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P55265

- DSRAD_HUMAN

UniProt

P55265 - DSRAD_HUMAN

Protein

Double-stranded RNA-specific adenosine deaminase

Gene

ADAR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 4 (30 Nov 2010)
      Previous versions | rss
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    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. 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.10 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi910 – 9101ZincPROSITE-ProRule annotation
    Active sitei912 – 9121Proton donorPROSITE-ProRule annotation
    Metal bindingi966 – 9661ZincPROSITE-ProRule annotation
    Metal bindingi1036 – 10361ZincPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi169 – 19527Add
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. double-stranded RNA adenosine deaminase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. adenosine to inosine editing Source: UniProtKB
    2. base conversion or substitution editing Source: MGI
    3. cytokine-mediated signaling pathway Source: Reactome
    4. defense response to virus Source: UniProtKB-KW
    5. gene expression Source: Reactome
    6. gene silencing by RNA Source: UniProtKB-KW
    7. innate immune response Source: UniProtKB
    8. mRNA modification Source: Reactome
    9. mRNA processing Source: UniProtKB-KW
    10. negative regulation of apoptotic process Source: Ensembl
    11. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
    12. positive regulation of viral genome replication Source: UniProtKB
    13. protein export from nucleus Source: UniProtKB
    14. protein import into nucleus Source: UniProtKB
    15. response to interferon-alpha Source: UniProtKB
    16. response to virus Source: UniProtKB
    17. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

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

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_1231. C6 deamination of adenosine.
    REACT_1966. Formation of editosomes by ADAR proteins.
    REACT_25162. Interferon alpha/beta signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Double-stranded RNA-specific adenosine deaminase (EC:3.5.4.37)
    Short name:
    DRADA
    Alternative name(s):
    136 kDa double-stranded RNA-binding protein
    Short name:
    p136
    Interferon-inducible protein 4
    Short name:
    IFI-4
    K88DSRBP
    Gene namesi
    Name:ADAR
    Synonyms:ADAR1, DSRAD, G1P1, IFI4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:225. ADAR.

    Subcellular locationi

    Isoform 1 : Cytoplasm. Nucleus
    Note: Shuttles between the cytoplasm and nucleus.
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. membrane Source: UniProtKB
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. supraspliceosomal complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti923 – 9231L → P in DSH. 1 Publication
    Corresponds to variant rs28936680 [ dbSNP | Ensembl ].
    VAR_017604
    Natural varianti966 – 9661C → F in DSH. 1 Publication
    VAR_021729
    Natural varianti1155 – 11551R → W in DSH. 1 Publication
    VAR_026669
    Natural varianti1165 – 11651F → S in DSH. 1 Publication
    Corresponds to variant rs28936681 [ dbSNP | Ensembl ].
    VAR_017605
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931P → A in AGS6. 1 Publication
    VAR_069535
    Natural varianti870 – 8701A → T in AGS6. 1 Publication
    VAR_069536
    Natural varianti872 – 8721I → T in AGS6. 1 Publication
    VAR_069537
    Natural varianti892 – 8921R → H in AGS6. 1 Publication
    VAR_069538
    Natural varianti999 – 9991K → N in AGS6. 1 Publication
    VAR_069539
    Natural varianti1007 – 10071G → R in AGS6. 1 Publication
    VAR_069540
    Natural varianti1112 – 11121Y → F in AGS6. 1 Publication
    VAR_069541
    Natural varianti1113 – 11131D → H in AGS6. 1 Publication
    VAR_069542

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi418 – 4181K → R: Abolishes sumoylation. 1 Publication

