EuRBPDB

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  • RBDs
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Description
Ensembl ID
ENSG00000138668 (Gene tree)
Gene ID
3184
Gene Symbol
HNRNPD
Alias
AUF1|HNRPD
Full Name
heterogeneous nuclear ribonucleoprotein D
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
22,006 bases
Position
chr4:82,352,498-82,374,503
Accession
5036
RBP type
canonical RBP
Summary
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It localizes to both the nucleus and the cytoplasm. This protein is implicated in the regulation of mRNA stability. Alternative splicing of this gene results in four transcript variants. [provided by RefSeq, Jul 2008]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000422615CBFNTPF08143.114.3e-1311
ENSP00000421952CBFNTPF08143.119.9e-1311
ENSP00000313327CBFNTPF08143.111.9e-1211
ENSP00000305860CBFNTPF08143.112.2e-1211
ENSP00000313199CBFNTPF08143.112.4e-1211
ENSP00000425439CBFNTPF08143.110.0001511
ENSP00000420926RRM_1PF00076.221.1e-3512
ENSP00000420926RRM_1PF00076.221.1e-3522
ENSP00000313327RRM_1PF00076.221.9e-3512
ENSP00000313327RRM_1PF00076.221.9e-3522
ENSP00000305860RRM_1PF00076.222.5e-3512
ENSP00000305860RRM_1PF00076.222.5e-3522
ENSP00000313199RRM_1PF00076.222.9e-3512
ENSP00000313199RRM_1PF00076.222.9e-3522
ENSP00000421952RRM_1PF00076.221.3e-2712
ENSP00000421952RRM_1PF00076.221.3e-2722
ENSP00000426666RRM_1PF00076.224.5e-2512
ENSP00000426666RRM_1PF00076.224.5e-2522
ENSP00000422615RRM_1PF00076.223.2e-1711
ENSP00000425439RRM_1PF00076.221.1e-0811
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 RNANascentRICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
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
20926381Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding affinity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands.J Biol Chem2010 Dec 10Zucconi BEdoi: 10.1074/jbc.M110.180182
20102719HuR/methyl-HuR and AUF1 regulate the MAT expressed during liver proliferation, differentiation, and carcinogenesis.Gastroenterology2010 MayVazquez-Chantada Mdoi: 10.1053/j.gastro.2010.01.032
11742537A+U-rich-element RNA-binding factor 1/heterogeneous nuclear ribonucleoprotein D gene expression is regulated by oestrogen in the rat uterus.Biochem J2002 Jan 1Arao Y-
11581272Thermodynamics and kinetics of Hsp70 association with A + U-rich mRNA-destabilizing sequences.J Biol Chem2001 Nov 30Wilson GM-
21733716MKP-1 regulates cytokine mRNA stability through selectively modulation subcellular translocation of AUF1.Cytokine2011 NovYu Hdoi: 10.1016/j.cyto.2011.06.006
20453031Aldosterone and vasopressin affect {alpha}- and {gamma}-ENaC mRNA translation.Nucleic Acids Res2010 SepPerlewitz Adoi: 10.1093/nar/gkq267
30104251Decreased c-Myc mRNA Stability via the MicroRNA 141-3p/AUF1 Axis Is Crucial for p63-and-alpha; Inhibition of Cyclin D1 Gene Transcription and Bladder Cancer Cell Tumorigenicity.Mol Cell Biol2018 Oct 15Li Xdoi: 10.1128/MCB.00273-18
7711075cDNA encoding a chicken protein (CRP1) with homology to hnRNP type A/B.Biochim Biophys Acta1995 Apr 4Cvekl A-
27836661Phosphorylation of poly(rC) binding protein 1 (PCBP1) contributes to stabilization of mu opioid receptor (MOR) mRNA via interaction with AU-rich element RNA-binding protein 1 (AUF1) and poly A binding protein (PABP).Gene2017 Jan 20Hwang CKdoi: 10.1016/j.gene.2016.11.003
10559216Assembly of AUF1 oligomers on U-rich RNA targets by sequential dimer association.J Biol Chem1999 Nov 19Wilson GM-
10080887Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0.J Mol Biol1999 Mar 26Nagata T-
9478192Structural determination in AUF1 required for high affinity binding to A + U-rich elements.Nucleic Acids Symp Ser1997DeMaria CT-
9346902Structural determinants in AUF1 required for high affinity binding to A + U-rich elements.J Biol Chem1997 Oct 31DeMaria CT-
12108548Analysis of the structural determinants for RNA binding of the human protein AUF1/hnRNP D.Biol Chem2002 MayMoraes KC-
11531333Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA.J Mol Biol2001 Aug 31Katahira M-
16782553The role of cytokine mRNA stability in the pathogenesis of autoimmune disease.Autoimmun Rev2006 MaySeko Y-
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-
23131833Picornavirus modification of a host mRNA decay protein.MBio2012 Nov 6Rozovics JMdoi: 10.1128/mBio.00431-12.
16954375Destabilization of interleukin-6 mRNA requires a putative RNA stem-loop structure, an AU-rich element, and the RNA-binding protein AUF1.Mol Cell Biol2006 NovPaschoud S-
22086907Association of the von Hippel-Lindau protein with AUF1 and posttranscriptional regulation of VEGFA mRNA.Mol Cancer Res2012 JanXin Hdoi: 10.1158/1541-7786.MCR-11-0435
23940053Assembly of functional ribonucleoprotein complexes by AU-rich element RNA-binding protein 1 (AUF1) requires base-dependent and -independent RNA contacts.J Biol Chem2013 Sep 27Zucconi BEdoi: 10.1074/jbc.M113.489559
25787750A Huaier polysaccharide reduced metastasis of human hepatocellular carcinoma SMMC-7721 cells via modulating AUF-1 signaling pathway.Tumour Biol2015 AugLi Cdoi: 10.1007/s13277-015-3314-5
25908445The superoxide dismutase 1 3'UTR maintains high expression of the SOD1 gene in cancer cells: The involvement of the RNA-binding protein AUF-1.Free Radic Biol Med2015 AugZhang Sdoi: 10.1016/j.freeradbiomed.2015.04.012
8874185Increased granulocyte-macrophage colony-stimulating factor mRNA instability in cord versus adult mononuclear cells is translation-dependent and associated with increased levels of A + U-rich element binding factor.Blood1996 Oct 15Buzby JS-
10373506Assembly of the alpha-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3' untranslated region determinant and poly(C) binding protein alphaCP.Mol Cell Biol1999 JulChkheidze AN-
11172920Heterogeneous nuclear ribonucleoprotein C binds exclusively to the functionally important UUUUU-motifs in the human papillomavirus type-1 AU-rich inhibitory element.Virus Res2001 MarSokolowski M-
10600550Characterization of the binding of the RNA-binding protein AUF1 to the human AT(1) receptor mRNA.Biochem Biophys Res Commun1999 Dec 20Pende A-
15192077Stability of A+U-rich element binding factor 1 (AUF1)-binding messenger ribonucleic acid correlates with the subcellular relocalization of AUF1 in the rat uterus upon estrogen treatment.Mol Endocrinol2004 SepArao Y-
23066106RNA-binding protein AUF1 represses Dicer expression.Nucleic Acids Res2012 DecAbdelmohsen Kdoi: 10.1093/nar/gks930
18029355Estradiol up-regulates AUF1p45 binding to stabilizing regions within the 3'-untranslated region of estrogen receptor alpha mRNA.J Biol Chem2008 Jan 18Ing NH-
22159912Involvement of the RNA-binding protein ARE/poly(U)-binding factor 1 (AUF1) in the cytotoxic effects of proinflammatory cytokines on pancreatic beta cells.Diabetologia2012 JunRoggli Edoi: 10.1007/s00125-011-2399-7
21917750AU-rich RNA binding proteins in hematopoiesis and leukemogenesis.Blood2011 Nov 24Baou Mdoi: 10.1182/blood-2011-07-347237
21233286Novel mRNA-containing cytoplasmic granules in ALK-transformed cells.Mol Biol Cell2011 Mar 15Fawal Mdoi: 10.1091/mbc.E10-07-0569
20621185Estradiol up-regulates expression of the A + U-rich binding factor 1 (AUF1) gene in the sheep uterus.J Steroid Biochem Mol Biol2010 OctIng NHdoi: 10.1016/j.jsbmb.2010.07.001
24891619RNA-binding protein AUF1 promotes myogenesis by regulating MEF2C expression levels.Mol Cell Biol2014 AugPanda ACdoi: 10.1128/MCB.00423-14
24687816Physiological networks and disease functions of RNA-binding protein AUF1.Wiley Interdiscip Rev RNA2014 Jul-AugMoore AEdoi: 10.1002/wrna.1230
24621334Reduction of TLR4 mRNA stability and protein expressions through inhibiting cytoplasmic translocation of HuR transcription factor by E and/or ER-and-alpha; in LPS-treated H9c2 cardiomyoblast cells.Chin J Physiol2014 Feb 28Fan MJdoi: 10.4077/CJP.2014.BAC197.
27453911RNA-binding Protein Immunoprecipitation (RIP) to Examine AUF1 Binding to Senescence-Associated Secretory Phenotype (SASP) Factor mRNA.Bio Protoc2015 May 20Alspach E-
28929622Endonuclease Regnase-1/Monocyte chemotactic protein-1-induced protein-1 (MCPIP1) in controlling immune responses and beyond.Wiley Interdiscip Rev RNA2018 JanTakeuchi Odoi: 10.1002/wrna.1449
9521873Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms.Genomics1998 Mar 1Wagner BJ-
9199324Adhesion-dependent regulation of an A+U-rich element-binding activity associated with AUF1.Mol Cell Biol1997 JulSirenko OI-
8647811AUF1 binding affinity to A+U-rich elements correlates with rapid mRNA degradation.J Biol Chem1996 May 24DeMaria CT-
8661052Localization and physical mapping of genes encoding the A+U-rich element RNA-binding protein AUF1 to human chromosomes 4 and X.Genomics1996 Jun 1Wagner BJ-
8246982Purification, characterization, and cDNA cloning of an AU-rich element RNA-binding protein, AUF1.Mol Cell Biol1993 DecZhang W-
7959009Characterization of cDNAs encoding the murine A+U-rich RNA-binding protein AUF1.Gene1994 Nov 18Ehrenman K-
10330146Regulation of AUF1 expression via conserved alternatively spliced elements in the 3' untranslated region.Mol Cell Biol1999 JunWilson GM-
7593227Characterization of adenosine-uridine-rich RNA binding factors.J Cell Physiol1995 DecNakamaki T-
16600875Posttranscriptional derepression of GADD45alpha by genotoxic stress.Mol Cell2006 Apr 7Lal A-
16603688JNK activation decreases PP2A regulatory subunit B56alpha expression and mRNA stability and increases AUF1 expression in cardiomyocytes.Am J Physiol Heart Circ Physiol2006 SepGlaser ND-
16569663NMDA induces post-transcriptional regulation of alpha2-guanylyl-cyclase-subunit expression in cerebellar granule cells.J Cell Sci2006 Apr 15Jurado S-
12819195Regulation of A + U-rich element-directed mRNA turnover involving reversible phosphorylation of AUF1.J Biol Chem2003 Aug 29Wilson GM-
12674497Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D).Biol Chem2003 JanMoraes KC-
12625834Identification of S1 proteins B2, C1 and D1 as AUF1 isoforms and their major role as heterogeneous nuclear ribonucleoprotein proteins.Biochem J2003 Jun 15Inoue A-
16514630AUF1-like protein binds specifically to DAS cis-acting element that regulates mouse alpha-fetoprotein gene expression.J Cell Biochem2006 Aug 1Jiao R-
12356764Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27.J Biol Chem2002 Dec 6Shchors K-
11027261Down-regulation of cyclin D1 expression by prostaglandin A(2) is mediated by enhanced cyclin D1 mRNA turnover.Mol Cell Biol2000 NovLin S-
10794726Heterogeneous nuclear ribonucleoprotein D0 contains transactivator and DNA-binding domains.Biochem J2000 May 15Tolnay M-
16291838Increased parathyroid hormone gene expression in secondary hyperparathyroidism of experimental uremia is reversed by calcimimetics: correlation with posttranslational modification of the trans acting factor AUF1.J Am Soc Nephrol2006 JanLevi R-
16109718Interaction of RNA-binding proteins HuR and AUF1 with the human ATF3 mRNA 3'-untranslated region regulates its amino acid limitation-induced stabilization.J Biol Chem2005 Oct 14Pan YX-
15734733Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D.J Biol Chem2005 May 13Enokizono Y-
16834569The ARE-associated factor AUF1 binds poly(A) in vitro in competition with PABP.Biochem J2006 Dec 1Sagliocco F-
15678155Increased stability of the p16 mRNA with replicative senescence.EMBO Rep2005 FebWang W-
15257295Concurrent versus individual binding of HuR and AUF1 to common labile target mRNAs.EMBO J2004 Aug 4Lal A-
14715706Interaction between 3' untranslated region of calcitonin receptor messenger ribonucleic acid (RNA) and adenylate/uridylate (AU)-rich element binding proteins (AU-rich RNA-binding factor 1 and Hu antigen R).Endocrinology2004 AprYasuda S-
20069554Hydrogen peroxide induces p16(INK4a) through an AUF1-dependent manner.J Cell Biochem2010 Apr 1Guo GEdoi: 10.1002/jcb.22474.
19858287Circadian amplitude of cryptochrome 1 is modulated by mRNA stability regulation via cytoplasmic hnRNP D oscillation.Mol Cell Biol2010 JanWoo KCdoi: 10.1128/MCB.01154-09.
19074427Similar regulation of human inducible nitric-oxide synthase expression by different isoforms of the RNA-binding protein AUF1.J Biol Chem2009 Jan 30Pautz Adoi: 10.1074/jbc.M809314200
19033365Identification of a signature motif in target mRNAs of RNA-binding protein AUF1.Nucleic Acids Res2009 JanMazan-Mamczarz Kdoi: 10.1093/nar/gkn929
18348177Characterization of RNA-binding proteins possibly involved in modulating human AT 1 receptor mRNA stability.Cell Biochem Funct2008 JunPende Adoi: 10.1002/cbf.1472.
18240226AUF1, the regulator of tumor necrosis factor alpha messenger RNA decay, is targeted by autoantibodies of patients with systemic rheumatic diseases.Arthritis Rheum2008 FebSkriner Kdoi: 10.1002/art.23306.
17914349Renal response to metabolic acidosis: role of mRNA stabilization.Kidney Int2008 JanIbrahim H-
17878526Post-transcriptional control of the MCT-1-associated protein DENR/DRP by RNA-binding protein AUF1.Cancer Genomics Proteomics2007 May-JunMazan-Mamczarz K-
17825504PLAUF binding to the 3'UTR of the H3.3 histone transcript affects mRNA stability.Gene2007 Dec 30Pulcrano G-
17512931Involvement of RNA binding proteins AUF1 in mammary gland differentiation.Exp Cell Res2007 Aug 1Nagaoka K-
17000771Upf1/Upf2 regulation of 3' untranslated region splice variants of AUF1 links nonsense-mediated and A+U-rich element-mediated mRNA decay.Mol Cell Biol2006 DecBanihashemi L-
22633954mRNA decay factor AUF1 maintains normal aging, telomere maintenance, and suppression of senescence by activation of telomerase transcription.Mol Cell2012 Jul 13Pont ARdoi: 10.1016/j.molcel.2012.04.019
22368252Sequence requirements for RNA binding by HuR and AUF1.J Biochem2012 AprBarker Adoi: 10.1093/jb/mvs010
23303783Combinatorial mRNA binding by AUF1 and Argonaute 2 controls decay of selected target mRNAs.Nucleic Acids Res2013 Feb 1Wu Xdoi: 10.1093/nar/gks1453
21622178Modulation of neoplastic gene regulatory pathways by the RNA-binding factor AUF1.Front Biosci (Landmark Ed)2011 Jun 1Zucconi BE-
21135123RNA-binding protein AUF1 regulates lipopolysaccharide-induced IL10 expression by activating IkappaB kinase complex in monocytes.Mol Cell Biol2011 FebSarkar Sdoi: 10.1128/MCB.00835-10
21161418Regulation of thrombospondin-1 expression through AU-rich elements in the 3'UTR of the mRNA.Cell Mol Biol Lett2011 MarMcGray AJdoi: 10.2478/s11658-010-0037-x
20805360Polyamines regulate the stability of JunD mRNA by modulating the competitive binding of its 3' untranslated region to HuR and AUF1.Mol Cell Biol2010 NovZou Tdoi: 10.1128/MCB.00807-10
23161671Post-transcriptional regulation of CD83 expression by AUF1 proteins.Nucleic Acids Res2013 Jan 7Ehlers Cdoi: 10.1093/nar/gks1069
20489206Leukotriene B(4) BLT receptor signaling regulates the level and stability of cyclooxygenase-2 (COX-2) mRNA through restricted activation of Ras/Raf/ERK/p42 AUF1 pathway.J Biol Chem2010 Jul 30Zhai Bdoi: 10.1074/jbc.M110.107623
20435889MicroRNAs distinguish translational from transcriptional silencing during endotoxin tolerance.J Biol Chem2010 Jul 2El Gazzar Mdoi: 10.1074/jbc.M110.115063
20438856Regulation of the expression of inducible nitric oxide synthase.Nitric Oxide2010 Sep 15Pautz Adoi: 10.1016/j.niox.2010.04.007
25720531AUF-1 and YB-1 independently regulate -and-beta;-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
25231991The cytokine IL-6 reactivates breast stromal fibroblasts through transcription factor STAT3-dependent up-regulation of the RNA-binding protein AUF1.J Biol Chem2014 Nov 7Hendrayani SFdoi: 10.1074/jbc.M114.594044
25261470MicroRNA-141 and microRNA-146b-5p inhibit the prometastatic mesenchymal characteristics through the RNA-binding protein AUF1 targeting the transcription factor ZEB1 and the protein kinase AKT.J Biol Chem2014 Nov 7Al-Khalaf HHdoi: 10.1074/jbc.M114.593004
25148713AUF1 is recruited to the stress granules induced by coxsackievirus B3.Virus Res2014 Nov 4Wu Sdoi: 10.1016/j.virusres.2014.08.003
25078689AUF1 p45 promotes West Nile virus replication by an RNA chaperone activity that supports cyclization of the viral genome.J Virol2014 OctFriedrich Sdoi: 10.1128/JVI.01283-14
24926617p53-directed translational control can shape and expand the universe of p53 target genes.Cell Death Differ2014 OctZaccara Sdoi: 10.1038/cdd.2014.79
24751163Structural determinants of human Zeta-globin mRNA stability.J Hematol Oncol2014 Apr 21He Zdoi: 10.1186/1756-8722-7-35.
24423872AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation.Nucleic Acids Res2014 AprLee KHdoi: 10.1093/nar/gkt1379
27760165The Role of the Trypanosoma cruzi TcNRBD1 Protein in Translation.PLoS One2016 Oct 19Oliveira Cdoi: 10.1371/journal.pone.0164650
27452471Targeted mRNA Decay by RNA Binding Protein AUF1 Regulates Adult Muscle Stem Cell Fate, Promoting Skeletal Muscle Integrity.Cell Rep2016 Aug 2Chenette DMdoi: 10.1016/j.celrep.2016.06.095
27248826The inflammatory/cancer-related IL-6/STAT3/NF-kB positive feedback loop includes AUF1 and maintains the active state of breast myofibroblasts.Oncotarget2016 Jul 5Hendrayani SFdoi: 10.18632/oncotarget.9633.
23572232Cytoplasmic redistribution and cleavage of AUF1 during coxsackievirus infection enhance the stability of its viral genome.FASEB J2013 JulWong Jdoi: 10.1096/fj.12-226498
