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P55265 (DSRAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Double-stranded RNA-specific adenosine deaminase

Short name=DRADA
EC=3.5.4.37
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1226 AA.
Sequence statusComplete.
Protein existenceEvidence 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.25 Ref.26 Ref.28 Ref.31 Ref.35 Ref.42

Catalytic activity

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

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.26 Ref.27

Subcellular location

Isoform 1: Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and nucleus. Ref.11 Ref.23 Ref.27

Isoform 5: Cytoplasm. Nucleus. Nucleusnucleolus. 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.27

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 symmetrica hereditaria (DSH) [MIM:127400]: An autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed on the face and the dorsal parts of the hands and feet, that appear in infancy or early childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.46 Ref.47 Ref.48

Aicardi-Goutieres syndrome 6 (AGS6) [MIM:615010]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.50

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 processAntiviral defense
Immunity
Innate immunity
mRNA processing
RNA-mediated gene silencing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DiseaseAicardi-Goutieres syndrome
Disease mutation
   DomainRepeat
   LigandDNA-binding
Metal-binding
RNA-binding
Zinc
   Molecular functionHydrolase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadenosine to inosine editing

Inferred from direct assay Ref.13Ref.28Ref.35. Source: UniProtKB

base conversion or substitution editing

Inferred from direct assay Ref.3. Source: MGI

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

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

innate immune response

Traceable author statement Ref.16. Source: UniProtKB

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: Ensembl

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from direct assay Ref.28. Source: UniProtKB

positive regulation of viral genome replication

Inferred from direct assay Ref.28. Source: UniProtKB

protein export from nucleus

Inferred from direct assay Ref.27. Source: UniProtKB

protein import into nucleus

Inferred from direct assay Ref.27. 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 signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.27. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.23Ref.27. Source: UniProtKB

supraspliceosomal complex

Inferred from direct assay Ref.23. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

double-stranded RNA adenosine deaminase activity

Non-traceable author statement Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB83EBI-2462104,EBI-6858501From a different organism.
DICER1Q9UPY38EBI-6913210,EBI-395506
TARBP2Q156333EBI-6913210,EBI-978581

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12261226Double-stranded RNA-specific adenosine deaminase
PRO_0000171774

Regions

Repeat133 – 20270DRADA 1
Repeat293 – 36068DRADA 2
Domain503 – 57169DRBM 1
Domain614 – 68269DRBM 2
Domain726 – 79469DRBM 3
Domain886 – 1221336A to I editase
DNA binding169 – 19527

Sites

Active site9121Proton donor By similarity
Metal binding9101Zinc By similarity
Metal binding9661Zinc By similarity
Metal binding10361Zinc By similarity

Amino acid modifications

Modified residue6011Phosphothreonine Ref.22 Ref.29
Modified residue6141Phosphoserine Ref.22
Modified residue8081Phosphothreonine Ref.17 Ref.18 Ref.21 Ref.29 Ref.32
Modified residue8231Phosphoserine Ref.22
Modified residue8251Phosphoserine Ref.22 Ref.32 Ref.38
Cross-link418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14

Natural variations

Alternative sequence1 – 295295Missing in isoform 5.
VSP_019235
Alternative sequence1 – 55MNPRQ → MMSPICDQTIDSRLKVEKAT WWGRVGGGSRPHWQPPGVRP CPEEVQDP in isoform 4.
VSP_008872
Alternative sequence694 – 71219Missing in isoform 3.
VSP_008873
Alternative sequence807 – 83226Missing in isoform 2 and isoform 3.
VSP_008874
Natural variant1001R → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.8
Corresponds to variant rs1466731 [ dbSNP | Ensembl ].
VAR_048725
Natural variant1931P → A in AGS6. Ref.50
VAR_069535
Natural variant3841K → R. Ref.2 Ref.3 Ref.4 Ref.5
Corresponds to variant rs2229857 [ dbSNP | Ensembl ].
VAR_017240
Natural variant5871Y → C.
Corresponds to variant rs17843865 [ dbSNP | Ensembl ].
VAR_024407
Natural variant8061E → V in a breast cancer sample; somatic mutation. Ref.49
VAR_035805
Natural variant8701A → T in AGS6. Ref.50
VAR_069536
Natural variant8721I → T in AGS6. Ref.50
VAR_069537
Natural variant8921R → H in AGS6. Ref.50
VAR_069538
Natural variant9231L → P in DSH. Ref.46
Corresponds to variant rs28936680 [ dbSNP | Ensembl ].
VAR_017604
Natural variant9661C → F in DSH. Ref.47
VAR_021729
Natural variant9991K → N in AGS6. Ref.50
VAR_069539
Natural variant10071G → R in AGS6. Ref.50
VAR_069540
Natural variant11121Y → F in AGS6. Ref.50
VAR_069541
Natural variant11131D → H in AGS6. Ref.50
VAR_069542
Natural variant11551R → W in DSH. Ref.48
VAR_026669
Natural variant11651F → S in DSH. Ref.46
Corresponds to variant rs28936681 [ dbSNP | Ensembl ].
VAR_017605

Experimental info

Mutagenesis4181K → R: Abolishes sumoylation. Ref.14
Sequence conflict531E → G in CAA55968. Ref.4
Sequence conflict2451F → L in CAE45853. Ref.5
Sequence conflict4821F → L in CAE45853. Ref.5
Sequence conflict8731I → V in CAE45853. Ref.5
Sequence conflict10931D → G in CAE45853. Ref.5
Sequence conflict11841E → K in CAA55967. Ref.4
Sequence conflict11841E → K in CAA55968. Ref.4
Sequence conflict11841E → K in CAA67169. Ref.4
Sequence conflict11841E → K in CAA67170. Ref.4
Isoform 4:
Sequence conflict131R → G in CAE45853. Ref.5

Secondary structure

............................... 1226
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ADAR-a) (ADAR1L) (p150) [UniParc].

