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Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)

 DSRAD_HUMAN             Reviewed;        1226 AA.
P55265; B1AQQ9; B1AQR0; D3DV76; O15223; O43859; O43860; Q9BYM3;
Q9BYM4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
25-OCT-2017, entry version 191.
RecName: Full=Double-stranded RNA-specific adenosine deaminase;
Short=DRADA {ECO:0000303|PubMed:7972084};
EC=3.5.4.37 {ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084};
AltName: Full=136 kDa double-stranded RNA-binding protein;
Short=p136;
AltName: Full=Interferon-inducible protein 4;
Short=IFI-4;
AltName: Full=K88DSRBP;
Name=ADAR; Synonyms=ADAR1, DSRAD, G1P1, IFI4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND VARIANT GLY-100.
PubMed=7972084; DOI=10.1073/pnas.91.24.11457;
Kim U., Wang Y., Sanford T., Zeng Y., Nishikura K.;
"Molecular cloning of cDNA for double-stranded RNA adenosine
deaminase, a candidate enzyme for nuclear RNA editing.";
Proc. Natl. Acad. Sci. U.S.A. 91:11457-11461(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, INDUCTION BY INTERFERON, AND VARIANTS GLY-100
AND ARG-384.
TISSUE=Kidney;
PubMed=7565688; DOI=10.1128/MCB.15.10.5376;
Patterson J.B., Samuel C.E.;
"Expression and regulation by interferon of a double-stranded-RNA-
specific adenosine deaminase from human cells: evidence for two forms
of the deaminase.";
Mol. Cell. Biol. 15:5376-5388(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
GLY-100 AND ARG-384.
TISSUE=Placenta;
PubMed=9020165; DOI=10.1074/jbc.272.7.4419;
Liu Y., George C.X., Patterson J.B., Samuel C.E.;
"Functionally distinct double-stranded RNA-binding domains associated
with alternative splice site variants of the interferon-inducible
double-stranded RNA-specific adenosine deaminase.";
J. Biol. Chem. 272:4419-4428(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), AND VARIANTS GLY-100
AND ARG-384.
TISSUE=Cervix carcinoma;
Deblandre G., Marinx O., Nols C., Defrance P., Berr P., Huez G.,
Caput D.;
"The gene coding for the interferon-inducible human dsRNA adenosine
deaminase is transcribed into several messengers specifying different
proteins.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
GLY-100 AND ARG-384.
TISSUE=Amygdala, and Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLY-100.
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
ALTERNATIVE PROMOTER USAGE, AND INDUCTION.
PubMed=10200312; DOI=10.1073/pnas.96.8.4621;
George C.X., Samuel C.E.;
"Human RNA-specific adenosine deaminase ADAR1 transcripts possess
alternative exon 1 structures that initiate from different promoters,
one constitutively active and the other interferon inducible.";
Proc. Natl. Acad. Sci. U.S.A. 96:4621-4626(1999).
[10]
FUNCTION, CATALYTIC ACTIVITY, HOMODIMERIZATION, AND SUBUNIT.
PubMed=12618436; DOI=10.1074/jbc.M213127200;
Cho D.-S.C., Yang W., Lee J.T., Shiekhattar R., Murray J.M.,
Nishikura K.;
"Requirement of dimerization for RNA editing activity of adenosine
deaminases acting on RNA.";
J. Biol. Chem. 278:17093-17102(2003).
[11]
SUBCELLULAR LOCATION.
PubMed=12665561; DOI=10.1242/jcs.00371;
Desterro J.M.P., Keegan L.P., Lafarga M., Berciano M.T., O'Connell M.,
Carmo-Fonseca M.;
"Dynamic association of RNA-editing enzymes with the nucleolus.";
J. Cell Sci. 116:1805-1818(2003).
[12]
FUNCTION.
PubMed=15556947; DOI=10.1074/jbc.M407876200;
Yang W., Wang Q., Howell K.L., Lee J.T., Cho D.-S.C., Murray J.M.,
Nishikura K.;
"ADAR1 RNA deaminase limits short interfering RNA efficacy in
mammalian cells.";
J. Biol. Chem. 280:3946-3953(2005).
[13]
FUNCTION.
PubMed=15858013; DOI=10.1128/JVI.79.10.6291-6298.2005;
Taylor D.R., Puig M., Darnell M.E., Mihalik K., Feinstone S.M.;
"New antiviral pathway that mediates hepatitis C virus replicon
interferon sensitivity through ADAR1.";
J. Virol. 79:6291-6298(2005).
[14]
FUNCTION, SUMOYLATION AT LYS-418, AND MUTAGENESIS OF LYS-418.
PubMed=16120648; DOI=10.1091/mbc.E05-06-0536;
Desterro J.M.P., Keegan L.P., Jaffray E., Hay R.T., O'Connell M.A.,
Carmo-Fonseca M.;
"SUMO-1 modification alters ADAR1 editing activity.";
Mol. Biol. Cell 16:5115-5126(2005).
[15]
INTERACTION WITH ILF2 AND ILF3.
PubMed=16055709; DOI=10.1128/MCB.25.16.6956-6963.2005;
Nie Y., Ding L., Kao P.N., Braun R., Yang J.-H.;
"ADAR1 interacts with NF90 through double-stranded RNA and regulates
NF90-mediated gene expression independently of RNA editing.";
Mol. Cell. Biol. 25:6956-6963(2005).
[16]
FUNCTION.