24213928AU-binding factor 1 expression was correlated with metadherin expression and progression of hepatocellular carcinoma.Tumour Biol2014 MarYang Ydoi: 10.1007/s13277-013-1362-2
281242573'UTR AU-Rich Elements (AREs) and the RNA-Binding Protein Tristetraprolin (TTP) Are Not Required for the LPS-Mediated Destabilization of Phospholipase-C-and-beta;-2 mRNA in Murine Macrophages.Inflammation2017 AprShukla Sdoi: 10.1007/s10753-017-0511-y.
27784781Autotaxin Expression Is Regulated at the Post-transcriptional Level by the RNA-binding Proteins HuR and AUF1.J Biol Chem2016 Dec 9Sun S-
27520967Arginine methylation enhances the RNA chaperone activity of the West Nile virus host factor AUF1 p45.RNA2016 OctFriedrich Sdoi: 10.1261/rna.055269.115
26990999Metformin-mediated increase in DICER1 regulates microRNA expression and cellular senescence.Aging Cell2016 JunNoren Hooten Ndoi: 10.1111/acel.12469
26656491Linc-RoR promotes c-Myc expression through hnRNP I and AUF1.Nucleic Acids Res2016 Apr 20Huang Jdoi: 10.1093/nar/gkv1353
26451954HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 and Promote Virus Translation and Replication.PLoS One2015 Oct 9Lin JYdoi: 10.1371/journal.pone.0140291
25992900Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.Biomolecules2015 May 18Thapar Rdoi: 10.3390/biom5020974.
28542332Non-canonical binding interactions of the RNA recognition motif (RRM) domains of P34 protein modulate binding within the 5S ribonucleoprotein particle (5S RNP).PLoS One2017 May 18Kamina ADdoi: 10.1371/journal.pone.0177890
28986222AUF1 modulates TGF--and-beta; signal in renal tubular epithelial cells via post-transcriptional regulation of Nedd4L expression.Biochim Biophys Acta Mol Cell Res2018 JanYan Jdoi: 10.1016/j.bbamcr.2017.10.001
29263261The Host Factor AUF1 p45 Supports Flavivirus Propagation by Triggering the RNA Switch Required for Viral Genome Cyclization.J Virol2018 Feb 26Friedrich Sdoi: 10.1128/JVI.01647-17
29416775The DNA methyl-transferase protein DNMT1 enhances tumor-promoting properties of breast stromal fibroblasts.Oncotarget2017 Dec 18Al-Kharashi LAdoi: 10.18632/oncotarget.23411
29579397Dicer1 Deficiency in the Idiopathic Pulmonary Fibrosis Fibroblastic Focus Promotes Fibrosis by Suppressing MicroRNA Biogenesis.Am J Respir Crit Care Med2018 Aug 15Herrera Jdoi: 10.1164/rccm.201709-1823OC.
29599909RNA-binding protein AUF1 suppresses miR-122 biogenesis by down-regulating Dicer1 in hepatocellular carcinoma.Oncotarget2018 Jan 9Wu Xdoi: 10.18632/oncotarget.24079
30296408Epigenetic upregulation of miR-126 induced by heat stress contributes to apoptosis of rat cardiomyocytes by promoting Tomm40 transcription.J Mol Cell Cardiol2019 AprWang Xdoi: 10.1016/j.yjmcc.2018.10.005
30524947Critical role of tristetraprolin and AU-rich element RNA-binding protein 1 in the suppression of cancer cell growth by globular adiponectin.FEBS Open Bio2018 Nov 12Tilija Pun Ndoi: 10.1002/2211-5463.12541
30578289The KH-type splicing regulatory protein (KSRP) regulates type III interferon expression post-transcriptionally.Biochem J2019 Jan 31Schmidtke Ldoi: 10.1042/BCJ20180522.
30799487Depletion of the RNA binding protein HNRNPD impairs homologous recombination by inhibiting DNA-end resection and inducing R-loop accumulation.Nucleic Acids Res2019 May 7Alfano Ldoi: 10.1093/nar/gkz076.
30870073METTL3 and ALKBH5 oppositely regulate m6A modification of TFEB mRNA, which dictates the fate of hypoxia/reoxygenation-treated cardiomyocytes.Autophagy2019 AugSong Hdoi: 10.1080/15548627.2019.1586246
30951406The RGG/RG motif of AUF1 isoform p45 is a key modulator of the protein's RNA chaperone and RNA annealing activities.RNA Biol2019 JulMeyer Adoi: 10.1080/15476286.2019.1602438
30993866A telomerase subunit homolog La protein from Trypanosomabrucei plays an essential role in ribosomal biogenesis.FEBS J2019 Apr 16Shan Fdoi: 10.1111/febs.14853
11226575Expression of deletion mutants of the hepatitis B virus protein HBx in E. coli and characterization of their RNA binding activities.Virus Res2001 AprRui E-
11124962Folding of A+U-rich RNA elements modulates AUF1 binding. Potential roles in regulation of mRNA turnover.J Biol Chem2001 Mar 23Wilson GM-
18789946AUF1 is upregulated by angiotensin II to destabilize cardiac Kv4.3 channel mRNA.J Mol Cell Cardiol2008 DecZhou Cdoi: 10.1016/j.yjmcc.2008.08.004
18262561Clonidine-induced enhancement of iNOS expression involves NF-kappaB.J Surg Res2008 SepSu NYdoi: 10.1016/j.jss.2007.11.725
19397786The calcium-sensing receptor regulates parathyroid hormone gene expression in transfected HEK293 cells.BMC Biol2009 Apr 27Galitzer Hdoi: 10.1186/1741-7007-7-17.
19048127A method for purification, identification and validation of DNMT1 mRNA binding proteins.Biol Proced Online2008Unterberger Adoi: 10.1251/bpo142
18413351Members of the NuRD chromatin remodeling complex interact with AUF1 in developing cortical neurons.Cereb Cortex2008 DecLee Cdoi: 10.1093/cercor/bhn051
20412850Thy-1 mRNA destabilization by norepinephrine a 3' UTR cAMP responsive decay element and involves RNA binding proteins.Brain Behav Immun2010 OctLaJevic MDdoi: 10.1016/j.bbi.2010.04.006
16556936Assembly of AUF1 with eIF4G-poly(A) binding protein complex suggests a translation function in AU-rich mRNA decay.RNA2006 MayLu JY-
11514570Structural remodeling of an A + U-rich RNA element by cation or AUF1 binding.J Biol Chem2001 Oct 19Wilson GM-
15459902Expression of the SH2D1A gene is regulated by a combination of transcriptional and post-transcriptional mechanisms.Eur J Immunol2004 NovOkamoto S-
23408619An RNA element in human interleukin 6 confers escape from degradation by the gammaherpesvirus SOX protein.J Virol2013 AprHutin Sdoi: 10.1128/JVI.00159-13
23012480AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus.RNA2012 NovLee Ndoi: 10.1261/rna.034900.112
17626845FRET-detectable interactions between the ARE binding proteins, HuR and p37AUF1.RNA2007 SepDavid PS-
22203679Direct binding of specific AUF1 isoforms to tandem zinc finger domains of tristetraprolin (TTP) family proteins.J Biol Chem2012 Feb 17Kedar VPdoi: 10.1074/jbc.M111.312652
25159612Reduction of AUF1-mediated follistatin mRNA decay during glucose starvation protects cells from apoptosis.Nucleic Acids Res2014Gao Xdoi: 10.1093/nar/gku778
23903828Cellular mRNA decay protein AUF1 negatively regulates enterovirus and human rhinovirus infections.J Virol2013 OctCathcart ALdoi: 10.1128/JVI.01049-13
27578251The long noncoding RNA ASNR regulates degradation of Bcl-2 mRNA through its interaction with AUF1.Sci Rep2016 Aug 31Chen Jdoi: 10.1038/srep32189.
26253535AUF1 promotes let-7b loading on Argonaute 2.Genes Dev2015 Aug 1Yoon JHdoi: 10.1101/gad.263749.115.
30181254Direct and Indirect Effects on Viral Translation and RNA Replication Are Required for AUF1 Restriction of Enterovirus Infections in Human Cells.MBio2018 Sep 4Ullmer Wdoi: 10.1128/mBio.01669-18.
30681073Berberine Promotes Apoptosis of Colorectal Cancer via Regulation of the Long Non-Coding RNA (lncRNA) Cancer Susceptibility Candidate 2 (CASC2)/AU-Binding Factor 1 (AUF1)/B-Cell CLL/Lymphoma 2 (Bcl-2) Axis.Med Sci Monit2019 Jan 25Dai Wdoi: 10.12659/MSM.912082.
31326364Two ways of escaping from oxidative RNA damage: Selective degradation and cell death.DNA Repair (Amst)2019 Jul 8:102666Ishii Tdoi: 10.1016/j.dnarep.2019.102666
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000353341HNRNPD-2031585-ENSP00000313327306 (aa)-Q14103
ENST00000507010HNRNPD-205748-ENSP00000421952221 (aa)-D6RAF8
ENST00000508119HNRNPD-206735--- (aa)--
ENST00000509107HNRNPD-207583-ENSP0000042543992 (aa)-D6RD83
ENST00000514671HNRNPD-2111089-ENSP00000426446210 (aa)-H0YA96
ENST00000503822HNRNPD-204607-ENSP00000422615155 (aa)-D6RBQ9
ENST00000515432HNRNPD-212545-ENSP00000426666111 (aa)-D6RF44
ENST00000352301HNRNPD-2021667-ENSP00000305860336 (aa)-Q14103
ENST00000313899HNRNPD-2013033-ENSP00000313199355 (aa)-Q14103
ENST00000513584HNRNPD-2091240-ENSP0000042400286 (aa)-D6RBP9
ENST00000509263HNRNPD-208782-ENSP00000420926260 (aa)-H0Y8G5
ENST00000514325HNRNPD-2104597--- (aa)--
Gene Model
Click here to download ENSG00000138668's gene model file
Phenotypes
ensgIDTraitpValuePubmed ID
ENSG00000138668Cholesterol, LDL4.3074566117337E-1217903299
GWAS
ensgIDSNPChromosomePositionSNP-risk TraitPubmedID95% CIOr or BEAT EFO ID
ENSG00000138668rs7691121482353055?Morning person30595370EFO_0008328
ENSG00000138668rs6846730482357888CChronotype306968231.0328273EFO_0008328
ENSG00000138668rs6846730482357888CMorning person306968231.0326312EFO_0008328
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000138668's network