Last modified November 30, 2010. Version 4.
Checksum: 9CE095D6F9C1BC79

FASTA1,226136,066
        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 

« Hide

Isoform 2 (ADAR-b) [UniParc].

Checksum: 4CB1B306DAC584FC
Show »

FASTA1,200133,274
Isoform 3 (ADAR-c) [UniParc].

Checksum: 9764C8AB27BE118E
Show »

FASTA1,181131,170
Isoform 4 [UniParc].

Checksum: BB9B1DF19B8D3BC8
Show »

FASTA1,269140,838
Isoform 5 (ADAR1S) (p110) [UniParc].

Checksum: 113B63CF165097FC
Show »

FASTA931103,642

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"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.
[31]"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.
[32]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"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].
[34]"RNA editing catalyzed by ADAR1 and its function in mammalian cells."
Wang Q.
Biochemistry (Mosc.) 76:900-911(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[35]"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.
[36]"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.
[37]"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.
[38]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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.
[49]"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. expand/collapse author list , 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.
[50]"Mutations in ADAR1 cause Aicardi-Goutieres syndrome associated with a type I interferon signature."
Rice G.I., Kasher P.R., Forte G.M., Mannion N.M., Greenwood S.M., Szynkiewicz M., Dickerson J.E., Bhaskar S.S., Zampini M., Briggs T.A., Jenkinson E.M., Bacino C.A., Battini R., Bertini E., Brogan P.A., Brueton L.A., Carpanelli M., De Laet C. expand/collapse author list , de Lonlay P., del Toro M., Desguerre I., Fazzi E., Garcia-Cazorla A., Heiberg A., Kawaguchi M., Kumar R., Lin J.P., Lourenco C.M., Male A.M., Marques W. Jr., Mignot C., Olivieri I., Orcesi S., Prabhakar P., Rasmussen M., Robinson R.A., Rozenberg F., Schmidt J.L., Steindl K., Tan T.Y., van der Merwe W.G., Vanderver A., Vassallo G., Wakeling E.L., Wassmer E., Whittaker E., Livingston J.H., Lebon P., Suzuki T., McLaughlin P.J., Keegan L.P., O'Connell M.A., Lovell S.C., Crow Y.J.
Nat. Genet. 44:1243-1248(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AGS6 ALA-193; THR-870; THR-872; HIS-892; ASN-999; ARG-1007; PHE-1112 AND HIS-1113.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10439 mRNA. Translation: AAB06697.1.
U75503 expand/collapse EMBL AC list , U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97116.1.
U75503 expand/collapse EMBL AC list , U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97117.1.
U75503 expand/collapse EMBL AC list , 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.
PIRS65593.
RefSeqNP_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.
UniGeneHs.12341.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QBJX-ray2.10A/B/C133-209[»]
1QGPNMR-A126-200[»]
1XMKX-ray0.97A294-366[»]
2ACJX-ray2.60A/B/C/D140-202[»]
2GXBX-ray2.25A/B140-202[»]
2L54NMR-A136-198[»]
3F21X-ray2.20A/B/C133-209[»]
3F22X-ray2.50A/B/C133-209[»]
3F23X-ray2.70A/B/C133-209[»]
3IRQX-ray2.80A/B/C/D140-202[»]
3IRRX-ray2.65A/B/C/D140-202[»]
ProteinModelPortalP55265.
SMRP55265. Positions 134-199, 294-366, 501-797, 829-1224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106617. 25 interactions.
DIPDIP-29310N.
IntActP55265. 13 interactions.
MINTMINT-4531596.
STRING9606.ENSP00000357459.

PTM databases

PhosphoSiteP55265.

Polymorphism databases

DMDM313104303.

Proteomic databases

PaxDbP55265.
PRIDEP55265.

Protocols and materials databases

DNASU103.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368471; ENSP00000357456; ENSG00000160710. [P55265-5]
ENST00000368474; ENSP00000357459; ENSG00000160710. [P55265-1]
GeneID103.
KEGGhsa:103.
UCSCuc001ffh.3. human. [P55265-1]
uc001ffi.3. human. [P55265-2]
uc001ffj.3. human. [P55265-3]

Organism-specific databases

CTD103.
GeneCardsGC01M154554.
HGNCHGNC:225. ADAR.
HPACAB056157.
HPA003890.
MIM127400. phenotype.
146920. gene.
615010. phenotype.
neXtProtNX_P55265.
Orphanet51. Aicardi-Goutieres syndrome.
41. Dyschromatosis symmetrica hereditaria.
PharmGKBPA24555.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292433.
HOVERGENHBG067087.
KOK12968.
OrthoDBEOG7VHSX4.
PhylomeDBP55265.
TreeFamTF315806.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP55265.
BgeeP55265.
CleanExHS_ADAR.
GenevestigatorP55265.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
3.30.160.20. 3 hits.
InterProIPR002466. A_deamin.
IPR014720. dsRNA-bd_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view]
PROSITEPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADAR. human.
EvolutionaryTraceP55265.
GeneWikiADAR.
GenomeRNAi103.
NextBio389.
PMAP-CutDBP55265.
PROP55265.
SOURCESearch...

Entry information

Entry nameDSRAD_HUMAN
AccessionPrimary (citable) accession number: P55265
Secondary accession number(s): B1AQQ9 expand/collapse secondary AC list , 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: April 16, 2014
This is version 156 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM