ADAR - Double-stranded RNA-specific adenosine deaminase

"RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR." Toth A.M., Li Z., Cattaneo R., Samuel ...

Anevidencedescribesthesourceofanannotation,e.g.anexperimentthathasbeenpublishedinthescientificliterature,anorthologousprotein,arecordfromanotherdatabase,etc.

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SkipHeader   UniProtKBxUniProtKBProteinknowledgebaseUniParcSequencearchiveHelpHelppages,FAQs,UniProtKBmanual,documents,newsarchiveandBiocurationprojects.UniRefSequenceclustersProteomesProteinsetsfromfullysequencedgenomesAnnotationsystemsSystemsusedtoautomaticallyannotateproteinswithhighaccuracy:UniRule(Expertlycuratedrules)ARBA(Systemgeneratedrules)SupportingdataSelectoneoftheoptionsbelowtotargetyoursearch:LiteraturecitationsTaxonomyKeywordsSubcellularlocationsCross-referenceddatabasesHumandiseasesAdvancedSearchxHomeBLASTAlignRetrieve/IDmappingPeptidesearchSPARQLContactHelpYouareusingaversionofbrowserthatmaynotdisplayallthefeaturesofthiswebsite.Pleaseconsiderupgradingyourbrowser. WewillbeswitchingtothenewUniProtwebsiteonTuesday,June28.Pleaseexploreandshareyourfeedback. TakemetoUniProtBETAxUniProtKB-P55265 (DSRAD_HUMAN)Basket0(max400entries)x Yourbasketiscurrentlyempty.i

WhenbrowsingthroughdifferentUniProtproteins,youcanusethe'basket'tosavethem,sothatyoucanbacktofindoranalysethemlater.

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Selectitem(s)andclickon"Addtobasket"tocreateyourowncollectionhere(400entriesmax)UniProtKB(0)UniRef(0)UniParc(0)AlignBLASTMapIdsDownloadFullViewRemoveClearDisplayHelpvideoEntryPublicationsFeatureviewerFeaturetableAllNoneFunctionNames&TaxonomySubcellularlocationSubcell.locationPathology&BiotechPathol./BiotechPTM/ProcessingExpressionInteractionStructureFamily&DomainsSequences(5+)SimilarproteinsCross-referencesEntryinformationMiscellaneousTopBLAST>sp|P55265|DSRAD_HUMANDouble-strandedRNA-specificadenosinedeaminaseOS=HomosapiensOX=9606GN=ADARPE=1SV=4 MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQLPEAPVIGKQ TPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLRSQGLQRGFQHPSPRGRSLPQ RGVDCLSSHFQELSIYQDQEQRILKFLEELGEGKATTAHDLSGKLGTPKKEINRVLYSLA KKGKLQKEAGTPPLWKIAVSTQAWNQHSGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSED LLEPFIAVSAQAWNQHSGVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIK EKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTPPIWHLTDKKR ERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNASNNMVTTEKVENGQEPVIKLE NRQEARPEPARLKPPVHYNGPSKAGYVDFENGQWATDDIPDDLNSIRAAPGEFRAIMEMP SFYSHGLPRCSPYKKLTECQLKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVV INGREFPPAEAGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQ TPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCVAVGAQTFPSV SAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPEGMISESLDNLESMMPNKVRKIGELV RYLNTNPVGGLLEYARSHGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQG KQEAADAALRVLIGENEKAERMGFTEVTPVTGASLRRTMLLLSRSPEAQPKTLPLTGSTF HDQIAMLSHRCFNTLTNSFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVKGDSLS LKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKGGEKLQIKKTVSFHLY ISTAPCGDGALFDKSCSDRAMESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVP TWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPIYLKSVTLGYLFSQGHLTRAI CCRVTRDGSAFEDGLRHPFIVNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILD GTRGTVDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETAKNYFK KGLKDMGYGNWISKPQEEKNFYLCPV AlignFormatAddtobasketAddedtobasketHistoryEntryversion222(25May2022)Sequenceversion4(30Nov2010)Previousversions|rssCommunitycuration()AddapublicationFeedbackProteinDouble-strandedRNA-specificadenosinedeaminaseGeneADAROrganismHomosapiens(Human)StatusReviewed-Annotationscore:Annotationscore:5outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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-Experimentalevidenceatproteinleveli

Thisindicatesthetypeofevidencethatsupportstheexistenceoftheprotein.Notethatthe'proteinexistence'evidencedoesnotgiveinformationontheaccuracyorcorrectnessofthesequence(s)displayed.

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Selectasectiononthelefttoseecontent.

Thissectionprovidesanyusefulinformationabouttheprotein,mostlybiologicalknowledge.

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FunctioniCatalyzesthehydrolyticdeaminationofadenosinetoinosineindouble-strandedRNA(dsRNA)referredtoasA-to-IRNAediting(PubMed:7972084,PubMed:7565688,PubMed:12618436).ThismayaffectgeneexpressionandfunctioninanumberofwaysthatincludemRNAtranslationbychangingcodonsandhencetheaminoacidsequenceofproteinssincethetranslationalmachineryreadtheinosineasaguanosine;pre-mRNAsplicingbyalteringsplicesiterecognitionsequences;RNAstabilitybychangingsequencesinvolvedinnucleaserecognition;geneticstabilityinthecaseofRNAvirusgenomesbychangingsequencesduringviralRNAreplication;andRNAstructure-dependentactivitiessuchasmicroRNAproductionortargetingorprotein-RNAinteractions.CaneditbothviralandcellularRNAsandcaneditRNAsatmultiplesites(hyper-editing)oratspecificsites(site-specificediting).ItscellularRNAsubstratesinclude:bladdercancer-associatedprotein(BLCAP),neurotransmitterreceptorsforglutamate(GRIA2)andserotonin(HTR2C)andGABAreceptor(GABRA3).Site-specificRNAeditingoftranscriptsencodingtheseproteinsresultsinaminoacidsubstitutionswhichconsequentlyalterstheirfunctionalactivities.Exhibitslow-leveleditingattheGRIA2Q/Rsite,buteditsefficientlyattheR/GsiteandHOTSPOT1.ItsviralRNAsubstratesinclude:hepatitisCvirus(HCV),vesicularstomatitisvirus(VSV),measlesvirus(MV),hepatitisdeltavirus(HDV),andhumanimmunodeficiencyvirustype1(HIV-1).Exhibitseitheraproviral(HDV,MV,VSVandHIV-1)oranantiviraleffect(HCV)andthiscanbeediting-dependent(HDVandHCV),editing-independent(VSVandMV)orboth(HIV-1).ImpairsHCVreplicationviaRNAeditingatmultiplesites.EnhancesthereplicationofMV,VSVandHIV-1throughanediting-independentmechanismviasuppressionofEIF2AK2/PKRactivationandfunction.StimulatesboththereleaseandinfectivityofHIV-1viralparticlesbyanediting-dependentmechanismwhereitassociateswithviralRNAsandeditsadenosinesinthe5'UTRandtheRevandTatcodingsequence.CanenhanceviralreplicationofHDVviaA-to-Ieditingatasitedesignatedasamber/W,therebychanginganUAGamberstopcodontoanUIGtryptophan(W)codonthatpermitssynthesisofthelargedeltaantigen(L-HDAg)whichhasakeyroleintheassemblyofviralparticles.However,highlevelsofADAR1inhibitHDVreplication.14Publications

Manuallycuratedinformationforwhichthereispublishedexperimentalevidence.

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ManualassertionbasedonexperimentiniRef.1"MolecularcloningofcDNAfordouble-strandedRNAadenosinedeaminase,acandidateenzymefornuclearRNAediting."KimU.,WangY.,SanfordT.,ZengY.,NishikuraK.Proc.Natl.Acad.Sci.U.S.A.91:11457-11461(1994)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),PARTIALPROTEINSEQUENCE,FUNCTION,CATALYTICACTIVITY,TISSUESPECIFICITY,VARIANTGLY-100.Ref.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.10"RequirementofdimerizationforRNAeditingactivityofadenosinedeaminasesactingonRNA."ChoD.-S.C.,YangW.,LeeJ.T.,ShiekhattarR.,MurrayJ.M.,NishikuraK.J.Biol.Chem.278:17093-17102(2003)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,CATALYTICACTIVITY,HOMODIMERIZATION,SUBUNIT.Ref.12"ADAR1RNAdeaminaselimitsshortinterferingRNAefficacyinmammaliancells."YangW.,WangQ.,HowellK.L.,LeeJ.T.,ChoD.-S.C.,MurrayJ.M.,NishikuraK.J.Biol.Chem.280:3946-3953(2005)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.13"NewantiviralpathwaythatmediateshepatitisCvirusrepliconinterferonsensitivitythroughADAR1."TaylorD.R.,PuigM.,DarnellM.E.,MihalikK.,FeinstoneS.M.J.Virol.79:6291-6298(2005)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.14"SUMO-1modificationaltersADAR1editingactivity."DesterroJ.M.P.,KeeganL.P.,JaffrayE.,HayR.T.,O'ConnellM.A.,Carmo-FonsecaM.Mol.Biol.Cell16:5115-5126(2005)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,SUMOYLATIONATLYS-418,MUTAGENESISOFLYS-418.Ref.16"ThelargeformofADAR1isresponsibleforenhancedhepatitisdeltavirusRNAeditingininterferon-alpha-stimulatedhostcells."HartwigD.,SchuetteC.,WarneckeJ.,DornI.,HennigH.,KirchnerH.,SchlenkeP.J.ViralHepat.13:150-157(2006)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.19"Double-strandedRNAdeaminaseADAR1increaseshostsusceptibilitytovirusinfection."NieY.,HammondG.L.,YangJ.H.J.Virol.81:917-923(2007)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,INTERACTIONWITHEIF2AK2.Ref.25"RNA-specificadenosinedeaminaseADAR1suppressesmeaslesvirus-inducedapoptosisandactivationofproteinkinasePKR."TothA.M.,LiZ.,CattaneoR.,SamuelC.E.J.Biol.Chem.284:29350-29356(2009)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.26"ADAR1interactswithPKRduringhumanimmunodeficiencyvirusinfectionoflymphocytesandcontributestoviralreplication."ClerziusG.,GelinasJ.F.,DaherA.,BonnetM.,MeursE.F.,GatignolA.J.Virol.83:10119-10128(2009)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,INTERACTIONWITHEIF2AK2.Ref.28"EditingofHIV-1RNAbythedouble-strandedRNAdeaminaseADAR1stimulatesviralinfection."DoriaM.,NeriF.,GalloA.,FaraceM.G.,MichienziA.NucleicAcidsRes.37:5848-5858(2009)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.31"HumanBLCAPtranscript:neweditingeventsinnormalandcanceroustissues."GaleanoF.,LeroyA.,RossettiC.,GromovaI.,GautierP.,KeeganL.P.,MassimiL.,DiRoccoC.,O'ConnellM.A.,GalloA.Int.J.Cancer127:127-137(2010)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.35"ADAR2editingenzymeisanovelhumanimmunodeficiencyvirus-1proviralfactor."DoriaM.,TomaselliS.,NeriF.,CiafreS.A.,FaraceM.G.,MichienziA.,GalloA.J.Gen.Virol.92:1228-1232(2011)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.42"AdenosinedeaminaseactingonRNA1(ADAR1)suppressestheinductionofinterferonbymeaslesvirus."LiZ.,OkonskiK.M.,SamuelC.E.J.Virol.86:3787-3794(2012)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.CautionTheN-terminusofisoform4hasbeenderivedfromESTandgenomicsequences.Curated

ThissubsectionoftheFunctionsectiondescribesthecatalyticactivityofanenzyme,i.e.achemicalreactionthattheenzymecatalyzes.

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Catalyticactivityiadenosineindouble-strandedRNASearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.+H+SearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.+H2OSearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.=inosineindouble-strandedRNASearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.+NH4+SearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.3PublicationsManualassertionbasedonexperimentiniRef.1"MolecularcloningofcDNAfordouble-strandedRNAadenosinedeaminase,acandidateenzymefornuclearRNAediting."KimU.,WangY.,SanfordT.,ZengY.,NishikuraK.Proc.Natl.Acad.Sci.U.S.A.91:11457-11461(1994)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),PARTIALPROTEINSEQUENCE,FUNCTION,CATALYTICACTIVITY,TISSUESPECIFICITY,VARIANTGLY-100.Ref.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.10"RequirementofdimerizationforRNAeditingactivityofadenosinedeaminasesactingonRNA."ChoD.-S.C.,YangW.,LeeJ.T.,ShiekhattarR.,MurrayJ.M.,NishikuraK.J.Biol.Chem.278:17093-17102(2003)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,CATALYTICACTIVITY,HOMODIMERIZATION,SUBUNIT.EC:3.5.4.37SearchproteinsinUniProtKBforthisECnumber.SeethedescriptionofthisECnumberinENZYME.SearchreactionsforthisECnumberinRhea.3PublicationsManualassertionbasedonexperimentiniRef.1"MolecularcloningofcDNAfordouble-strandedRNAadenosinedeaminase,acandidateenzymefornuclearRNAediting."KimU.,WangY.,SanfordT.,ZengY.,NishikuraK.Proc.Natl.Acad.Sci.U.S.A.91:11457-11461(1994)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),PARTIALPROTEINSEQUENCE,FUNCTION,CATALYTICACTIVITY,TISSUESPECIFICITY,VARIANTGLY-100.Ref.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.10"RequirementofdimerizationforRNAeditingactivityofadenosinedeaminasesactingonRNA."ChoD.-S.C.,YangW.,LeeJ.T.,ShiekhattarR.,MurrayJ.M.,NishikuraK.J.Biol.Chem.278:17093-17102(2003)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,CATALYTICACTIVITY,HOMODIMERIZATION,SUBUNIT.Source:RheaSearchforthisreactioninUniProtKB.SeethedescriptionofthisreactioninRhea..Show»«Hideadenosineindouble-strandedRNASearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.AMPresidueSearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.zoom+H+SearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.+H2OSearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.=inosineindouble-strandedRNASearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.IMPresidueSearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.zoom+NH4+SearchproteinsinUniProtKBforthismolecule.SearchchemicalreactionsinRheaforthismolecule.SeethedescriptionofthismoleculeinChEBI.zoomSitesFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

ThissubsectionoftheFunctionsectionindicatesatwhichpositiontheproteinbindsagivenmetalion.Thenatureofthemetalisindicatedinthe'Description'field.

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Metalbindingi910ZincPROSITE-ProRuleannotation

ManualvalidatedinformationwhichhasbeengeneratedbytheUniProtKBautomaticannotationsystem.

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ManualassertionaccordingtorulesiPROSITE-ProRule:PRU002401

ThissubsectionoftheFunctionsectionisusedforenzymesandindicatestheresiduesdirectlyinvolvedincatalysis.

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Activesitei912ProtondonorPROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU002401Metalbindingi966ZincPROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU002401Metalbindingi1036ZincPROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU002401

TheGeneOntology(GO)projectprovidesasetofhierarchicalcontrolledvocabularysplitinto3categories:

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GO-MolecularfunctioniDNAbindingSource:UniProtKB-KWdouble-strandedRNAadenosinedeaminaseactivitySource:MGI

InferredfromDirectAssay

Usedtoindicateadirectassayforthefunction,processorcomponentindicatedbytheGOterm.

