P55265 (DSRAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
Interferon-inducible protein 4
Short name=IFI-4
K88DSRBP

Gene names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

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

General annotation (Comments)

Function	Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. 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. Ref.12 Ref.13 Ref.16 Ref.19 Ref.24 Ref.25 Ref.27 Ref.30 Ref.34 Ref.41
Subunit structure	Homodimer. Homodimerization is essential for its catalytic activity. Isoform 5 can form heterodimers with ADARB1/ADAR2. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90. Binding to ILF3/NF90 up-regulates ILF3-mediated gene expression. Isoform 5 (via DRBM 3 domain) interacts with TNPO1. Isoform 5 (via DRBM domains) interacts with XPO5. Isoform 1 and isoform 5 can interact with EIF2AK2/PKR and UPF1. Ref.10 Ref.15 Ref.19 Ref.20 Ref.23 Ref.25 Ref.26
Subcellular location	Isoform 1: Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and nucleus. Ref.11 Ref.23 Ref.26 Isoform 5: Cytoplasm. Nucleus. Nucleus › nucleolus. Note: Predominantly nuclear but can shuttle between nucleus and cytoplasm. TNPO1 can mediate its nuclear import whereas XPO1 can mediate its nuclear export. Ref.11 Ref.23 Ref.26
Tissue specificity	Ubiquitously expressed, highest levels were found in brain and lung. 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. Ref.20
Induction	Isoform 1 is induced by interferon alpha. Isoform 5 is constitutively expressed. Ref.9
Post-translational modification	Sumoylation reduces RNA-editing activity. Ref.14
Involvement in disease	Dyschromatosis symmetrical hereditaria (DSH) [MIM:127400]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.45 Ref.46 Ref.47
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.
Sequence caution	The sequence CAE45853.1 differs from that shown. Reason: Erroneous termination at position 1227. Translated as stop.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity 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 Reference proteome
Gene Ontology (GO)
Biological_process	adenosine to inosine editing Inferred from direct assay Ref.13Ref.27Ref.34. Source: UniProtKB defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW gene expression Traceable author statement. Source: Reactome gene silencing by RNA Inferred from electronic annotation. Source: UniProtKB-KW mRNA modification Traceable author statement. Source: Reactome mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of protein kinase activity by regulation of protein phosphorylation Inferred from direct assay Ref.27. Source: UniProtKB positive regulation of viral genome replication Inferred from direct assay Ref.27. Source: UniProtKB protein export from nucleus Inferred from direct assay Ref.26. Source: UniProtKB protein import into nucleus Inferred from direct assay Ref.26. Source: UniProtKB response to interferon-alpha Inferred from direct assay Ref.16. Source: UniProtKB response to virus Inferred from mutant phenotype Ref.13. Source: UniProtKB type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from direct assay Ref.26. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome nucleus Inferred from direct assay Ref.26. Source: UniProtKB supraspliceosomal complex Inferred from direct assay Ref.23. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW double-stranded RNA adenosine deaminase activity Non-traceable author statement Ref.2. Source: UniProtKB double-stranded RNA binding Inferred from electronic annotation. Source: InterPro metal 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; ADAR1L; 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)

Also known as: ADAR1S; p110;

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.22 Ref.28

Modified residue

614

1

Phosphoserine Ref.22

Modified residue

808

1

Phosphothreonine Ref.17 Ref.18 Ref.21 Ref.28 Ref.31

Modified residue

823

1

Phosphoserine Ref.22

Modified residue

825

1

Phosphoserine Ref.22 Ref.31 Ref.37

Cross-link

418

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14

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

R → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.8
Corresponds to variant rs1466731 [ dbSNP | Ensembl ].

VAR_048725

Natural variant

384

1

K → R. Ref.2 Ref.3 Ref.4 Ref.5
Corresponds to variant rs2229857 [ dbSNP | Ensembl ].

VAR_017240

Natural variant

587

1

Y → C.
Corresponds to variant rs17843865 [ dbSNP | Ensembl ].

VAR_024407

Natural variant

806

1

E → V in a breast cancer sample; somatic mutation. Ref.48

VAR_035805

Natural variant

923

1

L → P in DSH. Ref.45
Corresponds to variant rs28936680 [ dbSNP | Ensembl ].

VAR_017604

Natural variant

966

1

C → F in DSH. Ref.46

VAR_021729

Natural variant

1155

1

R → W in DSH. Ref.47

VAR_026669

Natural variant

1165

1

F → S in DSH. Ref.45
Corresponds to variant rs28936681 [ dbSNP | Ensembl ].