PubMed=16475990; DOI=10.1111/j.1365-2893.2005.00663.x;
Hartwig D., Schuette C., Warnecke J., Dorn I., Hennig H., Kirchner H.,
Schlenke P.;
"The large form of ADAR 1 is responsible for enhanced hepatitis delta
virus RNA editing in interferon-alpha-stimulated host cells.";
J. Viral Hepat. 13:150-157(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[19]
FUNCTION, AND INTERACTION WITH EIF2AK2.
PubMed=17079286; DOI=10.1128/JVI.01527-06;
Nie Y., Hammond G.L., Yang J.H.;
"Double-stranded RNA deaminase ADAR1 increases host susceptibility to
virus infection.";
J. Virol. 81:917-923(2007).
[20]
ALTERNATIVE SPLICING, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=18178553; DOI=10.1074/jbc.M708316200;
Cenci C., Barzotti R., Galeano F., Corbelli S., Rota R., Massimi L.,
Di Rocco C., O'Connell M.A., Gallo A.;
"Down-regulation of RNA editing in pediatric astrocytomas: ADAR2
editing activity inhibits cell migration and proliferation.";
J. Biol. Chem. 283:7251-7260(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-614; SER-823
AND SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
INTERACTION WITH UPF1, AND SUBCELLULAR LOCATION.
PubMed=18362360; DOI=10.1073/pnas.0710576105;
Agranat L., Raitskin O., Sperling J., Sperling R.;
"The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1
interact in the cell nucleus.";
Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
FUNCTION.
PubMed=19710021; DOI=10.1074/jbc.M109.045146;
Toth A.M., Li Z., Cattaneo R., Samuel C.E.;
"RNA-specific adenosine deaminase ADAR1 suppresses measles virus-
induced apoptosis and activation of protein kinase PKR.";
J. Biol. Chem. 284:29350-29356(2009).
[26]
FUNCTION, AND INTERACTION WITH EIF2AK2.
PubMed=19605474; DOI=10.1128/JVI.02457-08;
Clerzius G., Gelinas J.F., Daher A., Bonnet M., Meurs E.F.,
Gatignol A.;
"ADAR1 interacts with PKR during human immunodeficiency virus
infection of lymphocytes and contributes to viral replication.";
J. Virol. 83:10119-10128(2009).
[27]
SUBCELLULAR LOCATION, INTERACTION WITH TNPO1 AND XPO5, AND DOMAIN.
PubMed=19124606; DOI=10.1128/MCB.01519-08;
Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P.,
Jantsch M.F.;
"RNA-regulated interaction of transportin-1 and exportin-5 with the
double-stranded RNA-binding domain regulates nucleocytoplasmic
shuttling of ADAR1.";
Mol. Cell. Biol. 29:1487-1497(2009).
[28]
FUNCTION.
PubMed=19651874; DOI=10.1093/nar/gkp604;
Doria M., Neri F., Gallo A., Farace M.G., Michienzi A.;
"Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1
stimulates viral infection.";
Nucleic Acids Res. 37:5848-5858(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601 AND THR-808, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
REVIEW.
PubMed=20192758; DOI=10.1146/annurev-biochem-060208-105251;
Nishikura K.;
"Functions and regulation of RNA editing by ADAR deaminases.";
Annu. Rev. Biochem. 79:321-349(2010).
[31]
FUNCTION.
PubMed=19908260; DOI=10.1002/ijc.25022;
Galeano F., Leroy A., Rossetti C., Gromova I., Gautier P.,
Keegan L.P., Massimi L., Di Rocco C., O'Connell M.A., Gallo A.;
"Human BLCAP transcript: new editing events in normal and cancerous
tissues.";
Int. J. Cancer 127:127-137(2010).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808 AND SER-825, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
REVIEW.
PubMed=22022963; DOI=10.1134/S0006297911080050;
Wang Q.;
"RNA editing catalyzed by ADAR1 and its function in mammalian cells.";
Biochemistry (Mosc.) 76:900-911(2011).
[35]
FUNCTION.
PubMed=21289159; DOI=10.1099/vir.0.028043-0;
Doria M., Tomaselli S., Neri F., Ciafre S.A., Farace M.G.,
Michienzi A., Gallo A.;
"ADAR2 editing enzyme is a novel human immunodeficiency virus-1
proviral factor.";
J. Gen. Virol. 92:1228-1232(2011).
[36]
REVIEW.
PubMed=21182352; DOI=10.1089/jir.2010.0097;
George C.X., Gan Z., Liu Y., Samuel C.E.;
"Adenosine deaminases acting on RNA, RNA editing, and interferon
action.";
J. Interferon Cytokine Res. 31:99-117(2011).
[37]
REVIEW.
PubMed=21490091; DOI=10.1128/JVI.00240-11;
Gelinas J.F., Clerzius G., Shaw E., Gatignol A.;
"Enhancement of replication of RNA viruses by ADAR1 via RNA editing
and inhibition of RNA-activated protein kinase.";
J. Virol. 85:8460-8466(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[39]
REVIEW.
PubMed=21211811; DOI=10.1016/j.virol.2010.12.004;
Samuel C.E.;
"Adenosine deaminases acting on RNA (ADARs) are both antiviral and
proviral.";
Virology 411:180-193(2011).
[40]
REVIEW.
PubMed=22988838; DOI=10.3109/10409238.2012.714350;
Mallela A., Nishikura K.;
"A-to-I editing of protein coding and noncoding RNAs.";
Crit. Rev. Biochem. Mol. Biol. 47:493-501(2012).