MoreinformationintheGOevidencecodeguide

InferredfromdirectassayiRef.3"Functionallydistinctdouble-strandedRNA-bindingdomainsassociatedwithalternativesplicesitevariantsoftheinterferon-inducibledouble-strandedRNA-specificadenosinedeaminase."LiuY.,GeorgeC.X.,PattersonJ.B.,SamuelC.E.J.Biol.Chem.272:4419-4428(1997)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[GENOMICDNA](ISOFORMS1;2AND3),VARIANTSGLY-100ANDARG-384.double-strandedRNAbindingSource:GO_Central

InferredfromBiologicalaspectofAncestor

Atypeofphylogeneticevidencewherebyanaspectofadescendentisinferredthroughthecharacterizationofanaspectofaancestralgene.

MoreinformationintheGOevidencecodeguide

Inferredfrombiologicalaspectofancestori"Phylogenetic-basedpropagationoffunctionalannotationswithintheGeneOntologyconsortium."GaudetP.,LivstoneM.S.,LewisS.E.,ThomasP.D.BriefBioinform12:449-462(2011)[PubMed][EuropePMC][Abstract]metalionbindingSource:UniProtKB-KWRNAbindingSource:UniProtKBInferredfromhighthroughputdirectassayi"InsightsintoRNAbiologyfromanatlasofmammalianmRNA-bindingproteins."CastelloA.,FischerB.,EichelbaumK.,HorosR.,BeckmannB.M.,StreinC.,DaveyN.E.,HumphreysD.T.,PreissT.,SteinmetzL.M.,KrijgsveldJ.,HentzeM.W.Cell149:1393-1406(2012)[PubMed][EuropePMC][Abstract]"ThemRNA-boundproteomeanditsglobaloccupancyprofileonprotein-codingtranscripts."BaltzA.G.,MunschauerM.,SchwanhausserB.,VasileA.,MurakawaY.,SchuelerM.,YoungsN.,Penfold-BrownD.,DrewK.,MilekM.,WylerE.,BonneauR.,SelbachM.,DieterichC.,LandthalerM.MolCell46:674-690(2012)[PubMed][EuropePMC][Abstract]tRNA-specificadenosinedeaminaseactivitySource:GO_CentralInferredfrombiologicalaspectofancestori"Phylogenetic-basedpropagationoffunctionalannotationswithintheGeneOntologyconsortium."GaudetP.,LivstoneM.S.,LewisS.E.,ThomasP.D.BriefBioinform12:449-462(2011)[PubMed][EuropePMC][Abstract]CompleteGOannotationonQuickGO...GO-BiologicalprocessiadenosinetoinosineeditingSource:UniProtKBInferredfromdirectassayiRef.13"NewantiviralpathwaythatmediateshepatitisCvirusrepliconinterferonsensitivitythroughADAR1."TaylorD.R.,PuigM.,DarnellM.E.,MihalikK.,FeinstoneS.M.J.Virol.79:6291-6298(2005)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.28"EditingofHIV-1RNAbythedouble-strandedRNAdeaminaseADAR1stimulatesviralinfection."DoriaM.,NeriF.,GalloA.,FaraceM.G.,MichienziA.NucleicAcidsRes.37:5848-5858(2009)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.Ref.35"ADAR2editingenzymeisanovelhumanimmunodeficiencyvirus-1proviralfactor."DoriaM.,TomaselliS.,NeriF.,CiafreS.A.,FaraceM.G.,MichienziA.,GalloA.J.Gen.Virol.92:1228-1232(2011)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.baseconversionorsubstitutioneditingSource:MGIInferredfromdirectassayiRef.3"Functionallydistinctdouble-strandedRNA-bindingdomainsassociatedwithalternativesplicesitevariantsoftheinterferon-inducibledouble-strandedRNA-specificadenosinedeaminase."LiuY.,GeorgeC.X.,PattersonJ.B.,SamuelC.E.J.Biol.Chem.272:4419-4428(1997)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[GENOMICDNA](ISOFORMS1;2AND3),VARIANTSGLY-100ANDARG-384.cellularresponsetovirusSource:EnsembldefenseresponsetovirusSource:UniProtKB-KWdefinitivehemopoiesisSource:EnsemblerythrocytedifferentiationSource:EnsemblhematopoieticprogenitorcelldifferentiationSource:EnsemblhematopoieticstemcellhomeostasisSource:EnsemblinnateimmuneresponseSource:UniProtKB

TraceableAuthorStatement

Usedforinformationfromreviewarticleswheretheoriginalexperimentsaretraceablethroughthatarticleandalsoforinformationfromtextbooksordictionaries.

MoreinformationintheGOevidencecodeguide

TraceableauthorstatementiRef.16"ThelargeformofADAR1isresponsibleforenhancedhepatitisdeltavirusRNAeditingininterferon-alpha-stimulatedhostcells."HartwigD.,SchuetteC.,WarneckeJ.,DornI.,HennigH.,KirchnerH.,SchlenkeP.J.ViralHepat.13:150-157(2006)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.miRNAloadingontoRISCinvolvedingenesilencingbymiRNASource:MGIInferredfromdirectassayi"ADAR1formsacomplexwithDicertopromotemicroRNAprocessingandRNA-inducedgenesilencing."OtaH.,SakuraiM.,GuptaR.,ValenteL.,WulffB.E.,AriyoshiK.,IizasaH.,DavuluriR.V.,NishikuraK.Cell153:575-589(2013)[PubMed][EuropePMC][Abstract]mRNAprocessingSource:UniProtKB-KWnegativeregulationofapoptoticprocessSource:EnsemblnegativeregulationofproteinkinaseactivitybyregulationofproteinphosphorylationSource:UniProtKBInferredfromdirectassayiRef.28"EditingofHIV-1RNAbythedouble-strandedRNAdeaminaseADAR1stimulatesviralinfection."DoriaM.,NeriF.,GalloA.,FaraceM.G.,MichienziA.NucleicAcidsRes.37:5848-5858(2009)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.negativeregulationofRNAinterferenceSource:EnsemblnegativeregulationoftypeIinterferon-mediatedsignalingpathwaySource:EnsemblosteoblastdifferentiationSource:EnsemblpositiveregulationofviralgenomereplicationSource:UniProtKBInferredfromdirectassayiRef.28"EditingofHIV-1RNAbythedouble-strandedRNAdeaminaseADAR1stimulatesviralinfection."DoriaM.,NeriF.,GalloA.,FaraceM.G.,MichienziA.NucleicAcidsRes.37:5848-5858(2009)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.pre-miRNAprocessingSource:MGIInferredfromdirectassayi"ADAR1formsacomplexwithDicertopromotemicroRNAprocessingandRNA-inducedgenesilencing."OtaH.,SakuraiM.,GuptaR.,ValenteL.,WulffB.E.,AriyoshiK.,IizasaH.,DavuluriR.V.,NishikuraK.Cell153:575-589(2013)[PubMed][EuropePMC][Abstract]proteinexportfromnucleusSource:UniProtKBInferredfromdirectassayiRef.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.proteinimportintonucleusSource:UniProtKBInferredfromdirectassayiRef.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.responsetointerferon-alphaSource:UniProtKBInferredfromdirectassayiRef.16"ThelargeformofADAR1isresponsibleforenhancedhepatitisdeltavirusRNAeditingininterferon-alpha-stimulatedhostcells."HartwigD.,SchuetteC.,WarneckeJ.,DornI.,HennigH.,KirchnerH.,SchlenkeP.J.ViralHepat.13:150-157(2006)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.responsetovirusSource:UniProtKB

InferredfromMutantPhenotype

Describesannotationsthatareconcludedfromlookingatvariationsorchangesinageneproductsuchasmutationsorabnormallevelsandincludestechniquessuchasknockouts,overexpression,anti-senseexperimentsanduseofspecificproteininhibitors.

MoreinformationintheGOevidencecodeguide

InferredfrommutantphenotypeiRef.13"NewantiviralpathwaythatmediateshepatitisCvirusrepliconinterferonsensitivitythroughADAR1."TaylorD.R.,PuigM.,DarnellM.E.,MihalikK.,FeinstoneS.M.J.Virol.79:6291-6298(2005)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION.RNAprocessingSource:GO_CentralInferredfrombiologicalaspectofancestori"Phylogenetic-basedpropagationoffunctionalannotationswithintheGeneOntologyconsortium."GaudetP.,LivstoneM.S.,LewisS.E.,ThomasP.D.BriefBioinform12:449-462(2011)[PubMed][EuropePMC][Abstract]somaticdiversificationofimmunereceptorsviasomaticmutationSource:EnsemblCompleteGOannotationonQuickGO...

UniProtKBKeywordsconstituteacontrolledvocabularywithahierarchicalstructure.KeywordssummarisethecontentofaUniProtKBentryandfacilitatethesearchforproteinsofinterest.

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KeywordsiMolecularfunctionDNA-binding,Hydrolase,RNA-bindingBiologicalprocessAntiviraldefense,Immunity,Innateimmunity,mRNAprocessing,RNA-mediatedgenesilencingLigandMetal-binding,ZincEnzymeandpathwaydatabasesBRENDAComprehensiveEnzymeInformationSystemMore...BRENDAi3.5.4.37,2681PathwayCommonswebresourceforbiologicalpathwaydataMore...PathwayCommonsiP55265Reactome-aknowledgebaseofbiologicalpathwaysandprocessesMore...ReactomeiR-HSA-75102,C6deaminationofadenosineR-HSA-77042,FormationofeditosomesbyADARproteinsR-HSA-909733,Interferonalpha/betasignalingSignaLink:asignalingpathwayresourcewithmulti-layeredregulatorynetworksMore...SignaLinkiP55265SIGNORSignalingNetworkOpenResourceMore...SIGNORiP55265

Thissectionprovidesinformationabouttheproteinandgenename(s)andsynonym(s)andabouttheorganismthatisthesourceoftheproteinsequence.

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Names&Taxonomyi

ThissubsectionoftheNamesandtaxonomysectionprovidesanexhaustivelistofallnamesoftheprotein,fromcommonlyusedtoobsolete,toallowunambiguousidentificationofaprotein.

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ProteinnamesiRecommendedname:Double-strandedRNA-specificadenosinedeaminase(EC:3.5.4.37SearchproteinsinUniProtKBforthisECnumber.SeethedescriptionofthisECnumberinENZYME.SearchreactionsforthisECnumberinRhea.2PublicationsManualassertionbasedonexperimentiniRef.1"MolecularcloningofcDNAfordouble-strandedRNAadenosinedeaminase,acandidateenzymefornuclearRNAediting."KimU.,WangY.,SanfordT.,ZengY.,NishikuraK.Proc.Natl.Acad.Sci.U.S.A.91:11457-11461(1994)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),PARTIALPROTEINSEQUENCE,FUNCTION,CATALYTICACTIVITY,TISSUESPECIFICITY,VARIANTGLY-100.Ref.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.)Shortname:DRADA1Publication

Manuallycuratedinformationthatisbasedonstatementsinscientificarticlesforwhichthereisnoexperimentalsupport.

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ManualassertionbasedonopinioniniRef.1"MolecularcloningofcDNAfordouble-strandedRNAadenosinedeaminase,acandidateenzymefornuclearRNAediting."KimU.,WangY.,SanfordT.,ZengY.,NishikuraK.Proc.Natl.Acad.Sci.U.S.A.91:11457-11461(1994)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),PARTIALPROTEINSEQUENCE,FUNCTION,CATALYTICACTIVITY,TISSUESPECIFICITY,VARIANTGLY-100.Alternativename(s):136kDadouble-strandedRNA-bindingproteinShortname:p136Interferon-inducibleprotein4Shortname:IFI-4K88DSRBP

ThissubsectionoftheNamesandtaxonomysectionindicatesthename(s)ofthegene(s)thatcodefortheproteinsequence(s)describedintheentry.Fourdistincttokensexist:'Name','Synonyms','Orderedlocusnames'and'ORFnames'.

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GenenamesiName:ADARSynonyms:ADAR1,DSRAD,G1P1,IFI4

ThissubsectionoftheNamesandtaxonomysectionprovidesinformationonthename(s)oftheorganismthatisthesourceoftheproteinsequence.

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OrganismiHomosapiens(Human)

ThissubsectionoftheNamesandtaxonomysectionshowstheuniqueidentifierassignedbytheNCBItothesourceorganismoftheprotein.Thisisknownasthe'taxonomicidentifier'or'taxid'.

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Taxonomicidentifieri9606[NCBI]

ThissubsectionoftheNamesandtaxonomysectioncontainsthetaxonomichierarchicalclassificationlineageofthesourceorganism.Itliststhenodesastheyappeartop-downinthetaxonomictree,withthemoregeneralgroupinglistedfirst.

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Taxonomiclineageicellularorganisms›Eukaryota›Opisthokonta›Metazoa›Eumetazoa›Bilateria›Deuterostomia›Chordata›Craniata›Vertebrata›Gnathostomata›Teleostomi›Euteleostomi›Sarcopterygii›Dipnotetrapodomorpha›Tetrapoda›Amniota›Mammalia›Theria›Eutheria›Boreoeutheria›Euarchontoglires›Primates›Haplorrhini›Simiiformes›Catarrhini›Hominoidea›Hominidae›Homininae›Homo

ThissubsectionoftheNamesandtaxonomysectionispresentforentriesthatarepartofaproteome,i.e.ofasetofproteinsthoughttobeexpressedbyorganismswhosegenomeshavebeencompletelysequenced.

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ProteomesiUP000005640

AUniProtproteomecanconsistofseveralcomponents.
Thecomponentnamereferstothegenomiccomponentencodingasetofproteins.

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Componenti:Chromosome1Organism-specificdatabasesHumanGeneNomenclatureDatabaseMore...HGNCiHGNC:225,ADAROnlineMendelianInheritanceinMan(OMIM)More...MIMi146920,geneneXtProt;thehumanproteinknowledgeplatformMore...neXtProtiNX_P55265EukaryoticPathogen,VectorandHostDatabaseResourcesMore...VEuPathDBiHostDB:ENSG00000160710

Thissectionprovidesinformationonthelocationandthetopologyofthematureproteininthecell.

