Reviewed, UniProtKB/Swiss-Prot P55265 (DSRAD_HUMAN)

Names and origin

Protein names

Recommended name:
    Double-stranded RNA-specific adenosine deaminase
      Short name=DRADA
    EC=3.5.4.-
Alternative name(s):
    136 kDa double-stranded RNA-binding protein
      Short name=p136
    K88DSRBP
    Interferon-inducible protein 4
      Short name=IFI-4

Gene names

Name:	ADAR
Synonyms:	ADAR1, DSRAD, G1P1, IFI4

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1226 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts multiple adenosines to inosines and creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequence specificity. Has been found to modify more frequently adenosines in AU-rich regions, probably due to the relative ease of melting A/U base pairs as compared to G/C pairs. Functions to modify viral RNA genomes and may be responsible for hypermutation of certain negative-stranded viruses. Edits the messenger RNAs for glutamate receptor (GLUR) subunits by site-selective adenosine deamination. Produces low-level editing at the GLUR-B Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Binds to short interfering RNAs (siRNA) without editing them and suppresses siRNA-mediated RNA interference. Binds to ILF3/NF90 and up-regulates ILF3-mediated gene expression. Ref.12
Subunit structure	Homodimer. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90. Ref.10 Ref.14
Subcellular location	Cytoplasm. Nucleus › nucleolus. Note: Isoform 1 is found predominantly in cytoplasm but appears to shuttle between the cytoplasm and nucleus. Isoform 5 is found exclusively in the nucleolus. Ref.11
Tissue specificity	Ubiquitously expressed, highest levels were found in brain and lung.
Induction	Isoform 1 is induced by interferon alpha. Isoform 5 is constitutively expressed. Ref.9
Post-translational modification	Sumoylation reduces RNA-editing activity.
Involvement in disease	Defects in ADAR are a cause of dyschromatosis symmetrical hereditaria (DSH) [MIM:127400]; also known as reticulate acropigmentation of Dohi. DSH is a pigmentary genodermatosis of autosomal dominant inheritance characterized by a mixture of hyperpigmented and hypopigmented macules distributed on the dorsal parts of the hands and feet. Ref.26 Ref.27 Ref.28
Sequence similarities	Contains 1 A to I editase domain. Contains 2 DRADA repeats. Contains 3 DRBM (double-stranded RNA-binding) domains.
Caution	The N-terminus of isoform 4 has been derived from EST and genomic sequences.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat
Ligand	DNA-binding Metal-binding RNA-binding Zinc
Molecular function	Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	base conversion or substitution editing Ref.3 Inferred from direct assay. Source: MGI gene silencing by RNA Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.2 Traceable author statement. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW double-stranded RNA adenosine deaminase activity Ref.2 Ref.3 Non-traceable author statement. Source: UniProtKB double-stranded RNA binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: P55265-1)

Also known as: ADAR-a; p150;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Produced by alternative promoter usage.

Isoform 2 (identifier: P55265-2)

Also known as: ADAR-b;

The sequence of this isoform differs from the canonical sequence as follows:
     807-832: Missing.

Note: Produced by alternative splicing of isoform 1.

Isoform 3 (identifier: P55265-3)

Also known as: ADAR-c;

The sequence of this isoform differs from the canonical sequence as follows:
     694-712: Missing.
     807-832: Missing.

Note: Produced by alternative splicing of isoform 1.

Isoform 4 (identifier: P55265-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MNPRQ → MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPEEVQDP

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available. The N-terminus has been derived from EST and genomic sequences.

Isoform 5 (identifier: P55265-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-295: Missing.

Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1226

1226

Double-stranded RNA-specific adenosine deaminase

PRO_0000171774

Regions

Repeat

133 – 202

70

DRADA 1

Repeat

293 – 360

68

DRADA 2

Domain

503 – 571

69

DRBM 1

Domain

614 – 682

69

DRBM 2

Domain

726 – 794

69

DRBM 3

Domain

886 – 1221

336

A to I editase

DNA binding

169 – 195

27

Sites

Active site

912

1

Proton donor By similarity

Metal binding

910

1

Zinc By similarity

Metal binding

966

1

Zinc By similarity

Metal binding

1036

1

Zinc By similarity

Amino acid modifications

Modified residue

601

1

Phosphothreonine Ref.20 Ref.22 Ref.23

Modified residue

603

1

Phosphothreonine Ref.23

Modified residue

614

1

Phosphoserine Ref.20

Modified residue

808

1

Phosphothreonine Ref.22 Ref.23 Ref.16 Ref.17 Ref.18

Modified residue

818

1

Phosphothreonine Ref.15

Modified residue

823

1

Phosphoserine Ref.20

Modified residue

825

1

Phosphoserine Ref.20 Ref.17 Ref.19

Cross-link

418

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence

1 – 295

295

Missing in isoform 5.

