ID DSRAD_HUMAN Reviewed; 1226 AA. AC P55265; B1AQQ9; B1AQR0; D3DV76; O15223; O43859; O43860; Q9BYM3; Q9BYM4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 4. DT 27-MAR-2024, entry version 232. DE RecName: Full=Double-stranded RNA-specific adenosine deaminase; DE Short=DRADA {ECO:0000303|PubMed:7972084}; DE EC=3.5.4.37 {ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084}; DE AltName: Full=136 kDa double-stranded RNA-binding protein; DE Short=p136; DE AltName: Full=Interferon-inducible protein 4; DE Short=IFI-4; DE AltName: Full=K88DSRBP; GN Name=ADAR; Synonyms=ADAR1, DSRAD, G1P1, IFI4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND VARIANT GLY-100. RX PubMed=7972084; DOI=10.1073/pnas.91.24.11457; RA Kim U., Wang Y., Sanford T., Zeng Y., Nishikura K.; RT "Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a RT candidate enzyme for nuclear RNA editing."; RL Proc. Natl. Acad. Sci. U.S.A. 91:11457-11461(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP SUBCELLULAR LOCATION, INDUCTION BY INTERFERON, AND VARIANTS GLY-100 AND RP ARG-384. RC TISSUE=Kidney; RX PubMed=7565688; DOI=10.1128/mcb.15.10.5376; RA Patterson J.B., Samuel C.E.; RT "Expression and regulation by interferon of a double-stranded-RNA-specific RT adenosine deaminase from human cells: evidence for two forms of the RT deaminase."; RL Mol. Cell. Biol. 15:5376-5388(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS RP GLY-100 AND ARG-384. RC TISSUE=Placenta; RX PubMed=9020165; DOI=10.1074/jbc.272.7.4419; RA Liu Y., George C.X., Patterson J.B., Samuel C.E.; RT "Functionally distinct double-stranded RNA-binding domains associated with RT alternative splice site variants of the interferon-inducible double- RT stranded RNA-specific adenosine deaminase."; RL J. Biol. Chem. 272:4419-4428(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), AND VARIANTS GLY-100 AND RP ARG-384. RC TISSUE=Cervix carcinoma; RA Deblandre G., Marinx O., Nols C., Defrance P., Berr P., Huez G., Caput D.; RT "The gene coding for the interferon-inducible human dsRNA adenosine RT deaminase is transcribed into several messengers specifying different RT proteins."; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS GLY-100 RP AND ARG-384. RC TISSUE=Amygdala, and Fetal kidney; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-100. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP ALTERNATIVE PROMOTER USAGE, AND INDUCTION. RX PubMed=10200312; DOI=10.1073/pnas.96.8.4621; RA George C.X., Samuel C.E.; RT "Human RNA-specific adenosine deaminase ADAR1 transcripts possess RT alternative exon 1 structures that initiate from different promoters, one RT constitutively active and the other interferon inducible."; RL Proc. Natl. Acad. Sci. U.S.A. 96:4621-4626(1999). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, HOMODIMERIZATION, AND SUBUNIT. RX PubMed=12618436; DOI=10.1074/jbc.m213127200; RA Cho D.-S.C., Yang W., Lee J.T., Shiekhattar R., Murray J.M., Nishikura K.; RT "Requirement of dimerization for RNA editing activity of adenosine RT deaminases acting on RNA."; RL J. Biol. Chem. 278:17093-17102(2003). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=12665561; DOI=10.1242/jcs.00371; RA Desterro J.M.P., Keegan L.P., Lafarga M., Berciano M.T., O'Connell M., RA Carmo-Fonseca M.; RT "Dynamic association of RNA-editing enzymes with the nucleolus."; RL J. Cell Sci. 116:1805-1818(2003). RN [12] RP FUNCTION. RX PubMed=15556947; DOI=10.1074/jbc.m407876200; RA Yang W., Wang Q., Howell K.L., Lee J.T., Cho D.-S.C., Murray J.M., RA Nishikura K.; RT "ADAR1 RNA deaminase limits short interfering RNA efficacy in mammalian RT cells."; RL J. Biol. Chem. 280:3946-3953(2005). RN [13] RP FUNCTION. RX PubMed=15858013; DOI=10.1128/jvi.79.10.6291-6298.2005; RA Taylor D.R., Puig M., Darnell M.E., Mihalik K., Feinstone S.M.; RT "New antiviral pathway that mediates hepatitis C virus replicon interferon RT sensitivity through ADAR1."; RL J. Virol. 79:6291-6298(2005). RN [14] RP FUNCTION, SUMOYLATION AT LYS-418, AND MUTAGENESIS OF LYS-418. RX PubMed=16120648; DOI=10.1091/mbc.e05-06-0536; RA Desterro J.M.P., Keegan L.P., Jaffray E., Hay R.T., O'Connell M.A., RA Carmo-Fonseca M.; RT "SUMO-1 modification alters ADAR1 editing activity."; RL Mol. Biol. Cell 16:5115-5126(2005). RN [15] RP INTERACTION WITH ILF2 AND ILF3. RX PubMed=16055709; DOI=10.1128/mcb.25.16.6956-6963.2005; RA Nie Y., Ding L., Kao P.N., Braun R., Yang J.-H.; RT "ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90- RT mediated gene expression independently of RNA editing."; RL Mol. Cell. Biol. 25:6956-6963(2005). RN [16] RP FUNCTION. RX PubMed=16475990; DOI=10.1111/j.1365-2893.2005.00663.x; RA Hartwig D., Schuette C., Warnecke J., Dorn I., Hennig H., Kirchner H., RA Schlenke P.; RT "The large form of ADAR 1 is responsible for enhanced hepatitis delta virus RT RNA editing in interferon-alpha-stimulated host cells."; RL J. Viral Hepat. 13:150-157(2006). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [19] RP FUNCTION, AND INTERACTION WITH EIF2AK2. RX PubMed=17079286; DOI=10.1128/jvi.01527-06; RA Nie Y., Hammond G.L., Yang J.H.; RT "Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus RT infection."; RL J. Virol. 81:917-923(2007). RN [20] RP ALTERNATIVE SPLICING, SUBUNIT, AND TISSUE SPECIFICITY. RX PubMed=18178553; DOI=10.1074/jbc.m708316200; RA Cenci C., Barzotti R., Galeano F., Corbelli S., Rota R., Massimi L., RA Di Rocco C., O'Connell M.A., Gallo A.; RT "Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing RT activity inhibits cell migration and proliferation."; RL J. Biol. Chem. 283:7251-7260(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-614; SER-823 AND RP SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [23] RP INTERACTION WITH UPF1, AND SUBCELLULAR LOCATION. RX PubMed=18362360; DOI=10.1073/pnas.0710576105; RA Agranat L., Raitskin O., Sperling J., Sperling R.; RT "The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact RT in the cell nucleus."