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SubcellularlocationiUniProtannotationGO-CellularcomponentIsoform1:CytoplasmandCytosolCytoplasm1PublicationManualassertionbasedonexperimentiniRef.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.NucleusNucleus2PublicationsManualassertionbasedonexperimentiniRef.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.Note:Shuttlesbetweenthecytoplasmandnucleus(PubMed:7565688,PubMed:24753571).NuclearimportismediatedbyTNPO1(PubMed:24753571).2PublicationsManualassertionbasedonexperimentiniRef.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.Isoform5:CytoplasmandCytosolCytoplasm1PublicationManualassertionbasedonexperimentiniRef.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.NucleusNucleus2PublicationsManualassertionbasedonexperimentiniRef.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.nucleolus1PublicationManualassertionbasedonexperimentiniRef.11"DynamicassociationofRNA-editingenzymeswiththenucleolus."DesterroJ.M.P.,KeeganL.P.,LafargaM.,BercianoM.T.,O'ConnellM.,Carmo-FonsecaM.J.CellSci.116:1805-1818(2003)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION.Note:Predominantlynuclearbutcanshuttlebetweennucleusandcytoplasm.TNPO1canmediateitsnuclearimportwhereasXPO5canmediateitsnuclearexport.1PublicationManualassertionbasedonexperimentiniRef.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.NucleusnucleolusSource:HPAnucleoplasmSource:HPAnucleusSource:UniProtKBInferredfromdirectassayiRef.23"TheeditingenzymeADAR1andthemRNAsurveillanceproteinhUpf1interactinthecellnucleus."AgranatL.,RaitskinO.,SperlingJ.,SperlingR.Proc.Natl.Acad.Sci.U.S.A.105:5028-5033(2008)[PubMed][EuropePMC][Abstract]Citedfor:INTERACTIONWITHUPF1,SUBCELLULARLOCATION."DHX9suppressesRNAprocessingdefectsoriginatingfromtheAluinvasionofthehumangenome."AktasT.,AvsarIlikI.,MaticzkaD.,BhardwajV.,PessoaRodriguesC.,MittlerG.,MankeT.,BackofenR.,AkhtarA.Nature544:115-119(2017)[PubMed][EuropePMC][Abstract]Ref.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.supraspliceosomalcomplexSource:UniProtKBInferredfromdirectassayiRef.23"TheeditingenzymeADAR1andthemRNAsurveillanceproteinhUpf1interactinthecellnucleus."AgranatL.,RaitskinO.,SperlingJ.,SperlingR.Proc.Natl.Acad.Sci.U.S.A.105:5028-5033(2008)[PubMed][EuropePMC][Abstract]Citedfor:INTERACTIONWITHUPF1,SUBCELLULARLOCATION.OtherlocationscytoplasmSource:UniProtKBInferredfromdirectassayi"DHX9suppressesRNAprocessingdefectsoriginatingfromtheAluinvasionofthehumangenome."AktasT.,AvsarIlikI.,MaticzkaD.,BhardwajV.,PessoaRodriguesC.,MittlerG.,MankeT.,BackofenR.,AkhtarA.Nature544:115-119(2017)[PubMed][EuropePMC][Abstract]Ref.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.membraneSource:UniProtKBInferredfromhighthroughputdirectassayi"DefiningthemembraneproteomeofNKcells."GhoshD.,LippertD.,KrokhinO.,CortensJ.P.,WilkinsJ.A.JMassSpectrom45:1-25(2010)[PubMed][EuropePMC][Abstract]CompleteGOannotationonQuickGO...Keywords-CellularcomponentiCytoplasm,Nucleus

Thissectionprovidesinformationonthedisease(s)andphenotype(s)associatedwithaprotein.

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Pathology&Biotechi

Thissubsectionofthe'PathologyandBiotech'sectionprovidesinformationonthedisease(s)associatedwithgeneticvariationsinagivenprotein.TheinformationisextractedfromthescientificliteratureanddiseasesthatarealsodescribedintheOMIMdatabasearerepresentedwithacontrolledvocabularyinthefollowingway:

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InvolvementindiseaseiDyschromatosissymmetricahereditaria(DSH)3PublicationsManualassertionbasedonexperimentiniRef.54"MutationsoftheRNA-specificadenosinedeaminasegene(DSRAD)areinvolvedindyschromatosissymmetricahereditaria."MiyamuraY.,SuzukiT.,KonoM.,InagakiK.,ItoS.,SuzukiN.,TomitaY.Am.J.Hum.Genet.73:693-699(2003)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSDSHPRO-923ANDSER-1165.Ref.55"SevennovelmutationsoftheADARgeneinChinesefamiliesandsporadicpatientswithdyschromatosissymmetricahereditaria(DSH)."ZhangX.-J.,HeP.-P.,LiM.,HeC.-D.,YanK.-L.,CuiY.,YangS.,ZhangK.-Y.,GaoM.,ChenJ.-J.,LiC.-R.,JinL.,ChenH.-D.,XuS.-J.,HuangW.Hum.Mutat.23:629-630(2004)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTDSHPHE-966.Ref.56"AnewargininesubstitutionmutationofDSRADgeneinaChinesefamilywithdyschromatosissymmetricahereditaria."LiC.-R.,LiM.,MaH.-J.,LuoD.,YangL.-J.,WangD.-G.,ZhuX.-H.,YueX.-Z.,ChenW.-Q.,ZhuW.-Y.J.Dermatol.Sci.37:95-99(2005)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTDSHTRP-1155.Thediseaseiscausedbyvariantsaffectingthegenerepresentedinthisentry.DiseasedescriptionAnautosomaldominantpigmentarygenodermatosischaracterizedbyamixtureofhyperpigmentedandhypopigmentedmaculesdistributedonthefaceandthedorsalpartsofthehandsandfeet,thatappearininfancyorearlychildhood.RelatedinformationinOMIMFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'Sequence'sectiondescribesnaturalvariant(s)oftheproteinsequence.

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NaturalvariantiVAR_017604923L→PinDSH.1PublicationManualassertionbasedonexperimentiniRef.54"MutationsoftheRNA-specificadenosinedeaminasegene(DSRAD)areinvolvedindyschromatosissymmetricahereditaria."MiyamuraY.,SuzukiT.,KonoM.,InagakiK.,ItoS.,SuzukiN.,TomitaY.Am.J.Hum.Genet.73:693-699(2003)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSDSHPRO-923ANDSER-1165.CorrespondstovariantdbSNP:rs28936680EnsemblClinVar.1NaturalvariantiVAR_021729966C→FinDSH.1PublicationManualassertionbasedonexperimentiniRef.55"SevennovelmutationsoftheADARgeneinChinesefamiliesandsporadicpatientswithdyschromatosissymmetricahereditaria(DSH)."ZhangX.-J.,HeP.-P.,LiM.,HeC.-D.,YanK.-L.,CuiY.,YangS.,ZhangK.-Y.,GaoM.,ChenJ.-J.,LiC.-R.,JinL.,ChenH.-D.,XuS.-J.,HuangW.Hum.Mutat.23:629-630(2004)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTDSHPHE-966.1NaturalvariantiVAR_0266691155R→WinDSH.1PublicationManualassertionbasedonexperimentiniRef.56"AnewargininesubstitutionmutationofDSRADgeneinaChinesefamilywithdyschromatosissymmetricahereditaria."LiC.-R.,LiM.,MaH.-J.,LuoD.,YangL.-J.,WangD.-G.,ZhuX.-H.,YueX.-Z.,ChenW.-Q.,ZhuW.-Y.J.Dermatol.Sci.37:95-99(2005)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTDSHTRP-1155.CorrespondstovariantdbSNP:rs1044845711Ensembl.1NaturalvariantiVAR_0176051165F→SinDSH.1PublicationManualassertionbasedonexperimentiniRef.54"MutationsoftheRNA-specificadenosinedeaminasegene(DSRAD)areinvolvedindyschromatosissymmetricahereditaria."MiyamuraY.,SuzukiT.,KonoM.,InagakiK.,ItoS.,SuzukiN.,TomitaY.Am.J.Hum.Genet.73:693-699(2003)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSDSHPRO-923ANDSER-1165.CorrespondstovariantdbSNP:rs28936681EnsemblClinVar.1Aicardi-Goutieressyndrome6(AGS6)1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.Thediseaseiscausedbyvariantsaffectingthegenerepresentedinthisentry.DiseasedescriptionAformofAicardi-Goutieressyndrome,ageneticallyheterogeneousdiseasecharacterizedbycerebralatrophy,leukoencephalopathy,intracranialcalcifications,chroniccerebrospinalfluid(CSF)lymphocytosis,increasedCSFalpha-interferon,andnegativeserologicinvestigationsforcommonprenatalinfection.Clinicalfeaturesasthrombocytopenia,hepatosplenomegalyandelevatedhepatictransaminasesalongwithintermittentfevermayerroneouslysuggestaninfectiveprocess.Severeneurologicaldysfunctionsmanifestininfancyasprogressivemicrocephaly,spasticity,dystonicposturingandprofoundpsychomotorretardation.Deathoftenoccursinearlychildhood.RelatedinformationinOMIMFeaturekeyPosition(s)DescriptionActionsGraphicalviewLengthNaturalvariantiVAR_069535193P→AinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs145588689EnsemblClinVar.1NaturalvariantiVAR_069536870A→TinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122893EnsemblClinVar.1NaturalvariantiVAR_069537872I→TinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122897EnsemblClinVar.1NaturalvariantiVAR_069538892R→HinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122892EnsemblClinVar.1NaturalvariantiVAR_069539999K→NinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122896EnsemblClinVar.1NaturalvariantiVAR_0695401007G→RinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122822EnsemblClinVar.1NaturalvariantiVAR_0695411112Y→FinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122895EnsemblClinVar.1NaturalvariantiVAR_0695421113D→HinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122894EnsemblClinVar.1MutagenesisFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'PathologyandBiotech'sectiondescribestheeffectoftheexperimentalmutationofoneormoreaminoacid(s)onthebiologicalpropertiesoftheprotein.

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Mutagenesisi418K→R:Abolishessumoylation.1PublicationManualassertionbasedonexperimentiniRef.14"SUMO-1modificationaltersADAR1editingactivity."DesterroJ.M.P.,KeeganL.P.,JaffrayE.,HayR.T.,O'ConnellM.A.,Carmo-FonsecaM.Mol.Biol.Cell16:5115-5126(2005)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,SUMOYLATIONATLYS-418,MUTAGENESISOFLYS-418.1Mutagenesisi708 – 801Missing:Abolishesnuclearlocation.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.AddBLAST94Mutagenesisi708 – 710MMP→AMA:Decreasednuclearandpartiallycytoplasmiclocation.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.3Mutagenesisi712 – 715KVRK→AVAA:Noeffectonnuclearlocation.NoeffectonRNAbinding.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.4Mutagenesisi716 – 724Missing:Disruptsthebi-partitenuclearlocalizationsignalandabolishesnuclearlocation.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.9Mutagenesisi716I→N:Disruptsthebi-partitenuclearlocalizationsignalandabolishesnuclearlocation;whenassociatedwithS-719andN-723.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.1Mutagenesisi718E→A:Noeffectonnuclearlocation;whenassociatedwithA-721andA-724.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.1Mutagenesisi719L→S:Disruptsthebi-partitenuclearlocalizationsignalandabolishesnuclearlocation;whenassociatedwithN-716andN-723.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.1Mutagenesisi721R→A:Noeffectonnuclearlocation;whenassociatedwithA-721andA-724.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.1Mutagenesisi723L→N:Disruptsthebi-partitenuclearlocalizationsignalandabolishesnuclearlocation;whenassociatedwithN-716andS-719.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.1Mutagenesisi724N→A:Noeffectonnuclearlocation;whenassociatedwithA-718andA-721.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.1Mutagenesisi725 – 801Missing:Disruptsnuclearlocalizationsignal.NoeffectonRNAbinding.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.AddBLAST77Mutagenesisi777 – 778KK→AA:StronglyimpairedRNAbinding.Noeffectonnuclearlocation.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.2Mutagenesisi801R→A:AbolishesinteractionwithTNPO1,TNPO1-mediatednuclearimportandnuclearlocation.1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.1Keywords-DiseaseiAicardi-Goutieressyndrome,DiseasevariantOrganism-specificdatabasesDisGeNETMore...DisGeNETi103GeneReviewsaresourceofexpert-authored,peer-revieweddiseasedescriptions.More...GeneReviewsiADARMalaCardshumandiseasedatabaseMore...MalaCardsiADARMIMi127400,phenotype615010,phenotypeOpenTargetsMore...OpenTargetsiENSG00000160710Orphanet;adatabasededicatedtoinformationonrarediseasesandorphandrugsMore...Orphaneti51,Aicardi-Goutieressyndrome41,Dyschromatosissymmetricahereditaria225154,FamilialinfantilebilateralstriatalnecrosisThePharmacogeneticsandPharmacogenomicsKnowledgeBaseMore...PharmGKBiPA24555MiscellaneousdatabasesPharosNIHDruggableGenomeKnowledgebaseMore...PharosiP55265,TbioGeneticvariationdatabasesBioMutacuratedsingle-nucleotidevariationanddiseaseassociationdatabaseMore...BioMutaiADARDomainmappingofdiseasemutations(DMDM)More...DMDMi313104303

Thissectiondescribespost-translationalmodifications(PTMs)and/orprocessingevents.

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PTM/ProcessingiMoleculeprocessingFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'PTM/Processing'sectiondescribestheextentofapolypeptidechaininthematureproteinfollowingprocessingorproteolyticcleavage.

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ChainiPRO_00001717741 – 1226Double-strandedRNA-specificadenosinedeaminaseAddBLAST1226AminoacidmodificationsFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'PTM/Processing'sectionspecifiesthepositionandtypeofeachmodifiedresidueexcludinglipids,glycansandproteincross-links.

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Modifiedresiduei26AsymmetricdimethylarginineCombinedsources

Manuallyvalidatedinformationinferredfromacombinationofexperimentalandcomputationalevidence.

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ManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.46"Immunoaffinityenrichmentandmassspectrometryanalysisofproteinmethylation."GuoA.,GuH.,ZhouJ.,MulhernD.,WangY.,LeeK.A.,YangV.,AguiarM.,KornhauserJ.,JiaX.,RenJ.,BeausoleilS.A.,SilvaJ.C.,VemulapalliV.,BedfordM.T.,CombM.J.Mol.Cell.Proteomics13:372-387(2014)[PubMed][EuropePMC][Abstract]Citedfor:METHYLATION[LARGESCALEANALYSIS]ATARG-26,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei285PhosphoserineBysimilarity

Manuallycuratedinformationwhichhasbeenpropagatedfromarelatedexperimentallycharacterizedprotein.

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ManualassertioninferredfromsequencesimilaritytoiUniProtKB:P55266 (DSRAD_RAT)1

ThissubsectionofthePTM/Processingsectiondescribescovalentlinkagesofvarioustypesformedbetweentwoproteins(interchaincross-links)orbetweentwopartsofthesameprotein(intrachaincross-links),exceptthedisulfidebondsthatareannotatedinthe'Disulfidebond'subsection.