VSP_019235

Alternative sequence

1 – 5

5

MNPRQ → MMSPICDQTIDSRLKVEKAT WWGRVGGGSRPHWQPPGVRP CPEEVQDP in isoform 4.

VSP_008872

Alternative sequence

694 – 712

19

Missing in isoform 3.

VSP_008873

Alternative sequence

807 – 832

26

Missing in isoform 2 and isoform 3.

VSP_008874

Natural variant

100

1

G → R: dbSNP rs1466731. Ref.6

VAR_048725

Natural variant

384

1

K → R: dbSNP rs2229857. Ref.2 Ref.3 Ref.4 Ref.5

VAR_017240

Natural variant

587

1

Y → C: dbSNP rs17843865.

VAR_024407

Natural variant

806

1

E → V in a breast cancer sample; somatic mutation. Ref.29

VAR_035805

Natural variant

923

1

L → P in DSH. dbSNP rs28936680. Ref.26

VAR_017604

Natural variant

966

1

C → F in DSH. Ref.27

VAR_021729

Natural variant

1155

1

R → W in DSH. Ref.28

VAR_026669

Natural variant

1165

1

F → S in DSH. dbSNP rs28936681. Ref.26

VAR_017605

Experimental info

Mutagenesis

418

1

K → R: Abolishes sumoylation. Ref.13

Sequence conflict

53

1

E → G in CAA55967. Ref.4

Sequence conflict

53

1

E → G in CAA55968. Ref.4

Sequence conflict

1184

1

E → K in CAA55967. Ref.4

Sequence conflict

1184

1

E → K in CAA55968. Ref.4

Secondary structure

1

.

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1226

Helix Strand Turn

Details...