* RBP PPI network refers to all genes directly bind to RBP
Paralogs
Ensembl IDGene SymbolCoverageIdentiy ParalogGene SymbolCoverageIdentiy
ENSG00000138668HNRNPD6836.842ENSG00000242389RBMY1E6344.231
ENSG00000138668HNRNPD9943.363ENSG00000120948TARDBP7738.194
ENSG00000138668HNRNPD7837.500ENSG00000213516RBMXL17736.364
ENSG00000138668HNRNPD7734.091ENSG00000119705SLIRP8633.846
ENSG00000138668HNRNPD7837.500ENSG00000147274RBMX8342.857
ENSG00000138668HNRNPD10038.462ENSG00000177733HNRNPA07137.443
ENSG00000138668HNRNPD8231.522ENSG00000179950PUF606731.522
ENSG00000138668HNRNPD6834.667ENSG00000102317RBM38034.109
ENSG00000138668HNRNPD10045.299ENSG00000170144HNRNPA36043.204
ENSG00000138668HNRNPD7330.337ENSG00000188529SRSF105430.337
ENSG00000138668HNRNPD10077.477ENSG00000197451HNRNPAB8368.727
ENSG00000138668HNRNPD9343.662ENSG00000099622CIRBP9155.172
ENSG00000138668HNRNPD7334.667ENSG00000132819RBM389734.667
ENSG00000138668HNRNPD6934.328ENSG00000100461RBM235734.328
ENSG00000138668HNRNPD10052.174ENSG00000135097MSI15247.619
ENSG00000138668HNRNPD5335.593ENSG00000116001TIA18838.182
ENSG00000138668HNRNPD10042.735ENSG00000122566HNRNPA2B17641.176
ENSG00000138668HNRNPD6935.821ENSG00000131051RBM396535.821
ENSG00000138668HNRNPD6836.842ENSG00000234414RBMY1A16344.231
ENSG00000138668HNRNPD10047.059ENSG00000135486HNRNPA19847.059
ENSG00000138668HNRNPD10045.299ENSG00000139675HNRNPA1L27241.475
ENSG00000138668HNRNPD9944.545ENSG00000071626DAZAP16237.681
ENSG00000138668HNRNPD6836.842ENSG00000244395RBMY1D6344.231
ENSG00000138668HNRNPD9034.286ENSG00000136527TRA2B5433.645
ENSG00000138668HNRNPD10077.477ENSG00000152795HNRNPDL9664.583
ENSG00000138668HNRNPD6836.842ENSG00000242875RBMY1B6344.231
ENSG00000138668HNRNPD9932.456ENSG00000143368SF3B45433.333
ENSG00000138668HNRNPD8631.304ENSG00000070756PABPC18931.624
ENSG00000138668HNRNPD9936.170ENSG00000107105ELAVL28930.000
ENSG00000138668HNRNPD10054.783ENSG00000153944MSI28853.488
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000138668HNRNPD10091.892ENSAPOG00000006184hnrnpd9289.474Acanthochromis_polyacanthus
ENSG00000138668HNRNPD100100.000ENSAMEG00000005158HNRNPD10098.113Ailuropoda_melanoleuca
ENSG00000138668HNRNPD10091.892ENSACIG00000008353hnrnpd7986.222Amphilophus_citrinellus
ENSG00000138668HNRNPD10091.892ENSAOCG00000014191hnrnpd9487.814Amphiprion_ocellaris
ENSG00000138668HNRNPD10091.892ENSAPEG00000005603hnrnpd9487.455Amphiprion_percula
ENSG00000138668HNRNPD10090.090ENSATEG00000007097hnrnpd9486.380Anabas_testudineus
ENSG00000138668HNRNPD10096.396ENSACAG00000010342HNRNPD10094.942Anolis_carolinensis
ENSG00000138668HNRNPD100100.000ENSANAG00000035221HNRNPD10099.405Aotus_nancymaae
ENSG00000138668HNRNPD10091.892ENSACLG00000026497hnrnpd10083.077Astatotilapia_calliptera
ENSG00000138668HNRNPD10091.892ENSACLG00000025213hnrnpd9484.229Astatotilapia_calliptera
ENSG00000138668HNRNPD10090.090ENSAMXG00000001477hnrnpd9085.000Astyanax_mexicanus
ENSG00000138668HNRNPD100100.000ENSBTAG00000013952HNRNPD10098.873Bos_taurus
ENSG00000138668HNRNPD100100.000ENSCJAG00000015165HNRNPD10099.405Callithrix_jacchus
ENSG00000138668HNRNPD100100.000ENSCAFG00000025045HNRNPD10099.437Canis_familiaris
ENSG00000138668HNRNPD100100.000ENSCAFG00020010713HNRNPD10099.437Canis_lupus_dingo
ENSG00000138668HNRNPD100100.000ENSCHIG00000022317HNRNPD10098.873Capra_hircus
ENSG00000138668HNRNPD100100.000ENSTSYG00000010395HNRNPD100100.000Carlito_syrichta
ENSG00000138668HNRNPD10082.883ENSCPOG00000040484HNRNPD8689.199Cavia_porcellus
ENSG00000138668HNRNPD100100.000ENSCCAG00000024528HNRNPD10099.405Cebus_capucinus
ENSG00000138668HNRNPD6571.006ENSCCAG00000021563-7271.831Cebus_capucinus
ENSG00000138668HNRNPD100100.000ENSCATG00000039829HNRNPD100100.000Cercocebus_atys
ENSG00000138668HNRNPD100100.000ENSCLAG00000006540HNRNPD92100.000Chinchilla_lanigera
ENSG00000138668HNRNPD100100.000ENSCSAG00000004463HNRNPD100100.000Chlorocebus_sabaeus
ENSG00000138668HNRNPD10099.099ENSCHOG00000000045HNRNPD10099.639Choloepus_hoffmanni
ENSG00000138668HNRNPD100100.000ENSCPBG00000008025HNRNPD8498.556Chrysemys_picta_bellii
ENSG00000138668HNRNPD100100.000ENSCANG00000018501HNRNPD10099.718Colobus_angolensis_palliatus
ENSG00000138668HNRNPD100100.000ENSCGRG00001014634Hnrnpd10097.917Cricetulus_griseus_chok1gshd
ENSG00000138668HNRNPD100100.000ENSCGRG00000007563Hnrnpd9899.639Cricetulus_griseus_crigri
ENSG00000138668HNRNPD10090.991ENSCSEG00000010909hnrnpd8878.648Cynoglossus_semilaevis
ENSG00000138668HNRNPD10089.189ENSCVAG00000019790hnrnpd8880.287Cyprinodon_variegatus
ENSG00000138668HNRNPD10090.090ENSDARG00000059246hnrnpd8986.022Danio_rerio
ENSG00000138668HNRNPD9482.323ENSDNOG00000045079-7375.424Dasypus_novemcinctus
ENSG00000138668HNRNPD100100.000ENSDNOG00000013830-10093.557Dasypus_novemcinctus
ENSG00000138668HNRNPD10072.072ENSDNOG00000041055-6977.841Dasypus_novemcinctus
ENSG00000138668HNRNPD100100.000ENSDORG00000012507Hnrnpd10098.969Dipodomys_ordii
ENSG00000138668HNRNPD100100.000ENSETEG00000016709HNRNPD10092.157Echinops_telfairi
ENSG00000138668HNRNPD100100.000ENSEASG00005016278HNRNPD10099.437Equus_asinus_asinus
ENSG00000138668HNRNPD100100.000ENSECAG00000009344HNRNPD10099.437Equus_caballus
ENSG00000138668HNRNPD100100.000ENSEEUG00000007552HNRNPD10083.099Erinaceus_europaeus
ENSG00000138668HNRNPD10086.486ENSELUG00000003230hnrnpd7782.533Esox_lucius
ENSG00000138668HNRNPD100100.000ENSFCAG00000027404HNRNPD10099.437Felis_catus
ENSG00000138668HNRNPD100100.000ENSFALG00000005716HNRNPD8399.636Ficedula_albicollis