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Cross-linki384Glycyllysineisopeptide(Lys-Gly)(interchainwithG-CterinSUMO2)CombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.49"Site-specificmappingofthehumanSUMOproteomerevealsco-modificationwithphosphorylation."HendriksI.A.,LyonD.,YoungC.,JensenL.J.,VertegaalA.C.,NielsenM.L.Nat.Struct.Mol.Biol.24:325-336(2017)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-384;LYS-408;LYS-418;LYS-580ANDLYS-875,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Cross-linki408Glycyllysineisopeptide(Lys-Gly)(interchainwithG-CterinSUMO2)CombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.49"Site-specificmappingofthehumanSUMOproteomerevealsco-modificationwithphosphorylation."HendriksI.A.,LyonD.,YoungC.,JensenL.J.,VertegaalA.C.,NielsenM.L.Nat.Struct.Mol.Biol.24:325-336(2017)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-384;LYS-408;LYS-418;LYS-580ANDLYS-875,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Cross-linki418Glycyllysineisopeptide(Lys-Gly)(interchainwithG-CterinSUMO);alternateCross-linki418Glycyllysineisopeptide(Lys-Gly)(interchainwithG-CterinSUMO1);alternateCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.47"MappingofSUMOsitesandanalysisofSUMOylationchangesinducedbyexternalstimuli."ImpensF.,RadoshevichL.,CossartP.,RibetD.Proc.Natl.Acad.Sci.U.S.A.111:12432-12437(2014)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-418,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Cross-linki418Glycyllysineisopeptide(Lys-Gly)(interchainwithG-CterinSUMO2);alternateCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.47"MappingofSUMOsitesandanalysisofSUMOylationchangesinducedbyexternalstimuli."ImpensF.,RadoshevichL.,CossartP.,RibetD.Proc.Natl.Acad.Sci.U.S.A.111:12432-12437(2014)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-418,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.48"System-wideanalysisofSUMOylationdynamicsinresponsetoreplicationstressrevealsnovelsmallubiquitin-likemodifiedtargetproteinsandacceptorlysinesrelevantforgenomestability."XiaoZ.,ChangJ.G.,HendriksI.A.,SigurdssonJ.O.,OlsenJ.V.,VertegaalA.C.Mol.Cell.Proteomics14:1419-1434(2015)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-418,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.49"Site-specificmappingofthehumanSUMOproteomerevealsco-modificationwithphosphorylation."HendriksI.A.,LyonD.,YoungC.,JensenL.J.,VertegaalA.C.,NielsenM.L.Nat.Struct.Mol.Biol.24:325-336(2017)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-384;LYS-408;LYS-418;LYS-580ANDLYS-875,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Modifiedresiduei481PhosphoserineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Cross-linki580Glycyllysineisopeptide(Lys-Gly)(interchainwithG-CterinSUMO2)CombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.49"Site-specificmappingofthehumanSUMOproteomerevealsco-modificationwithphosphorylation."HendriksI.A.,LyonD.,YoungC.,JensenL.J.,VertegaalA.C.,NielsenM.L.Nat.Struct.Mol.Biol.24:325-336(2017)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-384;LYS-408;LYS-418;LYS-580ANDLYS-875,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Modifiedresiduei601PhosphothreonineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.22"Aquantitativeatlasofmitoticphosphorylation."DephoureN.,ZhouC.,VillenJ.,BeausoleilS.A.,BakalarskiC.E.,ElledgeS.J.,GygiS.P.Proc.Natl.Acad.Sci.U.S.A.105:10762-10767(2008)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-601;SER-614;SER-823ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.29"QuantitativephosphoproteomicanalysisofTcellreceptorsignalingrevealssystem-widemodulationofprotein-proteininteractions."MayyaV.,LundgrenD.H.,HwangS.-I.,RezaulK.,WuL.,EngJ.K.,RodionovV.,HanD.K.Sci.Signal.2:RA46-RA46(2009)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-601ANDTHR-808,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei603PhosphothreonineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei614PhosphoserineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.22"Aquantitativeatlasofmitoticphosphorylation."DephoureN.,ZhouC.,VillenJ.,BeausoleilS.A.,BakalarskiC.E.,ElledgeS.J.,GygiS.P.Proc.Natl.Acad.Sci.U.S.A.105:10762-10767(2008)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-601;SER-614;SER-823ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei629PhosphoserineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei636PhosphoserineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei808PhosphothreonineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.17"Aprobability-basedapproachforhigh-throughputproteinphosphorylationanalysisandsitelocalization."BeausoleilS.A.,VillenJ.,GerberS.A.,RushJ.,GygiS.P.Nat.Biotechnol.24:1285-1292(2006)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-808,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.18"ImprovedtitaniumdioxideenrichmentofphosphopeptidesfromHeLacellsandhighconfidentphosphopeptideidentificationbycross-validationofMS/MSandMS/MS/MSspectra."YuL.R.,ZhuZ.,ChanK.C.,IssaqH.J.,DimitrovD.S.,VeenstraT.D.J.ProteomeRes.6:4150-4162(2007)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-808,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.21"Combiningprotein-basedIMAC,peptide-basedIMAC,andMudPITforefficientphosphoproteomicanalysis."CantinG.T.,YiW.,LuB.,ParkS.K.,XuT.,LeeJ.-D.,YatesJ.R.IIIJ.ProteomeRes.7:1346-1351(2008)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-808,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.29"QuantitativephosphoproteomicanalysisofTcellreceptorsignalingrevealssystem-widemodulationofprotein-proteininteractions."MayyaV.,LundgrenD.H.,HwangS.-I.,RezaulK.,WuL.,EngJ.K.,RodionovV.,HanD.K.Sci.Signal.2:RA46-RA46(2009)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-601ANDTHR-808,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.32"Quantitativephosphoproteomicsrevealswidespreadfullphosphorylationsiteoccupancyduringmitosis."OlsenJ.V.,VermeulenM.,SantamariaA.,KumarC.,MillerM.L.,JensenL.J.,GnadF.,CoxJ.,JensenT.S.,NiggE.A.,BrunakS.,MannM.Sci.Signal.3:RA3-RA3(2010)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-808ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei814PhosphoserineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei823PhosphoserineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.22"Aquantitativeatlasofmitoticphosphorylation."DephoureN.,ZhouC.,VillenJ.,BeausoleilS.A.,BakalarskiC.E.,ElledgeS.J.,GygiS.P.Proc.Natl.Acad.Sci.U.S.A.105:10762-10767(2008)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-601;SER-614;SER-823ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Modifiedresiduei825PhosphoserineCombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.22"Aquantitativeatlasofmitoticphosphorylation."DephoureN.,ZhouC.,VillenJ.,BeausoleilS.A.,BakalarskiC.E.,ElledgeS.J.,GygiS.P.Proc.Natl.Acad.Sci.U.S.A.105:10762-10767(2008)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-601;SER-614;SER-823ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.32"Quantitativephosphoproteomicsrevealswidespreadfullphosphorylationsiteoccupancyduringmitosis."OlsenJ.V.,VermeulenM.,SantamariaA.,KumarC.,MillerM.L.,JensenL.J.,GnadF.,CoxJ.,JensenT.S.,NiggE.A.,BrunakS.,MannM.Sci.Signal.3:RA3-RA3(2010)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATTHR-808ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.38"System-widetemporalcharacterizationoftheproteomeandphosphoproteomeofhumanembryonicstemcelldifferentiation."RigboltK.T.,ProkhorovaT.A.,AkimovV.,HenningsenJ.,JohansenP.T.,KratchmarovaI.,KassemM.,MannM.,OlsenJ.V.,BlagoevB.Sci.Signal.4:RS3-RS3(2011)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].Ref.44"Towardacomprehensivecharacterizationofahumancancercellphosphoproteome."ZhouH.,DiPalmaS.,PreisingerC.,PengM.,PolatA.N.,HeckA.J.,MohammedS.J.ProteomeRes.12:260-271(2013)[PubMed][EuropePMC][Abstract]Citedfor:PHOSPHORYLATION[LARGESCALEANALYSIS]ATSER-481;THR-601;THR-603;SER-629;SER-636;THR-808;SER-814ANDSER-825,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].1Cross-linki875Glycyllysineisopeptide(Lys-Gly)(interchainwithG-CterinSUMO2)CombinedsourcesManualassertioninferredfromcombinationofexperimentalandcomputationalevidenceiRef.49"Site-specificmappingofthehumanSUMOproteomerevealsco-modificationwithphosphorylation."HendriksI.A.,LyonD.,YoungC.,JensenL.J.,VertegaalA.C.,NielsenM.L.Nat.Struct.Mol.Biol.24:325-336(2017)[PubMed][EuropePMC][Abstract]Citedfor:SUMOYLATION[LARGESCALEANALYSIS]ATLYS-384;LYS-408;LYS-418;LYS-580ANDLYS-875,IDENTIFICATIONBYMASSSPECTROMETRY[LARGESCALEANALYSIS].

ThissubsectionofthePTM/processingsectiondescribespost-translationalmodifications(PTMs).Thissubsectioncomplementstheinformationprovidedatthesequencelevelordescribesmodificationsforwhichposition-specificdataisnotyetavailable.

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Post-translationalmodificationiSumoylationreducesRNA-editingactivity.1PublicationManualassertionbasedonexperimentiniRef.14"SUMO-1modificationaltersADAR1editingactivity."DesterroJ.M.P.,KeeganL.P.,JaffrayE.,HayR.T.,O'ConnellM.A.,Carmo-FonsecaM.Mol.Biol.Cell16:5115-5126(2005)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,SUMOYLATIONATLYS-418,MUTAGENESISOFLYS-418.Keywords-PTMiIsopeptidebond,Methylation,Phosphoprotein,UblconjugationProteomicdatabasesEncyclopediaofProteomeDynamicsMore...EPDiP55265jPOST-JapanProteomeStandardRepository/DatabaseMore...jPOSTiP55265MassIVE-MassSpectrometryInteractiveVirtualEnvironmentMore...MassIVEiP55265MaxQB-TheMaxQuantDataBaseMore...MaxQBiP55265PaxDb,adatabaseofproteinabundanceaveragesacrossallthreedomainsoflifeMore...PaxDbiP55265PeptideAtlasMore...PeptideAtlasiP55265PRoteomicsIDEntificationsdatabaseMore...PRIDEiP55265ProteomicsDB:amulti-organismproteomeresourceMore...ProteomicsDBi56826[P55265-1]56827[P55265-2]56828[P55265-3]56829[P55265-4]56830[P55265-5]PTMdatabasesGlyGen:ComputationalandInformaticsResourcesforGlycoscienceMore...GlyGeniP55265,4sites,2O-linkedglycans(4sites)iPTMnetintegratedresourceforPTMsinsystemsbiologycontextMore...iPTMnetiP55265MetOSitedatabaseofmethioninesulfoxidesitesMore...MetOSiteiP55265Comprehensiveresourceforthestudyofproteinpost-translationalmodifications(PTMs)inhuman,mouseandrat.More...PhosphoSitePlusiP55265SwissPalmdatabaseofS-palmitoylationeventsMore...SwissPalmiP55265

ThissectionprovidesinformationontheexpressionofageneatthemRNAorproteinlevelincellsorintissuesofmulticellularorganisms.

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Expressioni

Thissubsectionofthe'Expression'sectionprovidesinformationontheexpressionofageneatthemRNAorproteinlevelincellsorintissuesofmulticellularorganisms.Bydefault,theinformationisderivedfromexperimentsatthemRNAlevel,unlessspecified'atproteinlevel'.
Examples:P92958,Q8TDN4,O14734

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TissuespecificityiUbiquitouslyexpressed,highestlevelswerefoundinbrainandlung(PubMed:7972084).Isoform5isexpressedathigherlevelsinastrocytomasascomparedtonormalbraintissueandexpressionincreasesstrikinglywiththeseverityofthetumor,beinghigherinthemostaggressivetumors.2PublicationsManualassertionbasedonexperimentiniRef.1"MolecularcloningofcDNAfordouble-strandedRNAadenosinedeaminase,acandidateenzymefornuclearRNAediting."KimU.,WangY.,SanfordT.,ZengY.,NishikuraK.Proc.Natl.Acad.Sci.U.S.A.91:11457-11461(1994)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),PARTIALPROTEINSEQUENCE,FUNCTION,CATALYTICACTIVITY,TISSUESPECIFICITY,VARIANTGLY-100.Ref.20"Down-regulationofRNAeditinginpediatricastrocytomas:ADAR2editingactivityinhibitscellmigrationandproliferation."CenciC.,BarzottiR.,GaleanoF.,CorbelliS.,RotaR.,MassimiL.,DiRoccoC.,O'ConnellM.A.,GalloA.J.Biol.Chem.283:7251-7260(2008)[PubMed][EuropePMC][Abstract]Citedfor:ALTERNATIVESPLICING,SUBUNIT,TISSUESPECIFICITY.

Thissubsectionofthe'Expression'sectionreportstheexperimentallyproveneffectsofinducersandrepressors(usuallychemicalcompoundsorenvironmentalfactors)onthelevelofprotein(ormRNA)expression(up-regulation,down-regulation,constitutiveexpression).

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InductioniIsoform1isinducedbyinterferonalpha.Isoform5isconstitutivelyexpressed.2PublicationsManualassertionbasedonexperimentiniRef.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.9"HumanRNA-specificadenosinedeaminaseADAR1transcriptspossessalternativeexon1structuresthatinitiatefromdifferentpromoters,oneconstitutivelyactiveandtheotherinterferoninducible."GeorgeC.X.,SamuelC.E.Proc.Natl.Acad.Sci.U.S.A.96:4621-4626(1999)[PubMed][EuropePMC][Abstract]Citedfor:ALTERNATIVEPROMOTERUSAGE,INDUCTION.GeneexpressiondatabasesBgeedataBaseforGeneExpressionEvolutionMore...BgeeiENSG00000160710,Expressedintestisand249othertissuesExpressionAtlas,DifferentialandBaselineExpressionMore...ExpressionAtlasiP55265,baselineanddifferentialGenevisiblesearchportaltonormalizedandcuratedexpressiondatafromGenevestigatorMore...GenevisibleiP55265,HSOrganism-specificdatabasesHumanProteinAtlasMore...HPAiENSG00000160710,Lowtissuespecificity

Thissectionprovidesinformationonthequaternarystructureofaproteinandoninteraction(s)withotherproteinsorproteincomplexes.

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Interactioni

Thissubsectionofthe'Interaction'sectionprovidesinformationabouttheproteinquaternarystructureandinteraction(s)withotherproteinsorproteincomplexes(withtheexceptionofphysiologicalreceptor-ligandinteractionswhichareannotatedinthe'Function'section).

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SubunitstructureiHomodimer.Homodimerizationisessentialforitscatalyticactivity(PubMed:12618436).Isoform5canformheterodimerswithADARB1/ADAR2.Isoform1interactswithILF2/NF45andILF3/NF90(PubMed:16055709).BindingtoILF3/NF90up-regulatesILF3-mediatedgeneexpression.Isoform1andisoform5(viaDRBM3domain)interactwithTNPO1(PubMed:19124606,PubMed:24753571).Isoform5(viaDRBMdomains)interactswithXPO5(PubMed:19124606).Isoform1andisoform5caninteractwithEIF2AK2/PKRandUPF1(PubMed:17079286,PubMed:18362360).10PublicationsManualassertionbasedonexperimentiniRef.10"RequirementofdimerizationforRNAeditingactivityofadenosinedeaminasesactingonRNA."ChoD.-S.C.,YangW.,LeeJ.T.,ShiekhattarR.,MurrayJ.M.,NishikuraK.J.Biol.Chem.278:17093-17102(2003)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,CATALYTICACTIVITY,HOMODIMERIZATION,SUBUNIT.Ref.15"ADAR1interactswithNF90throughdouble-strandedRNAandregulatesNF90-mediatedgeneexpressionindependentlyofRNAediting."NieY.,DingL.,KaoP.N.,BraunR.,YangJ.-H.Mol.Cell.Biol.25:6956-6963(2005)[PubMed][EuropePMC][Abstract]Citedfor:INTERACTIONWITHILF2ANDILF3.Ref.19"Double-strandedRNAdeaminaseADAR1increaseshostsusceptibilitytovirusinfection."NieY.,HammondG.L.,YangJ.H.J.Virol.81:917-923(2007)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,INTERACTIONWITHEIF2AK2.Ref.20"Down-regulationofRNAeditinginpediatricastrocytomas:ADAR2editingactivityinhibitscellmigrationandproliferation."CenciC.,BarzottiR.,GaleanoF.,CorbelliS.,RotaR.,MassimiL.,DiRoccoC.,O'ConnellM.A.,GalloA.J.Biol.Chem.283:7251-7260(2008)[PubMed][EuropePMC][Abstract]Citedfor:ALTERNATIVESPLICING,SUBUNIT,TISSUESPECIFICITY.Ref.23"TheeditingenzymeADAR1andthemRNAsurveillanceproteinhUpf1interactinthecellnucleus."AgranatL.,RaitskinO.,SperlingJ.,SperlingR.Proc.Natl.Acad.Sci.U.S.A.105:5028-5033(2008)[PubMed][EuropePMC][Abstract]Citedfor:INTERACTIONWITHUPF1,SUBCELLULARLOCATION.Ref.26"ADAR1interactswithPKRduringhumanimmunodeficiencyvirusinfectionoflymphocytesandcontributestoviralreplication."ClerziusG.,GelinasJ.F.,DaherA.,BonnetM.,MeursE.F.,GatignolA.J.Virol.83:10119-10128(2009)[PubMed][EuropePMC][Abstract]Citedfor:FUNCTION,INTERACTIONWITHEIF2AK2.Ref.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.Ref.50"CrystalstructureoftheZalphadomainofthehumaneditingenzymeADAR1boundtoleft-handedZ-DNA."SchwartzT.,RouldM.A.,LowenhauptK.,HerbertA.,RichA.Science284:1841-1845(1999)[PubMed][EuropePMC][Abstract]Citedfor:X-RAYCRYSTALLOGRAPHY(2.1ANGSTROMS)OF133-209INCOMPLEXWITHZ-DNA,DOMAIN.Ref.51"ThesolutionstructureoftheZalphadomainofthehumanRNAeditingenzymeADAR1revealsaprepositionedbindingsurfaceforZ-DNA."SchadeM.,TurnerC.J.,KuehneR.,SchmiederP.,LowenhauptK.,HerbertA.,RichA.,OschkinatH.Proc.Natl.Acad.Sci.U.S.A.96:12465-12470(1999)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF125-201INCOMPLEXWITHZ-DNAANDALONE,DOMAIN.Ref.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.

