EuRBPDB

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  • Description
  • RBDs
  • RBPome
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • Phenotypes
  • GWAS
  • PPI
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000108256 (Gene tree)
Gene ID
57532
Gene Symbol
NUFIP2
Alias
KIAA1321|MGC117262|PIG1|182-FIP|FIP-82|82-FIP
Full Name
nuclear FMR1 interacting protein 2
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
38,313 bases
Position
chr17:29,255,836-29,294,148
Accession
17634
RBP type
canonical RBP
Summary
(Nuclear FMR1 Interacting Protein 2) is a Protein Coding gene. Diseases associated with NUFIP2 include Chromosome 17Q11.2 Deletion Syndrome, 1.4-Mb. Gene Ontology (GO) annotations related to this gene include RNA binding.
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000225388NUFIP2PF15293.65.4e-29711
ENSP00000463450NUFIP2PF15293.63e-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 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
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
15805463Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes.Genes Dev2005 Apr 15Darnell JC-
31289466Role of caprin-1 in carcinogenesis.Oncol Lett2019 JulYang ZSdoi: 10.3892/ol.2019.10295
19166269A novel function for fragile X mental retardation protein in translational activation.PLoS Biol2009 Jan 20Bechara EGdoi: 10.1371/journal.pbio.1000016.
17170008Fragile X related protein 1 isoforms differentially modulate the affinity of fragile X mental retardation protein for G-quartet RNA structure.Nucleic Acids Res2007Bechara E-
20570707The role of G-quadruplex in RNA metabolism: involvement of FMRP and FMR2P.Biochimie2010 AugMelko Mdoi: 10.1016/j.biochi.2010.05.018
24462888Fragile X Syndrome: from molecular pathology to therapy.Neurosci Biobehav Rev2014 OctMaurin Tdoi: 10.1016/j.neubiorev.2014.01.006
29352114Binding of NUFIP2 to Roquin promotes recognition and regulation of ICOS mRNA.Nat Commun2018 Jan 19Rehage Ndoi: 10.1038/s41467-017-02582-1.
16418001RNA binding proteins and the regulation of neuronal synaptic plasticity.Curr Opin Neurobiol2006 FebUle J-
17923234Analysis of mRNA translation in cultured hippocampal neurons.Methods Enzymol2007Huang YS-
26851502Neuron class-specific requirements for Fragile X Mental Retardation Protein in critical period development of calcium signaling in learning and memory circuitry.Neurobiol Dis2016 MayDoll CAdoi: 10.1016/j.nbd.2016.02.006
10546896Biology of the fragile X mental retardation protein, an RNA-binding protein.Biochem Cell Biol1999Khandjian EW-
10556305A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein.Hum Mol Genet1999 DecBardoni B-
9624140Purified recombinant Fmrp exhibits selective RNA binding as an intrinsic property of the fragile X mental retardation protein.J Biol Chem1998 Jun 19Brown V-
9030614Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes.J Neurosci1997 Mar 1Feng Y-
8895584A nuclear role for the Fragile X mental retardation protein.EMBO J1996 Oct 1Fridell RA-
16636078Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP.J Cell Sci2006 May 1Dolzhanskaya N-
16571602The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons.Hum Mol Genet2006 May 1Davidovic L-
12950170The N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding.Biochemistry2003 Sep 9Adinolfi S-
12594214The fragile X mental retardation protein FMRP binds elongation factor 1A mRNA and negatively regulates its translation in vivo.J Biol Chem2003 May 2Sung YJ-
16510718Fragile X mental retardation protein shifts between polyribosomes and stress granules after neuronal injury by arsenite stress or in vivo hippocampal electrode insertion.J Neurosci2006 Mar 1Kim SH-
12417522Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression.Hum Mol Genet2002 Nov 15Mazroui R-
