082.407ENSOCUG00000024588-8498.750Oryctolagus_cuniculus
ENSG00000065978YBX110054.942ENSORLG00000004225ybx110061.047Oryzias_latipes
ENSG00000065978YBX110054.942ENSORLG00020016155ybx110061.047Oryzias_latipes_hni
ENSG00000065978YBX110054.942ENSORLG00015008023ybx110061.047Oryzias_latipes_hsok
ENSG00000065978YBX110054.942ENSOMEG00000004798ybx110060.756Oryzias_melastigma
ENSG00000065978YBX19568.285ENSOGAG00000031268-9767.327Otolemur_garnettii
ENSG00000065978YBX19150.676ENSOGAG00000027987-8452.846Otolemur_garnettii
ENSG00000065978YBX19750.629ENSOGAG00000032745-7849.091Otolemur_garnettii
ENSG00000065978YBX16274.172ENSOGAG00000024472-9072.727Otolemur_garnettii
ENSG00000065978YBX18354.613ENSOGAG00000030360-9179.545Otolemur_garnettii
ENSG00000065978YBX19853.750ENSOGAG00000025792-9552.288Otolemur_garnettii
ENSG00000065978YBX18971.429ENSOGAG00000032929-8970.854Otolemur_garnettii
ENSG00000065978YBX110078.834ENSOGAG00000014939-9477.451Otolemur_garnettii
ENSG00000065978YBX18670.000ENSOGAG00000030653-9768.214Otolemur_garnettii
ENSG00000065978YBX18459.926ENSOGAG00000034677-9956.727Otolemur_garnettii
ENSG00000065978YBX19657.235ENSOGAG00000031537-9556.066Otolemur_garnettii
ENSG00000065978YBX19362.583ENSOGAG00000027853-9265.900Otolemur_garnettii
ENSG00000065978YBX18262.774ENSOGAG00000024681-9454.693Otolemur_garnettii
ENSG00000065978YBX19994.118ENSOARG00000020447YBX19594.118Ovis_aries
ENSG00000065978YBX110089.815ENSPPAG00000028526-9792.459Pan_paniscus
ENSG00000065978YBX1100100.000ENSPPAG00000030580-100100.000Pan_paniscus
ENSG00000065978YBX19967.601ENSPPAG00000032491-9566.667Pan_paniscus
ENSG00000065978YBX1100100.000ENSPPRG00000014539-100100.000Panthera_pardus
ENSG00000065978YBX18399.627ENSPTIG00000011422YBX18399.627Panthera_tigris_altaica
ENSG00000065978YBX110087.037ENSPTRG00000045241-10086.420Pan_troglodytes
ENSG00000065978YBX19598.710ENSPTRG00000006456-9798.710Pan_troglodytes
ENSG00000065978YBX110089.815ENSPTRG00000043077-10089.198Pan_troglodytes
ENSG00000065978YBX110089.362ENSPTRG00000046217-10089.666Pan_troglodytes
ENSG00000065978YBX18897.183ENSPTRG00000047244-9697.183Pan_troglodytes
ENSG00000065978YBX110089.362ENSPTRG00000052534-10089.666Pan_troglodytes
ENSG00000065978YBX110077.778ENSPANG00000007698-10070.427Papio_anubis
ENSG00000065978YBX189100.000ENSPANG00000016576-99100.000Papio_anubis
ENSG00000065978YBX18792.254ENSPANG00000005177-9792.254Papio_anubis
ENSG00000065978YBX1100100.000ENSPANG00000013156-100100.000Papio_anubis
ENSG00000065978YBX110055.389ENSPKIG00000013063ybx17659.794Paramormyrops_kingsleyae
ENSG00000065978YBX18768.707ENSPKIG00000012488ybx18162.018Paramormyrops_kingsleyae
ENSG00000065978YBX18396.283ENSPSIG00000011017-10096.283Pelodiscus_sinensis
ENSG00000065978YBX18446.886ENSPSIG00000009540-5664.062Pelodiscus_sinensis
ENSG00000065978YBX160100.000ENSPMGG00000007209ybx110065.421Periophthalmus_magnuspinnatus
ENSG00000065978YBX18887.762ENSPEMG00000011569-9089.247Peromyscus_maniculatus_bairdii
ENSG00000065978YBX110091.667ENSPCIG00000009151YBX110091.667Phascolarctos_cinereus
ENSG00000065978YBX19151.125ENSPCIG00000027274-7754.511Phascolarctos_cinereus
ENSG00000065978YBX110055.814ENSPFOG00000011441ybx110061.159Poecilia_formosa
ENSG00000065978YBX110054.545ENSPLAG00000017662ybx110062.537Poecilia_latipinna