ENSG00000138668HNRNPD100100.000ENSFDAG00000007958HNRNPD8299.278Fukomys_damarensis
ENSG00000138668HNRNPD10088.288ENSFHEG00000006838hnrnpd8882.079Fundulus_heteroclitus
ENSG00000138668HNRNPD10087.387ENSGMOG00000018481hnrnpd8876.596Gadus_morhua
ENSG00000138668HNRNPD10099.099ENSGALG00000011184HNRNPD10098.833Gallus_gallus
ENSG00000138668HNRNPD10089.189ENSGAFG00000003714hnrnpd8785.646Gambusia_affinis
ENSG00000138668HNRNPD10087.387ENSGACG00000015669hnrnpd9479.298Gasterosteus_aculeatus
ENSG00000138668HNRNPD100100.000ENSGAGG00000003656HNRNPD8797.288Gopherus_agassizii
ENSG00000138668HNRNPD100100.000ENSGGOG00000026760HNRNPD95100.000Gorilla_gorilla
ENSG00000138668HNRNPD10091.892ENSHBUG00000011794hnrnpd9484.229Haplochromis_burtoni
ENSG00000138668HNRNPD100100.000ENSHGLG00000004214HNRNPD10092.416Heterocephalus_glaber_female
ENSG00000138668HNRNPD100100.000ENSHGLG00100005996HNRNPD10099.611Heterocephalus_glaber_male
ENSG00000138668HNRNPD10088.288ENSHCOG00000000087hnrnpd8483.254Hippocampus_comes
ENSG00000138668HNRNPD10089.189ENSIPUG00000024954hnrnpd8979.496Ictalurus_punctatus
ENSG00000138668HNRNPD100100.000ENSSTOG00000013970HNRNPD10090.169Ictidomys_tridecemlineatus
ENSG00000138668HNRNPD100100.000ENSJJAG00000023387Hnrnpd9998.639Jaculus_jaculus
ENSG00000138668HNRNPD10091.892ENSKMAG00000004310hnrnpd8882.437Kryptolebias_marmoratus
ENSG00000138668HNRNPD10088.288ENSLBEG00000027508hnrnpd9479.928Labrus_bergylta
ENSG00000138668HNRNPD10098.198ENSLACG00000005306HNRNPD9089.892Latimeria_chalumnae
ENSG00000138668HNRNPD10092.793ENSLOCG00000010743hnrnpd8984.946Lepisosteus_oculatus
ENSG00000138668HNRNPD100100.000ENSLAFG00000016483HNRNPD10099.639Loxodonta_africana
ENSG00000138668HNRNPD100100.000ENSMFAG00000031674HNRNPD100100.000Macaca_fascicularis
ENSG00000138668HNRNPD100100.000ENSMMUG00000039018-100100.000Macaca_mulatta
ENSG00000138668HNRNPD100100.000ENSMNEG00000028199HNRNPD100100.000Macaca_nemestrina
ENSG00000138668HNRNPD100100.000ENSMLEG00000028370HNRNPD100100.000Mandrillus_leucophaeus
ENSG00000138668HNRNPD10090.090ENSMAMG00000004971hnrnpd8883.513Mastacembelus_armatus
ENSG00000138668HNRNPD10091.892ENSMZEG00005007558hnrnpd9484.229Maylandia_zebra
ENSG00000138668HNRNPD10099.099ENSMGAG00000008051HNRNPD10098.837Meleagris_gallopavo
ENSG00000138668HNRNPD100100.000ENSMAUG00000008830Hnrnpd10097.024Mesocricetus_auratus
ENSG00000138668HNRNPD100100.000ENSMICG00000010984HNRNPD88100.000Microcebus_murinus
ENSG00000138668HNRNPD100100.000ENSMOCG00000021398Hnrnpd10096.131Microtus_ochrogaster
ENSG00000138668HNRNPD10089.189ENSMMOG00000008627hnrnpd9479.570Mola_mola
ENSG00000138668HNRNPD10099.107ENSMODG00000011898HNRNPD7999.662Monodelphis_domestica
ENSG00000138668HNRNPD10090.991ENSMALG00000016024hnrnpd8986.331Monopterus_albus
ENSG00000138668HNRNPD100100.000MGP_CAROLIEiJ_G0027446Hnrnpd100100.000Mus_caroli
ENSG00000138668HNRNPD100100.000ENSMUSG00000000568Hnrnpd100100.000Mus_musculus
ENSG00000138668HNRNPD100100.000MGP_PahariEiJ_G0017224Hnrnpd100100.000Mus_pahari
ENSG00000138668HNRNPD100100.000MGP_SPRETEiJ_G0028443Hnrnpd100100.000Mus_spretus
ENSG00000138668HNRNPD100100.000ENSMPUG00000014782HNRNPD100100.000Mustela_putorius_furo
ENSG00000138668HNRNPD99100.000ENSMLUG00000010628HNRNPD10089.859Myotis_lucifugus
ENSG00000138668HNRNPD100100.000ENSNGAG00000013451Hnrnpd10097.024Nannospalax_galili
ENSG00000138668HNRNPD10091.892ENSNBRG00000019548hnrnpd9484.229Neolamprologus_brichardi
ENSG00000138668HNRNPD100100.000ENSNLEG00000008600HNRNPD10094.366Nomascus_leucogenys
ENSG00000138668HNRNPD71100.000ENSMEUG00000006804-58100.000Notamacropus_eugenii
ENSG00000138668HNRNPD100100.000ENSOPRG00000009336HNRNPD10083.193Ochotona_princeps
ENSG00000138668HNRNPD100100.000ENSODEG00000001897HNRNPD10092.113Octodon_degus
ENSG00000138668HNRNPD10091.892ENSONIG00000015390hnrnpd9484.229Oreochromis_niloticus
ENSG00000138668HNRNPD10099.099ENSOANG00000001932HNRNPD10099.611Ornithorhynchus_anatinus
ENSG00000138668HNRNPD100100.000ENSOCUG00000001357HNRNPD10099.278Oryctolagus_cuniculus
ENSG00000138668HNRNPD10088.288ENSORLG00000001833hnrnpd9484.364Oryzias_latipes
ENSG00000138668HNRNPD10087.387ENSORLG00020014780hnrnpd8383.636Oryzias_latipes_hni
ENSG00000138668HNRNPD10088.288ENSORLG00015002382hnrnpd9484.364Oryzias_latipes_hsok
ENSG00000138668HNRNPD10089.189ENSOMEG00000018558hnrnpd9480.727Oryzias_melastigma
ENSG00000138668HNRNPD100100.000ENSOGAG00000004075HNRNPD10098.592Otolemur_garnettii
ENSG00000138668HNRNPD100100.000ENSOARG00000000579HNRNPD100100.000Ovis_aries
ENSG00000138668HNRNPD100100.000ENSPPAG00000035750HNRNPD100100.000Pan_paniscus
ENSG00000138668HNRNPD100100.000ENSPPRG00000012258HNRNPD10099.437Panthera_pardus
ENSG00000138668HNRNPD100100.000ENSPTIG00000019434HNRNPD10099.672Panthera_tigris_altaica
ENSG00000138668HNRNPD100100.000ENSPTRG00000016215HNRNPD10099.719Pan_troglodytes
ENSG00000138668HNRNPD100100.000ENSPANG00000011785HNRNPD100100.000Papio_anubis
ENSG00000138668HNRNPD10091.892ENSPKIG00000025512hnrnpd8983.571Paramormyrops_kingsleyae
ENSG00000138668HNRNPD100100.000ENSPSIG00000017029HNRNPD9398.723Pelodiscus_sinensis
ENSG00000138668HNRNPD10085.586ENSPMGG00000017169hnrnpd7680.628Periophthalmus_magnuspinnatus
ENSG00000138668HNRNPD100100.000ENSPEMG00000014804Hnrnpd8799.639Peromyscus_maniculatus_bairdii
ENSG00000138668HNRNPD100100.000ENSPCIG00000003112HNRNPD7999.661Phascolarctos_cinereus
ENSG00000138668HNRNPD10089.189ENSPFOG00000002596hnrnpd8879.928Poecilia_formosa
ENSG00000138668HNRNPD10089.189ENSPLAG00000004297hnrnpd8879.928Poecilia_latipinna