VAR_017605

Experimental info

Mutagenesis

418

1

K → R: Abolishes sumoylation. Ref.14

Sequence conflict

53

1

E → G in CAA55968. Ref.4

Sequence conflict

245

1

F → L in CAE45853. Ref.5

Sequence conflict

482

1

F → L in CAE45853. Ref.5

Sequence conflict

873

1

I → V in CAE45853. Ref.5

Sequence conflict

1093

1

D → G in CAE45853. Ref.5

Sequence conflict

1184

1

E → K in CAA55967. Ref.4

Sequence conflict

1184

1

E → K in CAA55968. Ref.4

Sequence conflict

1184

1

E → K in CAA67169. Ref.4

Sequence conflict

1184

1

E → K in CAA67170. Ref.4

Isoform 4:

Sequence conflict

13

1

R → G in CAE45853. Ref.5

Secondary structure

1

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1226

Helix Strand Turn

Details...

Helix

127 – 130

4

Helix

135 – 150

16

Beta strand

152 – 154

3

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) (ADAR1L) (p150) [UniParc]. Last modified November 30, 2010. Version 4. Checksum: 9CE095D6F9C1BC79	FASTA	1,226	136,066
	10 20 30 40 50 60 MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ 70 80 90 100 110 120 TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR 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) [UniParc]. Checksum: 4CB1B306DAC584FC	FASTA	1,200	133,274
	10 20 30 40 50 60 MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ 70 80 90 100 110 120 TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR 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) [UniParc]. Checksum: 9764C8AB27BE118E	FASTA	1,181	131,170
	10 20 30 40 50 60 MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ 70 80 90 100 110 120 TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR 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 [UniParc]. Checksum: BB9B1DF19B8D3BC8	FASTA	1,269	140,838
	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 HLRSQGLQRG 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 (ADAR1S) (p110) [UniParc]. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT GLY-100.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-100 AND 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), VARIANTS GLY-100 AND 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), VARIANTS GLY-100 AND 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS GLY-100 AND 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-100. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"New antiviral pathway that mediates hepatitis C virus replicon interferon sensitivity through ADAR1." Taylor D.R., Puig M., Darnell M.E., Mihalik K., Feinstone S.M. J. Virol. 79:6291-6298(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"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] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-418, MUTAGENESIS OF LYS-418.
[15]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ILF2 AND ILF3.
[16]	"The large form of ADAR 1 is responsible for enhanced hepatitis delta virus RNA editing in interferon-alpha-stimulated host cells." Hartwig D., Schuette C., Warnecke J., Dorn I., Hennig H., Kirchner H., Schlenke P. J. Viral Hepat. 13:150-157(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus infection." Nie Y., Hammond G.L., Yang J.H. J. Virol. 81:917-923(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
[20]	"Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing activity inhibits cell migration and proliferation." Cenci C., Barzotti R., Galeano F., Corbelli S., Rota R., Massimi L., Di Rocco C., O'Connell M.A., Gallo A. J. Biol. Chem. 283:7251-7260(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, SUBUNIT, TISSUE SPECIFICITY.
[21]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-614; SER-823 AND SER-825, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact in the cell nucleus." Agranat L., Raitskin O., Sperling J., Sperling R. Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UPF1, SUBCELLULAR LOCATION.
[24]	"RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR." Toth A.M., Li Z., Cattaneo R., Samuel C.E. J. Biol. Chem. 284:29350-29356(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"ADAR1 interacts with PKR during human immunodeficiency virus infection of lymphocytes and contributes to viral replication." Clerzius G., Gelinas J.F., Daher A., Bonnet M., Meurs E.F., Gatignol A. J. Virol. 83:10119-10128(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
[26]	"RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1." Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., Jantsch M.F. Mol. Cell. Biol. 29:1487-1497(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TNFO1 AND XPO1.
[27]	"Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates viral infection." Doria M., Neri F., Gallo A., Farace M.G., Michienzi A. Nucleic Acids Res. 37:5848-5858(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[28]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601 AND THR-808, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[29]	"Functions and regulation of RNA editing by ADAR deaminases." Nishikura K. Annu. Rev. Biochem. 79:321-349(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[30]	"Human BLCAP transcript: new editing events in normal and cancerous tissues." Galeano F., Leroy A., Rossetti C., Gromova I., Gautier P., Keegan L.P., Massimi L., Di Rocco C., O'Connell M.A., Gallo A. Int. J. Cancer 127:127-137(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[31]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808 AND SER-825, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]	"RNA editing catalyzed by ADAR1 and its function in mammalian cells." Wang Q. Biokhimiia 76:900-911(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[34]	"ADAR2 editing enzyme is a novel human immunodeficiency virus-1 proviral factor." Doria M., Tomaselli S., Neri F., Ciafre S.A., Farace M.G., Michienzi A., Gallo A. J. Gen. Virol. 92:1228-1232(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[35]	"Adenosine deaminases acting on RNA, RNA editing, and interferon action." George C.X., Gan Z., Liu Y., Samuel C.E. J. Interferon Cytokine Res. 31:99-117(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[36]	"Enhancement of replication of RNA viruses by ADAR1 via RNA editing and inhibition of RNA-activated protein kinase." Gelinas J.F., Clerzius G., Shaw E., Gatignol A. J. Virol. 85:8460-8466(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[37]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, MASS SPECTROMETRY.
[38]	"Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral." Samuel C.E. Virology 411:180-193(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[39]	"A-to-I editing of protein coding and noncoding RNAs." Mallela A., Nishikura K. Crit. Rev. Biochem. Mol. Biol. 47:493-501(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[40]	"ADAR proteins: structure and catalytic mechanism." Goodman R.A., Macbeth M.R., Beal P.A. Curr. Top. Microbiol. Immunol. 353:1-33(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[41]	"Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction of interferon by measles virus." Li Z., Okonski K.M., Samuel C.E. J. Virol. 86:3787-3794(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[42]	"Activity regulation of adenosine deaminases acting on RNA (ADARs)." Orlandi C., Barbon A., Barlati S. Mol. Neurobiol. 45:61-75(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[43]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-209 IN COMPLEX WITH Z-DNA.
[44]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 125-201 IN COMPLEX WITH Z-DNA AND ALONE.
[45]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS DSH PRO-923 AND SER-1165.
[46]	"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] [Europe PMC] [Abstract] Cited for: VARIANT DSH PHE-966.
[47]	"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] [Europe PMC] [Abstract] Cited for: VARIANT DSH TRP-1155.
[48]	"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] [Europe PMC] [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. Sequence problems.
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.
CH471121 Genomic DNA. Translation: EAW53187.1.
BC038227 mRNA. Translation: AAH38227.1.