[41]
REVIEW.
PubMed=21769729; DOI=10.1007/82_2011_144;
Goodman R.A., Macbeth M.R., Beal P.A.;
"ADAR proteins: structure and catalytic mechanism.";
Curr. Top. Microbiol. Immunol. 353:1-33(2012).
[42]
FUNCTION.
PubMed=22278222; DOI=10.1128/JVI.06307-11;
Li Z., Okonski K.M., Samuel C.E.;
"Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction
of interferon by measles virus.";
J. Virol. 86:3787-3794(2012).
[43]
REVIEW.
PubMed=22113393; DOI=10.1007/s12035-011-8220-2;
Orlandi C., Barbon A., Barlati S.;
"Activity regulation of adenosine deaminases acting on RNA (ADARs).";
Mol. Neurobiol. 45:61-75(2012).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; THR-601; THR-603;
SER-629; SER-636; THR-808; SER-814 AND SER-825, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[46]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-26, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[47]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[48]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[49]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-408; LYS-418;
LYS-580 AND LYS-875, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[50]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-209 IN COMPLEX WITH
Z-DNA, AND DOMAIN.
PubMed=10364558; DOI=10.1126/science.284.5421.1841;
Schwartz T., Rould M.A., Lowenhaupt K., Herbert A., Rich A.;
"Crystal structure of the Z alpha domain of the human editing enzyme
ADAR1 bound to left-handed Z-DNA.";
Science 284:1841-1845(1999).
[51]
STRUCTURE BY NMR OF 125-201 IN COMPLEX WITH Z-DNA AND ALONE, AND
DOMAIN.
PubMed=10535945; DOI=10.1073/pnas.96.22.12465;
Schade M., Turner C.J., Kuehne R., Schmieder P., Lowenhaupt K.,
Herbert A., Rich A., Oschkinat H.;
"The solution structure of the Zalpha domain of the human RNA editing
enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA.";
Proc. Natl. Acad. Sci. U.S.A. 96:12465-12470(1999).
[52] {ECO:0000244|PDB:2ACJ}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 140-202 IN COMPLEX WITH DNA,
AND DOMAIN.
PubMed=16237447; DOI=10.1038/nature04088;
Ha S.C., Lowenhaupt K., Rich A., Kim Y.G., Kim K.K.;
"Crystal structure of a junction between B-DNA and Z-DNA reveals two
extruded bases.";
Nature 437:1183-1186(2005).
[53]
STRUCTURE BY NMR OF 708-801, DOMAIN, SUBCELLULAR LOCATION, INTERACTION
WITH TNPO1, AND MUTAGENESIS OF 708-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-778 AND
ARG-801.
PubMed=24753571; DOI=10.1073/pnas.1323698111;
Barraud P., Banerjee S., Mohamed W.I., Jantsch M.F., Allain F.H.;
"A bimodular nuclear localization signal assembled via an extended
double-stranded RNA-binding domain acts as an RNA-sensing signal for
transportin 1.";
Proc. Natl. Acad. Sci. U.S.A. 111:E1852-E1861(2014).
[54]
VARIANTS DSH PRO-923 AND SER-1165.
PubMed=12916015; DOI=10.1086/378209;
Miyamura Y., Suzuki T., Kono M., Inagaki K., Ito S., Suzuki N.,
Tomita Y.;
"Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are
involved in dyschromatosis symmetrica hereditaria.";
Am. J. Hum. Genet. 73:693-699(2003).
[55]
VARIANT DSH PHE-966.
PubMed=15146470; DOI=10.1002/humu.9246;
Zhang X.-J., He P.-P., Li M., He C.-D., Yan K.-L., Cui Y., Yang S.,
Zhang K.-Y., Gao M., Chen J.-J., Li C.-R., Jin L., Chen H.-D.,
Xu S.-J., Huang W.;
"Seven novel mutations of the ADAR gene in Chinese families and
sporadic patients with dyschromatosis symmetrica hereditaria (DSH).";
Hum. Mutat. 23:629-630(2004).
[56]
VARIANT DSH TRP-1155.
PubMed=15659327; DOI=10.1016/j.jdermsci.2004.11.004;
Li C.-R., Li M., Ma H.-J., Luo D., Yang L.-J., Wang D.-G., Zhu X.-H.,
Yue X.-Z., Chen W.-Q., Zhu W.-Y.;
"A new arginine substitution mutation of DSRAD gene in a Chinese
family with dyschromatosis symmetrica hereditaria.";
J. Dermatol. Sci. 37:95-99(2005).
[57]
VARIANT [LARGE SCALE ANALYSIS] VAL-806.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[58]
VARIANTS AGS6 ALA-193; THR-870; THR-872; HIS-892; ASN-999; ARG-1007;
PHE-1112 AND HIS-1113.