Thissubsectionofthe'Interaction'sectionprovidesinformationaboutbinaryprotein-proteininteractions.Thedatapresentedinthissectionareaquality-filteredsubsetofbinaryinteractionsautomaticallyderivedfromtheIntActdatabase.ItisupdatedateveryUniProtrelease.

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BinaryinteractionsiShowmoredetailsHidedetailsP55265With#Exp.IntActTARDBP[Q13148]3EBI-2462104,EBI-372899UPF1[Q92900]3EBI-2462104,EBI-373471NS[P03496]fromInfluenzaAvirus(strainA/PuertoRico/8/1934H1N1).8EBI-2462104,EBI-2547442SerineproteaseNS3(PRO_0000037965)fromDenguevirustype2(strainThailand/NGS-C/1944).2EBI-2462104,EBI-9825968Serineprotease/helicaseNS3(PRO_0000045599)fromHepatitisCvirusgenotype2a(isolateJFH-1).3EBI-2462104,EBI-6858501Isoform1[P55265-1]With#Exp.IntActDICER1[Q9UPY3]4EBI-6913056,EBI-395506TARBP2[Q15633]2EBI-6913056,EBI-978581Isoform5[P55265-5]With#Exp.IntActDICER1[Q9UPY3]8EBI-6913210,EBI-395506TARBP2[Q15633]3EBI-6913210,EBI-978581Protein-proteininteractiondatabasesTheBiologicalGeneralRepositoryforInteractionDatasets(BioGRID)More...BioGRIDi106617,162interactorsCORUMcomprehensiveresourceofmammalianproteincomplexesMore...CORUMiP55265DatabaseofinteractingproteinsMore...DIPiDIP-29310NProteininteractiondatabaseandanalysissystemMore...IntActiP55265,76interactorsMolecularINTeractiondatabaseMore...MINTiP55265STRING:functionalproteinassociationnetworksMore...STRINGi9606.ENSP00000357459MiscellaneousdatabasesRNAct,Protein-RNAinteractionpredictionsformodelorganisms.More...RNActiP55265,protein

Thissectionprovidesinformationonthetertiaryandsecondarystructureofaprotein.

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StructureiSecondarystructure11226Legend:HelixTurnBetastrandPDBStructureknownforthisareaShowmoredetailsHidedetailsFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'Structure'sectionisusedtoindicatethepositionsofexperimentallydeterminedhelicalregionswithintheproteinsequence.

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Helixi127 – 130Combinedsources

Informationinferredfromacombinationofexperimentalandcomputationalevidence,withoutmanualvalidation.

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AutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1QGP4Helixi135 – 150CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1QBJ16

Thissubsectionofthe'Structure'sectionisusedtoindicatethepositionsofexperimentallydeterminedbetastrandswithintheproteinsequence.

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Betastrandi152 – 154CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1QGP3Helixi158 – 165CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1QBJ8Helixi169 – 181CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1QBJ13Betastrandi184 – 192CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1QBJ9Betastrandi194 – 197CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1QBJ4Helixi294 – 309CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK16Helixi315 – 322CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK8Helixi324 – 326CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK3Helixi327 – 339CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK13Betastrandi342 – 346CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK5Betastrandi348 – 350CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK3Betastrandi352 – 355CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK4Helixi357 – 360CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK4

Thissubsectionofthe'Structure'sectionisusedtoindicatethepositionsofexperimentallydeterminedhydrogen-bondedturnswithintheproteinsequence.TheseelementscorrespondtotheDSSPsecondarystructurecode'T'.

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Turni361 – 363CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:1XMK3Helixi716 – 724CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:2MDR9Helixi727 – 738CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:2MDR12Betastrandi742 – 749CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:2MDR8Betastrandi758 – 764CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:2MDR7Betastrandi767 – 776CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:2MDR10Helixi777 – 796CombinedsourcesAutomaticassertioninferredfromcombinationofexperimentalandcomputationalevidenceiPDB:2MDR203DstructuredatabasesAlphaFoldProteinStructureDatabaseMore...AlphaFoldDBiP55265SWISS-MODELRepository-adatabaseofannotated3DproteinstructuremodelsMore...SMRiP55265DatabaseofcomparativeproteinstructuremodelsMore...ModBaseiSearch...ProteinDataBankinEurope-KnowledgeBaseMore...PDBe-KBiSearch...MiscellaneousdatabasesRelativeevolutionaryimportanceofaminoacidswithinaproteinsequenceMore...EvolutionaryTraceiP55265

Thissectionprovidesinformationonsequencesimilaritieswithotherproteinsandthedomain(s)presentinaprotein.

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Family&DomainsiDomainsandRepeatsFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

ThissubsectionoftheFamilyandDomainssectiondescribesthepositionandtypeofadomain,whichisdefinedasaspecificcombinationofsecondarystructuresorganizedintoacharacteristicthree-dimensionalstructureorfold.

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Domaini133 – 199Z-binding1PROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU000733PublicationsManualassertionbasedonexperimentiniRef.50"CrystalstructureoftheZalphadomainofthehumaneditingenzymeADAR1boundtoleft-handedZ-DNA."SchwartzT.,RouldM.A.,LowenhauptK.,HerbertA.,RichA.Science284:1841-1845(1999)[PubMed][EuropePMC][Abstract]Citedfor:X-RAYCRYSTALLOGRAPHY(2.1ANGSTROMS)OF133-209INCOMPLEXWITHZ-DNA,DOMAIN.Ref.51"ThesolutionstructureoftheZalphadomainofthehumanRNAeditingenzymeADAR1revealsaprepositionedbindingsurfaceforZ-DNA."SchadeM.,TurnerC.J.,KuehneR.,SchmiederP.,LowenhauptK.,HerbertA.,RichA.,OschkinatH.Proc.Natl.Acad.Sci.U.S.A.96:12465-12470(1999)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF125-201INCOMPLEXWITHZ-DNAANDALONE,DOMAIN.Ref.52"CrystalstructureofajunctionbetweenB-DNAandZ-DNArevealstwoextrudedbases."HaS.C.,LowenhauptK.,RichA.,KimY.G.,KimK.K.Nature437:1183-1186(2005)[PubMed][EuropePMC][Abstract]Citedfor:X-RAYCRYSTALLOGRAPHY(2.60ANGSTROMS)OF140-202INCOMPLEXWITHDNA,DOMAIN.AddBLAST67Domaini293 – 357Z-binding2PROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU00073AddBLAST65Domaini503 – 571DRBM1PROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU00266AddBLAST69Domaini614 – 682DRBM2PROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU00266AddBLAST69Domaini726 – 794DRBM3PROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU002661PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.AddBLAST69Domaini886 – 1221AtoIeditasePROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU00240AddBLAST336RegionFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'FamilyandDomains'sectiondescribesaregionofinterestthatcannotbedescribedinothersubsections.

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Regioni133 – 202InteractionwithZ-DNA3PublicationsManualassertionbasedonexperimentiniRef.50"CrystalstructureoftheZalphadomainofthehumaneditingenzymeADAR1boundtoleft-handedZ-DNA."SchwartzT.,RouldM.A.,LowenhauptK.,HerbertA.,RichA.Science284:1841-1845(1999)[PubMed][EuropePMC][Abstract]Citedfor:X-RAYCRYSTALLOGRAPHY(2.1ANGSTROMS)OF133-209INCOMPLEXWITHZ-DNA,DOMAIN.Ref.51"ThesolutionstructureoftheZalphadomainofthehumanRNAeditingenzymeADAR1revealsaprepositionedbindingsurfaceforZ-DNA."SchadeM.,TurnerC.J.,KuehneR.,SchmiederP.,LowenhauptK.,HerbertA.,RichA.,OschkinatH.Proc.Natl.Acad.Sci.U.S.A.96:12465-12470(1999)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF125-201INCOMPLEXWITHZ-DNAANDALONE,DOMAIN.Ref.52"CrystalstructureofajunctionbetweenB-DNAandZ-DNArevealstwoextrudedbases."HaS.C.,LowenhauptK.,RichA.,KimY.G.,KimK.K.Nature437:1183-1186(2005)[PubMed][EuropePMC][Abstract]Citedfor:X-RAYCRYSTALLOGRAPHY(2.60ANGSTROMS)OF140-202INCOMPLEXWITHDNA,DOMAIN.AddBLAST70Regioni208 – 238DisorderedSequenceanalysis

InformationwhichhasbeengeneratedbytheUniProtKBautomaticannotationsystem,withoutmanualvalidation.

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AutomaticassertionaccordingtosequenceanalysisiSAM:MobiDB-lite(MobiDB:P55265)AddBLAST31Regioni258 – 286DisorderedSequenceanalysisAutomaticassertionaccordingtosequenceanalysisiSAM:MobiDB-lite(MobiDB:P55265)AddBLAST29Regioni574 – 610DisorderedSequenceanalysisAutomaticassertionaccordingtosequenceanalysisiSAM:MobiDB-lite(MobiDB:P55265)AddBLAST37Regioni716 – 725N-terminalextensionofDRBM3andconstituentofabi-partitenuclearlocalizationsignal1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.10Regioni795 – 801C-terminalextensionofDRBM3andconstituentofabi-partitenuclearlocalizationsignal1PublicationManualassertionbasedonexperimentiniRef.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.7CompositionalbiasFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'FamilyandDomains'sectiondescribesthepositionofregionsofcompositionalbiaswithintheproteinandtheparticulartypeofaminoacidsthatareover-representedwithinthoseregions.

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Compositionalbiasi574 – 597BasicandacidicresiduesSequenceanalysisAutomaticassertionaccordingtosequenceanalysisiSAM:MobiDB-lite(MobiDB:P55265)AddBLAST24

Thissubsectionofthe'Familyanddomains'sectionprovidesgeneralinformationonthebiologicalroleofadomain.Theterm'domain'isintendedhereinitswideacceptation,itmaybeastructuraldomain,atransmembraneregionorafunctionaldomain.Severaldomainsaredescribedinthissubsection.

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DomainiThethirddsRNA-bindingdomain(DRBM3)containsanadditionalN-terminalalpha-helixthatispartofabi-partitenuclearlocalizationsignal,togetherwiththesequenceimmediatelyC-terminaltoDRBM3.ThepresenceofDRBM3isimportanttobringtogethertheN-terminalandtheC-terminalpartofthebi-partitenuclearlocalizationsignalforimportmediatedbyTNPO1(PubMed:24753571).RNAbindinginterfereswithnuclearimport(PubMed:19124606,PubMed:24753571).2PublicationsManualassertionbasedonexperimentiniRef.27"RNA-regulatedinteractionoftransportin-1andexportin-5withthedouble-strandedRNA-bindingdomainregulatesnucleocytoplasmicshuttlingofADAR1."FritzJ.,StrehblowA.,TaschnerA.,SchopoffS.,PasierbekP.,JantschM.F.Mol.Cell.Biol.29:1487-1497(2009)[PubMed][EuropePMC][Abstract]Citedfor:SUBCELLULARLOCATION,INTERACTIONWITHTNPO1ANDXPO5,DOMAIN.Ref.53"Abimodularnuclearlocalizationsignalassembledviaanextendeddouble-strandedRNA-bindingdomainactsasanRNA-sensingsignalfortransportin1."BarraudP.,BanerjeeS.,MohamedW.I.,JantschM.F.,AllainF.H.Proc.Natl.Acad.Sci.U.S.A.111:E1852-E1861(2014)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF708-801,DOMAIN,SUBCELLULARLOCATION,INTERACTIONWITHTNPO1,MUTAGENESISOF708-MET--PRO-710;708-MET--ARG-801;712-LYS--LYS-715;716-ILE--ASN-724;ILE-716;GLU-718;LEU-719;ARG-721;LEU-723;ASN-724;725-THR--ARG-801;777-LYS-LYS-778ANDARG-801.ThefirstZ-bindingdomainbindsZ-DNA.PROSITE-ProRuleannotationManualassertionaccordingtorulesiPROSITE-ProRule:PRU000733PublicationsManualassertionbasedonexperimentiniRef.50"CrystalstructureoftheZalphadomainofthehumaneditingenzymeADAR1boundtoleft-handedZ-DNA."SchwartzT.,RouldM.A.,LowenhauptK.,HerbertA.,RichA.Science284:1841-1845(1999)[PubMed][EuropePMC][Abstract]Citedfor:X-RAYCRYSTALLOGRAPHY(2.1ANGSTROMS)OF133-209INCOMPLEXWITHZ-DNA,DOMAIN.Ref.51"ThesolutionstructureoftheZalphadomainofthehumanRNAeditingenzymeADAR1revealsaprepositionedbindingsurfaceforZ-DNA."SchadeM.,TurnerC.J.,KuehneR.,SchmiederP.,LowenhauptK.,HerbertA.,RichA.,OschkinatH.Proc.Natl.Acad.Sci.U.S.A.96:12465-12470(1999)[PubMed][EuropePMC][Abstract]Citedfor:STRUCTUREBYNMROF125-201INCOMPLEXWITHZ-DNAANDALONE,DOMAIN.Ref.52"CrystalstructureofajunctionbetweenB-DNAandZ-DNArevealstwoextrudedbases."HaS.C.,LowenhauptK.,RichA.,KimY.G.,KimK.K.Nature437:1183-1186(2005)[PubMed][EuropePMC][Abstract]Citedfor:X-RAYCRYSTALLOGRAPHY(2.60ANGSTROMS)OF140-202INCOMPLEXWITHDNA,DOMAIN.Keywords-DomainiRepeatPhylogenomicdatabasesevolutionarygenealogyofgenes:Non-supervisedOrthologousGroupsMore...eggNOGiKOG2777,EukaryotaEnsemblGeneTreeMore...GeneTreeiENSGT00940000157243TheHOGENOMDatabaseofHomologousGenesfromFullySequencedOrganismsMore...HOGENOMiCLU_005382_0_0_1InParanoid:EukaryoticOrthologGroupsMore...InParanoidiP55265IdentificationofOrthologsfromCompleteGenomeDataMore...OMAiMQMRLKADatabaseofOrthologousGroupsMore...OrthoDBi947117at2759DatabaseforcompletecollectionsofgenephylogeniesMore...PhylomeDBiP55265TreeFamdatabaseofanimalgenetreesMore...TreeFamiTF315806FamilyanddomaindatabasesConservedDomainsDatabaseMore...CDDicd19913,DSRM_DRADA_rpt1,1hitcd19915,DSRM_DRADA_rpt3,1hitGene3DStructuralandFunctionalAnnotationofProteinFamiliesMore...Gene3Di1.10.10.10,2hitsIntegratedresourceofproteinfamilies,domainsandfunctionalsitesMore...InterProiViewproteininInterProIPR002466,A_deaminIPR044456,ADAR1_DSRM_1IPR044457,ADAR1_DSRM_3IPR014720,dsRBD_domIPR036388,WH-like_DNA-bd_sfIPR036390,WH_DNA-bd_sfIPR042371,Z_domPfamproteindomaindatabaseMore...PfamiViewproteininPfamPF02137,A_deamin,1hitPF00035,dsrm,3hitsPF02295,z-alpha,2hitsSimpleModularArchitectureResearchTool;aproteindomaindatabaseMore...SMARTiViewproteininSMARTSM00552,ADEAMc,1hitSM00358,DSRM,3hitsSM00550,Zalpha,2hitsSuperfamilydatabaseofstructuralandfunctionalannotationMore...SUPFAMiSSF46785,SSF46785,2hitsPROSITE;aproteindomainandfamilydatabaseMore...PROSITEiViewproteininPROSITEPS50141,A_DEAMIN_EDITASE,1hitPS50137,DS_RBD,3hitsPS50139,Z_BINDING,2hits