12378270Methylation of the arginine-glycine-rich region in the fragile X mental retardation protein FMRP differentially affects RNA binding.Cell Mol Biol Lett2002Denman RB-
11440196Subcellular localization of fragile X mental retardation protein with the I304N mutation in the RNA-binding domain in cultured hippocampal neurons.Cell Mol Neurobiol2001 FebCastren M-
11039725Sensory stimulation increases cortical expression of the fragile X mental retardation protein in vivo.Brain Res Mol Brain Res2000 Aug 14Todd PK-
16006558Fragile X mental retardation protein (FMRP) binds specifically to the brain cytoplasmic RNAs BC1/BC200 via a novel RNA-binding motif.J Biol Chem2005 Sep 30Zalfa F-
15548614Fragile X mental retardation protein is necessary for neurotransmitter-activated protein translation at synapses.Proc Natl Acad Sci U S A2004 Dec 14Weiler IJ-
15516998RNA and microRNAs in fragile X mental retardation.Nat Cell Biol2004 NovJin P-
16809002The RNA binding and transport proteins staufen and fragile X mental retardation protein are expressed by rat primary afferent neurons and localize to peripheral and central axons.Neuroscience2006 Sep 15Price TJ-
15317853Fragile X mental retardation protein is associated with translating polyribosomes in neuronal cells.J Neurosci2004 Aug 18Stefani G-
15183715The Drosophila fragile X-related gene regulates axoneme differentiation during spermatogenesis.Dev Biol2004 Jun 15Zhang YQ-
14532325Fragile X Mental Retardation protein determinants required for its association with polyribosomal mRNPs.Hum Mol Genet2003 Dec 1Mazroui R-
23401597Expression of fragile X mental retardation protein and Fmr1 mRNA during folliculogenesis in the rat.Reproduction2013 Apr 15Ferder Idoi: 10.1530/REP-12-0305
23115170Regulation of neuronal excitability by interaction of fragile X mental retardation protein with slack potassium channels.J Neurosci2012 Oct 31Zhang Ydoi: 10.1523/JNEUROSCI.2162-12.2012.
20122915Proteomic analysis reveals CCT is a target of Fragile X mental retardation protein regulation in Drosophila.Dev Biol2010 Apr 15Monzo Kdoi: 10.1016/j.ydbio.2010.01.028
19837168Fragile X mental retardation protein control of neuronal mRNA metabolism: Insights into mRNA stability.Mol Cell Neurosci2010 JanDe Rubeis Sdoi: 10.1016/j.mcn.2009.09.013
19487368Discrimination of common and unique RNA-binding activities among Fragile X mental retardation protein paralogs.Hum Mol Genet2009 Sep 1Darnell JCdoi: 10.1093/hmg/ddp255
19214804The fragile X mental retardation protein in circadian rhythmicity and memory consolidation.Mol Neurobiol2009 AprGatto CLdoi: 10.1007/s12035-009-8057-0
19005212Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly.Mol Biol Cell2009 JanDidiot MCdoi: 10.1091/mbc.E08-07-0737
18936162Fragile X mental retardation protein FMRP binds mRNAs in the nucleus.Mol Cell Biol2009 JanKim Mdoi: 10.1128/MCB.01377-08
22993428Learning and memory deficits consequent to reduction of the fragile X mental retardation protein result from metabotropic glutamate receptor-mediated inhibition of cAMP signaling in Drosophila.J Neurosci2012 Sep 19Kanellopoulos AK-
18638539Modest alterations in patterns of motor neuron dendrite morphology in the Fmr1 knockout mouse model for fragile X.Int J Dev Neurosci2008 NovThomas CCdoi: 10.1016/j.ijdevneu.2008.06.003
22961479Expression of microRNA machinery proteins in different types of chronic rhinosinusitis.Laryngoscope2012 DecZhang YNdoi: 10.1002/lary.23517
18474609S6K1 phosphorylates and regulates fragile X mental retardation protein (FMRP) with the neuronal protein synthesis-dependent mammalian target of rapamycin (mTOR) signaling cascade.J Biol Chem2008 Jul 4Narayanan Udoi: 10.1074/jbc.C800055200
18272470Metabotropic glutamate receptors and fragile x mental retardation protein: partners in translational regulation at the synapse.Sci Signal2008 Feb 5Ronesi JAdoi: 10.1126/stke.15pe6.