PubMed=23001123; DOI=10.1038/ng.2414;
Rice G.I., Kasher P.R., Forte G.M., Mannion N.M., Greenwood S.M.,
Szynkiewicz M., Dickerson J.E., Bhaskar S.S., Zampini M., Briggs T.A.,
Jenkinson E.M., Bacino C.A., Battini R., Bertini E., Brogan P.A.,
Brueton L.A., Carpanelli M., De Laet C., de Lonlay P., del Toro M.,
Desguerre I., Fazzi E., Garcia-Cazorla A., Heiberg A., Kawaguchi M.,
Kumar R., Lin J.P., Lourenco C.M., Male A.M., Marques W. Jr.,
Mignot C., Olivieri I., Orcesi S., Prabhakar P., Rasmussen M.,
Robinson R.A., Rozenberg F., Schmidt J.L., Steindl K., Tan T.Y.,
van der Merwe W.G., Vanderver A., Vassallo G., Wakeling E.L.,
Wassmer E., Whittaker E., Livingston J.H., Lebon P., Suzuki T.,
McLaughlin P.J., Keegan L.P., O'Connell M.A., Lovell S.C., Crow Y.J.;
"Mutations in ADAR1 cause Aicardi-Goutieres syndrome associated with a
type I interferon signature.";
Nat. Genet. 44:1243-1248(2012).
-!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine to
inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA
editing (PubMed:7972084, PubMed:7565688, PubMed:12618436). This
may affect gene expression and function in a number of ways that
include mRNA translation by changing codons and hence the amino
acid sequence of proteins; pre-mRNA splicing by altering splice
site recognition sequences; RNA stability by changing sequences
involved in nuclease recognition; genetic stability in the case of
RNA virus genomes by changing sequences during viral RNA
replication; and RNA structure-dependent activities such as
microRNA production or targeting or protein-RNA interactions. Can
edit both viral and cellular RNAs and can edit RNAs at multiple
sites (hyper-editing) or at specific sites (site-specific
editing). Its cellular RNA substrates include: bladder cancer-
associated protein (BLCAP), neurotransmitter receptors for
glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor
(GABRA3). Site-specific RNA editing of transcripts encoding these
proteins results in amino acid substitutions which consequently
alters their functional activities. Exhibits low-level editing at
the GRIA2 Q/R site, but edits efficiently at the R/G site and
HOTSPOT1. Its viral RNA substrates include: hepatitis C virus
(HCV), vesicular stomatitis virus (VSV), measles virus (MV),
hepatitis delta virus (HDV), and human immunodeficiency virus type
1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or
an antiviral effect (HCV) and this can be editing-dependent (HDV
and HCV), editing-independent (VSV and MV) or both (HIV-1).
Impairs HCV replication via RNA editing at multiple sites.
Enhances the replication of MV, VSV and HIV-1 through an editing-
independent mechanism via suppression of EIF2AK2/PKR activation
and function. Stimulates both the release and infectivity of HIV-1
viral particles by an editing-dependent mechanism where it
associates with viral RNAs and edits adenosines in the 5'UTR and
the Rev and Tat coding sequence. Can enhance viral replication of
HDV via A-to-I editing at a site designated as amber/W, thereby
changing an UAG amber stop codon to an UIG tryptophan (W) codon
that permits synthesis of the large delta antigen (L-HDAg) which
has a key role in the assembly of viral particles. However, high
levels of ADAR1 inhibit HDV replication.
{ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:15556947,
ECO:0000269|PubMed:15858013, ECO:0000269|PubMed:16120648,
ECO:0000269|PubMed:16475990, ECO:0000269|PubMed:17079286,
ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:19651874,
ECO:0000269|PubMed:19710021, ECO:0000269|PubMed:19908260,
ECO:0000269|PubMed:21289159, ECO:0000269|PubMed:22278222,
ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084}.
-!- CATALYTIC ACTIVITY: Adenine in double-stranded RNA + H(2)O =
hypoxanthine in double-stranded RNA + NH(3).
{ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:7565688,
ECO:0000269|PubMed:7972084}.
-!- SUBUNIT: Homodimer. Homodimerization is essential for its
catalytic activity (PubMed:12618436). Isoform 5 can form
heterodimers with ADARB1/ADAR2. Isoform 1 interacts with ILF2/NF45
and ILF3/NF90 (PubMed:16055709). Binding to ILF3/NF90 up-regulates
ILF3-mediated gene expression. Isoform 1 and isoform 5 (via DRBM 3
domain) interact with TNPO1 (PubMed:19124606, PubMed:24753571).
Isoform 5 (via DRBM domains) interacts with XPO5
(PubMed:19124606). Isoform 1 and isoform 5 can interact with
EIF2AK2/PKR and UPF1 (PubMed:17079286, PubMed:18362360).
{ECO:0000269|PubMed:10364558, ECO:0000269|PubMed:10535945,
ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:16055709,
ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:18178553,
ECO:0000269|PubMed:18362360, ECO:0000269|PubMed:19124606,
ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:24753571}.
-!- INTERACTION:
P14340:- (xeno); NbExp=2; IntAct=EBI-2462104, EBI-9825968;
Q99IB8:- (xeno); NbExp=3; IntAct=EBI-2462104, EBI-6858501;
Q9UPY3:DICER1; NbExp=8; IntAct=EBI-6913210, EBI-395506;
P03496:NS (xeno); NbExp=8; IntAct=EBI-2462104, EBI-2547442;
Q15633:TARBP2; NbExp=3; IntAct=EBI-6913210, EBI-978581;
Q92900:UPF1; NbExp=3; IntAct=EBI-2462104, EBI-373471;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:7565688}. Nucleus
{ECO:0000269|PubMed:24753571, ECO:0000269|PubMed:7565688}.
Note=Shuttles between the cytoplasm and nucleus (PubMed:7565688,
PubMed:24753571). Nuclear import is mediated by TNPO1
(PubMed:24753571). {ECO:0000269|PubMed:24753571,
ECO:0000269|PubMed:7565688}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm
{ECO:0000269|PubMed:19124606}. Nucleus
{ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:7565688}.