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [25] RP FUNCTION. RX PubMed=19710021; DOI=10.1074/jbc.m109.045146; RA Toth A.M., Li Z., Cattaneo R., Samuel C.E.; RT "RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced RT apoptosis and activation of protein kinase PKR."; RL J. Biol. Chem. 284:29350-29356(2009). RN [26] RP FUNCTION, AND INTERACTION WITH EIF2AK2. RX PubMed=19605474; DOI=10.1128/jvi.02457-08; RA Clerzius G., Gelinas J.F., Daher A., Bonnet M., Meurs E.F., Gatignol A.; RT "ADAR1 interacts with PKR during human immunodeficiency virus infection of RT lymphocytes and contributes to viral replication."; RL J. Virol. 83:10119-10128(2009). RN [27] RP SUBCELLULAR LOCATION, INTERACTION WITH TNPO1 AND XPO5, AND DOMAIN. RX PubMed=19124606; DOI=10.1128/mcb.01519-08; RA Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., RA Jantsch M.F.; RT "RNA-regulated interaction of transportin-1 and exportin-5 with the double- RT stranded RNA-binding domain regulates nucleocytoplasmic shuttling of RT ADAR1."; RL Mol. Cell. Biol. 29:1487-1497(2009). RN [28] RP FUNCTION. RX PubMed=19651874; DOI=10.1093/nar/gkp604; RA Doria M., Neri F., Gallo A., Farace M.G., Michienzi A.; RT "Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates RT viral infection."; RL Nucleic Acids Res. 37:5848-5858(2009). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601 AND THR-808, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [30] RP REVIEW. RX PubMed=20192758; DOI=10.1146/annurev-biochem-060208-105251; RA Nishikura K.; RT "Functions and regulation of RNA editing by ADAR deaminases."; RL Annu. Rev. Biochem. 79:321-349(2010). RN [31] RP FUNCTION. RX PubMed=19908260; DOI=10.1002/ijc.25022; RA Galeano F., Leroy A., Rossetti C., Gromova I., Gautier P., Keegan L.P., RA Massimi L., Di Rocco C., O'Connell M.A., Gallo A.; RT "Human BLCAP transcript: new editing events in normal and cancerous RT tissues."; RL Int. J. Cancer 127:127-137(2010). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808 AND SER-825, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [34] RP REVIEW. RX PubMed=22022963; DOI=10.1134/s0006297911080050; RA Wang Q.; RT "RNA editing catalyzed by ADAR1 and its function in mammalian cells."; RL Biochemistry (Mosc.) 76:900-911(2011). RN [35] RP FUNCTION. RX PubMed=21289159; DOI=10.1099/vir.0.028043-0; RA Doria M., Tomaselli S., Neri F., Ciafre S.A., Farace M.G., Michienzi A., RA Gallo A.; RT "ADAR2 editing enzyme is a novel human immunodeficiency virus-1 proviral RT factor."; RL J. Gen. Virol. 92:1228-1232(2011). RN [36] RP REVIEW. RX PubMed=21182352; DOI=10.1089/jir.2010.0097; RA George C.X., Gan Z., Liu Y., Samuel C.E.; RT "Adenosine deaminases acting on RNA, RNA editing, and interferon action."; RL J. Interferon Cytokine Res. 31:99-117(2011). RN [37] RP REVIEW. RX PubMed=21490091; DOI=10.1128/jvi.00240-11; RA Gelinas J.F., Clerzius G., Shaw E., Gatignol A.; RT "Enhancement of replication of RNA viruses by ADAR1 via RNA editing and RT inhibition of RNA-activated protein kinase."; RL J. Virol. 85:8460-8466(2011). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [39] RP REVIEW. RX PubMed=21211811; DOI=10.1016/j.virol.2010.12.004; RA Samuel C.E.; RT "Adenosine deaminases acting on RNA (ADARs) are both antiviral and RT proviral."; RL Virology 411:180-193(2011). RN [40] RP REVIEW. RX PubMed=22988838; DOI=10.3109/10409238.2012.714350; RA Mallela A., Nishikura K.; RT "A-to-I editing of protein coding and noncoding RNAs."; RL Crit. Rev. Biochem. Mol. Biol. 47:493-501(2012). RN [41] RP REVIEW. RX PubMed=21769729; DOI=10.1007/82_2011_144; RA Goodman R.A., Macbeth M.R., Beal P.A.; RT "ADAR proteins: structure and catalytic mechanism."; RL Curr. Top. Microbiol. Immunol. 353:1-33(2012). RN [42] RP FUNCTION. RX PubMed=22278222; DOI=10.1128/jvi.06307-11; RA Li Z., Okonski K.M., Samuel C.E.; RT "Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction of RT interferon by measles virus."; RL J. Virol. 86:3787-3794(2012). RN [43] RP REVIEW. RX PubMed=22113393; DOI=10.1007/s12035-011-8220-2; RA Orlandi C., Barbon A., Barlati S.; RT "Activity regulation of adenosine deaminases acting on RNA (ADARs)."; RL Mol. Neurobiol. 45:61-75(2012). RN [44] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; THR-601; THR-603; RP SER-629; SER-636; THR-808; SER-814 AND SER-825, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [45] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [46] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-26, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [47] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [48] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [49] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-408; LYS-418; LYS-580 RP AND LYS-875, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [50] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-209 IN COMPLEX WITH Z-DNA, AND RP DOMAIN. RX PubMed=10364558; DOI=10.1126/science.284.5421.1841; RA Schwartz T., Rould M.A., Lowenhaupt K., Herbert A., Rich A.; RT "Crystal structure of the Z alpha domain of the human editing enzyme ADAR1 RT bound to left-handed Z-DNA."; RL Science 284:1841-1845(1999). RN [51] RP STRUCTURE BY NMR OF 125-201 IN COMPLEX WITH Z-DNA AND ALONE, AND DOMAIN. RX PubMed=10535945; DOI=10.1073/pnas.96.22.12465; RA Schade M., Turner C.J., Kuehne R., Schmieder P., Lowenhaupt K., Herbert A., RA Rich