18184799On BC1 RNA and the fragile X mental retardation protein.Proc Natl Acad Sci U S A2008 Jan 15Iacoangeli Adoi: 10.1073/pnas.0710991105
17978095Dynamic association of the fragile X mental retardation protein as a messenger ribonucleoprotein between microtubules and polyribosomes.Mol Biol Cell2008 JanWang H-
17881561Fragile X mental retardation protein deficiency leads to excessive mGluR5-dependent internalization of AMPA receptors.Proc Natl Acad Sci U S A2007 Sep 25Nakamoto M-
17417632A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability.Nat Neurosci2007 MayZalfa F-
17376973Fragile X mental retardation protein induces synapse loss through acute postsynaptic translational regulation.J Neurosci2007 Mar 21Pfeiffer BE-
17132937Lost once, the Fragile X Mental Retardation protein is now back onto brain polyribosomes.RNA Biol2005 JanDavidovic L-
22737234Fragile X mental retardation protein interacts with the RNA-binding protein Caprin1 in neuronal RiboNucleoProtein complexes [corrected].PLoS One2012El Fatimy Rdoi: 10.1371/journal.pone.0039338
22539853Evidence for a fragile X mental retardation protein-mediated translational switch in metabotropic glutamate receptor-triggered Arc translation and long-term depression.J Neurosci2012 Apr 25Niere Fdoi: 10.1523/JNEUROSCI.4650-11.2012.
23313071Linking the Fragile X mental retardation protein to the lipoxygenase pathway.Med Hypotheses2013 MarBeaulieu MAdoi: 10.1016/j.mehy.2012.11.046
21772992Conformational-dependent and independent RNA binding to the fragile x mental retardation protein.J Nucleic Acids2011Yan Xdoi: 10.4061/2011/246127
21404421Heads-up: new roles for the fragile X mental retardation protein in neural stem and progenitor cells.Genesis2011 JunCallan MAdoi: 10.1002/dvg.20745
21307257Fragile X mental retardation protein regulates new neuron differentiation in the adult olfactory bulb.J Neurosci2011 Feb 9Scotto-Lomassese Sdoi: 10.1523/JNEUROSCI.5514-10.2011.
20713728Altered mRNA transport, docking, and protein translation in neurons lacking fragile X mental retardation protein.Proc Natl Acad Sci U S A2010 Aug 31Kao DIdoi: 10.1073/pnas.1010564107
20685971Fragile X mental retardation protein is required for rapid experience-dependent regulation of the potassium channel Kv3.1b.J Neurosci2010 Aug 4Strumbos JGdoi: 10.1523/JNEUROSCI.1125-10.2010.
20691595Bicaudal-D regulates fragile X mental retardation protein levels, motility, and function during neuronal morphogenesis.Curr Biol2010 Aug 24Bianco Adoi: 10.1016/j.cub.2010.07.016
20512134Fragile X mental retardation protein controls gating of the sodium-activated potassium channel Slack.Nat Neurosci2010 JulBrown MRdoi: 10.1038/nn.2563
20457613Roles of fragile X mental retardation protein in dopaminergic stimulation-induced synapse-associated protein synthesis and subsequent alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-4-propionate (AMPA) receptor internalization.J Biol Chem2010 Jul 9Wang Hdoi: 10.1074/jbc.M110.116293
20463240Short- and long-term memory are modulated by multiple isoforms of the fragile X mental retardation protein.J Neurosci2010 May 12Banerjee Pdoi: 10.1523/JNEUROSCI.6369-09.2010.
20434996Fragile X mental retardation protein is required for synapse elimination by the activity-dependent transcription factor MEF2.Neuron2010 Apr 29Pfeiffer BEdoi: 10.1016/j.neuron.2010.03.017.
28257890A novel role of fragile X mental retardation protein in pre-mRNA alternative splicing through RNA-binding protein 14.Neuroscience2017 May 4Zhou LTdoi: 10.1016/j.neuroscience.2017.02.044
25681562Fragile X mental retardation protein (FMRP) interacting proteins exhibit different expression patterns during development.Int J Dev Neurosci2015 MayBonaccorso CMdoi: 10.1016/j.ijdevneu.2015.02.004
25701550Fragile X mental retardation protein: A paradigm for translational control by RNA-binding proteins.Biochimie2015 JulChen Edoi: 10.1016/j.biochi.2015.02.005
25250047Low-normal FMR1 CGG repeat length: phenotypic associations.Front Genet2014 Sep 9Mailick MRdoi: 10.3389/fgene.2014.00309
25215498SnapShot: FMRP mRNA targets and diseases.Cell2014 Sep 11Pasciuto Edoi: 10.1016/j.cell.2014.08.035.