Helix

127 – 130

4

Helix

135 – 150

16

Helix

158 – 165

8

Helix

169 – 181

13

Beta strand

184 – 192

9

Beta strand

194 – 197

4

Helix

294 – 309

16

Helix

315 – 322

8

Helix

324 – 326

3

Helix

327 – 339

13

Beta strand

342 – 346

5

Beta strand

348 – 350

3

Beta strand

352 – 355

4

Helix

357 – 360

4

Turn

361 – 363

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ADAR-a) (p150) [UniParc]. Last modified December 16, 2008. Version 3. Checksum: 02CA60C7F881E88F	FASTA	1,226	135,967
	10 20 30 40 50 60 MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ 70 80 90 100 110 120 TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLG SQGLQRGFQH PSPRGRSLPQ 130 140 150 160 170 180 RGVDCLSSHF QELSIYQDQE QRILKFLEEL GEGKATTAHD LSGKLGTPKK EINRVLYSLA 190 200 210 220 230 240 KKGKLQKEAG TPPLWKIAVS TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED 250 260 270 280 290 300 LLEPFIAVSA QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK 310 320 330 340 350 360 EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP PIWHLTDKKR 370 380 390 400 410 420 ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS NNMVTTEKVE NGQEPVIKLE 430 440 450 460 470 480 NRQEARPEPA RLKPPVHYNG PSKAGYVDFE NGQWATDDIP DDLNSIRAAP GEFRAIMEMP 490 500 510 520 530 540 SFYSHGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV 550 560 570 580 590 600 INGREFPPAE AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ 610 620 630 640 650 660 TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV AVGAQTFPSV 670 680 690 700 710 720 SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQPEGMISE SLDNLESMMP NKVRKIGELV 730 740 750 760 770 780 RYLNTNPVGG LLEYARSHGF AAEFKLVDQS GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG 790 800 810 820 830 840 KQEAADAALR VLIGENEKAE RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF 850 860 870 880 890 900 HDQIAMLSHR CFNTLTNSFQ PSLLGRKILA AIIMKKDSED MGVVVSLGTG NRCVKGDSLS 910 920 930 940 950 960 LKGETVNDCH AEIISRRGFI RFLYSELMKY NSQTAKDSIF EPAKGGEKLQ IKKTVSFHLY 970 980 990 1000 1010 1020 ISTAPCGDGA LFDKSCSDRA MESTESRHYP VFENPKQGKL RTKVENGEGT IPVESSDIVP 1030 1040 1050 1060 1070 1080 TWDGIRLGER LRTMSCSDKI LRWNVLGLQG ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI 1090 1100 1110 1120 1130 1140 CCRVTRDGSA FEDGLRHPFI VNHPKVGRVS IYDSKRQSGK TKETSVNWCL ADGYDLEILD 1150 1160 1170 1180 1190 1200 GTRGTVDGPR NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK 1210 1220 KGLKDMGYGN WISKPQEEKN FYLCPV
	Isoform 2 (ADAR-b). Checksum: 3D6DAF076CE124BC	FASTA	1,200	133,175
	10 20 30 40 50 60 MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ 70 80 90 100 110 120 TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLG SQGLQRGFQH PSPRGRSLPQ 130 140 150 160 170 180 RGVDCLSSHF QELSIYQDQE QRILKFLEEL GEGKATTAHD LSGKLGTPKK EINRVLYSLA 190 200 210 220 230 240 KKGKLQKEAG TPPLWKIAVS TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED 250 260 270 280 290 300 LLEPFIAVSA QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK 310 320 330 340 350 360 EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP PIWHLTDKKR 370 380 390 400 410 420 ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS NNMVTTEKVE NGQEPVIKLE 430 440 450 460 470 480 NRQEARPEPA RLKPPVHYNG PSKAGYVDFE NGQWATDDIP DDLNSIRAAP GEFRAIMEMP 490 500 510 520 530 540 SFYSHGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV 550 560 570 580 590 600 INGREFPPAE AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ 610 620 630 640 650 660 TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV AVGAQTFPSV 670 680 690 700 710 720 SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQPEGMISE SLDNLESMMP NKVRKIGELV 730 740 750 760 770 780 RYLNTNPVGG LLEYARSHGF AAEFKLVDQS GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG 790 800 810 820 830 840 KQEAADAALR VLIGENEKAE RMGFTELPLT GSTFHDQIAM LSHRCFNTLT NSFQPSLLGR 850 860 870 880 890 900 KILAAIIMKK DSEDMGVVVS LGTGNRCVKG DSLSLKGETV NDCHAEIISR RGFIRFLYSE 910 920 930 940 950 960 LMKYNSQTAK DSIFEPAKGG EKLQIKKTVS FHLYISTAPC GDGALFDKSC SDRAMESTES 970 980 990 1000 1010 1020 RHYPVFENPK QGKLRTKVEN GEGTIPVESS DIVPTWDGIR LGERLRTMSC SDKILRWNVL 1030 1040 1050 1060 1070 1080 GLQGALLTHF LQPIYLKSVT LGYLFSQGHL TRAICCRVTR DGSAFEDGLR HPFIVNHPKV 1090 1100 1110 1120 1130 1140 GRVSIYDSKR QSGKTKETSV NWCLADGYDL EILDGTRGTV DGPRNELSRV SKKNIFLLFK 1150 1160 1170 1180 1190 1200 KLCSFRYRRD LLRLSYGEAK KAARDYETAK NYFKKGLKDM GYGNWISKPQ EEKNFYLCPV
