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Protein

Double-stranded RNA-specific adenosine deaminase

Gene

Adar

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Does not affect polyomavirus replication but provides protection against virus-induced cytopathic effects. Essential for embryonic development and cell survival and plays a critical role in the maintenance of hematopoietic stem cells.3 Publications

Catalytic activityi

Adenine in double-stranded RNA + H2O = hypoxanthine in double-stranded RNA + NH3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi859 – 8591ZincPROSITE-ProRule annotation
Active sitei861 – 8611Proton donorPROSITE-ProRule annotation
Metal bindingi915 – 9151ZincPROSITE-ProRule annotation
Metal bindingi985 – 9851ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi171 – 19727By similarityAdd
BLAST

GO - Molecular functioni

  • double-stranded RNA adenosine deaminase activity Source: MGI
  • left-handed Z-DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: MGI

GO - Biological processi

  • adenosine to inosine editing Source: UniProtKB
  • base conversion or substitution editing Source: MGI
  • cellular response to virus Source: UniProtKB
  • defense response to virus Source: MGI
  • definitive hemopoiesis Source: MGI
  • erythrocyte differentiation Source: MGI
  • hematopoietic progenitor cell differentiation Source: MGI
  • hematopoietic stem cell homeostasis Source: MGI
  • innate immune response Source: UniProtKB-KW
  • in utero embryonic development Source: MGI
  • miRNA loading onto RISC involved in gene silencing by miRNA Source: MGI
  • mRNA processing Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of RNA interference Source: MGI
  • negative regulation of type I interferon-mediated signaling pathway Source: MGI
  • negative regulation of viral genome replication Source: MGI
  • osteoblast differentiation Source: MGI
  • positive regulation of viral genome replication Source: UniProtKB
  • pre-miRNA processing Source: MGI
  • production of miRNAs involved in gene silencing by miRNA Source: MGI
  • protein export from nucleus Source: MGI
  • protein import into nucleus Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to interferon-alpha Source: UniProtKB
  • response to virus Source: UniProtKB
  • somatic diversification of immune receptors via somatic mutation Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, mRNA processing, RNA-mediated gene silencing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.37. 3474.
ReactomeiR-MMU-75102. C6 deamination of adenosine.
R-MMU-77042. Formation of editosomes by ADAR proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Double-stranded RNA-specific adenosine deaminase (EC:3.5.4.37)
Short name:
DRADA
Alternative name(s):
RNA adenosine deaminase 1
Gene namesi
Name:Adar
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1889575. Adar.

Subcellular locationi

Isoform 1 :
  • Cytoplasm
  • Nucleusnucleolus

  • Note: Long forms starting at Met-1 are found predominantly in cytoplasm. Shuttles between the cytoplasm and nucleus.
Isoform 2 :
Isoform 3 :
  • Nucleusnucleolus

  • Note: Short forms starting at Met-519 are found exclusively in the nucleolus.
Isoform 4 :
  • Nucleusnucleolus

  • Note: Short forms starting at Met-519 are found exclusively in the nucleolus.

GO - Cellular componenti

  • cytoplasm Source: MGI
  • membrane Source: MGI
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • supraspliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice do not survive past E11.0-E12.5 and embryos display widespread apoptosis, a rapidly disintegrating liver structure and severe defects in hematopoiesis.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11781178Double-stranded RNA-specific adenosine deaminasePRO_0000171775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei238 – 2381PhosphoserineBy similarity
Cross-linki371 – 371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki371 – 371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki371 – 371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei567 – 5671PhosphoserineBy similarity
Modified residuei582 – 5821PhosphoserineCombined sources
Modified residuei589 – 5891PhosphoserineBy similarity
Modified residuei757 – 7571PhosphothreonineBy similarity
Modified residuei763 – 7631PhosphoserineBy similarity
Modified residuei772 – 7721PhosphoserineBy similarity
Modified residuei774 – 7741PhosphoserineBy similarity

Post-translational modificationi

Sumoylation reduces RNA-editing activity.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99MU3.
MaxQBiQ99MU3.
PaxDbiQ99MU3.
PeptideAtlasiQ99MU3.
PRIDEiQ99MU3.