Thissectiondisplaysbydefaultthecanonicalproteinsequenceanduponrequestallisoformsdescribedintheentry.Italsoincludesinformationpertinenttothesequence(s),includinglengthandmolecularweight.Theinformationisfiledindifferentsubsections.Thecurrentsubsectionsandtheircontentarelistedbelow:

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Sequences(5+)i

ThissubsectionoftheSequencesectionindicatesifthecanonicalsequencedisplayedbydefaultintheentryiscompleteornot.

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Sequencestatusi:Complete.Thisentrydescribes5

Thissubsectionofthe'Sequence'sectionliststhealternativeproteinsequences(isoforms)thatcanbegeneratedfromthesamegenebyasingleorbythecombinationofuptofourbiologicalevents(alternativepromoterusage,alternativesplicing,alternativeinitiationandribosomalframeshifting).Additionally,thissectiongivesrelevantinformationoneachalternativeproteinisoform.

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isoformsiproducedbyalternativepromoterusageandalternativesplicing.AlignAddtobasketAddedtobasketThisentryhas5describedisoformsand8potentialisoformsthatarecomputationallymapped.ShowallAlignAllIsoform1(identifier:P55265-1)[UniParc]FASTAAddtobasketAddedtobasketAlsoknownas:ADAR-a,ADAR1L,p150Thisisoformhasbeenchosenasthe

Whatisthecanonicalsequence?

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canonicalisequence.Allpositionalinformationinthisentryreferstoit.Thisisalsothesequencethatappearsinthedownloadableversionsoftheentry.«Hide1020304050MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQ60708090100LPEAPVIGKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLR110120130140150SQGLQRGFQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEEL160170180190200GEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVS210220230240250TQAWNQHSGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSEDLLEPFIAVSA260270280290300QAWNQHSGVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIK310320330340350EKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTP360370380390400PIWHLTDKKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNAS410420430440450NNMVTTEKVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAGYVDFE460470480490500NGQWATDDIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQ510520530540550LKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAE560570580590600AGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQ610620630640650TPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCV660670680690700AVGAQTFPSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPEGMISE710720730740750SLDNLESMMPNKVRKIGELVRYLNTNPVGGLLEYARSHGFAAEFKLVDQS760770780790800GPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGENEKAE810820830840850RMGFTEVTPVTGASLRRTMLLLSRSPEAQPKTLPLTGSTFHDQIAMLSHR860870880890900CFNTLTNSFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVKGDSLS910920930940950LKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKGGEKLQ9609709809901000IKKTVSFHLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENPKQGKL10101020103010401050RTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQG10601070108010901100ALLTHFLQPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGLRHPFI11101120113011401150VNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGTVDGPR11601170118011901200NELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETAKNYFK12101220KGLKDMGYGNWISKPQEEKNFYLCPVNote:Producedbyalternativepromoterusage.Show»Length:1,226Mass(Da):136,066Lastmodified:November30,2010-v4

Thechecksumisaformofredundancycheckthatiscalculated fromthesequence.Itisusefulfortrackingsequenceupdates.

Itshouldbenotedthatwhile,intheory,twodifferentsequencescould havethesamechecksumvalue,thelikelihoodthatthiswouldhappen isextremelylow.

HoweverUniProtKBmaycontainentrieswithidenticalsequencesincase ofmultiplegenes(paralogs).

Thechecksumiscomputedasthesequence64-bitCyclicRedundancyCheckvalue(CRC64) usingthegeneratorpolynomial:x⁶⁴+x⁴+x³+x+1. ThealgorithmisdescribedintheISO3309standard.

PressW.H.,FlanneryB.P.,TeukolskyS.A.andVetterlingW.T.
Cyclicredundancyandotherchecksums
NumericalrecipesinC2nded.,pp896-902,CambridgeUniversityPress(1993))

Checksum:i9CE095D6F9C1BC79BLASTProtParamProtScaleComputepI/MWPeptideMassPeptideCutterGOIsoform2(identifier:P55265-2)[UniParc]FASTAAddtobasketAddedtobasketAlsoknownas:ADAR-bThesequenceofthisisoformdiffersfromthecanonicalsequenceasfollows:     807-832:Missing.«Hide1020304050MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQ60708090100LPEAPVIGKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLR110120130140150SQGLQRGFQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEEL160170180190200GEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVS210220230240250TQAWNQHSGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSEDLLEPFIAVSA260270280290300QAWNQHSGVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIK310320330340350EKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTP360370380390400PIWHLTDKKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNAS410420430440450NNMVTTEKVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAGYVDFE460470480490500NGQWATDDIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQ510520530540550LKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAE560570580590600AGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQ610620630640650TPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCV660670680690700AVGAQTFPSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPEGMISE710720730740750SLDNLESMMPNKVRKIGELVRYLNTNPVGGLLEYARSHGFAAEFKLVDQS760770780790800GPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGENEKAE810820830840850RMGFTELPLTGSTFHDQIAMLSHRCFNTLTNSFQPSLLGRKILAAIIMKK860870880890900DSEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSE910920930940950LMKYNSQTAKDSIFEPAKGGEKLQIKKTVSFHLYISTAPCGDGALFDKSC9609709809901000SDRAMESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVPTWDGIR10101020103010401050LGERLRTMSCSDKILRWNVLGLQGALLTHFLQPIYLKSVTLGYLFSQGHL10601070108010901100TRAICCRVTRDGSAFEDGLRHPFIVNHPKVGRVSIYDSKRQSGKTKETSV11101120113011401150NWCLADGYDLEILDGTRGTVDGPRNELSRVSKKNIFLLFKKLCSFRYRRD11601170118011901200LLRLSYGEAKKAARDYETAKNYFKKGLKDMGYGNWISKPQEEKNFYLCPVNote:Producedbyalternativesplicingofisoform1.CuratedShow»Length:1,200Mass(Da):133,274Checksum:i4CB1B306DAC584FCBLASTProtParamProtScaleComputepI/MWPeptideMassPeptideCutterGOIsoform3(identifier:P55265-3)[UniParc]FASTAAddtobasketAddedtobasketAlsoknownas:ADAR-cThesequenceofthisisoformdiffersfromthecanonicalsequenceasfollows:     694-712:Missing.     807-832:Missing.«Hide1020304050MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQ60708090100LPEAPVIGKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLR110120130140150SQGLQRGFQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEEL160170180190200GEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVS210220230240250TQAWNQHSGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSEDLLEPFIAVSA260270280290300QAWNQHSGVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIK310320330340350EKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTP360370380390400PIWHLTDKKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNAS410420430440450NNMVTTEKVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAGYVDFE460470480490500NGQWATDDIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQ510520530540550LKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAE560570580590600AGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQ610620630640650TPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCV660670680690700AVGAQTFPSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQVRKIGEL710720730740750VRYLNTNPVGGLLEYARSHGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWF760770780790800PAVCAHSKKQGKQEAADAALRVLIGENEKAERMGFTELPLTGSTFHDQIA810820830840850MLSHRCFNTLTNSFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVK860870880890900GDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKG910920930940950GEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENP9609709809901000KQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNV10101020103010401050LGLQGALLTHFLQPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGL10601070108010901100RHPFIVNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGT11101120113011401150VDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETA116011701180KNYFKKGLKDMGYGNWISKPQEEKNFYLCPVNote:Producedbyalternativesplicingofisoform1.CuratedShow»Length:1,181Mass(Da):131,170Checksum:i9764C8AB27BE118EBLASTProtParamProtScaleComputepI/MWPeptideMassPeptideCutterGOIsoform4(identifier:P55265-4)[UniParc]FASTAAddtobasketAddedtobasketThesequenceofthisisoformdiffersfromthecanonicalsequenceasfollows:     1-5:MNPRQ → MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPEEVQDP«Hide1020304050MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPEEVQDPGY60708090100SLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQLPEAPVI110120130140150GKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLRSQGLQRG160170180190200FQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEELGEGKATT210220230240250AHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVSTQAWNQH260270280290300SGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSEDLLEPFIAVSAQAWNQHS310320330340350GVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIKEKICDYL360370380390400FNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTPPIWHLTD410420430440450KKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNASNNMVTTE460470480490500KVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAGYVDFENGQWATD510520530540550DIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQLKNPISG560570580590600LLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAEAGSKKVA610620630640650KQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQTPTPSAT660670680690700SFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCVAVGAQTF710720730740750PSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPEGMISESLDNLES760770780790800MMPNKVRKIGELVRYLNTNPVGGLLEYARSHGFAAEFKLVDQSGPPHEPK810820830840850FVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGENEKAERMGFTEV860870880890900TPVTGASLRRTMLLLSRSPEAQPKTLPLTGSTFHDQIAMLSHRCFNTLTN910920930940950SFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVKGDSLSLKGETVN9609709809901000DCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKGGEKLQIKKTVSF10101020103010401050HLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENPKQGKLRTKVENG10601070108010901100EGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFL11101120113011401150QPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGLRHPFIVNHPKVG11601170118011901200RVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGTVDGPRNELSRVS12101220123012401250KKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETAKNYFKKGLKDMG1260YGNWISKPQEEKNFYLCPVNote:Producedbyalternativesplicingofisoform1.CuratedShow»Length:1,269Mass(Da):140,838Checksum:iBB9B1DF19B8D3BC8BLASTProtParamProtScaleComputepI/MWPeptideMassPeptideCutterGOIsoform5(identifier:P55265-5)[UniParc]FASTAAddtobasketAddedtobasketAlsoknownas:ADAR1S,p110Thesequenceofthisisoformdiffersfromthecanonicalsequenceasfollows:     1-295:Missing.«Hide1020304050MAEIKEKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYR60708090100QGTTPPIWHLTDKKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIP110120130140150TSNASNNMVTTEKVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAG160170180190200YVDFENGQWATDDIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKK210220230240250LTECQLKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGRE260270280290300FPPAEAGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEK310320330340350TAESQTPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPK360370380390400FQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPE410420430440450GMISESLDNLESMMPNKVRKIGELVRYLNTNPVGGLLEYARSHGFAAEFK460470480490500LVDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGE510520530540550NEKAERMGFTEVTPVTGASLRRTMLLLSRSPEAQPKTLPLTGSTFHDQIA560570580590600MLSHRCFNTLTNSFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVK610620630640650GDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKG660670680690700GEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENP710720730740750KQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNV760770780790800LGLQGALLTHFLQPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGL810820830840850RHPFIVNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGT860870880890900VDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETA910920930KNYFKKGLKDMGYGNWISKPQEEKNFYLCPVNote:Producedbyalternativepromoterusage.CuratedShow»Length:931Mass(Da):103,642Checksum:i113B63CF165097FCBLASTProtParamProtScaleComputepI/MWPeptideMassPeptideCutterGO

Ineukaryoticreferenceproteomes,unreviewedentriesthatarelikelytobelongtothesamegenearecomputationallymapped,basedongeneidentifiersfromEnsembl,EnsemblGenomesandmodelorganismdatabases.

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ComputationallymappedpotentialisoformsequencesiThereare8potentialisoformsmappedtothisentry.BLASTAlignShowallAddtobasketEntryEntrynameProteinnamesGenenamesLengthAnnotationA0A3B3IRQ9A0A3B3IRQ9_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminaseADAR1,158Annotationscore:Annotationscore:2outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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A0A3B3ISU1A0A3B3ISU1_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminaseADAR1,046Annotationscore:Annotationscore:1outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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A0A7P0Z4F9A0A7P0Z4F9_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminaseADAR912Annotationscore:Annotationscore:1outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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A0A7P0Z4K3A0A7P0Z4K3_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminaseADAR1,165Annotationscore:Annotationscore:1outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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A0A3B3ITG9A0A3B3ITG9_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminaseADAR350Annotationscore:Annotationscore:1outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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A0A3B3ISX1A0A3B3ISX1_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminaseADAR788Annotationscore:Annotationscore:1outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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A0A7P0TA14A0A7P0TA14_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminaseADAR263Annotationscore:Annotationscore:1outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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A2IBT1A2IBT1_HUMANDouble-strandedRNA-specificadenos...Double-strandedRNA-specificadenosinedeaminase(TruncatedadenosinedeaminaseactingonRNA1-A)ADAR87Annotationscore:Annotationscore:1outof5

TheannotationscoreprovidesaheuristicmeasureoftheannotationcontentofaUniProtKBentryorproteome.Thisscorecannotbeusedasameasureoftheaccuracyoftheannotationaswecannotdefinethe'correctannotation'foranygivenprotein.

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Thissubsectionofthe'Sequence'sectionreportsdifference(s)betweentheproteinsequenceshownintheUniProtKBentryandotheravailableproteinsequencesderivedfromthesamegene.

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SequencecautioniThesequenceCAE45853differsfromthatshown.Reason:Erroneoustermination.ExtendedC-terminus.CuratedExperimentalInfoFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'Sequence'sectionreportsdifference(s)betweenthecanonicalsequence(displayedbydefaultintheentry)andthedifferentsequencesubmissionsmergedintheentry.Thesevarioussubmissionsmayoriginatefromdifferentsequencingprojects,differenttypesofexperiments,ordifferentbiologicalsamples.Sequenceconflictsareusuallyofunknownorigin.