Nucleus, nucleolus {ECO:0000269|PubMed:12665561}.
Note=Predominantly nuclear but can shuttle between nucleus and
cytoplasm. TNPO1 can mediate its nuclear import whereas XPO5 can
mediate its nuclear export. {ECO:0000269|PubMed:19124606}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
Name=1; Synonyms=ADAR-a, ADAR1L, p150;
IsoId=P55265-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=ADAR-b;
IsoId=P55265-2; Sequence=VSP_008874;
Note=Produced by alternative splicing of isoform 1.;
Name=3; Synonyms=ADAR-c;
IsoId=P55265-3; Sequence=VSP_008873, VSP_008874;
Note=Produced by alternative splicing of isoform 1.;
Name=4;
IsoId=P55265-4; Sequence=VSP_008872;
Note=Produced by alternative splicing of isoform 1. No
experimental confirmation available. The N-terminus has been
derived from EST and genomic sequences. Ref.5 (CAE45853)
sequence is in conflict in position: 13:R->G. {ECO:0000305};
Name=5; Synonyms=ADAR1S, p110;
IsoId=P55265-5; Sequence=VSP_019235;
Note=Produced by alternative promoter usage.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, highest levels were
found in brain and lung (PubMed:7972084). Isoform 5 is expressed
at higher levels in astrocytomas as compared to normal brain
tissue and expression increases strikingly with the severity of
the tumor, being higher in the most aggressive tumors.
{ECO:0000269|PubMed:18178553, ECO:0000269|PubMed:7972084}.
-!- INDUCTION: Isoform 1 is induced by interferon alpha. Isoform 5 is
constitutively expressed. {ECO:0000269|PubMed:10200312,
ECO:0000269|PubMed:7565688}.
-!- DOMAIN: The first DRADA repeat binds Z-DNA.
{ECO:0000269|PubMed:10364558, ECO:0000269|PubMed:10535945,
ECO:0000269|PubMed:16237447}.
-!- DOMAIN: The third dsRNA-binding domain (DRBM 3) contains an
additional N-terminal alpha-helix that is part of a bi-partite
nuclear localization signal, together with the sequence
immediately C-terminal to DRBM 3. The presence of DRBM 3 is
important to bring together the N-terminal and the C-terminal part
of the bi-partite nuclear localization signal for import mediated
by TNPO1 (PubMed:24753571). RNA binding interferes with nuclear
import (PubMed:19124606, PubMed:24753571).
{ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:24753571}.
-!- PTM: Sumoylation reduces RNA-editing activity.
{ECO:0000269|PubMed:16120648}.
-!- DISEASE: Dyschromatosis symmetrica hereditaria (DSH) [MIM:127400]:
An autosomal dominant pigmentary genodermatosis characterized by a
mixture of hyperpigmented and hypopigmented macules distributed on
the face and the dorsal parts of the hands and feet, that appear
in infancy or early childhood. {ECO:0000269|PubMed:12916015,
ECO:0000269|PubMed:15146470, ECO:0000269|PubMed:15659327}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Aicardi-Goutieres syndrome 6 (AGS6) [MIM:615010]: A form
of Aicardi-Goutieres syndrome, a genetically heterogeneous disease
characterized by cerebral atrophy, leukoencephalopathy,
intracranial calcifications, chronic cerebrospinal fluid (CSF)
lymphocytosis, increased CSF alpha-interferon, and negative
serologic investigations for common prenatal infection. Clinical
features as thrombocytopenia, hepatosplenomegaly and elevated
hepatic transaminases along with intermittent fever may
erroneously suggest an infective process. Severe neurological
dysfunctions manifest in infancy as progressive microcephaly,
spasticity, dystonic posturing and profound psychomotor
retardation. Death often occurs in early childhood.
{ECO:0000269|PubMed:23001123}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: The N-terminus of isoform 4 has been derived from EST and
genomic sequences. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAE45853.1; Type=Erroneous termination; Positions=1227; Note=Translated as stop.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U10439; AAB06697.1; -; mRNA.
EMBL; U75503; AAB97116.1; -; Genomic_DNA.
EMBL; U75489; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75490; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75491; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75492; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75493; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75494; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75495; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75496; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75497; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75498; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75499; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75500; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75501; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75502; AAB97116.1; JOINED; Genomic_DNA.
EMBL; U75503; AAB97117.1; -; Genomic_DNA.
EMBL; U75489; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75490; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75491; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75492; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75493; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75494; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75495; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75496; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75497; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75498; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75499; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75500; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75501; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75502; AAB97117.1; JOINED; Genomic_DNA.
EMBL; U75503; AAB97118.1; -; Genomic_DNA.
EMBL; U75489; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75490; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75491; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75492; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75493; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75494; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75495; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75496; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75497; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75498; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75499; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75500; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75501; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U75502; AAB97118.1; JOINED; Genomic_DNA.
EMBL; U18121; AAC13782.1; -; mRNA.
EMBL; X79448; CAA55967.1; -; mRNA.
EMBL; X79449; CAA55968.1; -; mRNA.
EMBL; X98559; CAA67169.1; -; mRNA.
EMBL; X98559; CAA67170.1; -; mRNA.
EMBL; BX538232; CAD98075.1; -; mRNA.
EMBL; BX640741; CAE45853.1; ALT_SEQ; mRNA.