PTM databases

iPTMnetiQ99MU3.
PhosphoSiteiQ99MU3.

Expressioni

Tissue specificityi

Highest levels in brain and spleen. Lowest levels in liver.1 Publication

Inductioni

By inflammation. Under normal conditions, long forms starting at Met-1 are dominant. Inflammation causes selective induction of short forms starting at Met-519.2 Publications

Gene expression databases

BgeeiQ99MU3.
CleanExiMM_ADAR.
GenevisibleiQ99MU3. MM.

Interactioni

Subunit structurei

Homodimer. Homodimerization is essential for its catalytic activity. Isoform 5 can form heterodimers with ADARB1/ADAR2. 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 UPF1 (By similarity). Isoform 1 interacts with ILF2/NF45 and ILF3/NF90. Binding to ILF3/NF90 up-regulates ILF3-mediated gene expression. Isoform 1 and isoform 5 interact with EIF2AK2/PKR.By similarity2 Publications

Protein-protein interaction databases

BioGridi207963. 1 interaction.
IntActiQ99MU3. 1 interaction.
MINTiMINT-4093631.
STRINGi10090.ENSMUSP00000103028.

Structurei

3D structure databases

ProteinModelPortaliQ99MU3.
SMRiQ99MU3. Positions 142-199, 247-319, 657-750.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati135 – 20470DRADA 1Add
BLAST
Repeati246 – 31368DRADA 2Add
BLAST
Domaini456 – 52469DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini567 – 63569DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini675 – 74369DRBM 3PROSITE-ProRule annotationAdd
BLAST
Domaini835 – 1170336A to I editasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 A to I editase domain.PROSITE-ProRule annotation
Contains 2 DRADA repeats.PROSITE-ProRule annotation
Contains 3 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOVERGENiHBG067087.
InParanoidiQ99MU3.
KOiK12968.
OMAiDPKFQYC.
OrthoDBiEOG7VHSX4.
PhylomeDBiQ99MU3.
TreeFamiTF315806.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
3.30.160.20. 3 hits.
InterProiIPR002466. A_deamin.
IPR014720. dsRBD_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99MU3-1) [UniParc]FASTAAdd to basket

Also known as: ADAR1Lb, 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.