24811383Fragile X mental retardation protein regulates synaptic and behavioral plasticity to repeated cocaine administration.Neuron2014 May 7Smith LNdoi: 10.1016/j.neuron.2014.03.028.
24175909Myosin Va is required for the transport of fragile X mental retardation protein (FMRP) granules.Biol Cell2014 FebLindsay AJdoi: 10.1111/boc.201200076
27462983Tracking the Fragile X Mental Retardation Protein in a Highly Ordered Neuronal RiboNucleoParticles Population: A Link between Stalled Polyribosomes and RNA Granules.PLoS Genet2016 Jul 27El Fatimy Rdoi: 10.1371/journal.pgen.1006192
26719241Fragile X Mental Retardation Protein expression in the retina is regulated by light.Exp Eye Res2016 MayGuimaraes-Souza EMdoi: 10.1016/j.exer.2015.11.025
26020477GABAB receptor upregulates fragile X mental retardation protein expression in neurons.Sci Rep2015 May 28Zhang Wdoi: 10.1038/srep10468.
25908854The Drosophila fragile X mental retardation protein participates in the piRNA pathway.J Cell Sci2015 Jun 1Bozzetti MPdoi: 10.1242/jcs.161810
25917509Fragile X mental retardation protein regulates olfactory sensitivity but not odorant discrimination.Chem Senses2015 JunSchilit Nitenson Adoi: 10.1093/chemse/bjv019
27829268Altered Translational Control of Fragile X Mental Retardation Protein on Myelin Proteins in Neuropsychiatric Disorders.Biomol Ther (Seoul)2017 May 1Jeon SJdoi: 10.4062/biomolther.2016.042.
28685837Proteomic analyses of nucleus laminaris identified candidate targets of the fragile X mental retardation protein.J Comp Neurol2017 Oct 15Sakano Hdoi: 10.1002/cne.24281
29668986HITS-CLIP in various brain areas reveals new targets and new modalities of RNA binding by fragile X mental retardation protein.Nucleic Acids Res2018 Jul 6Maurin Tdoi: 10.1093/nar/gky267.
30107516Fragile X mental retardation protein modulates the stability of its m6A-marked messenger RNA targets.Hum Mol Genet2018 Nov 15Zhang Fdoi: 10.1093/hmg/ddy292.
30240639Fragile X mental retardation protein regulates accumulation of the active zone protein Munc18-1 in presynapses via local translation in axons during synaptogenesis.Neurosci Res2019 SepParvin Sdoi: 10.1016/j.neures.2018.09.013
30893603Widespread Alterations in Translation Elongation in the Brain of Juvenile Fmr1 Knockout Mice.Cell Rep2019 Mar 19Das Sharma Sdoi: 10.1016/j.celrep.2019.02.086.
31118285Kinase pathway inhibition restores PSD95 induction in neurons lacking fragile X mental retardation protein.Proc Natl Acad Sci U S A2019 Jun 11Yang Ydoi: 10.1073/pnas.1812056116
15659339Mechanisms of translational control by the 3' UTR in development and differentiation.Semin Cell Dev Biol2005 Febde Moor CH-
19396385Fragile X mental retardation protein recognition of G quadruplex structure per se is sufficient for high affinity binding to RNA.Mol Biosyst2008 DecBole Mdoi: 10.1039/b812537f
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000225388NUFIP2-20110850XM_017024896ENSP00000225388695 (aa)XP_016880385Q7Z417
ENST00000579665NUFIP2-202559-ENSP00000463450120 (aa)-Q7Z417
Gene Model
Click here to download ENSG00000108256's gene model file
Phenotypes
ensgIDTraitpValuePubmed ID