	Isoform 3 (ADAR-c). Checksum: 8DC9ADBF22BA108A	FASTA	1,181	131,071
	10 20 30 40 50 60 MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ 70 80 90 100 110 120 TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLG SQGLQRGFQH PSPRGRSLPQ 130 140 150 160 170 180 RGVDCLSSHF QELSIYQDQE QRILKFLEEL GEGKATTAHD LSGKLGTPKK EINRVLYSLA 190 200 210 220 230 240 KKGKLQKEAG TPPLWKIAVS TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED 250 260 270 280 290 300 LLEPFIAVSA QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK 310 320 330 340 350 360 EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP PIWHLTDKKR 370 380 390 400 410 420 ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS NNMVTTEKVE NGQEPVIKLE 430 440 450 460 470 480 NRQEARPEPA RLKPPVHYNG PSKAGYVDFE NGQWATDDIP DDLNSIRAAP GEFRAIMEMP 490 500 510 520 530 540 SFYSHGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV 550 560 570 580 590 600 INGREFPPAE AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ 610 620 630 640 650 660 TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV AVGAQTFPSV 670 680 690 700 710 720 SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQVRKIGEL VRYLNTNPVG GLLEYARSHG 730 740 750 760 770 780 FAAEFKLVDQ SGPPHEPKFV YQAKVGGRWF PAVCAHSKKQ GKQEAADAAL RVLIGENEKA 790 800 810 820 830 840 ERMGFTELPL TGSTFHDQIA MLSHRCFNTL TNSFQPSLLG RKILAAIIMK KDSEDMGVVV 850 860 870 880 890 900 SLGTGNRCVK GDSLSLKGET VNDCHAEIIS RRGFIRFLYS ELMKYNSQTA KDSIFEPAKG 910 920 930 940 950 960 GEKLQIKKTV SFHLYISTAP CGDGALFDKS CSDRAMESTE SRHYPVFENP KQGKLRTKVE 970 980 990 1000 1010 1020 NGEGTIPVES SDIVPTWDGI RLGERLRTMS CSDKILRWNV LGLQGALLTH FLQPIYLKSV 1030 1040 1050 1060 1070 1080 TLGYLFSQGH LTRAICCRVT RDGSAFEDGL RHPFIVNHPK VGRVSIYDSK RQSGKTKETS 1090 1100 1110 1120 1130 1140 VNWCLADGYD LEILDGTRGT VDGPRNELSR VSKKNIFLLF KKLCSFRYRR DLLRLSYGEA 1150 1160 1170 1180 KKAARDYETA KNYFKKGLKD MGYGNWISKP QEEKNFYLCP V
	Isoform 4. Checksum: 25B1E8E09ACD6F3E	FASTA	1,269	140,739
	10 20 30 40 50 60 MMSPICDQTI DSRLKVEKAT WWGRVGGGSR PHWQPPGVRP CPEEVQDPGY SLSGYYTHPF 70 80 90 100 110 120 QGYEHRQLRY QQPGPGSSPS SFLLKQIEFL KGQLPEAPVI GKQTPSLPPS LPGLRPRFPV 130 140 150 160 170 180 LLASSTRGRQ VDIRGVPRGV HLGSQGLQRG FQHPSPRGRS LPQRGVDCLS SHFQELSIYQ 190 200 210 220 230 240 DQEQRILKFL EELGEGKATT AHDLSGKLGT PKKEINRVLY SLAKKGKLQK EAGTPPLWKI 250 260 270 280 290 300 AVSTQAWNQH SGVVRPDGHS QGAPNSDPSL EPEDRNSTSV SEDLLEPFIA VSAQAWNQHS 310 320 330 340 350 360 GVVRPDSHSQ GSPNSDPGLE PEDSNSTSAL EDPLEFLDMA EIKEKICDYL FNVSDSSALN 370 380 390 400 410 420 LAKNIGLTKA RDINAVLIDM ERQGDVYRQG TTPPIWHLTD KKRERMQIKR NTNSVPETAP 430 440 450 460 470 480 AAIPETKRNA EFLTCNIPTS NASNNMVTTE KVENGQEPVI KLENRQEARP EPARLKPPVH 490 500 510 520 530 540 YNGPSKAGYV DFENGQWATD DIPDDLNSIR AAPGEFRAIM EMPSFYSHGL PRCSPYKKLT 550 560 570 580 590 600 ECQLKNPISG LLEYAQFASQ TCEFNMIEQS GPPHEPRFKF QVVINGREFP PAEAGSKKVA 610 620 630 640 650 660 KQDAAMKAMT ILLEEAKAKD SGKSEESSHY STEKESEKTA ESQTPTPSAT SFFSGKSPVT 670 680 690 700 710 720 TLLECMHKLG NSCEFRLLSK EGPAHEPKFQ YCVAVGAQTF PSVSAPSKKV AKQMAAEEAM 730 740 750 760 770 780 KALHGEATNS MASDNQPEGM ISESLDNLES MMPNKVRKIG ELVRYLNTNP VGGLLEYARS 790 800 810 820 830 840 HGFAAEFKLV DQSGPPHEPK FVYQAKVGGR WFPAVCAHSK KQGKQEAADA ALRVLIGENE 850 860 870 880 890 900 KAERMGFTEV TPVTGASLRR TMLLLSRSPE AQPKTLPLTG STFHDQIAML SHRCFNTLTN 910 920 930 940 950 960 SFQPSLLGRK ILAAIIMKKD SEDMGVVVSL GTGNRCVKGD SLSLKGETVN DCHAEIISRR 970 980 990 1000 1010 1020 GFIRFLYSEL MKYNSQTAKD SIFEPAKGGE KLQIKKTVSF HLYISTAPCG DGALFDKSCS 1030 1040 1050 1060 1070 1080 DRAMESTESR HYPVFENPKQ GKLRTKVENG EGTIPVESSD IVPTWDGIRL GERLRTMSCS 1090 1100 1110 1120 1130 1140 DKILRWNVLG LQGALLTHFL QPIYLKSVTL GYLFSQGHLT RAICCRVTRD GSAFEDGLRH 1150 1160 1170 1180 1190 1200 PFIVNHPKVG RVSIYDSKRQ SGKTKETSVN WCLADGYDLE ILDGTRGTVD GPRNELSRVS 1210 1220 1230 1240 1250 1260 KKNIFLLFKK LCSFRYRRDL LRLSYGEAKK AARDYETAKN YFKKGLKDMG YGNWISKPQE EKNFYLCPV