ENSG00000138668HNRNPD10089.189ENSPMEG00000000152hnrnpd8879.928Poecilia_mexicana
ENSG00000138668HNRNPD10089.189ENSPREG00000018081hnrnpd9577.778Poecilia_reticulata
ENSG00000138668HNRNPD100100.000ENSPPYG00000014885HNRNPD100100.000Pongo_abelii
ENSG00000138668HNRNPD10088.525ENSPPYG00000020411-9981.529Pongo_abelii
ENSG00000138668HNRNPD10097.191ENSPCAG00000002182HNRNPD10097.191Procavia_capensis
ENSG00000138668HNRNPD100100.000ENSPCOG00000021331HNRNPD10099.437Propithecus_coquereli
ENSG00000138668HNRNPD100100.000ENSPVAG00000000003HNRNPD10098.592Pteropus_vampyrus
ENSG00000138668HNRNPD10091.892ENSPNYG00000004884hnrnpd9484.229Pundamilia_nyererei
ENSG00000138668HNRNPD10090.991ENSPNAG00000016368hnrnpd8980.797Pygocentrus_nattereri
ENSG00000138668HNRNPD10099.099ENSRNOG00000002292Hnrnpd10096.732Rattus_norvegicus
ENSG00000138668HNRNPD100100.000ENSRBIG00000035345HNRNPD100100.000Rhinopithecus_bieti
ENSG00000138668HNRNPD100100.000ENSRROG00000011888HNRNPD100100.000Rhinopithecus_roxellana
ENSG00000138668HNRNPD100100.000ENSSBOG00000032881HNRNPD10099.702Saimiri_boliviensis_boliviensis
ENSG00000138668HNRNPD100100.000ENSSHAG00000013312HNRNPD100100.000Sarcophilus_harrisii
ENSG00000138668HNRNPD10090.991ENSSFOG00015005913hnrnpd8985.000Scleropages_formosus
ENSG00000138668HNRNPD10089.189ENSSMAG00000009686hnrnpd8880.714Scophthalmus_maximus
ENSG00000138668HNRNPD10090.991ENSSDUG00000010792hnrnpd9487.097Seriola_dumerili
ENSG00000138668HNRNPD9891.743ENSSLDG00000015962hnrnpd8878.495Seriola_lalandi_dorsalis
ENSG00000138668HNRNPD100100.000ENSSARG00000006883HNRNPD10098.195Sorex_araneus
ENSG00000138668HNRNPD10099.099ENSSPUG00000013677HNRNPD10093.385Sphenodon_punctatus
ENSG00000138668HNRNPD10091.892ENSSPAG00000021014hnrnpd9289.474Stegastes_partitus
ENSG00000138668HNRNPD100100.000ENSSSCG00000009249HNRNPD10098.512Sus_scrofa
ENSG00000138668HNRNPD100100.000ENSTGUG00000002858HNRNPD9093.220Taeniopygia_guttata
ENSG00000138668HNRNPD10090.090ENSTRUG00000018450hnrnpd8877.899Takifugu_rubripes
ENSG00000138668HNRNPD10087.500ENSTNIG00000013499hnrnpd9581.517Tetraodon_nigroviridis
ENSG00000138668HNRNPD10091.892ENSTBEG00000002327HNRNPD10094.946Tupaia_belangeri
ENSG00000138668HNRNPD100100.000ENSTTRG00000007592HNRNPD10099.437Tursiops_truncatus
ENSG00000138668HNRNPD100100.000ENSUAMG00000011374HNRNPD75100.000Ursus_americanus
ENSG00000138668HNRNPD100100.000ENSUMAG00000008685HNRNPD84100.000Ursus_maritimus
ENSG00000138668HNRNPD100100.000ENSVPAG00000004374HNRNPD100100.000Vicugna_pacos
ENSG00000138668HNRNPD100100.000ENSVVUG00000024658HNRNPD10099.437Vulpes_vulpes
ENSG00000138668HNRNPD10096.396ENSXETG00000012569hnrnpd9481.949Xenopus_tropicalis
ENSG00000138668HNRNPD10089.189ENSXCOG00000017639hnrnpd10078.846Xiphophorus_couchianus
ENSG00000138668HNRNPD10089.189ENSXMAG00000019151hnrnpd8979.570Xiphophorus_maculatus
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0000398mRNA splicing, via spliceosome-TASProcess
GO:0001889liver development-IEAProcess
GO:0003680AT DNA binding21873635.IBAFunction
GO:0003682chromatin binding-IEAFunction
GO:0003723RNA binding22658674.22681889.HDAFunction
GO:0003723RNA binding21873635.IBAFunction
GO:0003723RNA binding8321232.IDAFunction
GO:0003723RNA binding3754960.NASFunction
GO:0003729mRNA binding21873635.IBAFunction
GO:0005515protein binding12107167.22365833.23603392.24423872.26496610.30021884.IPIFunction
GO:0005634nucleus21873635.IBAComponent
GO:0005634nucleus1433497.NASComponent
GO:0005654nucleoplasm21873635.IBAComponent
GO:0005654nucleoplasm-IDAComponent
GO:0005654nucleoplasm-TASComponent
GO:0005829cytosol-TASComponent
GO:0006355regulation of transcription, DNA-templated1433497.NASProcess
GO:0006396RNA processing10205060.TASProcess
GO:0006401RNA catabolic process10205060.TASProcess
GO:0008134transcription factor binding-IEAFunction
GO:0016070RNA metabolic process-TASProcess
GO:0021549cerebellum development-IEAProcess
GO:0032204regulation of telomere maintenance-ISSProcess
GO:0035925mRNA 3'-UTR AU-rich region binding21873635.IBAFunction
GO:0042162telomeric DNA binding8321232.IDAFunction
GO:0042752regulation of circadian rhythm24423872.IMPProcess
GO:0042826histone deacetylase binding-IEAFunction
GO:0043488regulation of mRNA stability-TASProcess
GO:0043565sequence-specific DNA binding21873635.IBAFunction
GO:0045202synapse-IEAComponent
GO:0045727positive regulation of translation24423872.IMPProcess
GO:0045893positive regulation of transcription, DNA-templated1433497.NASProcess
GO:0048255mRNA stabilization-IEAProcess
GO:0051592response to calcium ion-IEAProcess
GO:0051602response to electrical stimulus-IEAProcess
GO:00611583'-UTR-mediated mRNA destabilization-IEAProcess
GO:0071230cellular response to amino acid stimulus-IEAProcess
GO:0071392cellular response to estradiol stimulus-IEAProcess
GO:0071732cellular response to nitric oxide-IEAProcess
GO:0097167circadian regulation of translation24423872.IMPProcess
GO:1901355response to rapamycin-IEAProcess
GO:1904355positive regulation of telomere capping-ISSProcess
GO:1904383response to sodium phosphate-IEAProcess
GO:1904586cellular response to putrescine-IEAProcess
GO:1905663positive regulation of telomerase RNA reverse transcriptase activity-ISSProcess
GO:1990828hepatocyte dedifferentiation-IEAProcess
GO:1990837sequence-specific double-stranded DNA binding21873635.IBAFunction
GO:1990904ribonucleoprotein complex21873635.IBAComponent
GO:1990904ribonucleoprotein complex17289661.IDAComponent