IPI

IPI00025057.
IPI00025058.
IPI00394665.
IPI00394668.
IPI00760588.

PIR

S65593.

RefSeq

NP_001020278.1. NM_001025107.2.
NP_001102.2. NM_001111.4.
NP_001180424.1. NM_001193495.1.
NP_056655.2. NM_015840.3.
NP_056656.2. NM_015841.3.

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	[»]
2L54	NMR	-	A	136-198	[»]
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	[»]
3IRQ	X-ray	2.80	A/B/C/D	140-202	[»]
3IRR	X-ray	2.65	A/B/C/D	140-202	[»]

ProteinModelPortal

P55265.

SMR

P55265. Positions 134-199, 294-366, 511-575, 731-797.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29310N.

IntAct

P55265. 8 interactions.

STRING

9606.ENSP00000357459.

PTM databases

PhosphoSite

P55265.

Proteomic databases

PaxDb

P55265.

PRIDE

P55265.

Protocols and materials databases

DNASU

103.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368471; ENSP00000357456; ENSG00000160710.
ENST00000368474; ENSP00000357459; ENSG00000160710.

GeneID

103.

KEGG

hsa:103.

UCSC

uc001ffh.3. human.
uc001ffi.3. human.
uc001ffj.3. human.

Organism-specific databases

CTD

103.

GeneCards

GC01M154554.

HGNC

HGNC:225. ADAR.

HPA

CAB056157.
HPA003890.

MIM

127400. phenotype.
146920. gene.

neXtProt

NX_P55265.

Orphanet

41. Acropigmentation of Dohi.

PharmGKB

PA24555.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG292433.

HOVERGEN

HBG067087.

KO

K12968.

OrthoDB

EOG4HDSSW.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P55265.

Bgee

P55265.

CleanEx

HS_ADAR.

Genevestigator

P55265.

GermOnline

ENSG00000160710. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 2 hits.
3.30.160.20. 3 hits.

InterPro

IPR002466. A_deamin.
IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

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

ChiTaRS

ADAR. human.

EvolutionaryTrace

P55265.

GenomeRNAi

103.

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, D3DV76, O15223, O43859, O43860, Q9BYM3, Q9BYM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 146 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.