	Isoform 5. Checksum: 113B63CF165097FC	FASTA	931	103,642
	10 20 30 40 50 60 MAEIKEKICD YLFNVSDSSA LNLAKNIGLT KARDINAVLI DMERQGDVYR QGTTPPIWHL 70 80 90 100 110 120 TDKKRERMQI KRNTNSVPET APAAIPETKR NAEFLTCNIP TSNASNNMVT TEKVENGQEP 130 140 150 160 170 180 VIKLENRQEA RPEPARLKPP VHYNGPSKAG YVDFENGQWA TDDIPDDLNS IRAAPGEFRA 190 200 210 220 230 240 IMEMPSFYSH GLPRCSPYKK LTECQLKNPI SGLLEYAQFA SQTCEFNMIE QSGPPHEPRF 250 260 270 280 290 300 KFQVVINGRE FPPAEAGSKK VAKQDAAMKA MTILLEEAKA KDSGKSEESS HYSTEKESEK 310 320 330 340 350 360 TAESQTPTPS ATSFFSGKSP VTTLLECMHK LGNSCEFRLL SKEGPAHEPK FQYCVAVGAQ 370 380 390 400 410 420 TFPSVSAPSK KVAKQMAAEE AMKALHGEAT NSMASDNQPE GMISESLDNL ESMMPNKVRK 430 440 450 460 470 480 IGELVRYLNT NPVGGLLEYA RSHGFAAEFK LVDQSGPPHE PKFVYQAKVG GRWFPAVCAH 490 500 510 520 530 540 SKKQGKQEAA DAALRVLIGE NEKAERMGFT EVTPVTGASL RRTMLLLSRS PEAQPKTLPL 550 560 570 580 590 600 TGSTFHDQIA MLSHRCFNTL TNSFQPSLLG RKILAAIIMK KDSEDMGVVV SLGTGNRCVK 610 620 630 640 650 660 GDSLSLKGET VNDCHAEIIS RRGFIRFLYS ELMKYNSQTA KDSIFEPAKG GEKLQIKKTV 670 680 690 700 710 720 SFHLYISTAP CGDGALFDKS CSDRAMESTE SRHYPVFENP KQGKLRTKVE NGEGTIPVES 730 740 750 760 770 780 SDIVPTWDGI RLGERLRTMS CSDKILRWNV LGLQGALLTH FLQPIYLKSV TLGYLFSQGH 790 800 810 820 830 840 LTRAICCRVT RDGSAFEDGL RHPFIVNHPK VGRVSIYDSK RQSGKTKETS VNWCLADGYD 850 860 870 880 890 900 LEILDGTRGT VDGPRNELSR VSKKNIFLLF KKLCSFRYRR DLLRLSYGEA KKAARDYETA 910 920 930 KNYFKKGLKD MGYGNWISKP QEEKNFYLCP V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing." Kim U., Wang Y., Sanford T., Zeng Y., Nishikura K. Proc. Natl. Acad. Sci. U.S.A. 91:11457-11461(1994) [PubMed: 7972084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]	"Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase." Patterson J.B., Samuel C.E. Mol. Cell. Biol. 15:5376-5388(1995) [PubMed: 7565688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-384. Tissue: Kidney.
[3]	"Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase." Liu Y., George C.X., Patterson J.B., Samuel C.E. J. Biol. Chem. 272:4419-4428(1997) [PubMed: 9020165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), VARIANT ARG-384. Tissue: Placenta.
[4]	"The gene coding for the interferon-inducible human dsRNA adenosine deaminase is transcribed into several messengers specifying different proteins." Deblandre G., Marinx O., Nols C., Defrance P., Berr P., Huez G., Caput D. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), VARIANT ARG-384. Tissue: Cervix carcinoma.
[5]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT ARG-384. Tissue: Amygdala and Fetal kidney.
[6]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-100.
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph.
[9]	"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." George C.X., Samuel C.E. Proc. Natl. Acad. Sci. U.S.A. 96:4621-4626(1999) [PubMed: 10200312] [Abstract] Cited for: ALTERNATIVE PROMOTER USAGE, INDUCTION.
[10]	"Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNA." Cho D.-S.C., Yang W., Lee J.T., Shiekhattar R., Murray J.M., Nishikura K. J. Biol. Chem. 278:17093-17102(2003) [PubMed: 12618436] [Abstract] Cited for: HOMODIMERIZATION.
[11]	"Dynamic association of RNA-editing enzymes with the nucleolus." Desterro J.M.P., Keegan L.P., Lafarga M., Berciano M.T., O'Connell M., Carmo-Fonseca M. J. Cell Sci. 116:1805-1818(2003) [PubMed: 12665561] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"ADAR1 RNA deaminase limits short interfering RNA efficacy in mammalian cells." Yang W., Wang Q., Howell K.L., Lee J.T., Cho D.-S.C., Murray J.M., Nishikura K. J. Biol. Chem. 280:3946-3953(2005) [PubMed: 15556947] [Abstract] Cited for: FUNCTION.