Cancer associated literatures
PIDTitleArticle TimeAuthorDoi
14585195Increased interleukin-10 mRNA stability in melanoma cells is associated with decreased levels of A + U-rich element binding factor AUF1.J Interferon Cytokine Res2003 OctBrewer G-
26805816Unraveling Molecular Differences of Gastric Cancer by Label-Free Quantitative Proteomics Analysis.Int J Mol Sci2016 Jan 21Dai Pdoi: 10.3390/ijms17010069.
25908445The superoxide dismutase 1 3'UTR maintains high expression of the SOD1 gene in cancer cells: The involvement of the RNA-binding protein AUF-1.Free Radic Biol Med2015 AugZhang Sdoi: 10.1016/j.freeradbiomed.2015.04.012
26318153Nuclear heterogeneous nuclear ribonucleoprotein D is associated with poor prognosis and interactome analysis reveals its novel binding partners in oral cancer.J Transl Med2015 Aug 30Kumar Mdoi: 10.1186/s12967-015-0637-3.
27784781Autotaxin Expression Is Regulated at the Post-transcriptional Level by the RNA-binding Proteins HuR and AUF1.J Biol Chem2016 Dec 9Sun S-
27248826The inflammatory/cancer-related IL-6/STAT3/NF-??B positive feedback loop includes AUF1 and maintains the active state of breast myofibroblasts.Oncotarget2016 Jul 5Hendrayani SFdoi: 10.18632/oncotarget.9633.