ENSG00000065978YBX110053.709ENSPMEG00000015332ybx110062.537Poecilia_mexicana
ENSG00000065978YBX110052.819ENSPREG00000017082ybx110061.357Poecilia_reticulata
ENSG00000065978YBX110096.296ENSPPYG00000001466YBX110096.296Pongo_abelii
ENSG00000065978YBX110092.901ENSPCAG00000008397YBX110092.901Procavia_capensis
ENSG00000065978YBX110086.769ENSPCOG00000021167-10081.682Propithecus_coquereli
ENSG00000065978YBX19590.476ENSPCOG00000022604-9388.350Propithecus_coquereli
ENSG00000065978YBX18285.768ENSPCOG00000019145-9685.019Propithecus_coquereli
ENSG00000065978YBX18597.826ENSPCOG00000009057-9897.826Propithecus_coquereli
ENSG00000065978YBX18991.379ENSPCOG00000025486-9391.549Propithecus_coquereli
ENSG00000065978YBX19586.364ENSPCOG00000025488-9983.660Propithecus_coquereli
ENSG00000065978YBX110083.077ENSPCOG00000025273-10084.308Propithecus_coquereli
ENSG00000065978YBX110084.923ENSPCOG00000023362-10085.263Propithecus_coquereli
ENSG00000065978YBX18883.275ENSPCOG00000022587-9382.394Propithecus_coquereli
ENSG00000065978YBX110098.457ENSPVAG00000005504YBX110098.457Pteropus_vampyrus
ENSG00000065978YBX110054.227ENSPNYG00000010076ybx110060.588Pundamilia_nyererei
ENSG00000065978YBX110068.468ENSPNAG00000028799ybx110067.568Pygocentrus_nattereri
ENSG00000065978YBX110097.222ENSRNOG00000032902Ybx1-ps310097.222Rattus_norvegicus
ENSG00000065978YBX110097.256ENSRNOG00000023786Ybx110097.256Rattus_norvegicus
ENSG00000065978YBX18797.518ENSRBIG00000029840-9997.518Rhinopithecus_bieti
ENSG00000065978YBX110087.037ENSRBIG00000035792-88100.000Rhinopithecus_bieti
ENSG00000065978YBX18795.745ENSRROG00000034332-9995.745Rhinopithecus_roxellana
ENSG00000065978YBX183100.000ENSRROG00000032663YBX183100.000Rhinopithecus_roxellana
ENSG00000065978YBX19997.214ENSRROG00000006964-10097.214Rhinopithecus_roxellana
ENSG00000065978YBX19470.588ENSSBOG00000025607-9968.944Saimiri_boliviensis_boliviensis
ENSG00000065978YBX110077.778ENSSBOG00000006100-10077.469Saimiri_boliviensis_boliviensis
ENSG00000065978YBX110087.346ENSSBOG00000027723-10084.404Saimiri_boliviensis_boliviensis
ENSG00000065978YBX183100.000ENSSBOG00000028808-9879.235Saimiri_boliviensis_boliviensis
ENSG00000065978YBX18781.625ENSSBOG00000027517-10075.000Saimiri_boliviensis_boliviensis
ENSG00000065978YBX18498.155ENSSHAG00000014452YBX19198.155Sarcophilus_harrisii
ENSG00000065978YBX17447.967ENSSHAG00000011350-9945.528Sarcophilus_harrisii
ENSG00000065978YBX110061.905ENSSFOG00015008173ybx110065.282Scleropages_formosus
ENSG00000065978YBX110055.523ENSSMAG00000011351ybx110059.012Scophthalmus_maximus
ENSG00000065978YBX18559.322ENSSDUG00000020859ybx110061.290Seriola_dumerili
ENSG00000065978YBX18559.322ENSSLDG00000024354ybx110070.248Seriola_lalandi_dorsalis
ENSG00000065978YBX176100.000ENSSARG00000007896-76100.000Sorex_araneus
ENSG00000065978YBX19981.677ENSSARG00000012628-9083.489Sorex_araneus
ENSG00000065978YBX18793.793ENSSPUG00000009200YBX110085.546Sphenodon_punctatus
ENSG00000065978YBX110058.841ENSSPAG00000020399ybx110060.290Stegastes_partitus
ENSG00000065978YBX18552.920ENSSSCG00000034021-9553.285Sus_scrofa
ENSG00000065978YBX19699.678ENSSSCG00000028485-8999.576Sus_scrofa
ENSG00000065978YBX19455.700ENSSSCG00000040884-9056.934Sus_scrofa
ENSG00000065978YBX110066.667ENSSSCG00000015308-10065.123Sus_scrofa