A., Oschkinat H.; RT "The solution structure of the Zalpha domain of the human RNA editing RT enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA."; RL Proc. Natl. Acad. Sci. U.S.A. 96:12465-12470(1999). RN [52] {ECO:0007744|PDB:2ACJ} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 140-202 IN COMPLEX WITH DNA, AND RP DOMAIN. RX PubMed=16237447; DOI=10.1038/nature04088; RA Ha S.C., Lowenhaupt K., Rich A., Kim Y.G., Kim K.K.; RT "Crystal structure of a junction between B-DNA and Z-DNA reveals two RT extruded bases."; RL Nature 437:1183-1186(2005). RN [53] RP STRUCTURE BY NMR OF 708-801, DOMAIN, SUBCELLULAR LOCATION, INTERACTION WITH RP TNPO1, AND MUTAGENESIS OF 708-MET--PRO-710; 708-MET--ARG-801; RP 712-LYS--LYS-715; 716-ILE--ASN-724; ILE-716; GLU-718; LEU-719; ARG-721; RP LEU-723; ASN-724; 725-THR--ARG-801; 777-LYS-LYS-778 AND ARG-801. RX PubMed=24753571; DOI=10.1073/pnas.1323698111; RA Barraud P., Banerjee S., Mohamed W.I., Jantsch M.F., Allain F.H.; RT "A bimodular nuclear localization signal assembled via an extended double- RT stranded RNA-binding domain acts as an RNA-sensing signal for transportin RT 1."; RL Proc. Natl. Acad. Sci. U.S.A. 111:E1852-E1861(2014). RN [54] RP VARIANTS DSH PRO-923 AND SER-1165. RX PubMed=12916015; DOI=10.1086/378209; RA Miyamura Y., Suzuki T., Kono M., Inagaki K., Ito S., Suzuki N., Tomita Y.; RT "Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are RT involved in dyschromatosis symmetrica hereditaria."; RL Am. J. Hum. Genet. 73:693-699(2003). RN [55] RP VARIANT DSH PHE-966. RX PubMed=15146470; DOI=10.1002/humu.9246; RA Zhang X.-J., He P.-P., Li M., He C.-D., Yan K.-L., Cui Y., Yang S., RA Zhang K.-Y., Gao M., Chen J.-J., Li C.-R., Jin L., Chen H.-D., Xu S.-J., RA Huang W.; RT "Seven novel mutations of the ADAR gene in Chinese families and sporadic RT patients with dyschromatosis symmetrica hereditaria (DSH)."; RL Hum. Mutat. 23:629-630(2004). RN [56] RP VARIANT DSH TRP-1155. RX PubMed=15659327; DOI=10.1016/j.jdermsci.2004.11.004; RA Li C.-R., Li M., Ma H.-J., Luo D., Yang L.-J., Wang D.-G., Zhu X.-H., RA Yue X.-Z., Chen W.-Q., Zhu W.-Y.; RT "A new arginine substitution mutation of DSRAD gene in a Chinese family RT with dyschromatosis symmetrica hereditaria."; RL J. Dermatol. Sci. 37:95-99(2005). RN [57] RP VARIANT [LARGE SCALE ANALYSIS] VAL-806. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [58] RP VARIANTS AGS6 ALA-193; THR-870; THR-872; HIS-892; ASN-999; ARG-1007; RP PHE-1112 AND HIS-1113. RX PubMed=23001123; DOI=10.1038/ng.2414; RA Rice G.I., Kasher P.R., Forte G.M., Mannion N.M., Greenwood S.M., RA Szynkiewicz M., Dickerson J.E., Bhaskar S.S., Zampini M., Briggs T.A., RA Jenkinson E.M., Bacino C.A., Battini R., Bertini E., Brogan P.A., RA Brueton L.A., Carpanelli M., De Laet C., de Lonlay P., del Toro M., RA Desguerre I., Fazzi E., Garcia-Cazorla A., Heiberg A., Kawaguchi M., RA Kumar R., Lin J.P., Lourenco C.M., Male A.M., Marques W. Jr., Mignot C., RA Olivieri I., Orcesi S., Prabhakar P., Rasmussen M., Robinson R.A., RA Rozenberg F., Schmidt J.L., Steindl K., Tan T.Y., van der Merwe W.G., RA Vanderver A., Vassallo G., Wakeling E.L., Wassmer E., Whittaker E., RA Livingston J.H., Lebon P., Suzuki T., McLaughlin P.J., Keegan L.P., RA O'Connell M.A., Lovell S.C., Crow Y.J.; RT "Mutations in ADAR1 cause Aicardi-Goutieres syndrome associated with a type RT I interferon signature."; RL Nat. Genet. 44:1243-1248(2012). CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine CC in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing CC (PubMed:7972084, PubMed:7565688, PubMed:12618436). This may affect gene CC expression and function in a number of ways that include mRNA CC translation by changing codons and hence the amino acid sequence of CC proteins since the translational machinery read the inosine as a CC guanosine; pre-mRNA splicing by altering splice site recognition CC sequences; RNA stability by changing sequences involved in nuclease CC recognition; genetic stability in the case of RNA virus genomes by CC changing sequences during viral RNA replication; and RNA structure- CC dependent activities such as microRNA production or targeting or CC protein-RNA interactions. Can edit both viral and cellular RNAs and can CC edit RNAs at multiple sites (hyper-editing) or at specific sites (site- CC specific editing). Its cellular RNA substrates include: bladder cancer- CC associated protein (BLCAP), neurotransmitter receptors for glutamate CC (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific CC RNA editing of transcripts encoding these proteins results in amino CC acid substitutions which consequently alters their functional CC activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits CC efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates CC include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), CC measles virus (MV), hepatitis delta virus (HDV), and human CC immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, CC MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be CC editing-dependent (HDV and HCV), editing-independent (VSV and MV) or CC both (HIV-1). Impairs HCV replication via RNA editing at multiple CC sites. Enhances the replication of MV, VSV and HIV-1 through an CC editing-independent mechanism via suppression of EIF2AK2/PKR activation CC and function. Stimulates both the release and infectivity of HIV-1 CC viral particles by an editing-dependent mechanism where it associates CC with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat CC coding sequence. Can enhance viral replication of HDV via A-to-I CC editing at a site designated as amber/W, thereby changing an UAG amber CC stop