    Keywords - Diseasei

    Aicardi-Goutieres syndrome, Disease mutation

    Organism-specific databases

    MIMi127400. phenotype.
    615010. phenotype.
    Orphaneti51. Aicardi-Goutieres syndrome.
    41. Dyschromatosis symmetrica hereditaria.
    225154. Familial infantile bilateral striatal necrosis.
    PharmGKBiPA24555.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12261226Double-stranded RNA-specific adenosine deaminasePRO_0000171774Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki418 – 418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei601 – 6011Phosphothreonine2 Publications
    Modified residuei614 – 6141Phosphoserine1 Publication
    Modified residuei808 – 8081Phosphothreonine5 Publications
    Modified residuei823 – 8231Phosphoserine1 Publication
    Modified residuei825 – 8251Phosphoserine3 Publications

    Post-translational modificationi

    Sumoylation reduces RNA-editing activity.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP55265.
    PaxDbiP55265.
    PRIDEiP55265.

    PTM databases

    PhosphoSiteiP55265.

    Miscellaneous databases

    PMAP-CutDBP55265.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Inductioni

    Isoform 1 is induced by interferon alpha. Isoform 5 is constitutively expressed.1 Publication

    Gene expression databases

    ArrayExpressiP55265.
    BgeeiP55265.
    CleanExiHS_ADAR.
    GenevestigatoriP55265.

    Organism-specific databases

    HPAiCAB056157.
    HPA003890.

    Interactioni

    Subunit structurei

    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 UPF1.8 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi106617. 34 interactions.
    DIPiDIP-29310N.
    IntActiP55265. 13 interactions.
    MINTiMINT-4531596.
    STRINGi9606.ENSP00000357459.

    Structurei

    Secondary structure

    1
    1226
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi127 – 1304
    Helixi135 – 15016
    Beta strandi152 – 1543
    Helixi158 – 1658
    Helixi169 – 18113
    Beta strandi184 – 1929
    Beta strandi194 – 1974
    Helixi294 – 30916
    Helixi315 – 3228
    Helixi324 – 3263
    Helixi327 – 33913
    Beta strandi342 – 3465
    Beta strandi348 – 3503
    Beta strandi352 – 3554
    Helixi357 – 3604
    Turni361 – 3633
    Helixi716 – 7249
    Helixi727 – 73812
    Beta strandi742 – 7498
    Beta strandi758 – 7647
    Beta strandi767 – 77610
    Helixi777 – 79620

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QBJX-ray2.10A/B/C133-209[»]
    1QGPNMR-A125-200[»]
    1XMKX-ray0.97A294-366[»]
    2ACJX-ray2.60A/B/C/D140-202[»]
    2GXBX-ray2.25A/B140-202[»]
    2L54NMR-A136-198[»]
    2MDRNMR-A708-801[»]
    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[»]
    ProteinModelPortaliP55265.
    SMRiP55265. Positions 134-199, 294-366, 511-575, 612-681, 731-797.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55265.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati133 – 20270DRADA 1Add
    BLAST
    Repeati293 – 36068DRADA 2Add
    BLAST
    Domaini503 – 57169DRBM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini614 – 68269DRBM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini726 – 79469DRBM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini886 – 1221336A 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

    eggNOGiNOG292433.
    HOVERGENiHBG067087.
    KOiK12968.
    OrthoDBiEOG7VHSX4.
    PhylomeDBiP55265.
    TreeFamiTF315806.

    Family and domain databases

    Gene3Di1.10.10.10. 2 hits.
    3.30.160.20. 3 hits.
    InterProiIPR002466. A_deamin.
    IPR014720. dsRNA-bd_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]
    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 promoter usage and alternative splicing. Align