ENSG00000065978YBX110088.923ENSTGUG00000017262YBX110088.923Taeniopygia_guttata
ENSG00000065978YBX110056.891ENSTRUG00000024170ybx110059.587Takifugu_rubripes
ENSG00000065978YBX110056.176ENSTNIG00000011989ybx110059.292Tetraodon_nigroviridis
ENSG00000065978YBX110074.899ENSTBEG00000015642-9884.298Tupaia_belangeri
ENSG00000065978YBX110089.970ENSTTRG00000001353-10089.666Tursiops_truncatus
ENSG00000065978YBX110092.284ENSUAMG00000015447YBX110092.284Ursus_americanus
ENSG00000065978YBX18770.922ENSUAMG00000018624-8470.922Ursus_americanus
ENSG00000065978YBX18389.552ENSVPAG00000000068-10089.552Vicugna_pacos
ENSG00000065978YBX19354.783ENSVVUG00000006706-7066.087Vulpes_vulpes
ENSG00000065978YBX110079.573ENSXETG00000013436ybx19188.530Xenopus_tropicalis
ENSG00000065978YBX110054.839ENSXCOG00000003395ybx110062.609Xiphophorus_couchianus
ENSG00000065978YBX110053.709ENSXMAG00000018674ybx110062.537Xiphophorus_maculatus
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0000398mRNA splicing, via spliceosome-TASProcess
GO:0000978RNA polymerase II proximal promoter sequence-specific DNA binding18809583.IDAFunction
GO:0000981DNA-binding transcription factor activity, RNA polymerase II-specific-ISAFunction
GO:0000981DNA-binding transcription factor activity, RNA polymerase II-specific19274049.ISMFunction
GO:0000981DNA-binding transcription factor activity, RNA polymerase II-specific19274049.NASFunction
GO:0001228DNA-binding transcription activator activity, RNA polymerase II-specific18809583.IDAFunction
GO:0003677DNA binding18809583.IDAFunction
GO:0003677DNA binding2977358.8188694.TASFunction
GO:0003690double-stranded DNA binding1738588.TASFunction
GO:0003697single-stranded DNA binding1738588.TASFunction
GO:0003700DNA-binding transcription factor activity3174636.TASFunction
GO:0003723RNA binding22658674.22681889.HDAFunction
GO:0003723RNA binding19561594.IDAFunction
GO:0005515protein binding12674497.15229244.16797541.17289661.17572683.17932509.18335541.18809583.18851979.19174163.20856196.21849455.22118625.22365833.23986595.24965446.25497084.IPIFunction
GO:0005576extracellular region-TASComponent
GO:0005634nucleus3174636.TASComponent
GO:0005654nucleoplasm-TASComponent
GO:0005689U12-type spliceosomal complex15146077.IDAComponent
GO:0005737cytoplasm24965446.IDAComponent
GO:0005829cytosol-IDAComponent
GO:0006355regulation of transcription, DNA-templated18809583.IDAProcess
GO:0006366transcription by RNA polymerase II3174636.TASProcess
GO:0007219Notch signaling pathway-TASProcess
GO:0010494cytoplasmic stress granule18335541.IDAComponent
GO:0031965nuclear membrane-IDAComponent
GO:0043231intracellular membrane-bounded organelle-IDAComponent
GO:0045944positive regulation of transcription by RNA polymerase II18809583.IDAProcess
GO:0051020GTPase binding24337748.IPIFunction
GO:0051781positive regulation of cell division-IEAProcess
GO:0070062extracellular exosome20458337.HDAComponent
GO:0070934CRD-mediated mRNA stabilization19029303.IMPProcess
GO:0070937CRD-mediated mRNA stability complex19029303.IDAComponent
GO:0071204histone pre-mRNA 3'end processing complex-ISSComponent
GO:1903608protein localization to cytoplasmic stress granule24965446.IMPProcess
GO:1990904ribonucleoprotein complex17289661.IDAComponent