codon to an UIG tryptophan (W) codon that permits synthesis of the CC large delta antigen (L-HDAg) which has a key role in the assembly of CC viral particles. However, high levels of ADAR1 inhibit HDV replication. CC {ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:15556947, CC ECO:0000269|PubMed:15858013, ECO:0000269|PubMed:16120648, CC ECO:0000269|PubMed:16475990, ECO:0000269|PubMed:17079286, CC ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:19651874, CC ECO:0000269|PubMed:19710021, ECO:0000269|PubMed:19908260, CC ECO:0000269|PubMed:21289159, ECO:0000269|PubMed:22278222, CC ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine in double-stranded RNA + H(+) + H2O = inosine in CC double-stranded RNA + NH4(+); Xref=Rhea:RHEA:10120, Rhea:RHEA- CC COMP:13885, Rhea:RHEA-COMP:13886, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, CC ChEBI:CHEBI:82852; EC=3.5.4.37; CC Evidence={ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:7565688, CC ECO:0000269|PubMed:7972084}; CC -!- SUBUNIT: Homodimer. Homodimerization is essential for its catalytic CC activity (PubMed:12618436). Isoform 5 can form heterodimers with CC ADARB1/ADAR2. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90 CC (PubMed:16055709). Binding to ILF3/NF90 up-regulates ILF3-mediated gene CC expression. Isoform 1 and isoform 5 (via DRBM 3 domain) interact with CC TNPO1 (PubMed:19124606, PubMed:24753571). Isoform 5 (via DRBM domains) CC interacts with XPO5 (PubMed:19124606). Isoform 1 and isoform 5 can CC interact with EIF2AK2/PKR and UPF1 (PubMed:17079286, PubMed:18362360). CC {ECO:0000269|PubMed:10364558, ECO:0000269|PubMed:10535945, CC ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:16055709, CC ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:18178553, CC ECO:0000269|PubMed:18362360, ECO:0000269|PubMed:19124606, CC ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:24753571}. CC -!- INTERACTION: CC P55265; Q13148: TARDBP; NbExp=3; IntAct=EBI-2462104, EBI-372899; CC P55265; Q92900: UPF1; NbExp=3; IntAct=EBI-2462104, EBI-373471; CC P55265; P03496: NS; Xeno; NbExp=8; IntAct=EBI-2462104, EBI-2547442; CC P55265; PRO_0000037965 [P14340]; Xeno; NbExp=2; IntAct=EBI-2462104, EBI-9825968; CC P55265; PRO_0000045599 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-2462104, EBI-6858501; CC P55265-1; Q9UPY3: DICER1; NbExp=4; IntAct=EBI-6913056, EBI-395506; CC P55265-1; Q15633: TARBP2; NbExp=2; IntAct=EBI-6913056, EBI-978581; CC P55265-5; Q9UPY3: DICER1; NbExp=8; IntAct=EBI-6913210, EBI-395506; CC P55265-5; Q15633: TARBP2; NbExp=3; IntAct=EBI-6913210, EBI-978581; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000269|PubMed:7565688}. Nucleus {ECO:0000269|PubMed:24753571, CC ECO:0000269|PubMed:7565688}. Note=Shuttles between the cytoplasm and CC nucleus (PubMed:7565688, PubMed:24753571). Nuclear import is mediated CC by TNPO1 (PubMed:24753571). {ECO:0000269|PubMed:24753571, CC ECO:0000269|PubMed:7565688}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm CC {ECO:0000269|PubMed:19124606}. Nucleus {ECO:0000269|PubMed:19124606, CC ECO:0000269|PubMed:7565688}. Nucleus, nucleolus CC {ECO:0000269|PubMed:12665561}. Note=Predominantly nuclear but can CC shuttle between nucleus and cytoplasm. TNPO1 can mediate its nuclear CC import whereas XPO5 can mediate its nuclear export. CC {ECO:0000269|PubMed:19124606}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=ADAR-a, ADAR1L, p150; CC IsoId=P55265-1; Sequence=Displayed; CC Name=2; Synonyms=ADAR-b; CC IsoId=P55265-2; Sequence=VSP_008874; CC Name=3; Synonyms=ADAR-c; CC IsoId=P55265-3; Sequence=VSP_008873, VSP_008874; CC Name=4; CC IsoId=P55265-4; Sequence=VSP_008872; CC Name=5; Synonyms=ADAR1S, p110; CC IsoId=P55265-5; Sequence=VSP_019235; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, highest levels were found CC in brain and lung (PubMed:7972084). Isoform 5 is expressed at higher CC levels in astrocytomas as compared to normal brain tissue and CC expression increases strikingly with the severity of the tumor, being CC higher in the most aggressive tumors. {ECO:0000269|PubMed:18178553, CC ECO:0000269|PubMed:7972084}. CC -!- INDUCTION: Isoform 1 is induced by interferon alpha. Isoform 5 is CC constitutively expressed. {ECO:0000269|PubMed:10200312, CC ECO:0000269|PubMed:7565688}. CC -!- DOMAIN: The third dsRNA-binding domain (DRBM 3) contains an additional CC N-terminal alpha-helix that is part of a bi-partite nuclear CC localization signal, together with the sequence immediately C-terminal CC to DRBM 3. The presence of DRBM 3 is important to bring together the N- CC terminal and the C-terminal part of the bi-partite nuclear localization CC signal for import mediated by TNPO1 (PubMed:24753571). RNA binding CC interferes with nuclear import (PubMed:19124606, PubMed:24753571). CC {ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:24753571}. CC -!- DOMAIN: The first Z-binding domain binds Z-DNA. {ECO:0000255|PROSITE- CC ProRule:PRU00073, ECO:0000269|PubMed:10364558, CC ECO:0000269|PubMed:10535945, ECO:0000269|PubMed:16237447}. CC -!- PTM: Sumoylation reduces RNA-editing activity. CC {ECO:0000269|PubMed:16120648}. CC -!