« Hide

        10         20         30         40         50
MSQGFRGPTG VFPHQTQSYL DPSHEHSKWR YPQPQGPESY PRSFQLQQIE
60 70 80 90 100
FLKGRLPEAP LIGIQTQSLP PFLPGHWPRF PGPPAQDRQL EIWEFPRSVT
110 120 130 140 150
LRNQGFHIGP PLPPPHSRGT PWRGADGLCS HFRELSISQS PEQKVLNRLE
160 170 180 190 200
ELGEGKATTA HVLARELRIP KRDINRILYS LEKKGKLHRG RGKPPLWSLV
210 220 230 240 250
PLSQAWTQPP GVVNPDSCIQ EFPRGEPGLD SEDGDPASDL EGPSEPLDMA
260 270 280 290 300
EIKEKICDYL FNVSNSSALN LAKNIGLTKA RDVTSVLIDL ERQGDVYRQG
310 320 330 340 350
ATPPIWYLTD KKRERLQMKR STHSAPAPTP TAVPEATRSP SFPACHPPPA
360 370 380 390 400
GASSSVAASK RVENGQEPAI KHESRHEARP GPMRLRPHAY HNGPSRAGYV
410 420 430 440 450
ASENGQWATD DIPDNLNSIH TAPGEFRAIM EMPSFYSPTL PRCSPYKKLT
460 470 480 490 500
ECQLKNPVSG LLEYAQFTSQ TCDFNLIEQS GPSHEPRFKF QVVINGREFP
510 520 530 540 550
PAEAGSKKVA KQDAAVKAMA ILLREAKAKD SGQPEDLSHC PMEEDSEKPA
560 570 580 590 600
EAQAPSSSAT SLFSGKSPVT TLLECMHKLG NSCEFRLLSK EGPAHDPKFQ
610 620 630 640 650
YCVAVGAQTF PPVSAPSKKV AKQMAAEEAM KALQEEAASS ADDQSGGANT
660 670 680 690 700
DSLDESMAPN KIRRIGELVR YLNTNPVGGL LEYARSHGFA AEFKLIDQSG
710 720 730 740 750
PPHEPKFVYQ AKVGGRWFPA VCAHSKKQGK QDAADAALRV LIGESEKAEQ
760 770 780 790 800
LGFAEVTPVT GASLRRTMLL LSRSPDAHPK TLPLSGSTFH DQIAMLSHRC
810 820 830 840 850
FNALTNSFQP SLLGRKILAA IIMKRDPEDM GVVVSLGTGN RCVKGDSLSL
860 870 880 890 900
KGETVNDCHA EIISRRGFIR FLYSELMKYN HHTAKNSIFE LARGGEKLQI
910 920 930 940 950
KKTVSFHLYI STAPCGDGAL FDKSCSDRAV ESTESRHYPV FENPKQGKLR
960 970 980 990 1000
TKVENGEGTI PVESSDIVPT WDGIRLGERL RTMSCSDKIL RWNVLGLQGA
1010 1020 1030 1040 1050
LLTHFLQPVY LKSVTLGYLF SQGHLTRAIC CRVTRDGKAF EDGLRYPFIV
1060 1070 1080 1090 1100
NHPKVGRVSV YDSKRQSGKT KETSVNWCMA DGYDLEILDG TRGTVDGPGK
1110 1120 1130 1140 1150
ELSRVSKKNI FLQFKKLCSF RARRDLLQLS YGEAKKAARD YDLAKNYFKK
1160 1170
SLRDMGYGNW ISKPQEEKNF YLCPVPND
Length:1,178
Mass (Da):130,447
Last modified:November 14, 2003 - v2
Checksum:i8C28B71F00744724
GO
Isoform 2 (identifier: Q99MU3-2) [UniParc]FASTAAdd to basket

Also known as: ADAR1La

The sequence of this isoform differs from the canonical sequence as follows:
     756-781: Missing.

Show »
Length:1,152
Mass (Da):127,660
Checksum:i084406057050D3EB
GO
Isoform 3 (identifier: Q99MU3-3) [UniParc]FASTAAdd to basket

Also known as: ADAR1Sa

The sequence of this isoform differs from the canonical sequence as follows:
     1-518: Missing.
     756-781: Missing.

Show »
Length:634
Mass (Da):70,102
Checksum:iFF1AE77D36F08920
GO
Isoform 4 (identifier: Q99MU3-4) [UniParc]FASTAAdd to basket

Also known as: ADAR1Sb, p80

The sequence of this isoform differs from the canonical sequence as follows:
     1-518: Missing.

Show »
Length:660
Mass (Da):72,889
Checksum:i4FEA49B89A5B9B75
GO
Isoform 5 (identifier: Q99MU3-5) [UniParc]FASTAAdd to basket

Also known as: p110

The sequence of this isoform differs from the canonical sequence as follows:
     1-248: Missing.