Cancer associated literatures
PIDTitleArticle TimeAuthorDoi
20398058Y-box binding protein-1 is a novel molecular target for tumor vessels.Cancer Sci2010 JunTakahashi Mdoi: 10.1111/j.1349-7006.2010.01534.x
26193840The value of cytoplasmic Y-box-binding protein 1 as a prognostic marker for breast cancer in Korean.Breast Cancer2016 SepLee Adoi: 10.1007/s12282-015-0625-8
24443788High prevalence of Y-box protein-1/p18 fragment in plasma of patients with malignancies of different origin.BMC Cancer2014 Jan 20Tacke Fdoi: 10.1186/1471-2407-14-33.
23178914miR-137 restoration sensitizes multidrug-resistant MCF-7/ADM cells to anticancer agents by targeting YB-1.Acta Biochim Biophys Sin (Shanghai)2013 FebZhu Xdoi: 10.1093/abbs/gms099
18809583Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1.Mol Cell Biol2008 DecChattopadhyay Rdoi: 10.1128/MCB.00244-08
29113949Dysregulated Expression of the MicroRNA miR-137 and Its Target YBX1 Contribute to the Invasive Characteristics of Malignant Pleural Mesothelioma.J Thorac Oncol2018 FebJohnson TGdoi: 10.1016/j.jtho.2017.10.016
20011972Discovery of YB-1 as a new immunological target in neuroblastoma by vaccination in the context of regulatory T cell blockade.Acta Biochim Biophys Sin (Shanghai)2009 DecZheng J-
26318844Critical role of phosphorylation of serine 165 of YBX1 on the activation of NF-??B in colon cancer.Oncotarget2015 Oct 6Prabhu Ldoi: 10.18632/oncotarget.5120.
25877750Overexpression of YB1 and EZH2 are associated with cancer metastasis and poor prognosis in renal cell carcinomas.Tumour Biol2015 SepWang Ydoi: 10.1007/s13277-015-3417-z
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19930682Nuclear detection of Y-box protein-1 (YB-1) closely associates with progesterone receptor negativity and is a strong adverse survival factor in human breast cancer.BMC Cancer2009 Nov 24Dahl Edoi: 10.1186/1471-2407-9-410.
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20596676Y-box binding protein 1 is up-regulated in proliferative breast cancer and its inhibition deregulates the cell cycle.Int J Oncol2010 AugYu YN-
20332234Y-box binding protein-1 induces the expression of CD44 and CD49f leading to enhanced self-renewal, mammosphere growth, and drug resistance.Cancer Res2010 Apr 1To Kdoi: 10.1158/0008-5472.CAN-09-3155
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Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr142696801Missense_MutationNAE172K0.09
BLCAchr142700917Missense_MutationnovelE293K0.12
BRCAchr142700837Missense_MutationNAN266S0.43
BRCAchr142696203Missense_MutationNAA90V0.4CSD
CESCchr1427022453'UTRnovel0.19
CESCchr142696898Missense_Mutationrs780773403R204H0.34
CESCchr142697247Missense_MutationnovelR242T0.09
COADchr1427010163'UTRnovel0.16
COADchr142697185SilentNAA221A0.34
COADchr142696711Missense_MutationNAR142C0.26
COADchr142700912Missense_MutationNAR291H0.28
COADchr142683429Missense_MutationnovelW65G0.3CSD
COADchr142700978Missense_Mutationrs141968223S313L0.23
COADchr142696727Missense_MutationNAR147H0.15
ESCAchr142700896Missense_MutationnovelN286D0.12
ESCAchr1427020543'UTRnovel0.13
ESCAchr142700933Missense_MutationnovelQ298L0.34
ESCAchr142696730Missense_Mutationrs772212080Y148C0.37
ESCAchr1427023113'UTRNA0.11
GBMchr142697198Missense_MutationnovelA226T0.07