EMBL; AL606500; CAH71907.1; -; Genomic_DNA.
EMBL; AL592078; CAH71907.1; JOINED; Genomic_DNA.
EMBL; AL691488; CAH71907.1; JOINED; Genomic_DNA.
EMBL; AL606500; CAH71908.1; -; Genomic_DNA.
EMBL; AL592078; CAH71908.1; JOINED; Genomic_DNA.
EMBL; AL691488; CAH71908.1; JOINED; Genomic_DNA.
EMBL; AL592078; CAI16183.1; -; Genomic_DNA.
EMBL; AL606500; CAI16183.1; JOINED; Genomic_DNA.
EMBL; AL691488; CAI16183.1; JOINED; Genomic_DNA.
EMBL; AL592078; CAI16185.1; -; Genomic_DNA.
EMBL; AL606500; CAI16185.1; JOINED; Genomic_DNA.
EMBL; AL691488; CAI16185.1; JOINED; Genomic_DNA.
EMBL; AL691488; CAI17375.1; -; Genomic_DNA.
EMBL; AL592078; CAI17375.1; JOINED; Genomic_DNA.
EMBL; AL606500; CAI17375.1; JOINED; Genomic_DNA.
EMBL; AL691488; CAI17376.1; -; Genomic_DNA.
EMBL; AL592078; CAI17376.1; JOINED; Genomic_DNA.
EMBL; AL606500; CAI17376.1; JOINED; Genomic_DNA.
EMBL; CH471121; EAW53183.1; -; Genomic_DNA.
EMBL; CH471121; EAW53187.1; -; Genomic_DNA.
EMBL; BC038227; AAH38227.1; -; mRNA.
CCDS; CCDS1071.1; -. [P55265-1]
CCDS; CCDS30879.1; -. [P55265-5]
PIR; S65593; S65593.
RefSeq; NP_001020278.1; NM_001025107.2. [P55265-5]
RefSeq; NP_001102.2; NM_001111.4.
RefSeq; NP_001180424.1; NM_001193495.1. [P55265-5]
RefSeq; NP_056655.2; NM_015840.3.
RefSeq; NP_056656.2; NM_015841.3.
RefSeq; XP_006711174.1; XM_006711111.3. [P55265-5]
RefSeq; XP_006711175.1; XM_006711112.2. [P55265-5]
RefSeq; XP_006711176.1; XM_006711113.2. [P55265-5]
UniGene; Hs.12341; -.
PDB; 1QBJ; X-ray; 2.10 A; A/B/C=133-209.
PDB; 1QGP; NMR; -; A=125-200.
PDB; 1XMK; X-ray; 0.97 A; A=294-366.
PDB; 2ACJ; X-ray; 2.60 A; A/B/C/D=140-202.
PDB; 2GXB; X-ray; 2.25 A; A/B=140-202.
PDB; 2L54; NMR; -; A=136-198.
PDB; 2MDR; NMR; -; A=708-801.
PDB; 3F21; X-ray; 2.20 A; A/B/C=133-209.
PDB; 3F22; X-ray; 2.50 A; A/B/C=133-209.
PDB; 3F23; X-ray; 2.70 A; A/B/C=133-209.
PDB; 3IRQ; X-ray; 2.80 A; A/B/C/D=140-202.
PDB; 3IRR; X-ray; 2.65 A; A/B/C/D=140-202.
PDBsum; 1QBJ; -.
PDBsum; 1QGP; -.
PDBsum; 1XMK; -.
PDBsum; 2ACJ; -.
PDBsum; 2GXB; -.
PDBsum; 2L54; -.
PDBsum; 2MDR; -.
PDBsum; 3F21; -.
PDBsum; 3F22; -.
PDBsum; 3F23; -.
PDBsum; 3IRQ; -.
PDBsum; 3IRR; -.
ProteinModelPortal; P55265; -.
SMR; P55265; -.
BioGrid; 106617; 69.
CORUM; P55265; -.
DIP; DIP-29310N; -.
IntAct; P55265; 53.
MINT; MINT-4531596; -.
STRING; 9606.ENSP00000357459; -.
iPTMnet; P55265; -.
PhosphoSitePlus; P55265; -.
SwissPalm; P55265; -.
BioMuta; ADAR; -.
DMDM; 313104303; -.
EPD; P55265; -.
MaxQB; P55265; -.
PaxDb; P55265; -.
PeptideAtlas; P55265; -.
PRIDE; P55265; -.
DNASU; 103; -.
Ensembl; ENST00000368471; ENSP00000357456; ENSG00000160710. [P55265-5]
Ensembl; ENST00000368474; ENSP00000357459; ENSG00000160710. [P55265-1]
GeneID; 103; -.
KEGG; hsa:103; -.
UCSC; uc001ffh.4; human. [P55265-1]
CTD; 103; -.
DisGeNET; 103; -.
EuPathDB; HostDB:ENSG00000160710.15; -.
GeneCards; ADAR; -.
HGNC; HGNC:225; ADAR.
HPA; CAB056157; -.
HPA; HPA003890; -.
HPA; HPA051519; -.
MalaCards; ADAR; -.
MIM; 127400; phenotype.
MIM; 146920; gene.
MIM; 615010; phenotype.
neXtProt; NX_P55265; -.
OpenTargets; ENSG00000160710; -.
Orphanet; 51; Aicardi-Goutieres syndrome.