    Isoform 1 (identifier: P55265-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ     50
    LPEAPVIGKQ TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR 100
    SQGLQRGFQH PSPRGRSLPQ RGVDCLSSHF QELSIYQDQE QRILKFLEEL 150
    GEGKATTAHD LSGKLGTPKK EINRVLYSLA KKGKLQKEAG TPPLWKIAVS 200
    TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED LLEPFIAVSA 250
    QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK 300
    EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP 350
    PIWHLTDKKR ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS 400
    NNMVTTEKVE NGQEPVIKLE NRQEARPEPA RLKPPVHYNG PSKAGYVDFE 450
    NGQWATDDIP DDLNSIRAAP GEFRAIMEMP SFYSHGLPRC SPYKKLTECQ 500
    LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV INGREFPPAE 550
    AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ 600
    TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV 650
    AVGAQTFPSV SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQPEGMISE 700
    SLDNLESMMP NKVRKIGELV RYLNTNPVGG LLEYARSHGF AAEFKLVDQS 750
    GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG KQEAADAALR VLIGENEKAE 800
    RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF HDQIAMLSHR 850
    CFNTLTNSFQ PSLLGRKILA AIIMKKDSED MGVVVSLGTG NRCVKGDSLS 900
    LKGETVNDCH AEIISRRGFI RFLYSELMKY NSQTAKDSIF EPAKGGEKLQ 950
    IKKTVSFHLY ISTAPCGDGA LFDKSCSDRA MESTESRHYP VFENPKQGKL 1000
    RTKVENGEGT IPVESSDIVP TWDGIRLGER LRTMSCSDKI LRWNVLGLQG 1050
    ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI CCRVTRDGSA FEDGLRHPFI 1100
    VNHPKVGRVS IYDSKRQSGK TKETSVNWCL ADGYDLEILD GTRGTVDGPR 1150
    NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK 1200
    KGLKDMGYGN WISKPQEEKN FYLCPV 1226

    Note: Produced by alternative promoter usage.

    Length:1,226
    Mass (Da):136,066
    Last modified:November 30, 2010 - v4
    Checksum:i9CE095D6F9C1BC79
    GO
    Isoform 2 (identifier: P55265-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,200
    Mass (Da):133,274
    Checksum:i4CB1B306DAC584FC
    GO
    Isoform 3 (identifier: P55265-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,181
    Mass (Da):131,170
    Checksum:i9764C8AB27BE118E
    GO
    Isoform 4 (identifier: P55265-4) [UniParc]FASTAAdd to Basket

    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.Curated

    Show »
    Length:1,269
    Mass (Da):140,838
    Checksum:iBB9B1DF19B8D3BC8
    GO
    Isoform 5 (identifier: P55265-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:931
    Mass (Da):103,642
    Checksum:i113B63CF165097FC
    GO

    Sequence cautioni

    The sequence CAE45853.1 differs from that shown. Reason: Erroneous termination at position 1227. Translated as stop.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531E → G in CAA55968. 1 PublicationCurated
    Sequence conflicti245 – 2451F → L in CAE45853. (PubMed:17974005)Curated
    Sequence conflicti482 – 4821F → L in CAE45853. (PubMed:17974005)Curated
    Sequence conflicti873 – 8731I → V in CAE45853. (PubMed:17974005)Curated
    Sequence conflicti1093 – 10931D → G in CAE45853. (PubMed:17974005)Curated
    Sequence conflicti1184 – 11841E → K in CAA55967. 1 PublicationCurated
    Sequence conflicti1184 – 11841E → K in CAA55968. 1 PublicationCurated
    Sequence conflicti1184 – 11841E → K in CAA67169. 1 PublicationCurated
    Sequence conflicti1184 – 11841E → K in CAA67170. 1 PublicationCurated
    Isoform 4 (identifier: P55265-4)
    Sequence conflicti13 – 131R → G in CAE45853. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001R → G.6 Publications
    Corresponds to variant rs1466731 [ dbSNP | Ensembl ].
    VAR_048725
    Natural varianti193 – 1931P → A in AGS6. 1 Publication
    VAR_069535
    Natural varianti384 – 3841K → R.4 Publications
    Corresponds to variant rs2229857 [ dbSNP | Ensembl ].
    VAR_017240
    Natural varianti587 – 5871Y → C.
    Corresponds to variant rs17843865 [ dbSNP | Ensembl ].
    VAR_024407
    Natural varianti806 – 8061E → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035805
    Natural varianti870 – 8701A → T in AGS6. 1 Publication
    VAR_069536
    Natural varianti872 – 8721I → T in AGS6. 1 Publication
    VAR_069537
    Natural varianti892 – 8921R → H in AGS6. 1 Publication
    VAR_069538
    Natural varianti923 – 9231L → P in DSH. 1 Publication
    Corresponds to variant rs28936680 [ dbSNP | Ensembl ].
    VAR_017604
    Natural varianti966 – 9661C → F in DSH. 1 Publication
    VAR_021729
    Natural varianti999 – 9991K → N in AGS6. 1 Publication
    VAR_069539
    Natural varianti1007 – 10071G → R in AGS6. 1 Publication
    VAR_069540
    Natural varianti1112 – 11121Y → F in AGS6. 1 Publication
    VAR_069541
    Natural varianti1113 – 11131D → H in AGS6. 1 Publication
    VAR_069542
    Natural varianti1155 – 11551R → W in DSH. 1 Publication
    VAR_026669
    Natural varianti1165 – 11651F → S in DSH. 1 Publication
    Corresponds to variant rs28936681 [ dbSNP | Ensembl ].
    VAR_017605