GBMchr142700900Missense_MutationnovelY287C0.35
HNSCchr142700897Missense_MutationnovelN286S0.34
LIHCchr142697257SilentNAF245F0.31
LUADchr142696679Missense_MutationNAV131A0.44
LUADchr142700999Missense_MutationNAQ320L0.4
LUADchr142701004Missense_Mutationrs780578040G322R0.44
LUSCchr142700988Silentrs371842681P316P0.35
LUSCchr142696235Missense_MutationNAR101C0.69
OVchr142696722SilentnovelY145Y0.06
OVchr142683448Missense_MutationNAG71V0.14CSD
OVchr142696733Missense_MutationNAP149R0.16
OVchr142700988Silentrs371842681P316P0.14
OVchr142697186Missense_MutationNAD222H0.17
PRADchr142697254SilentnovelR244R0.21
PRADchr142696735Missense_MutationnovelR150C0.47
SARCchr1427020543'UTRnovel0.19
SKCMchr142700978Missense_Mutationrs141968223S313L0.29
SKCMchr142700966Missense_Mutationrs753899176P309L0.29
SKCMchr142700914Missense_MutationNAP292S0.15
SKCMchr142696710SilentnovelD141D0.1
STADchr142697237Missense_Mutationrs774310804R239W0.2
STADchr142700861Missense_MutationNAQ274P0.15
STADchr142696646Missense_MutationNAA120V0.32
UCECchr142697212SilentnovelG230G0.1
UCECchr1427020143'UTRnovel0.41
UCECchr142697258Missense_Mutationrs760390285R246C0.51
UCECchr1427022543'UTRnovel0.27
UCECchr142696882Missense_Mutationrs762784015R199W0.48
UCECchr142700905Missense_Mutationrs768111769R289C0.4
UCECchr142700875Missense_Mutationrs371459628R279C0.27
UCECchr142696754Missense_Mutationrs369858905R156H0.51
UCECchr142700807Missense_MutationnovelR256T0.36
UCECchr1427022893'UTRnovel0.31
UCECchr142700914Missense_MutationnovelP292T0.24
UCECchr1427021703'UTRnovel0.35
UCECchr1427022403'UTRnovel0.48
UCECchr142700926Missense_MutationnovelK296E0.06
UCECchr142700912Missense_MutationNAR291H0.31
UCECchr1427021023'UTRnovel0.35
UCECchr142696858SilentnovelR191R0.38
UCECchr1427023293'UTRnovel0.56
UCECchr142696897Missense_MutationnovelR204C0.31
UCECchr142700798Missense_MutationNAR253T0.43
UCECchr142696224Missense_MutationnovelR97M0.2
UCECchr142696235Missense_MutationNAR101C0.35
UCECchr142696767SilentNAQ160Q0.18
UCECchr142683452SilentnovelY72Y0.27
UCECchr142696749SilentnovelP154P0.29
UCECchr142696897Missense_MutationnovelR204C0.23
UCECchr142700814Silentrs752849643D258D0.27
UCECchr142700978Missense_Mutationrs141968223S313L0.2
UCECchr1427020403'UTRnovel0.49
UCECchr142696670Missense_MutationnovelP128L0.23

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
DLBCDEL0.10420.011841
LUADAMP0.18410.040181
PAADAMP0.02720.22288
TGCTDEL0.15330.00046313

Survival Analysis
CancerP-value Q-value
KIRC0.03

Kaplan-Meier Survival Analysis

STAD0.024

Kaplan-Meier Survival Analysis

SARC0.00051

Kaplan-Meier Survival Analysis

MESO0.0026

Kaplan-Meier Survival Analysis

ACC0.0001

Kaplan-Meier Survival Analysis

PRAD0.049

Kaplan-Meier Survival Analysis

KIRP0.0045

Kaplan-Meier Survival Analysis

COAD0.0064

Kaplan-Meier Survival Analysis

PCPG0.041

Kaplan-Meier Survival Analysis

KICH0.0097

Kaplan-Meier Survival Analysis

UCEC0.004

Kaplan-Meier Survival Analysis

GBM0.046

Kaplan-Meier Survival Analysis

LUAD0.03

Kaplan-Meier Survival Analysis

UVM0.02

Kaplan-Meier Survival Analysis

OV0.0055

Kaplan-Meier Survival Analysis

Drugs

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Input Cell Line :


Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742


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