ENSG00000108256Body Mass Index7.65346517690446E-517903300
ENSG00000108256Cholesterol, HDL4.75951132718611E-717903299
GWAS
ensgIDSNPChromosomePositionSNP-risk TraitPubmedID95% CIOr or BEAT EFO ID
ENSG00000108256rs86141729261788AHeadache29397368[0.007-0.014] unit increase0.0105HP_0002315
ENSG00000108256rs86141729261788ASelf-reported math ability (MTAG)30038396[0.0085-0.0175] unit decrease0.013EFO_0004875
ENSG00000108256rs86141729261788AHighest math class taken (MTAG)30038396[0.0093-0.0175] unit decrease0.0134EFO_0004875
ENSG00000108256rs37859611729264307?Adolescent idiopathic scoliosis30019117EFO_0005423
ENSG00000108256rs620651971729266624?Red cell distribution width30595370EFO_0005192
ENSG00000108256rs86141729261788ASmoking initiation (ever regular vs never regular) (MTAG)30643251[0.0063-0.0117] unit increase0.00898031EFO_0006527
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000108256's network

* RBP PPI network refers to all genes directly bind to RBP
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000108256NUFIP29796.429ENSAMEG00000004332NUFIP29595.606Ailuropoda_melanoleuca
ENSG00000108256NUFIP28856.474ENSACAG00000012887NUFIP28756.563Anolis_carolinensis
ENSG00000108256NUFIP2100100.000ENSANAG00000037766NUFIP2100100.000Aotus_nancymaae
ENSG00000108256NUFIP29195.411ENSBTAG00000033077NUFIP29195.411Bos_taurus
ENSG00000108256NUFIP2100100.000ENSCJAG00000013508NUFIP2100100.000Callithrix_jacchus
ENSG00000108256NUFIP210096.429ENSCAFG00000018888NUFIP29494.545Canis_familiaris
ENSG00000108256NUFIP210096.429ENSCAFG00020011598NUFIP29494.545Canis_lupus_dingo
ENSG00000108256NUFIP210097.826ENSCHIG00000015671NUFIP210095.252Capra_hircus
ENSG00000108256NUFIP2100100.000ENSTSYG00000030053NUFIP2100100.000Carlito_syrichta
ENSG00000108256NUFIP26193.333ENSCAPG00000012965NUFIP210093.333Cavia_aperea
ENSG00000108256NUFIP210089.353ENSCPOG00000002815NUFIP210089.353Cavia_porcellus
ENSG00000108256NUFIP2100100.000ENSCCAG00000024630NUFIP2100100.000Cebus_capucinus
ENSG00000108256NUFIP2100100.000ENSCATG00000031290NUFIP2100100.000Cercocebus_atys
ENSG00000108256NUFIP2100100.000ENSCLAG00000007711NUFIP210095.108Chinchilla_lanigera
ENSG00000108256NUFIP2100100.000ENSCSAG00000007009NUFIP210099.137Chlorocebus_sabaeus
ENSG00000108256NUFIP210096.429ENSCHOG00000002740-6495.270Choloepus_hoffmanni
ENSG00000108256NUFIP2100100.000ENSCHOG00000003393-9593.333Choloepus_hoffmanni
ENSG00000108256NUFIP28981.059ENSCPBG00000020115NUFIP29778.733Chrysemys_picta_bellii
ENSG00000108256NUFIP2100100.000ENSCANG00000019856NUFIP2100100.000Colobus_angolensis_palliatus
ENSG00000108256NUFIP2100100.000ENSCGRG00001019451Nufip29493.636Cricetulus_griseus_chok1gshd
ENSG00000108256NUFIP28689.465ENSCGRG00000011209-9689.465Cricetulus_griseus_crigri
ENSG00000108256NUFIP29190.032ENSCGRG00000001173-9390.032Cricetulus_griseus_crigri
ENSG00000108256NUFIP29394.574ENSDNOG00000014525NUFIP29294.242Dasypus_novemcinctus
ENSG00000108256NUFIP29294.237ENSDORG00000023937Nufip29594.246Dipodomys_ordii
ENSG00000108256NUFIP29390.358ENSETEG00000003312NUFIP29490.202Echinops_telfairi
ENSG00000108256NUFIP210098.913ENSEASG00005009801NUFIP210096.403Equus_asinus_asinus
ENSG00000108256NUFIP210097.849ENSECAG00000004975NUFIP210096.408Equus_caballus
ENSG00000108256NUFIP28788.704ENSEEUG00000008482NUFIP210088.704Erinaceus_europaeus
ENSG00000108256NUFIP29882.143ENSFCAG00000039498-9573.282Felis_catus
ENSG00000108256NUFIP210097.826ENSFCAG00000007193-10097.826Felis_catus
ENSG00000108256NUFIP28779.174ENSFALG00000006268NUFIP29279.008Ficedula_albicollis
ENSG00000108256NUFIP2100100.000ENSFDAG00000010640NUFIP210094.388Fukomys_damarensis
ENSG00000108256NUFIP29067.727ENSGALG00000004042NUFIP29468.045Gallus_gallus
ENSG00000108256NUFIP2100100.000ENSGGOG00000008590NUFIP2100100.000Gorilla_gorilla
ENSG00000108256NUFIP2100100.000ENSHGLG00000006811-10094.532Heterocephalus_glaber_female
ENSG00000108256NUFIP29886.283ENSHGLG00000005730-9686.187Heterocephalus_glaber_female
ENSG00000108256NUFIP29886.136ENSHGLG00100009259-9686.043Heterocephalus_glaber_male
ENSG00000108256NUFIP2100100.000ENSHGLG00100018426-9594.545Heterocephalus_glaber_male
ENSG00000108256NUFIP29285.826ENSSTOG00000022663-9883.036Ictidomys_tridecemlineatus
ENSG00000108256NUFIP2100100.000ENSSTOG00000003701-9595.909Ictidomys_tridecemlineatus
ENSG00000108256NUFIP29191.139ENSJJAG00000020851-9290.506Jaculus_jaculus
ENSG00000108256NUFIP29580.152ENSJJAG00000022944-9479.576Jaculus_jaculus
ENSG00000108256NUFIP29064.297ENSLACG00000012838NUFIP29763.020Latimeria_chalumnae
ENSG00000108256NUFIP29394.401ENSLAFG00000012294NUFIP29994.182Loxodonta_africana
ENSG00000108256NUFIP2100100.000ENSMFAG00000040845NUFIP2100100.000Macaca_fascicularis
ENSG00000108256NUFIP2100100.000ENSMMUG00000012856NUFIP2100100.000Macaca_mulatta
ENSG00000108256NUFIP2100100.000ENSMNEG00000038891NUFIP2100100.000Macaca_nemestrina
ENSG00000108256NUFIP2100100.000ENSMLEG00000036478NUFIP2100100.000Mandrillus_leucophaeus
ENSG00000108256NUFIP28771.782ENSMGAG00000005925NUFIP210072.442Meleagris_gallopavo
ENSG00000108256NUFIP28792.359ENSMAUG00000005650Nufip210092.359Mesocricetus_auratus
ENSG00000108256NUFIP2100100.000ENSMICG00000016380NUFIP2100100.000Microcebus_murinus
ENSG00000108256NUFIP2100100.000ENSMOCG00000022086Nufip29593.788Microtus_ochrogaster
ENSG00000108256NUFIP28983.037ENSMODG00000019327NUFIP28483.333Monodelphis_domestica
ENSG00000108256NUFIP2100100.000ENSMUSG00000037857Nufip29593.333Mus_musculus
ENSG00000108256NUFIP2100100.000MGP_SPRETEiJ_G0017622Nufip29588.252Mus_spretus
ENSG00000108256NUFIP29280.835ENSMPUG00000014002NUFIP29480.835Mustela_putorius_furo
ENSG00000108256NUFIP210096.774ENSMLUG00000016685NUFIP210096.774Myotis_lucifugus
ENSG00000108256NUFIP29073.642ENSNGAG00000018948-9473.642Nannospalax_galili
ENSG00000108256NUFIP210096.429ENSNGAG00000016940-9493.636Nannospalax_galili
ENSG00000108256NUFIP2100100.000ENSNLEG00000003299NUFIP2100100.000Nomascus_leucogenys
ENSG00000108256NUFIP29186.772ENSNLEG00000006740-9186.820Nomascus_leucogenys
ENSG00000108256NUFIP25980.630ENSMEUG00000016377-5979.903Notamacropus_eugenii
ENSG00000108256NUFIP2100100.000ENSOPRG00000011583NUFIP29595.159Ochotona_princeps
ENSG00000108256NUFIP2100100.000ENSODEG00000009679NUFIP210094.245Octodon_degus
ENSG00000108256NUFIP210096.429ENSOANG00000012647NUFIP29478.614Ornithorhynchus_anatinus
ENSG00000108256NUFIP2100100.000ENSOCUG00000016483NUFIP29595.909Oryctolagus_cuniculus