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr482356859Missense_MutationnovelQ264E0.39
BLCAchr482357358SilentnovelV236V0.28
BLCAchr482356619Frame_Shift_InsnovelY307Ifs*20.11
BLCAchr482355271Intronnovel0.46
BLCAchr482359520Nonsense_MutationnovelS137*0.83
BLCAchr482359550Missense_MutationNAT127I0.25
BRCAchr482356542Missense_MutationNAY332C0.71
CESCchr4823537823'UTRnovel0.43
CESCchr4823738595'UTRnovel1
CESCchr4823536593'UTRnovel0.09
CESCchr482358740Silentrs747143356P180P0.19
CESCchr4823738775'UTRnovel0.23
CESCchr482356855Frame_Shift_InsnovelQ265Lfs*80.15
COADchr482356811Missense_MutationNAR280C0.2
COADchr482373502Silentrs374147423G59G0.34
COADchr482358752Missense_MutationnovelK176N0.34
COADchr482358754Missense_MutationnovelK176Q0.26
COADchr482356601SilentNAY312Y0.28
COADchr482358715Missense_MutationnovelL189I0.21
COADchr482373530In_Frame_DelnovelG49_G50del0.24
COADchr482355350Missense_MutationnovelS351N0.31
COADchr482358816Missense_MutationnovelM155T0.35
DLBCchr482373530Missense_MutationnovelG50E0.28
DLBCchr482373603Nonsense_MutationnovelQ26*0.3
ESCAchr482358782SilentnovelV166V0.08
ESCAchr482357396Missense_MutationnovelG224R0.3
HNSCchr482358657Splice_SitenovelX207_splice0.23
HNSCchr482359579Missense_MutationnovelF117L0.23
HNSCchr482359581Frame_Shift_InsnovelF117Vfs*60.37
HNSCchr482358694Missense_MutationnovelE196Q0.38
KIRCchr482359560Missense_MutationNAV124I0.19
KIRPchr482355296Splice_Regionnovel0.24
KIRPchr482358688Missense_MutationnovelI198V0.48
LIHCchr482356866Frame_Shift_InsnovelQ262Tfs*110.18
LIHCchr482373565SilentnovelA38A0.1
LUADchr482358740SilentNAP180P0.32
LUADchr482356872Frame_Shift_DelnovelK260Rfs*1090.24
LUADchr482356573Missense_MutationnovelG322C0.33
LUADchr482355370Missense_MutationNAR344S0.15
LUSCchr482359523Missense_MutationnovelR136P0.12
LUSCchr482359514Frame_Shift_DelnovelG139Vfs*130.58
LUSCchr482357441Nonsense_MutationNAE209*0.82
LUSCchr482355372SilentnovelR344R0.2
OVchr482356893Splice_RegionNAC252C0.29
OVchr482356589SilentnovelG316G0.07
READchr482355344Missense_MutationnovelK353T0.06
READchr482358752Missense_MutationnovelK176N0.05
SARCchr482359577Missense_MutationnovelS118F0.41
SARCchr482357420Missense_MutationnovelD216H0.18
SKCMchr4823553273'UTRnovel0.36
SKCMchr482356850Missense_MutationnovelQ267E0.23
SKCMchr482356552Missense_MutationNAY329H0.29
SKCMchr482356873Missense_MutationnovelS259L0.26
STADchr482355302Splice_SiteNA0.38
STADchr482356876Missense_MutationnovelM258T0.11
THCAchr482359574Missense_MutationnovelK119R0.19
UCECchr482358777Missense_MutationnovelD168G0.17
UCECchr4823537433'UTRrs1422464310.29
UCECchr482359516Missense_MutationnovelR138S0.36
UCECchr4823540963'UTRnovel0.39
UCECchr482356872Silentrs760389308S259S0.07
UCECchr482355010Intronnovel0.33
UCECchr482358658Splice_SitenovelX207_splice0.28
UCECchr4823535873'UTRnovel0.29
UCECchr482357441Missense_MutationNAE209K0.19
UCECchr482357398Missense_MutationnovelR223H0.17
UCECchr482358730Frame_Shift_DelNAI184Ffs*150.4
UCECchr4823539173'UTRnovel0.43
UCECchr482357345Missense_MutationnovelE241K0.31
UCECchr482358805Nonsense_MutationnovelE159*0.5
UCECchr482354981Intronnovel0.44
UCECchr4823540473'UTRnovel0.33
UCECchr482356600Missense_MutationnovelG313S0.3
UCECchr482358729Missense_Mutationrs777691534I184N0.31
UCECchr482355127Intronnovel0.21
UCECchr4823539983'UTRnovel0.44
UCECchr482354899Intronnovel0.42
UCECchr482358805Nonsense_MutationnovelE159*0.45
UCECchr482373463Missense_MutationnovelK72N0.11CBFNT
UCECchr482354938Intronnovel0.2
UCECchr482356834Missense_MutationNAR272K0.33
UCECchr4823540453'UTRnovel0.32
UCECchr482358754Nonsense_MutationnovelK176*0.33
UCECchr482356855Nonsense_MutationNAY263_Q265delins*0.49
UCECchr482355001Intronrs7740732090.22
UCECchr4823537433'UTRrs1422464310.22
UCECchr4823540003'UTRnovel0.1
UCECchr4823538693'UTRnovel0.48
UCECchr482355354Missense_MutationnovelN350H0.35
UCECchr482354927Intronnovel0.25
UCECchr482355170Intronnovel0.15
UCECchr482357340Missense_MutationNAK242N0.25
UCECchr482358731Missense_MutationNAK183N0.11
UCECchr4823538213'UTRnovel0.48
UCECchr482356672Frame_Shift_InsnovelN289Efs*70.04
UCECchr482356673Frame_Shift_InsnovelQ288Hfs*150.04
UCECchr482355208Intronnovel0.08
UCECchr482357353Missense_MutationnovelK238T0.3
UCECchr482373444Splice_SitenovelX78_splice0.28
UCECchr482359573Frame_Shift_DelnovelK119Nfs*60.4
UCECchr482358730Frame_Shift_DelNAI184Ffs*150.31
UCECchr482358805Nonsense_MutationnovelE159*0.35
UCECchr482359523Missense_MutationnovelR136Q0.38
UCSchr482358731Missense_MutationnovelK183N0.22
UCSchr482359486Silentrs750707981S148S0.36

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
LIHCDEL0.42433.0903e-07
LUADDEL0.18990.050802
MESODEL0.39080.075661

Survival Analysis
CancerP-value Q-value
THYM0.0028

Kaplan-Meier Survival Analysis

SARC0.0099

Kaplan-Meier Survival Analysis

ACC0.00013

Kaplan-Meier Survival Analysis

PRAD0.013

Kaplan-Meier Survival Analysis

BRCA0.025

Kaplan-Meier Survival Analysis

ESCA0.027

Kaplan-Meier Survival Analysis

KIRP0.03

Kaplan-Meier Survival Analysis

PAAD0.028

Kaplan-Meier Survival Analysis

BLCA0.016

Kaplan-Meier Survival Analysis

CESC0.0091

Kaplan-Meier Survival Analysis

LIHC0.00069

Kaplan-Meier Survival Analysis

LUAD0.015

Kaplan-Meier Survival Analysis

OV0.02

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742


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