Note: No experimental confirmation available.
Show »
Length:930
Mass (Da):102,580
Checksum:i94CDFC1E3EFBA538
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti415 – 4151N → D in AAK16102 (PubMed:12954622).Curated
Sequence conflicti644 – 6441Q → K in AAC06233 (Ref. 3) Curated
Sequence conflicti730 – 7301K → R in AAC06233 (Ref. 3) Curated
Sequence conflicti920 – 9201L → H in AAC06233 (Ref. 3) Curated
Sequence conflicti1003 – 10031T → A in BAC40888 (PubMed:16141072).Curated
Sequence conflicti1098 – 10981P → S in AAK16102 (PubMed:12954622).Curated
Sequence conflicti1149 – 11491K → R in AAK16102 (PubMed:12954622).Curated
Sequence conflicti1173 – 11731C → R in BAC40888 (PubMed:16141072).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201L → S in strain: Czech II. 1 Publication
Natural varianti32 – 321P → L in strain: Czech II. 1 Publication
Natural varianti120 – 1201T → P in strain: Czech II.
Natural varianti330 – 3301P → L in strain: Czech II. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 518518Missing in isoform 3 and isoform 4. 1 PublicationVSP_019236Add
BLAST
Alternative sequencei1 – 248248Missing in isoform 5. 1 PublicationVSP_019237Add
BLAST
Alternative sequencei756 – 78126Missing in isoform 2 and isoform 3. 4 PublicationsVSP_008875Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291875 mRNA. Translation: AAK16101.1.
AF291876 mRNA. Translation: AAK16102.1.
AF291877 mRNA. Translation: AAK16103.1.
AF291050 mRNA. Translation: AAK17103.1.
AF052506 mRNA. Translation: AAC06233.1.
BC042505 mRNA. Translation: AAH42505.1.
AK089451 mRNA. Translation: BAC40888.2.
CCDSiCCDS17513.1. [Q99MU3-2]
CCDS17514.1. [Q99MU3-5]
CCDS50963.1. [Q99MU3-1]
RefSeqiNP_001139768.1. NM_001146296.1. [Q99MU3-1]
NP_062629.3. NM_019655.3. [Q99MU3-2]
XP_006501817.1. XM_006501754.2. [Q99MU3-5]
UniGeneiMm.316628.

Genome annotation databases

EnsembliENSMUST00000029563; ENSMUSP00000029563; ENSMUSG00000027951. [Q99MU3-2]
ENSMUST00000098924; ENSMUSP00000096525; ENSMUSG00000027951. [Q99MU3-5]
ENSMUST00000107405; ENSMUSP00000103028; ENSMUSG00000027951. [Q99MU3-1]
ENSMUST00000118341; ENSMUSP00000113453; ENSMUSG00000027951. [Q99MU3-4]
ENSMUST00000121094; ENSMUSP00000112969; ENSMUSG00000027951. [Q99MU3-3]
GeneIDi56417.
KEGGimmu:56417.
UCSCiuc008pzv.2. mouse. [Q99MU3-1]
uc008pzw.2. mouse. [Q99MU3-2]
uc008pzy.2. mouse. [Q99MU3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291875 mRNA. Translation: AAK16101.1.
AF291876 mRNA. Translation: AAK16102.1.
AF291877 mRNA. Translation: AAK16103.1.
AF291050 mRNA. Translation: AAK17103.1.
AF052506 mRNA. Translation: AAC06233.1.
BC042505 mRNA. Translation: AAH42505.1.
AK089451 mRNA. Translation: BAC40888.2.
CCDSiCCDS17513.1. [Q99MU3-2]
CCDS17514.1. [Q99MU3-5]
CCDS50963.1. [Q99MU3-1]
RefSeqiNP_001139768.1. NM_001146296.1. [Q99MU3-1]
NP_062629.3. NM_019655.3. [Q99MU3-2]
XP_006501817.1. XM_006501754.2. [Q99MU3-5]
UniGeneiMm.316628.

3D structure databases

ProteinModelPortaliQ99MU3.
SMRiQ99MU3. Positions 142-199, 247-319, 657-750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207963. 1 interaction.
IntActiQ99MU3. 1 interaction.
MINTiMINT-4093631.
STRINGi10090.ENSMUSP00000103028.

PTM databases

iPTMnetiQ99MU3.
PhosphoSiteiQ99MU3.