Orphanet; 41; Dyschromatosis symmetrica hereditaria.
Orphanet; 225154; Familial infantile bilateral striatal necrosis.
PharmGKB; PA24555; -.
eggNOG; KOG2777; Eukaryota.
eggNOG; ENOG410XT0Z; LUCA.
GeneTree; ENSGT00550000074412; -.
HOVERGEN; HBG067087; -.
InParanoid; P55265; -.
KO; K12968; -.
OMA; DPKFQYC; -.
OrthoDB; EOG091G0MZP; -.
PhylomeDB; P55265; -.
TreeFam; TF315806; -.
BRENDA; 3.5.4.37; 2681.
Reactome; R-HSA-75102; C6 deamination of adenosine.
Reactome; R-HSA-77042; Formation of editosomes by ADAR proteins.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
ChiTaRS; ADAR; human.
EvolutionaryTrace; P55265; -.
GeneWiki; ADAR; -.
GenomeRNAi; 103; -.
PMAP-CutDB; P55265; -.
PRO; PR:P55265; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160710; -.
CleanEx; HS_ADAR; -.
ExpressionAtlas; P55265; baseline and differential.
Genevisible; P55265; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB.
GO; GO:0016553; P:base conversion or substitution editing; IDA:MGI.
GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:1900369; P:negative regulation of RNA interference; IEA:Ensembl.
GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0045070; P:positive regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
GO; GO:0002566; P:somatic diversification of immune receptors via somatic mutation; IEA:Ensembl.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 1.10.10.10; -; 2.
InterPro; IPR002466; A_deamin.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR000607; dsRNA_A_deaminase.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF02137; A_deamin; 1.
Pfam; PF00035; dsrm; 3.
Pfam; PF02295; z-alpha; 2.
SMART; SM00552; ADEAMc; 1.
SMART; SM00358; DSRM; 3.
SMART; SM00550; Zalpha; 2.
SUPFAM; SSF46785; SSF46785; 2.
PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
PROSITE; PS50139; DRADA_REPEAT; 2.
PROSITE; PS50137; DS_RBD; 3.
1: Evidence at protein level;
3D-structure; Aicardi-Goutieres syndrome; Alternative promoter usage;
Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; DNA-binding; Hydrolase;
Immunity; Innate immunity; Isopeptide bond; Metal-binding;
Methylation; mRNA processing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
Ubl conjugation; Zinc.
CHAIN 1 1226 Double-stranded RNA-specific adenosine
deaminase.
/FTId=PRO_0000171774.
REPEAT 133 202 DRADA 1. {ECO:0000255|PROSITE-
ProRule:PRU00073,
ECO:0000269|PubMed:10364558,
ECO:0000269|PubMed:10535945,
ECO:0000269|PubMed:16237447}.
REPEAT 293 360 DRADA 2. {ECO:0000255|PROSITE-
ProRule:PRU00073}.
DOMAIN 503 571 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 614 682 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 726 794 DRBM 3. {ECO:0000255|PROSITE-
ProRule:PRU00266,
ECO:0000269|PubMed:24753571}.
DOMAIN 886 1221 A to I editase. {ECO:0000255|PROSITE-
ProRule:PRU00240}.
REGION 133 202 Interaction with Z-DNA.
{ECO:0000269|PubMed:10364558,
ECO:0000269|PubMed:10535945,
ECO:0000269|PubMed:16237447}.
REGION 716 725 N-terminal extension of DRBM 3 and
constituent of a bi-partite nuclear
localization signal.
{ECO:0000269|PubMed:24753571}.
REGION 795 801 C-terminal extension of DRBM 3 and
constituent of a bi-partite nuclear
localization signal.
{ECO:0000269|PubMed:24753571}.
ACT_SITE 912 912 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU00240}.
METAL 910 910 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00240}.
METAL 966 966 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00240}.
METAL 1036 1036 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00240}.
MOD_RES 26 26 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:P55266}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 601 601 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 603 603 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 629 629 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 808 808 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 814 814 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 823 823 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 384 384 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 408 408 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 418 418 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 418 418 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 418 418 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 580 580 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 875 875 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 295 Missing (in isoform 5).
{ECO:0000303|Ref.4}.
/FTId=VSP_019235.
VAR_SEQ 1 5 MNPRQ -> MMSPICDQTIDSRLKVEKATWWGRVGGGSRPH
WQPPGVRPCPEEVQDP (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_008872.
VAR_SEQ 694 712 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_008873.
VAR_SEQ 807 832 Missing (in isoform 2 and isoform 3).
{ECO:0000305}.
/FTId=VSP_008874.
VARIANT 100 100 R -> G (in dbSNP:rs1466731).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:7565688,
ECO:0000269|PubMed:7972084,
ECO:0000269|PubMed:9020165,
ECO:0000269|Ref.4}.
/FTId=VAR_048725.
VARIANT 193 193 P -> A (in AGS6; dbSNP:rs145588689).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069535.
VARIANT 384 384 K -> R (in dbSNP:rs2229857).
{ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:7565688,
ECO:0000269|PubMed:9020165,
ECO:0000269|Ref.4}.
/FTId=VAR_017240.
VARIANT 587 587 Y -> C (in dbSNP:rs17843865).
/FTId=VAR_024407.
VARIANT 806 806 E -> V (in a breast cancer sample;
somatic mutation; dbSNP:rs144119808).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035805.
VARIANT 870 870 A -> T (in AGS6; dbSNP:rs398122893).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069536.