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Sequenceconflicti53E→GinCAA55968(Ref.4)Curated1Sequenceconflicti245F→LinCAE45853(PubMed:17974005).Curated1Sequenceconflicti482F→LinCAE45853(PubMed:17974005).Curated1Sequenceconflicti873I→VinCAE45853(PubMed:17974005).Curated1Sequenceconflicti1093D→GinCAE45853(PubMed:17974005).Curated1Sequenceconflicti1184E→KinCAA55967(Ref.4)Curated1Sequenceconflicti1184E→KinCAA55968(Ref.4)Curated1Sequenceconflicti1184E→KinCAA67169(Ref.4)Curated1Sequenceconflicti1184E→KinCAA67170(Ref.4)Curated1Isoform4(identifier:P55265-4)Sequenceconflicti13R→GinCAE45853(PubMed:17974005).Curated1NaturalvariantFeaturekeyPosition(s)DescriptionActionsGraphicalviewLengthNaturalvariantiVAR_048725100R→G6PublicationsManualassertionbasedonexperimentiniRef.1"MolecularcloningofcDNAfordouble-strandedRNAadenosinedeaminase,acandidateenzymefornuclearRNAediting."KimU.,WangY.,SanfordT.,ZengY.,NishikuraK.Proc.Natl.Acad.Sci.U.S.A.91:11457-11461(1994)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),PARTIALPROTEINSEQUENCE,FUNCTION,CATALYTICACTIVITY,TISSUESPECIFICITY,VARIANTGLY-100.Ref.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.3"Functionallydistinctdouble-strandedRNA-bindingdomainsassociatedwithalternativesplicesitevariantsoftheinterferon-inducibledouble-strandedRNA-specificadenosinedeaminase."LiuY.,GeorgeC.X.,PattersonJ.B.,SamuelC.E.J.Biol.Chem.272:4419-4428(1997)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[GENOMICDNA](ISOFORMS1;2AND3),VARIANTSGLY-100ANDARG-384.Ref.4"Thegenecodingfortheinterferon-induciblehumandsRNAadenosinedeaminaseistranscribedintoseveralmessengersspecifyingdifferentproteins."DeblandreG.,MarinxO.,NolsC.,DefranceP.,BerrP.,HuezG.,CaputD.Submitted(JUN-1996)totheEMBL/GenBank/DDBJdatabasesCitedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORMS1AND5),VARIANTSGLY-100ANDARG-384.Ref.5"Thefull-ORFcloneresourceoftheGermancDNAconsortium."BechtelS.,RosenfelderH.,DudaA.,SchmidtC.P.,ErnstU.,WellenreutherR.,MehrleA.,SchusterC.,BahrA.,BloeckerH.,HeubnerD.,HoerleinA.,MichelG.,WedlerH.,KoehrerK.,OttenwaelderB.,PoustkaA.,WiemannS.,SchuppI.BMCGenomics8:399-399(2007)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[LARGESCALEMRNA](ISOFORM4),VARIANTSGLY-100ANDARG-384.Ref.8"Thestatus,quality,andexpansionoftheNIHfull-lengthcDNAproject:theMammalianGeneCollection(MGC)."TheMGCProjectTeamGenomeRes.14:2121-2127(2004)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[LARGESCALEMRNA](ISOFORM1),VARIANTGLY-100.CorrespondstovariantdbSNP:rs1466731EnsemblClinVar.1NaturalvariantiVAR_069535193P→AinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs145588689EnsemblClinVar.1NaturalvariantiVAR_017240384K→R4PublicationsManualassertionbasedonexperimentiniRef.2"Expressionandregulationbyinterferonofadouble-stranded-RNA-specificadenosinedeaminasefromhumancells:evidencefortwoformsofthedeaminase."PattersonJ.B.,SamuelC.E.Mol.Cell.Biol.15:5376-5388(1995)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORM1),FUNCTION,CATALYTICACTIVITY,SUBCELLULARLOCATION,INDUCTIONBYINTERFERON,VARIANTSGLY-100ANDARG-384.Ref.3"Functionallydistinctdouble-strandedRNA-bindingdomainsassociatedwithalternativesplicesitevariantsoftheinterferon-inducibledouble-strandedRNA-specificadenosinedeaminase."LiuY.,GeorgeC.X.,PattersonJ.B.,SamuelC.E.J.Biol.Chem.272:4419-4428(1997)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[GENOMICDNA](ISOFORMS1;2AND3),VARIANTSGLY-100ANDARG-384.Ref.4"Thegenecodingfortheinterferon-induciblehumandsRNAadenosinedeaminaseistranscribedintoseveralmessengersspecifyingdifferentproteins."DeblandreG.,MarinxO.,NolsC.,DefranceP.,BerrP.,HuezG.,CaputD.Submitted(JUN-1996)totheEMBL/GenBank/DDBJdatabasesCitedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORMS1AND5),VARIANTSGLY-100ANDARG-384.Ref.5"Thefull-ORFcloneresourceoftheGermancDNAconsortium."BechtelS.,RosenfelderH.,DudaA.,SchmidtC.P.,ErnstU.,WellenreutherR.,MehrleA.,SchusterC.,BahrA.,BloeckerH.,HeubnerD.,HoerleinA.,MichelG.,WedlerH.,KoehrerK.,OttenwaelderB.,PoustkaA.,WiemannS.,SchuppI.BMCGenomics8:399-399(2007)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[LARGESCALEMRNA](ISOFORM4),VARIANTSGLY-100ANDARG-384.CorrespondstovariantdbSNP:rs2229857EnsemblClinVar.1NaturalvariantiVAR_024407587Y→C.CorrespondstovariantdbSNP:rs17843865EnsemblClinVar.1NaturalvariantiVAR_035805806E→Vinabreastcancersample;somaticmutation.1PublicationManualassertionbasedonexperimentiniRef.57"Theconsensuscodingsequencesofhumanbreastandcolorectalcancers."SjoeblomT.,JonesS.,WoodL.D.,ParsonsD.W.,LinJ.,BarberT.D.,MandelkerD.,LearyR.J.,PtakJ.,SillimanN.,SzaboS.,BuckhaultsP.,FarrellC.,MeehP.,MarkowitzS.D.,WillisJ.,DawsonD.,WillsonJ.K.V.,GazdarA.F.,HartiganJ.,WuL.,LiuC.,ParmigianiG.,ParkB.H.,BachmanK.E.,PapadopoulosN.,VogelsteinB.,KinzlerK.W.,VelculescuV.E.Science314:268-274(2006)[PubMed][EuropePMC][Abstract]Citedfor:VARIANT[LARGESCALEANALYSIS]VAL-806.CorrespondstovariantdbSNP:rs144119808Ensembl.1NaturalvariantiVAR_069536870A→TinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122893EnsemblClinVar.1NaturalvariantiVAR_069537872I→TinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122897EnsemblClinVar.1NaturalvariantiVAR_069538892R→HinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122892EnsemblClinVar.1NaturalvariantiVAR_017604923L→PinDSH.1PublicationManualassertionbasedonexperimentiniRef.54"MutationsoftheRNA-specificadenosinedeaminasegene(DSRAD)areinvolvedindyschromatosissymmetricahereditaria."MiyamuraY.,SuzukiT.,KonoM.,InagakiK.,ItoS.,SuzukiN.,TomitaY.Am.J.Hum.Genet.73:693-699(2003)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSDSHPRO-923ANDSER-1165.CorrespondstovariantdbSNP:rs28936680EnsemblClinVar.1NaturalvariantiVAR_021729966C→FinDSH.1PublicationManualassertionbasedonexperimentiniRef.55"SevennovelmutationsoftheADARgeneinChinesefamiliesandsporadicpatientswithdyschromatosissymmetricahereditaria(DSH)."ZhangX.-J.,HeP.-P.,LiM.,HeC.-D.,YanK.-L.,CuiY.,YangS.,ZhangK.-Y.,GaoM.,ChenJ.-J.,LiC.-R.,JinL.,ChenH.-D.,XuS.-J.,HuangW.Hum.Mutat.23:629-630(2004)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTDSHPHE-966.1NaturalvariantiVAR_069539999K→NinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122896EnsemblClinVar.1NaturalvariantiVAR_0695401007G→RinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122822EnsemblClinVar.1NaturalvariantiVAR_0695411112Y→FinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122895EnsemblClinVar.1NaturalvariantiVAR_0695421113D→HinAGS6.1PublicationManualassertionbasedonexperimentiniRef.58"MutationsinADAR1causeAicardi-GoutieressyndromeassociatedwithatypeIinterferonsignature."RiceG.I.,KasherP.R.,ForteG.M.,MannionN.M.,GreenwoodS.M.,SzynkiewiczM.,DickersonJ.E.,BhaskarS.S.,ZampiniM.,BriggsT.A.,JenkinsonE.M.,BacinoC.A.,BattiniR.,BertiniE.,BroganP.A.,BruetonL.A.,CarpanelliM.,DeLaetC.,deLonlayP.,delToroM.,DesguerreI.,FazziE.,Garcia-CazorlaA.,HeibergA.,KawaguchiM.,KumarR.,LinJ.P.,LourencoC.M.,MaleA.M.,MarquesW.Jr.,MignotC.,OlivieriI.,OrcesiS.,PrabhakarP.,RasmussenM.,RobinsonR.A.,RozenbergF.,SchmidtJ.L.,SteindlK.,TanT.Y.,vanderMerweW.G.,VanderverA.,VassalloG.,WakelingE.L.,WassmerE.,WhittakerE.,LivingstonJ.H.,LebonP.,SuzukiT.,McLaughlinP.J.,KeeganL.P.,O'ConnellM.A.,LovellS.C.,CrowY.J.Nat.Genet.44:1243-1248(2012)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSAGS6ALA-193;THR-870;THR-872;HIS-892;ASN-999;ARG-1007;PHE-1112ANDHIS-1113.CorrespondstovariantdbSNP:rs398122894EnsemblClinVar.1NaturalvariantiVAR_0266691155R→WinDSH.1PublicationManualassertionbasedonexperimentiniRef.56"AnewargininesubstitutionmutationofDSRADgeneinaChinesefamilywithdyschromatosissymmetricahereditaria."LiC.-R.,LiM.,MaH.-J.,LuoD.,YangL.-J.,WangD.-G.,ZhuX.-H.,YueX.-Z.,ChenW.-Q.,ZhuW.-Y.J.Dermatol.Sci.37:95-99(2005)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTDSHTRP-1155.CorrespondstovariantdbSNP:rs1044845711Ensembl.1NaturalvariantiVAR_0176051165F→SinDSH.1PublicationManualassertionbasedonexperimentiniRef.54"MutationsoftheRNA-specificadenosinedeaminasegene(DSRAD)areinvolvedindyschromatosissymmetricahereditaria."MiyamuraY.,SuzukiT.,KonoM.,InagakiK.,ItoS.,SuzukiN.,TomitaY.Am.J.Hum.Genet.73:693-699(2003)[PubMed][EuropePMC][Abstract]Citedfor:VARIANTSDSHPRO-923ANDSER-1165.CorrespondstovariantdbSNP:rs28936681EnsemblClinVar.1AlternativesequenceFeaturekeyPosition(s)DescriptionActionsGraphicalviewLength

Thissubsectionofthe'Sequence'sectiondescribesthesequenceofnaturallyoccurringalternativeproteinisoform(s).Thechangesintheaminoacidsequencemaybeduetoalternativesplicing,alternativepromoterusage,alternativeinitiation,orribosomalframeshifting.

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AlternativesequenceiVSP_0192351 – 295Missinginisoform5.1PublicationManualassertionbasedonopinioniniRef.4"Thegenecodingfortheinterferon-induciblehumandsRNAadenosinedeaminaseistranscribedintoseveralmessengersspecifyingdifferentproteins."DeblandreG.,MarinxO.,NolsC.,DefranceP.,BerrP.,HuezG.,CaputD.Submitted(JUN-1996)totheEMBL/GenBank/DDBJdatabasesCitedfor:NUCLEOTIDESEQUENCE[MRNA](ISOFORMS1AND5),VARIANTSGLY-100ANDARG-384.AddBLAST295AlternativesequenceiVSP_0088721 – 5MNPRQ→MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPEEVQDPinisoform4.1PublicationManualassertionbasedonopinioniniRef.5"Thefull-ORFcloneresourceoftheGermancDNAconsortium."BechtelS.,RosenfelderH.,DudaA.,SchmidtC.P.,ErnstU.,WellenreutherR.,MehrleA.,SchusterC.,BahrA.,BloeckerH.,HeubnerD.,HoerleinA.,MichelG.,WedlerH.,KoehrerK.,OttenwaelderB.,PoustkaA.,WiemannS.,SchuppI.BMCGenomics8:399-399(2007)[PubMed][EuropePMC][Abstract]Citedfor:NUCLEOTIDESEQUENCE[LARGESCALEMRNA](ISOFORM4),VARIANTSGLY-100ANDARG-384.5AlternativesequenceiVSP_008873694 – 712Missinginisoform3.CuratedAddBLAST19AlternativesequenceiVSP_008874807 – 832Missinginisoform2andisoform3.CuratedAddBLAST26SequencedatabasesSelectthelinkdestinations:EMBLnucleotidesequencedatabaseMore...EMBLiGenBanknucleotidesequencedatabaseMore...GenBankiDNADataBankofJapan;anucleotidesequencedatabaseMore...DDBJiLinksUpdatedU10439mRNATranslation:AAB06697.1U75503,U75489,U75490,U75491,U75492,U75493,U75494,U75495,U75496,U75497,U75498,U75499,U75500,U75501,U75502GenomicDNATranslation:AAB97116.1U75503,U75489,U75490,U75491,U75492,U75493,U75494,U75495,U75496,U75497,U75498,U75499,U75500,U75501,U75502GenomicDNATranslation:AAB97117.1U75503,U75489,U75490,U75491,U75492,U75493,U75494,U75495,U75496,U75497,U75498,U75499,U75500,U75501,U75502GenomicDNATranslation:AAB97118.1U18121mRNATranslation:AAC13782.1X79448mRNATranslation:CAA55967.1X79449mRNATranslation:CAA55968.1X98559mRNATranslation:CAA67169.1X98559mRNATranslation:CAA67170.1BX538232mRNATranslation:CAD98075.1BX640741mRNATranslation:CAE45853.1Sequenceproblems.AL592078GenomicDNANotranslationavailable.AL606500GenomicDNANotranslationavailable.AL691488GenomicDNANotranslationavailable.CH471121GenomicDNATranslation:EAW53183.1CH471121GenomicDNATranslation:EAW53187.1BC038227mRNATranslation:AAH38227.1TheConsensusCDS(CCDS)projectMore...CCDSiCCDS1071.1[P55265-1]CCDS30879.1[P55265-5]ProteinsequencedatabaseoftheProteinInformationResourceMore...PIRiS65593NCBIReferenceSequencesMore...RefSeqiNP_001020278.1,NM_001025107.2[P55265-5]NP_001102.2,NM_001111.4[P55265-1]NP_001180424.1,NM_001193495.1[P55265-5]NP_056655.2,NM_015840.3[P55265-2]NP_056656.2,NM_015841.3[P55265-3]XP_006711174.1,XM_006711111.3XP_006711175.1,XM_006711112.2XP_006711176.1,XM_006711113.2[P55265-5]GenomeannotationdatabasesEnsembleukaryoticgenomeannotationprojectMore...EnsembliENST00000368471.8;ENSP00000357456.3;ENSG00000160710.18[P55265-5]ENST00000368474.9;ENSP00000357459.4;ENSG00000160710.18ENST00000529168.2;ENSP00000431794.2;ENSG00000160710.18[P55265-2]ENST00000648231.2;ENSP00000497555.1;ENSG00000160710.18[P55265-5]ENST00000648311.1;ENSP00000498137.1;ENSG00000160710.18[P55265-5]ENST00000649022.2;ENSP00000496896.2;ENSG00000160710.18[P55265-5]ENST00000649042.1;ENSP00000497790.1;ENSG00000160710.18[P55265-5]ENST00000649724.1;ENSP00000497932.1;ENSG00000160710.18[P55265-5]ENST00000649749.1;ENSP00000497210.1;ENSG00000160710.18[P55265-5]ENST00000680270.1;ENSP00000505532.1;ENSG00000160710.18[P55265-5]ENST00000681056.1;ENSP00000506234.1;ENSG00000160710.18[P55265-5]ENST00000681683.1;ENSP00000506666.1;ENSG00000160710.18[P55265-5]DatabaseofgenesfromNCBIRefSeqgenomesMore...GeneIDi103KEGG:KyotoEncyclopediaofGenesandGenomesMore...KEGGihsa:103MatchedAnnotationfromNCBIandEMBL-EBI(MANE)-PhaseoneMore...MANE-SelectiENST00000368474.9;ENSP00000357459.4;NM_001111.5;NP_001102.3UCSCgenomebrowserMore...UCSCiuc001ffh.4,human[P55265-1]Keywords-CodingsequencediversityiAlternativepromoterusage,Alternativesplicing

Thissectionprovideslinkstoproteinsthataresimilartotheproteinsequence(s)describedinthisentryatdifferentlevelsofsequenceidentitythresholds(100%,90%and50%)basedontheirmembershipinUniProtReferenceClusters(UniRef).