- DISEASE: Dyschromatosis symmetrica hereditaria (DSH) [MIM:127400]: An CC autosomal dominant pigmentary genodermatosis characterized by a mixture CC of hyperpigmented and hypopigmented macules distributed on the face and CC the dorsal parts of the hands and feet, that appear in infancy or early CC childhood. {ECO:0000269|PubMed:12916015, ECO:0000269|PubMed:15146470, CC ECO:0000269|PubMed:15659327}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Aicardi-Goutieres syndrome 6 (AGS6) [MIM:615010]: A form of CC Aicardi-Goutieres syndrome, a genetically heterogeneous disease CC characterized by cerebral atrophy, leukoencephalopathy, intracranial CC calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, CC increased CSF alpha-interferon, and negative serologic investigations CC for common prenatal infection. Clinical features as thrombocytopenia, CC hepatosplenomegaly and elevated hepatic transaminases along with CC intermittent fever may erroneously suggest an infective process. Severe CC neurological dysfunctions manifest in infancy as progressive CC microcephaly, spasticity, dystonic posturing and profound psychomotor CC retardation. Death often occurs in early childhood. CC {ECO:0000269|PubMed:23001123}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- CAUTION: The N-terminus of isoform 4 has been derived from EST and CC genomic sequences. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAE45853.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U10439; AAB06697.1; -; mRNA. DR EMBL; U75503; AAB97116.1; -; Genomic_DNA. DR EMBL; U75489; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75490; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75491; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75492; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75493; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75494; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75495; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75496; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75497; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75498; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75499; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75500; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75501; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75502; AAB97116.1; JOINED; Genomic_DNA. DR EMBL; U75503; AAB97117.1; -; Genomic_DNA. DR EMBL; U75489; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75490; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75491; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75492; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75493; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75494; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75495; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75496; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75497; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75498; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75499; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75500; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75501; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75502; AAB97117.1; JOINED; Genomic_DNA. DR EMBL; U75503; AAB97118.1; -; Genomic_DNA. DR EMBL; U75489; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75490; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75491; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75492; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75493; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75494; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75495; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75496; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75497; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75498; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75499; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75500; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75501; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U75502; AAB97118.1; JOINED; Genomic_DNA. DR EMBL; U18121; AAC13782.1; -; mRNA. DR EMBL; X79448; CAA55967.1; -; mRNA. DR EMBL; X79449; CAA55968.1; -; mRNA. DR EMBL; X98559; CAA67169.1; -; mRNA. DR EMBL; X98559; CAA67170.1; -; mRNA. DR EMBL; BX538232; CAD98075.1; -; mRNA. DR EMBL; BX640741; CAE45853.1; ALT_SEQ; mRNA. DR EMBL; AL592078; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL606500; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL691488; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53183.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53187.1; -; Genomic_DNA. DR EMBL; BC038227; AAH38227.1; -; mRNA. DR CCDS; CCDS1071.1; -. [P55265-1] DR CCDS; CCDS30879.1; -. [P55265-5] DR CCDS; CCDS44231.1; -. [P55265-2] DR PIR; S65593; S65593. DR RefSeq; NP_001020278.1; NM_001025107.2. [P55265-5] DR RefSeq; NP_001102.2; NM_001111.4. [P55265-1] DR RefSeq; NP_001180424.1; NM_001193495.1. [P55265-5] DR RefSeq; NP_056655.2; NM_015840.3. [P55265-2] DR RefSeq; NP_056656.2; NM_015841.3. [P55265-3] DR RefSeq; XP_006711174.1; XM_006711111.3. DR RefSeq; XP_006711175.1; XM_006711112.2. DR RefSeq; XP_006711176.1; XM_006711113.2. DR PDB; 1QBJ; X-ray; 2.10 A; A/B/C=133-209. DR PDB; 1QGP; NMR; -; A=125-200. DR PDB; 1XMK; X-ray; 0.97 A; A=294-366. DR PDB; 2ACJ; X-ray; 2.60 A; A/B/C/D=140-202. DR PDB; 2GXB; X-ray; 2.25 A; A/B=140-202. DR PDB; 2L54; NMR; -; A=136-198. DR PDB; 2MDR; NMR; -; A=708-801. DR PDB; 3F21; X-ray; 2.20 A; A/B/C=133-209. DR PDB; 3F22; X-ray; 2.50 A; A/B/C=133-209. DR PDB; 3F23; X-ray; 2.70 A; A/B/C=133-209. DR PDB; 3IRQ; X-ray; 2.80 A; A/B/C/D=140-202. DR PDB; 3IRR; X-ray; 2.65 A; A/B/C/D=140-202. DR PDB; 5ZU1; X-ray; 3.01 A; A/B/C/D=140-198. DR PDB; 5ZUO; X-ray; 2.90 A; A/B/C/D=140-202. DR PDB; 5ZUP; X-ray; 2.90 A; A/B/C/D=140-202. DR PDB; 7C0I; X-ray; 2.40 A; A/B/C=170-184. DR PDB; 7ZJ1; X-ray; 1.65 A; A/B=716-797. DR PDB; 7ZLQ; X-ray; 2.80 A; A/B=716-797. DR PDB; 8GBC; NMR; -; A=140-202. DR PDB; 8GBD; NMR; -; A=140-202. DR PDBsum; 1QBJ; -. DR PDBsum; 1QGP; -. DR PDBsum; 1XMK; -. DR PDBsum; 2ACJ; -. DR PDBsum; 2GXB; -. DR PDBsum; 2L54; -. DR PDBsum; 2MDR; -. DR PDBsum; 3F21; -. DR PDBsum; 3F22; -. DR PDBsum; 