ENSG00000108256NUFIP210096.809ENSOGAG00000007400NUFIP29595.000Otolemur_garnettii
ENSG00000108256NUFIP210096.429ENSOARG00000006644NUFIP29695.303Ovis_aries
ENSG00000108256NUFIP2100100.000ENSPPAG00000030125NUFIP2100100.000Pan_paniscus
ENSG00000108256NUFIP28795.349ENSPPRG00000003571NUFIP29992.663Panthera_pardus
ENSG00000108256NUFIP28795.349ENSPTIG00000017161NUFIP28795.349Panthera_tigris_altaica
ENSG00000108256NUFIP2100100.000ENSPTRG00000008947NUFIP2100100.000Pan_troglodytes
ENSG00000108256NUFIP2100100.000ENSPANG00000023299NUFIP2100100.000Papio_anubis
ENSG00000108256NUFIP27777.239ENSPSIG00000004369NUFIP210077.425Pelodiscus_sinensis
ENSG00000108256NUFIP2100100.000ENSPEMG00000011656Nufip29594.242Peromyscus_maniculatus_bairdii
ENSG00000108256NUFIP29184.044ENSPCIG00000014922NUFIP29082.175Phascolarctos_cinereus
ENSG00000108256NUFIP2100100.000ENSPPYG00000008121NUFIP210099.424Pongo_abelii
ENSG00000108256NUFIP29995.699ENSPCAG00000006342NUFIP27993.117Procavia_capensis
ENSG00000108256NUFIP2100100.000ENSPCOG00000017278NUFIP2100100.000Propithecus_coquereli
ENSG00000108256NUFIP210096.429ENSPVAG00000012645NUFIP29595.000Pteropus_vampyrus
ENSG00000108256NUFIP29590.332ENSRNOG00000008382AABR07046727.19889.879Rattus_norvegicus
ENSG00000108256NUFIP2100100.000ENSRNOG00000024964Nufip210093.525Rattus_norvegicus
ENSG00000108256NUFIP2100100.000ENSRBIG00000032631NUFIP2100100.000Rhinopithecus_bieti
ENSG00000108256NUFIP2100100.000ENSRROG00000042054NUFIP2100100.000Rhinopithecus_roxellana
ENSG00000108256NUFIP2100100.000ENSSBOG00000036071-100100.000Saimiri_boliviensis_boliviensis
ENSG00000108256NUFIP29596.552ENSSBOG00000031116-10086.735Saimiri_boliviensis_boliviensis
ENSG00000108256NUFIP28784.793ENSSHAG00000016442NUFIP29984.793Sarcophilus_harrisii
ENSG00000108256NUFIP25888.353ENSSARG00000007216-5788.353Sorex_araneus
ENSG00000108256NUFIP28770.936ENSSPUG00000005093NUFIP210071.100Sphenodon_punctatus
ENSG00000108256NUFIP210096.429ENSSSCG00000017785NUFIP29494.713Sus_scrofa
ENSG00000108256NUFIP28779.669ENSTGUG00000006298NUFIP210079.669Taeniopygia_guttata
ENSG00000108256NUFIP28794.020ENSTBEG00000008374NUFIP210094.020Tupaia_belangeri
ENSG00000108256NUFIP28791.030ENSTTRG00000016328NUFIP28791.030Tursiops_truncatus
ENSG00000108256NUFIP28795.688ENSUAMG00000014575NUFIP29595.688Ursus_americanus
ENSG00000108256NUFIP28995.624ENSUMAG00000010751NUFIP29395.624Ursus_maritimus
ENSG00000108256NUFIP210096.429ENSVVUG00000020998NUFIP29494.394Vulpes_vulpes
ENSG00000108256NUFIP28091.667ENSXETG00000009447nufip29655.951Xenopus_tropicalis
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0003723RNA binding22658674.22681889.HDAFunction
GO:0003723RNA binding12837692.IDAFunction
GO:0005515protein binding12837692.16407062.25416956.26184334.IPIFunction
GO:0005634nucleus12837692.26184334.IDAComponent
GO:0005654nucleoplasm-IDAComponent
GO:0005737cytoplasm12837692.26184334.IDAComponent
GO:0005829cytosol-IDAComponent
GO:0010494cytoplasmic stress granule26184334.IDAComponent
GO:0016020membrane19946888.HDAComponent
GO:0016604nuclear body-IDAComponent
GO:0042788polysomal ribosome12837692.IDAComponent

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