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Similarproteinsi100%Identity90%Identity50%IdentityProteinSimilarproteinsSpeciesScoreLengthSourceP55265-3Adenosinedeaminase,RNA-specific,isoformCRA_bHUMAN886UniRef100_D3DV75P55265-4Isoform5ofDouble-strandedRNA-specificadenosinedeaminaseHUMAN931UniRef100_P55265-4Double-strandedRNA-specificadenosinedeaminase(Fragment)HUMAN350FullviewProteinSimilarproteinsSpeciesScoreLengthSourceP55265Isoform4ofDouble-strandedRNA-specificadenosinedeaminaseHUMAN1269UniRef90_P55265AdenosinedeaminaseRNAspecificGORGO1229AdenosinedeaminaseRNAspecificPANTR1229AdenosinedeaminaseRNAspecificPONAB1226AdenosinedeaminaseRNAspecificPANPA193+24P55265-2AdenosinedeaminaseRNAspecificMACNE1364UniRef90_P55265-2AdenosinedeaminaseRNAspecificCERAT1316UncharacterizedproteinMACMU1269UncharacterizedproteinMACFA1268AdenosinedeaminaseRNAspecificPAPAN1260+84FullviewProteinSimilarproteinsSpeciesScoreLengthSourceP55265Double-strandedRNA-specificadenosinedeaminaseMOUSE1178UniRef50_P55265Double-strandedRNA-specificadenosinedeaminaseRAT1175Isoform4ofDouble-strandedRNA-specificadenosinedeaminaseHUMAN1269AdenosinedeaminaseRNAspecificGORGO1229AdenosinedeaminaseRNAspecificPANTR1229+396Fullview

ThissectionisusedtopointtoinformationrelatedtoentriesandfoundindatacollectionsotherthanUniProtKB.

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Cross-referencesiSequencedatabasesSelectthelinkdestinations:EMBLiGenBankiDDBJiLinksUpdatedU10439mRNATranslation:AAB06697.1U75503,U75489,U75490,U75491,U75492,U75493,U75494,U75495,U75496,U75497,U75498,U75499,U75500,U75501,U75502GenomicDNATranslation:AAB97116.1U75503,U75489,U75490,U75491,U75492,U75493,U75494,U75495,U75496,U75497,U75498,U75499,U75500,U75501,U75502GenomicDNATranslation:AAB97117.1U75503,U75489,U75490,U75491,U75492,U75493,U75494,U75495,U75496,U75497,U75498,U75499,U75500,U75501,U75502GenomicDNATranslation:AAB97118.1U18121mRNATranslation:AAC13782.1X79448mRNATranslation:CAA55967.1X79449mRNATranslation:CAA55968.1X98559mRNATranslation:CAA67169.1X98559mRNATranslation:CAA67170.1BX538232mRNATranslation:CAD98075.1BX640741mRNATranslation:CAE45853.1Sequenceproblems.AL592078GenomicDNANotranslationavailable.AL606500GenomicDNANotranslationavailable.AL691488GenomicDNANotranslationavailable.CH471121GenomicDNATranslation:EAW53183.1CH471121GenomicDNATranslation:EAW53187.1BC038227mRNATranslation:AAH38227.1CCDSiCCDS1071.1[P55265-1]CCDS30879.1[P55265-5]PIRiS65593RefSeqiNP_001020278.1,NM_001025107.2[P55265-5]NP_001102.2,NM_001111.4[P55265-1]NP_001180424.1,NM_001193495.1[P55265-5]NP_056655.2,NM_015840.3[P55265-2]NP_056656.2,NM_015841.3[P55265-3]XP_006711174.1,XM_006711111.3XP_006711175.1,XM_006711112.2XP_006711176.1,XM_006711113.2[P55265-5]3DstructuredatabasesSelectthelinkdestinations:ProteinDataBankEuropeMore...PDBeiProteinDataBankRCSBMore...RCSBPDBiProteinDataBankJapanMore...PDBjiLinksUpdatedPDBentryMethodResolution(Å)ChainPositionsPDBsum1QBJX-ray2.10A/B/C133-209[»]1QGPNMR-A125-200[»]1XMKX-ray0.97A294-366[»]2ACJX-ray2.60A/B/C/D140-202[»]2GXBX-ray2.25A/B140-202[»]2L54NMR-A136-198[»]2MDRNMR-A708-801[»]3F21X-ray2.20A/B/C133-209[»]3F22X-ray2.50A/B/C133-209[»]3F23X-ray2.70A/B/C133-209[»]3IRQX-ray2.80A/B/C/D140-202[»]3IRRX-ray2.65A/B/C/D140-202[»]5ZU1X-ray3.01A/B/C/D140-198[»]5ZUOX-ray2.90A/B/C/D140-202[»]5ZUPX-ray2.90A/B/C/D140-202[»]7C0IX-ray2.40A/B/C170-184[»]AlphaFoldDBiP55265SMRiP55265ModBaseiSearch...PDBe-KBiSearch...Protein-proteininteractiondatabasesBioGRIDi106617,162interactorsCORUMiP55265DIPiDIP-29310NIntActiP55265,76interactorsMINTiP55265STRINGi9606.ENSP00000357459PTMdatabasesGlyGeniP55265,4sites,2O-linkedglycans(4sites)iPTMnetiP55265MetOSiteiP55265PhosphoSitePlusiP55265SwissPalmiP55265GeneticvariationdatabasesBioMutaiADARDMDMi313104303ProteomicdatabasesEPDiP55265jPOSTiP55265MassIVEiP55265MaxQBiP55265PaxDbiP55265PeptideAtlasiP55265PRIDEiP55265ProteomicsDBi56826[P55265-1]56827[P55265-2]56828[P55265-3]56829[P55265-4]56830[P55265-5]ProtocolsandmaterialsdatabasesAntibodypediaaportalforvalidatedantibodiesMore...Antibodypediai1280,278antibodiesfrom32providersTheDNASUplasmidrepositoryMore...DNASUi103GenomeannotationdatabasesEnsembliENST00000368471.8;ENSP00000357456.3;ENSG00000160710.18[P55265-5]ENST00000368474.9;ENSP00000357459.4;ENSG00000160710.18ENST00000529168.2;ENSP00000431794.2;ENSG00000160710.18[P55265-2]ENST00000648231.2;ENSP00000497555.1;ENSG00000160710.18[P55265-5]ENST00000648311.1;ENSP00000498137.1;ENSG00000160710.18[P55265-5]ENST00000649022.2;ENSP00000496896.2;ENSG00000160710.18[P55265-5]ENST00000649042.1;ENSP00000497790.1;ENSG00000160710.18[P55265-5]ENST00000649724.1;ENSP00000497932.1;ENSG00000160710.18[P55265-5]ENST00000649749.1;ENSP00000497210.1;ENSG00000160710.18[P55265-5]ENST00000680270.1;ENSP00000505532.1;ENSG00000160710.18[P55265-5]ENST00000681056.1;ENSP00000506234.1;ENSG00000160710.18[P55265-5]ENST00000681683.1;ENSP00000506666.1;ENSG00000160710.18[P55265-5]GeneIDi103KEGGihsa:103MANE-SelectiENST00000368474.9;ENSP00000357459.4;NM_001111.5;NP_001102.3UCSCiuc001ffh.4,human[P55265-1]Organism-specificdatabasesComparativeToxicogenomicsDatabaseMore...CTDi103DisGeNETi103GeneCards:humangenes,proteinanddiseasesMore...GeneCardsiADARGeneReviewsiADARHGNCiHGNC:225,ADARHPAiENSG00000160710,LowtissuespecificityMalaCardsiADARMIMi127400,phenotype146920,gene615010,phenotypeneXtProtiNX_P55265OpenTargetsiENSG00000160710Orphaneti51,Aicardi-Goutieressyndrome41,Dyschromatosissymmetricahereditaria225154,FamilialinfantilebilateralstriatalnecrosisPharmGKBiPA24555VEuPathDBiHostDB:ENSG00000160710GenAtlas:humangenedatabaseMore...GenAtlasiSearch...PhylogenomicdatabaseseggNOGiKOG2777,EukaryotaGeneTreeiENSGT00940000157243HOGENOMiCLU_005382_0_0_1InParanoidiP55265OMAiMQMRLKAOrthoDBi947117at2759PhylomeDBiP55265TreeFamiTF315806EnzymeandpathwaydatabasesBRENDAi3.5.4.37,2681PathwayCommonsiP55265ReactomeiR-HSA-75102,C6deaminationofadenosineR-HSA-77042,FormationofeditosomesbyADARproteinsR-HSA-909733,Interferonalpha/betasignalingSignaLinkiP55265SIGNORiP55265MiscellaneousdatabasesBioGRIDORCSdatabaseofCRISPRphenotypescreensMore...BioGRID-ORCSi103,284hitsin1085CRISPRscreensChiTaRS:adatabaseofhuman,mouseandfruitflychimerictranscriptsandRNA-sequencingdataMore...ChiTaRSiADAR,humanEvolutionaryTraceiP55265TheGeneWikicollectionofpagesonhumangenesandproteinsMore...GeneWikiiADARDatabaseofphenotypesfromRNAinterferencescreensinDrosophilaandHomosapiensMore...GenomeRNAii103PharosiP55265,TbioProteinOntologyMore...PROiPR:P55265RNActiP55265,proteinTheStanfordOnlineUniversalResourceforClonesandESTsMore...SOURCEiSearch...GeneexpressiondatabasesBgeeiENSG00000160710,Expressedintestisand249othertissuesExpressionAtlasiP55265,baselineanddifferentialGenevisibleiP55265,HSFamilyanddomaindatabasesCDDicd19913,DSRM_DRADA_rpt1,1hitcd19915,DSRM_DRADA_rpt3,1hitGene3Di1.10.10.10,2hitsInterProiViewproteininInterProIPR002466,A_deaminIPR044456,ADAR1_DSRM_1IPR044457,ADAR1_DSRM_3IPR014720,dsRBD_domIPR036388,WH-like_DNA-bd_sfIPR036390,WH_DNA-bd_sfIPR042371,Z_domPfamiViewproteininPfamPF02137,A_deamin,1hitPF00035,dsrm,3hitsPF02295,z-alpha,2hitsSMARTiViewproteininSMARTSM00552,ADEAMc,1hitSM00358,DSRM,3hitsSM00550,Zalpha,2hitsSUPFAMiSSF46785,SSF46785,2hitsPROSITEiViewproteininPROSITEPS50141,A_DEAMIN_EDITASE,1hitPS50137,DS_RBD,3hitsPS50139,Z_BINDING,2hitsMobiDB:adatabaseofproteindisorderandmobilityannotationsMore...MobiDBiSearch...

Thissectionprovidesgeneralinformationontheentry.

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Entryinformationi

Thissubsectionofthe'Entryinformation'sectionprovidesamnemonicidentifierforaUniProtKBentry,butitisnotastableidentifier.EachreviewedentryisassignedauniqueentrynameuponintegrationintoUniProtKB/Swiss-Prot.

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EntrynameiDSRAD_HUMAN

Thissubsectionofthe'Entryinformation'sectionprovidesoneormoreaccessionnumber(s).ThesearestableidentifiersandshouldbeusedtociteUniProtKBentries.UponintegrationintoUniProtKB,eachentryisassignedauniqueaccessionnumber,whichiscalled'Primary(citable)accessionnumber'.

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AccessioniP55265Primary(citable)accessionnumber:P55265Secondaryaccessionnumber(s):B1AQQ9,B1AQR0,D3DV76,O15223,O43859,O43860,Q9BYM3,Q9BYM4

Thissubsectionofthe'Entryinformation'sectionshowsthedateofintegrationoftheentryintoUniProtKB,thedateofthelastsequenceupdateandthedateofthelastannotationmodification('Lastmodified').Theversionnumberforboththeentryandthecanonicalsequencearealsodisplayed.

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EntryhistoryiIntegratedintoUniProtKB/Swiss-Prot:October1,1996Lastsequenceupdate:November30,2010Lastmodified:May25,2022Thisisversion222oftheentryandversion4ofthesequence.Seecompletehistory.

Thissubsectionofthe'Entryinformation'sectionindicateswhethertheentryhasbeenmanuallyannotatedandreviewedbyUniProtKBcuratorsornot,inotherwords,iftheentrybelongstotheSwiss-ProtsectionofUniProtKB(reviewed)ortothecomputer-annotatedTrEMBLsection(unreviewed).

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EntrystatusiReviewed(UniProtKB/Swiss-Prot)AnnotationprogramChordataProteinAnnotationProgramDisclaimerAnymedicalorgeneticinformationpresentinthisentryisprovidedforresearch,educationalandinformationalpurposesonly.Itisnotinanywayintendedtobeusedasasubstituteforprofessionalmedicaladvice,diagnosis,treatmentorcare.

Thissectioncontainsanyrelevantinformationthatdoesn'tfitinanyotherdefinedsections

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MiscellaneousiKeywords-Technicaltermi3D-structure,Directproteinsequencing,ReferenceproteomeDocumentsHumanchromosome1Humanchromosome1:entries,genenamesandcross-referencestoMIMHumanentrieswithgeneticvariantsListofhumanentrieswithgeneticvariantsHumanvariantscuratedfromliteraturereportsIndexofhumanvariantscuratedfromliteraturereportsMIMcross-referencesOnlineMendelianInheritanceinMan(MIM)cross-referencesinUniProtKB/Swiss-ProtPDBcross-referencesIndexofProteinDataBank(PDB)cross-referencesUniProtisanELIXIRcoredataresource Mainfundingby: NationalInstitutesofHealthTheEuropeanMolecularBiologyLaboratoryStateSecretariatforEducation,ResearchandInnovationSERIWe'dliketoinformyouthatwehaveupdatedourPrivacyNoticetocomply withEurope’snewGeneralDataProtectionRegulation(GDPR)thatappliessince25May2018.Donotshowthisbanneragain