[13]	"SUMO-1 modification alters ADAR1 editing activity." Desterro J.M.P., Keegan L.P., Jaffray E., Hay R.T., O'Connell M.A., Carmo-Fonseca M. Mol. Biol. Cell 16:5115-5126(2005) [PubMed: 16120648] [Abstract] Cited for: SUMOYLATION AT LYS-418, MUTAGENESIS OF LYS-418.
[14]	"ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing." Nie Y., Ding L., Kao P.N., Braun R., Yang J.-H. Mol. Cell. Biol. 25:6956-6963(2005) [PubMed: 16055709] [Abstract] Cited for: INTERACTION WITH ILF2 AND ILF3.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-818, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"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." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808 AND SER-825, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, MASS SPECTROMETRY.
[19]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, MASS SPECTROMETRY.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-614; SER-823 AND SER-825, MASS SPECTROMETRY.
[21]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601 AND THR-808, MASS SPECTROMETRY.
[23]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; THR-603 AND THR-808, MASS SPECTROMETRY. Tissue: T-cell.
[24]	"Crystal structure of the Z alpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA." Schwartz T., Rould M.A., Lowenhaupt K., Herbert A., Rich A. Science 284:1841-1845(1999) [PubMed: 10364558] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-209 IN COMPLEX WITH Z-DNA.
[25]	"The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA." Schade M., Turner C.J., Kuehne R., Schmieder P., Lowenhaupt K., Herbert A., Rich A., Oschkinat H. Proc. Natl. Acad. Sci. U.S.A. 96:12465-12470(1999) [PubMed: 10535945] [Abstract] Cited for: STRUCTURE BY NMR OF 125-201 IN COMPLEX WITH Z-DNA AND ALONE.
[26]	"Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are involved in dyschromatosis symmetrica hereditaria." Miyamura Y., Suzuki T., Kono M., Inagaki K., Ito S., Suzuki N., Tomita Y. Am. J. Hum. Genet. 73:693-699(2003) [PubMed: 12916015] [Abstract] Cited for: VARIANTS DSH PRO-923 AND SER-1165.
[27]	"Seven novel mutations of the ADAR gene in Chinese families and sporadic patients with dyschromatosis symmetrica hereditaria (DSH)." 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. Hum. Mutat. 23:629-630(2004) [PubMed: 15146470] [Abstract] Cited for: VARIANT DSH PHE-966.
[28]	"A new arginine substitution mutation of DSRAD gene in a Chinese family with dyschromatosis symmetrica hereditaria." 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. J. Dermatol. Sci. 37:95-99(2005) [PubMed: 15659327] [Abstract] Cited for: VARIANT DSH TRP-1155.
[29]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-806.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U10439 mRNA. Translation: AAB06697.1.
U75503 , U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97116.1.
U75503 , U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97117.1.
U75503 , U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97118.1.
U18121 mRNA. Translation: AAC13782.1.
X79448 mRNA. Translation: CAA55967.1.
X79449 mRNA. Translation: CAA55968.1.
X98559 mRNA. Translation: CAA67169.1.
X98559 mRNA. Translation: CAA67170.1.
BX538232 mRNA. Translation: CAD98075.1.
BX640741 mRNA. Translation: CAE45853.1.
AL606500, AL592078, AL691488 Genomic DNA. Translation: CAH71907.1.
AL606500, AL592078, AL691488 Genomic DNA. Translation: CAH71908.1.
AL592078, AL606500, AL691488 Genomic DNA. Translation: CAI16183.1.
AL592078, AL606500, AL691488 Genomic DNA. Translation: CAI16185.1.
AL691488, AL592078, AL606500 Genomic DNA. Translation: CAI17375.1.
AL691488, AL592078, AL606500 Genomic DNA. Translation: CAI17376.1.
CH471121 Genomic DNA. Translation: EAW53183.1.
BC038227 mRNA. Translation: AAH38227.1.

IPI

IPI00025057.
IPI00025058.
IPI00394665.
IPI00394668.
IPI00760588.

PIR

S65593.

RefSeq

NP_001020278.1.
NP_001102.2.
NP_056655.2.
NP_056656.2.

UniGene

Hs.12341

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QBJ	X-ray	2.10	A/B/C	133-209	[»]
1QGP	NMR	-	A	126-200	[»]
1XMK	X-ray	0.97	A	294-366	[»]
2ACJ	X-ray	2.60	A/B/C/D	140-202	[»]
2GXB	X-ray	2.25	A/B	140-202	[»]
3F21	X-ray	2.20	A/B/C	133-209	[»]
3F22	X-ray	2.50	A/B/C	133-209	[»]
3F23	X-ray	2.70	A/B/C	133-209	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29310N.

STRING

P55265.

PTM databases

PhosphoSite

P55265.

Proteomic databases

PRIDE

P55265.

Genome annotation databases

Ensembl

ENST00000368474; ENSP00000357459; ENSG00000160710; Homo sapiens. [Genome view]

GeneID

103.

KEGG

hsa:103.

UCSC

uc001ffi.1. human.
uc001ffj.1. human.

Organism-specific databases

CTD

103.

GeneCards

GC01M152821.

H-InvDB

HIX0001101.

HGNC

HGNC:225. ADAR.

HPA

HPA003890.

MIM

127400. phenotype.
146920. gene.

Orphanet

41. Acropigmentation of Dohi.

PharmGKB

PA24555.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P55265.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.

Gene expression databases

ArrayExpress

P55265.

Bgee

P55265.

CleanEx

HS_ADAR.

Genevestigator

P55265.

GermOnline

ENSG00000160710. Homo sapiens.

Family and domain databases

InterPro

IPR002466. A_deamin.
IPR001159. Ds-RNA_bd.
IPR014720. dsRNA-bd-like.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.30.160.20. dsRNA-bd-like. 3 hits.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.

Pfam

PF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]

SMART

SM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view]

PROSITE

PS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

389.

PMAP-CutDB

P55265.

SOURCE

Search...

Entry information

Entry name

DSRAD_HUMAN

Accession

Primary (citable) accession number: P55265
Secondary accession number(s): B1AQQ9 , B1AQR0, O15223, O43859, O43860, Q9BYM3, Q9BYM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.