Proteomic databases

EPDiQ99MU3.
MaxQBiQ99MU3.
PaxDbiQ99MU3.
PeptideAtlasiQ99MU3.
PRIDEiQ99MU3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029563; ENSMUSP00000029563; ENSMUSG00000027951. [Q99MU3-2]
ENSMUST00000098924; ENSMUSP00000096525; ENSMUSG00000027951. [Q99MU3-5]
ENSMUST00000107405; ENSMUSP00000103028; ENSMUSG00000027951. [Q99MU3-1]
ENSMUST00000118341; ENSMUSP00000113453; ENSMUSG00000027951. [Q99MU3-4]
ENSMUST00000121094; ENSMUSP00000112969; ENSMUSG00000027951. [Q99MU3-3]
GeneIDi56417.
KEGGimmu:56417.
UCSCiuc008pzv.2. mouse. [Q99MU3-1]
uc008pzw.2. mouse. [Q99MU3-2]
uc008pzy.2. mouse. [Q99MU3-3]

Organism-specific databases

CTDi103.
MGIiMGI:1889575. Adar.

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOVERGENiHBG067087.
InParanoidiQ99MU3.
KOiK12968.
OMAiDPKFQYC.
OrthoDBiEOG7VHSX4.
PhylomeDBiQ99MU3.
TreeFamiTF315806.

Enzyme and pathway databases

BRENDAi3.5.4.37. 3474.
ReactomeiR-MMU-75102. C6 deamination of adenosine.
R-MMU-77042. Formation of editosomes by ADAR proteins.

Miscellaneous databases

ChiTaRSiAdar. mouse.
PROiQ99MU3.
SOURCEiSearch...

Gene expression databases

BgeeiQ99MU3.
CleanExiMM_ADAR.
GenevisibleiQ99MU3. MM.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
3.30.160.20. 3 hits.
InterProiIPR002466. A_deamin.
IPR014720. dsRBD_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Intracellular localization of differentially regulated RNA-specific adenosine deaminase isoforms in inflammation."
    Yang J.-H., Nie Y., Zhao Q., Su Y., Pypaert M., Su H., Rabinovici R.
    J. Biol. Chem. 278:45833-45842(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6J.
    Tissue: Spleen.
  2. "Widespread inosine-containing mRNA in lymphocytes regulated by ADAR1 in response to inflammation."
    Yang J.-H., Luo X., Nie Y., Su Y., Zhao Q., Kabir K., Zhang D.-X., Rabinovici R.
    Immunology 109:15-23(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, INDUCTION.
  3. "cDNA for mouse double-stranded RNA-specific adenosine deaminase (ADAR1)."
    Young S.B., Carmichael G.G.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fibroblast.
  4. "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 2), VARIANTS SER-20; LEU-32 AND LEU-330.
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1173 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Dendritic cell.
  6. "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.
  7. "Liver disintegration in the mouse embryo caused by deficiency in the RNA-editing enzyme ADAR1."
    Hartner J.C., Schmittwolf C., Kispert A., Mueller A.M., Higuchi M., Seeburg P.H.
    J. Biol. Chem. 279:4894-4902(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "Stress-induced apoptosis associated with null mutation of ADAR1 RNA editing deaminase gene."
    Wang Q., Miyakoda M., Yang W., Khillan J., Stachura D.L., Weiss M.J., Nishikura K.
    J. Biol. Chem. 279:4952-4961(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "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.
  10. "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.
  11. "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.
  12. "Editing modifies the GABA(A) receptor subunit alpha3."
    Ohlson J., Pedersen J.S., Haussler D., Ohman M.
    RNA 13:698-703(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Spleen.
  14. "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.

Entry informationi

Entry nameiDSRAD_MOUSE
AccessioniPrimary (citable) accession number: Q99MU3
Secondary accession number(s): O70375
, Q80UZ6, Q8C222, Q99MU2, Q99MU4, Q99MU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: July 6, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.