3F23; -. DR PDBsum; 3IRQ; -. DR PDBsum; 3IRR; -. DR PDBsum; 5ZU1; -. DR PDBsum; 5ZUO; -. DR PDBsum; 5ZUP; -. DR PDBsum; 7C0I; -. DR PDBsum; 7ZJ1; -. DR PDBsum; 7ZLQ; -. DR PDBsum; 8GBC; -. DR PDBsum; 8GBD; -. DR AlphaFoldDB; P55265; -. DR SMR; P55265; -. DR BioGRID; 106617; 283. DR CORUM; P55265; -. DR DIP; DIP-29310N; -. DR IntAct; P55265; 80. DR MINT; P55265; -. DR STRING; 9606.ENSP00000357459; -. DR GlyCosmos; P55265; 4 sites, 2 glycans. DR GlyGen; P55265; 10 sites, 2 O-linked glycans (10 sites). DR iPTMnet; P55265; -. DR MetOSite; P55265; -. DR PhosphoSitePlus; P55265; -. DR SwissPalm; P55265; -. DR BioMuta; ADAR; -. DR DMDM; 313104303; -. DR EPD; P55265; -. DR jPOST; P55265; -. DR MassIVE; P55265; -. DR MaxQB; P55265; -. DR PaxDb; 9606-ENSP00000357459; -. DR PeptideAtlas; P55265; -. DR ProteomicsDB; 56826; -. [P55265-1] DR ProteomicsDB; 56827; -. [P55265-2] DR ProteomicsDB; 56828; -. [P55265-3] DR ProteomicsDB; 56829; -. [P55265-4] DR ProteomicsDB; 56830; -. [P55265-5] DR Pumba; P55265; -. DR Antibodypedia; 1280; 342 antibodies from 32 providers. DR DNASU; 103; -. DR Ensembl; ENST00000368471.8; ENSP00000357456.3; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000368474.9; ENSP00000357459.4; ENSG00000160710.18. [P55265-1] DR Ensembl; ENST00000529168.2; ENSP00000431794.2; ENSG00000160710.18. [P55265-2] DR Ensembl; ENST00000648231.2; ENSP00000497555.1; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000648311.1; ENSP00000498137.1; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000649022.2; ENSP00000496896.2; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000649042.1; ENSP00000497790.1; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000649724.1; ENSP00000497932.1; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000649749.1; ENSP00000497210.1; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000680270.1; ENSP00000505532.1; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000681056.1; ENSP00000506234.1; ENSG00000160710.18. [P55265-5] DR Ensembl; ENST00000681683.1; ENSP00000506666.1; ENSG00000160710.18. [P55265-5] DR GeneID; 103; -. DR KEGG; hsa:103; -. DR MANE-Select; ENST00000368474.9; ENSP00000357459.4; NM_001111.5; NP_001102.3. DR UCSC; uc001ffh.4; human. [P55265-1] DR AGR; HGNC:225; -. DR CTD; 103; -. DR DisGeNET; 103; -. DR GeneCards; ADAR; -. DR GeneReviews; ADAR; -. DR HGNC; HGNC:225; ADAR. DR HPA; ENSG00000160710; Low tissue specificity. DR MalaCards; ADAR; -. DR MIM; 127400; phenotype. DR MIM; 146920; gene. DR MIM; 615010; phenotype. DR neXtProt; NX_P55265; -. DR OpenTargets; ENSG00000160710; -. DR Orphanet; 51; Aicardi-Goutieres syndrome. DR Orphanet; 41; Dyschromatosis symmetrica hereditaria. DR Orphanet; 225154; Familial infantile bilateral striatal necrosis. DR PharmGKB; PA24555; -. DR VEuPathDB; HostDB:ENSG00000160710; -. DR eggNOG; KOG2777; Eukaryota. DR GeneTree; ENSGT00940000157243; -. DR HOGENOM; CLU_005382_0_0_1; -. DR InParanoid; P55265; -. DR OMA; ERMQMKR; -. DR OrthoDB; 118472at2759; -. DR PhylomeDB; P55265; -. DR TreeFam; TF315806; -. DR BRENDA; 3.5.4.37; 2681. DR PathwayCommons; P55265; -. DR Reactome; R-HSA-75102; C6 deamination of adenosine. DR Reactome; R-HSA-77042; Formation of editosomes by ADAR proteins. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; P55265; -. DR SIGNOR; P55265; -. DR BioGRID-ORCS; 103; 289 hits in 1164 CRISPR screens. DR ChiTaRS; ADAR; human. DR EvolutionaryTrace; P55265; -. DR GeneWiki; ADAR; -. DR GenomeRNAi; 103; -. DR Pharos; P55265; Tbio. DR PRO; PR:P55265; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P55265; Protein. DR Bgee; ENSG00000160710; Expressed in endothelial cell and 210 other cell types or tissues. DR ExpressionAtlas; P55265; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IDA:MGI. DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IBA:GO_Central. DR GO; GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB. DR GO; GO:0016553; P:base conversion or substitution editing; IDA:MGI. DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl. DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl. DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl. DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IEA:Ensembl. DR GO; GO:1900369; P:negative regulation of post-transcriptional gene silencing by regulatory ncRNA; IEA:Ensembl. DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB. DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0045070; P:positive regulation of viral genome replication; IDA:UniProtKB. DR GO; GO:0031054; P:pre-miRNA processing; IDA:MGI. DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB. DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB. DR GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB. DR GO; GO:0009615; P:response to virus; IMP:UniProtKB. DR GO; GO:0070922; P:RISC complex assembly; IDA:MGI. DR GO; GO:0006396; P:RNA processing; IBA:GO_Central. DR GO; GO:0002566; P:somatic diversification of immune receptors via somatic mutation; IEA:Ensembl. DR CDD; cd19913; DSRM_DRADA_rpt1; 1. DR CDD; cd19914; DSRM_DRADA_rpt2; 1. DR CDD; cd19915; DSRM_DRADA_rpt3; 1. DR Gene3D; 3.30.160.20; -; 3. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR002466; A_deamin. DR InterPro; IPR044456; ADAR1_DSRM_1. DR InterPro; IPR044457; ADAR1_DSRM_3. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR InterPro; IPR042371; Z_dom. DR PANTHER; PTHR10910:SF107; DOUBLE-STRANDED RNA-SPECIFIC ADENOSINE DEAMINASE; 1. DR PANTHER; PTHR10910; EUKARYOTE SPECIFIC DSRNA BINDING PROTEIN; 1. DR Pfam; PF02137; A_deamin; 1. DR Pfam; PF00035; dsrm; 3. DR Pfam; PF02295; z-alpha; 2. DR SMART; SM00552; ADEAMc; 1. DR SMART; SM00358; DSRM; 3. DR SMART; SM00550; Zalpha; 2. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 3. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2. DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1. DR PROSITE; PS50137; DS_RBD; 3. DR PROSITE; PS50139; Z_BINDING; 2. DR Genevisible; P55265; HS. PE 1: Evidence at protein level; KW 3D-structure; Aicardi-Goutieres syndrome; Alternative promoter usage; KW Alternative splicing; Antiviral defense; Cytoplasm; KW Direct protein sequencing; Disease variant; DNA-binding; Hydrolase; KW Immunity; Innate immunity; Isopeptide bond; Metal-binding; Methylation; KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW RNA-binding; RNA-mediated gene silencing; Ubl conjugation; Zinc. FT CHAIN 1..1226 FT /note="Double-stranded RNA-specific adenosine deaminase" FT /id="PRO_0000171774" FT DOMAIN 133..199 FT /note="Z-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00073, FT ECO:0000269|PubMed:10364558, ECO:0000269|PubMed:10535945, FT ECO:0000269|PubMed:16237447" FT DOMAIN 293..357 FT /note="Z-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00073" FT DOMAIN 503..571 FT /note="DRBM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 614..682 FT /note="DRBM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 726..794 FT /note="DRBM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266, FT ECO:0000269|PubMed:24753571" FT DOMAIN 886..1221 FT /note="A to I editase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240" FT REGION 133..202 FT /note="Interaction with Z-DNA" FT /evidence="ECO:0000269|PubMed:10364558, FT ECO:0000269|PubMed:10535945, ECO:0000269|PubMed:16237447" FT REGION 208..238 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 258..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 574..610 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 716..725 FT /note="N-terminal extension of DRBM 3 and constituent of a FT bi-partite nuclear localization signal" FT /evidence="ECO:0000269|PubMed:24753571" FT REGION 795..801 FT /note="C-terminal extension of DRBM 3 and constituent of a FT bi-partite nuclear localization signal" FT /evidence="ECO:0000269|PubMed:24753571" FT COMPBIAS 574..597 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 912 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240" FT BINDING 910 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240" FT BINDING 966 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240" FT BINDING 1036 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240" FT MOD_RES 26 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55266" FT MOD_RES 481 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 601 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 603 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 614 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 629 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 636 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 808 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 814 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 823 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 825 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 384 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 408 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 418 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT CROSSLNK 418 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 418 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 580 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 875 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..295 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_019235" FT VAR_SEQ 1..5 FT /note="MNPRQ -> MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPE FT EVQDP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_008872" FT VAR_SEQ 694..712 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_008873" FT VAR_SEQ 807..832 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_008874" FT VARIANT 100 FT /note="R -> G (in dbSNP:rs1466731)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:7565688, FT ECO:0000269|PubMed:7972084, ECO:0000269|PubMed:9020165, FT ECO:0000269|Ref.4" FT /id="VAR_048725" FT VARIANT 193 FT /note="P -> A (in AGS6; dbSNP:rs145588689)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069535" FT VARIANT 384 FT /note="K -> R (in dbSNP:rs2229857)" FT /evidence="ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:9020165, FT ECO:0000269|Ref.4" FT /id="VAR_017240" FT VARIANT 587 FT /note="Y -> C (in dbSNP:rs17843865)" FT /id="VAR_024407" FT VARIANT 806 FT /note="E -> V (in a breast cancer sample; somatic mutation; FT dbSNP:rs144119808)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035805" FT VARIANT 870 FT /note="A -> T (in AGS6; dbSNP:rs398122893)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069536" FT VARIANT 872 FT /note="I -> T (in AGS6; dbSNP:rs398122897)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069537" FT VARIANT 892 FT /note="R -> H (in AGS6; dbSNP:rs398122892)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069538" FT VARIANT 923 FT /note="L -> P (in DSH; dbSNP:rs28936680)" FT /evidence="ECO:0000269|PubMed:12916015" FT /id="VAR_017604" FT VARIANT 966 FT /note="C -> F (in DSH)" FT /evidence="ECO:0000269|PubMed:15146470" FT /id="VAR_021729" FT VARIANT 999 FT /note="K -> N (in AGS6; dbSNP:rs398122896)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069539" FT VARIANT 1007 FT /note="G -> R (in AGS6; dbSNP:rs398122822)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069540" FT VARIANT 1112 FT /note="Y -> F (in AGS6; dbSNP:rs398122895)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069541" FT VARIANT 1113 FT /note="D -> H (in AGS6; dbSNP:rs398122894)" FT /evidence="ECO:0000269|PubMed:23001123" FT /id="VAR_069542" FT VARIANT 1155 FT /note="R -> W (in DSH; dbSNP:rs1044845711)" FT /evidence="ECO:0000269|PubMed:15659327" FT /id="VAR_026669" FT VARIANT 1165 FT /note="F -> S (in DSH; dbSNP:rs28936681)" FT /evidence="ECO:0000269|PubMed:12916015" FT /id="VAR_017605" FT MUTAGEN 418 FT /note="K->R: Abolishes sumoylation." FT /evidence="ECO:0000269|PubMed:16120648" FT MUTAGEN 708..801 FT /note="Missing: Abolishes nuclear location." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 708..710 FT /note="MMP->AMA: Decreased nuclear and partially FT cytoplasmic location." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 712..715 FT /note="KVRK->AVAA: No effect on nuclear location. No effect FT on RNA binding." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 716..724 FT /note="Missing: Disrupts the bi-partite nuclear FT localization signal and abolishes nuclear location." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 716 FT /note="I->N: Disrupts the bi-partite nuclear localization FT signal and abolishes nuclear location; when associated with FT S-719 and N-723." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 718 FT /note="E->A: No effect on nuclear location; when associated FT with A-721 and A-724." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 719 FT /note="L->S: Disrupts the bi-partite nuclear localization FT signal and abolishes nuclear location; when associated with FT N-716 and N-723." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 721 FT /note="R->A: No effect on nuclear location; when associated FT with A-721 and A-724." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 723 FT /note="L->N: Disrupts the bi-partite nuclear localization FT signal and abolishes nuclear location; when associated with FT N-716 and S-719." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 724 FT /note="N->A: No effect on nuclear location; when associated FT with A-718 and A-721." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 725..801 FT /note="Missing: Disrupts nuclear localization signal. No FT effect on RNA binding." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 777..778 FT /note="KK->AA: Strongly impaired RNA binding. No effect on FT nuclear location." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 801 FT /note="R->A: Abolishes interaction with TNPO1, FT TNPO1-mediated nuclear import and nuclear location." FT /evidence="ECO:0000269|PubMed:24753571" FT CONFLICT 53 FT /note="E -> G (in Ref. 4; CAA55968)" FT /evidence="ECO:0000305" FT CONFLICT 245 FT /note="F -> L (in Ref. 5; CAE45853)" FT /evidence="ECO:0000305" FT CONFLICT 482 FT /note="F -> L (in Ref. 5; CAE45853)" FT /evidence="ECO:0000305" FT CONFLICT 873 FT /note="I -> V (in Ref. 5; CAE45853)" FT /evidence="ECO:0000305" FT CONFLICT 1093 FT /note="D -> G (in Ref. 5; CAE45853)" FT /evidence="ECO:0000305" FT CONFLICT 1184 FT /note="E -> K (in Ref. 4; FT CAA55967/CAA55968/CAA67169/CAA67170)" FT /evidence="ECO:0000305" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:1QGP" FT HELIX 135..150 FT /evidence="ECO:0007829|PDB:1QBJ" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:1QGP" FT HELIX 158..165 FT /evidence="ECO:0007829|PDB:1QBJ" FT HELIX 169..181 FT /evidence="ECO:0007829|PDB:1QBJ" FT STRAND 184..192 FT /evidence="ECO:0007829|PDB:1QBJ" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:1QBJ" FT HELIX 294..309 FT /evidence="ECO:0007829|PDB:1XMK" FT HELIX 315..322 FT /evidence="ECO:0007829|PDB:1XMK" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:1XMK" FT HELIX 327..339 FT /evidence="ECO:0007829|PDB:1XMK" FT STRAND 342..346 FT /evidence="ECO:0007829|PDB:1XMK" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:1XMK" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:1XMK" FT HELIX 357..360 FT /evidence="ECO:0007829|PDB:1XMK" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:1XMK" FT HELIX 716..724 FT /evidence="ECO:0007829|PDB:2MDR" FT HELIX 727..738 FT /evidence="ECO:0007829|PDB:2MDR" FT STRAND 742..749 FT /evidence="ECO:0007829|PDB:2MDR" FT STRAND 758..764 FT /evidence="ECO:0007829|PDB:2MDR" FT STRAND 767..776 FT /evidence="ECO:0007829|PDB:2MDR" FT HELIX 777..796 FT /evidence="ECO:0007829|PDB:2MDR" FT CONFLICT P55265-4:13 FT /note="R -> G (in Ref. 5; CAE45853)" FT /evidence="ECO:0000305" SQ SEQUENCE 1226 AA; 136066 MW; 9CE095D6F9C1BC79 CRC64; MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR SQGLQRGFQH PSPRGRSLPQ RGVDCLSSHF QELSIYQDQE QRILKFLEEL GEGKATTAHD LSGKLGTPKK EINRVLYSLA KKGKLQKEAG TPPLWKIAVS TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED LLEPFIAVSA QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP PIWHLTDKKR ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS NNMVTTEKVE NGQEPVIKLE NRQEARPEPA RLKPPVHYNG PSKAGYVDFE NGQWATDDIP DDLNSIRAAP GEFRAIMEMP SFYSHGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV INGREFPPAE AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV AVGAQTFPSV SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQPEGMISE SLDNLESMMP NKVRKIGELV RYLNTNPVGG LLEYARSHGF AAEFKLVDQS GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG KQEAADAALR VLIGENEKAE RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF HDQIAMLSHR CFNTLTNSFQ PSLLGRKILA AIIMKKDSED MGVVVSLGTG NRCVKGDSLS LKGETVNDCH AEIISRRGFI RFLYSELMKY NSQTAKDSIF EPAKGGEKLQ IKKTVSFHLY ISTAPCGDGA LFDKSCSDRA MESTESRHYP VFENPKQGKL RTKVENGEGT IPVESSDIVP TWDGIRLGER LRTMSCSDKI LRWNVLGLQG ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI CCRVTRDGSA FEDGLRHPFI VNHPKVGRVS IYDSKRQSGK TKETSVNWCL ADGYDLEILD GTRGTVDGPR NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK KGLKDMGYGN WISKPQEEKN FYLCPV //