VARIANT 872 872 I -> T (in AGS6; dbSNP:rs398122897).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069537.
VARIANT 892 892 R -> H (in AGS6; dbSNP:rs398122892).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069538.
VARIANT 923 923 L -> P (in DSH; dbSNP:rs28936680).
{ECO:0000269|PubMed:12916015}.
/FTId=VAR_017604.
VARIANT 966 966 C -> F (in DSH).
{ECO:0000269|PubMed:15146470}.
/FTId=VAR_021729.
VARIANT 999 999 K -> N (in AGS6; dbSNP:rs398122896).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069539.
VARIANT 1007 1007 G -> R (in AGS6; dbSNP:rs398122822).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069540.
VARIANT 1112 1112 Y -> F (in AGS6; dbSNP:rs398122895).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069541.
VARIANT 1113 1113 D -> H (in AGS6; dbSNP:rs398122894).
{ECO:0000269|PubMed:23001123}.
/FTId=VAR_069542.
VARIANT 1155 1155 R -> W (in DSH).
{ECO:0000269|PubMed:15659327}.
/FTId=VAR_026669.
VARIANT 1165 1165 F -> S (in DSH; dbSNP:rs28936681).
{ECO:0000269|PubMed:12916015}.
/FTId=VAR_017605.
MUTAGEN 418 418 K->R: Abolishes sumoylation.
{ECO:0000269|PubMed:16120648}.
MUTAGEN 708 801 Missing: Abolishes nuclear location.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 708 710 MMP->AMA: Decreased nuclear and partially
cytoplasmic location.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 712 715 KVRK->AVAA: No effect on nuclear
location. No effect on RNA binding.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 716 724 Missing: Disrupts the bi-partite nuclear
localization signal and abolishes nuclear
location. {ECO:0000269|PubMed:24753571}.
MUTAGEN 716 716 I->N: Disrupts the bi-partite nuclear
localization signal and abolishes nuclear
location; when associated with S-719 and
N-723. {ECO:0000269|PubMed:24753571}.
MUTAGEN 718 718 E->A: No effect on nuclear location; when
associated with A-721 and A-724.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 719 719 L->S: Disrupts the bi-partite nuclear
localization signal and abolishes nuclear
location; when associated with N-716 and
N-723. {ECO:0000269|PubMed:24753571}.
MUTAGEN 721 721 R->A: No effect on nuclear location; when
associated with A-721 and A-724.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 723 723 L->N: Disrupts the bi-partite nuclear
localization signal and abolishes nuclear
location; when associated with N-716 and
S-719. {ECO:0000269|PubMed:24753571}.
MUTAGEN 724 724 N->A: No effect on nuclear location; when
associated with A-718 and A-721.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 725 801 Missing: Disrupts nuclear localization
signal. No effect on RNA binding.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 777 778 KK->AA: Strongly impaired RNA binding. No
effect on nuclear location.
{ECO:0000269|PubMed:24753571}.
MUTAGEN 801 801 R->A: Abolishes interaction with TNPO1,
TNPO1-mediated nuclear import and nuclear
location. {ECO:0000269|PubMed:24753571}.
CONFLICT 53 53 E -> G (in Ref. 4; CAA55968).
{ECO:0000305}.
CONFLICT 245 245 F -> L (in Ref. 5; CAE45853).
{ECO:0000305}.
CONFLICT 482 482 F -> L (in Ref. 5; CAE45853).
{ECO:0000305}.
CONFLICT 873 873 I -> V (in Ref. 5; CAE45853).
{ECO:0000305}.
CONFLICT 1093 1093 D -> G (in Ref. 5; CAE45853).
{ECO:0000305}.
CONFLICT 1184 1184 E -> K (in Ref. 4; CAA55967/CAA55968/
CAA67169/CAA67170). {ECO:0000305}.
HELIX 127 130 {ECO:0000244|PDB:1QGP}.
HELIX 135 150 {ECO:0000244|PDB:1QBJ}.
STRAND 152 154 {ECO:0000244|PDB:1QGP}.
HELIX 158 165 {ECO:0000244|PDB:1QBJ}.
HELIX 169 181 {ECO:0000244|PDB:1QBJ}.
STRAND 184 192 {ECO:0000244|PDB:1QBJ}.
STRAND 194 197 {ECO:0000244|PDB:1QBJ}.
HELIX 294 309 {ECO:0000244|PDB:1XMK}.
HELIX 315 322 {ECO:0000244|PDB:1XMK}.
HELIX 324 326 {ECO:0000244|PDB:1XMK}.
HELIX 327 339 {ECO:0000244|PDB:1XMK}.
STRAND 342 346 {ECO:0000244|PDB:1XMK}.
STRAND 348 350 {ECO:0000244|PDB:1XMK}.
STRAND 352 355 {ECO:0000244|PDB:1XMK}.
HELIX 357 360 {ECO:0000244|PDB:1XMK}.
TURN 361 363 {ECO:0000244|PDB:1XMK}.
HELIX 716 724 {ECO:0000244|PDB:2MDR}.
HELIX 727 738 {ECO:0000244|PDB:2MDR}.
STRAND 742 749 {ECO:0000244|PDB:2MDR}.
STRAND 758 764 {ECO:0000244|PDB:2MDR}.
STRAND 767 776 {ECO:0000244|PDB:2MDR}.
HELIX 777 796 {ECO:0000244|PDB:2MDR}.
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


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