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 295295Missing in isoform 5. 1 PublicationVSP_019235Add
    BLAST
    Alternative sequencei1 – 55MNPRQ → MMSPICDQTIDSRLKVEKAT WWGRVGGGSRPHWQPPGVRP CPEEVQDP in isoform 4. 1 PublicationVSP_008872
    Alternative sequencei694 – 71219Missing in isoform 3. CuratedVSP_008873Add
    BLAST
    Alternative sequencei807 – 83226Missing in isoform 2 and isoform 3. CuratedVSP_008874Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1071.1. [P55265-1]
    CCDS30879.1. [P55265-5]
    PIRiS65593.
    RefSeqiNP_001020278.1. NM_001025107.2. [P55265-5]
    NP_001102.2. NM_001111.4.
    NP_001180424.1. NM_001193495.1. [P55265-5]
    NP_056655.2. NM_015840.3.
    NP_056656.2. NM_015841.3.
    XP_006711174.1. XM_006711111.1. [P55265-5]
    XP_006711175.1. XM_006711112.1. [P55265-5]
    XP_006711176.1. XM_006711113.1. [P55265-5]
    UniGeneiHs.12341.

    Genome annotation databases

    EnsembliENST00000368471; ENSP00000357456; ENSG00000160710. [P55265-5]
    ENST00000368474; ENSP00000357459; ENSG00000160710. [P55265-1]
    GeneIDi103.
    KEGGihsa:103.
    UCSCiuc001ffh.3. human. [P55265-1]
    uc001ffi.3. human. [P55265-2]
    uc001ffj.3. human. [P55265-3]

    Polymorphism databases

    DMDMi313104303.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1071.1. [P55265-1 ]
    CCDS30879.1. [P55265-5 ]
    PIRi S65593.
    RefSeqi NP_001020278.1. NM_001025107.2. [P55265-5 ]
    NP_001102.2. NM_001111.4.
    NP_001180424.1. NM_001193495.1. [P55265-5 ]
    NP_056655.2. NM_015840.3.
    NP_056656.2. NM_015841.3.
    XP_006711174.1. XM_006711111.1. [P55265-5 ]
    XP_006711175.1. XM_006711112.1. [P55265-5 ]
    XP_006711176.1. XM_006711113.1. [P55265-5 ]
    UniGenei Hs.12341.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QBJ X-ray 2.10 A/B/C 133-209 [» ]
    1QGP NMR - A 125-200 [» ]
    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 [» ]
    2MDR NMR - A 708-801 [» ]
    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 [» ]
    ProteinModelPortali P55265.
    SMRi P55265. Positions 134-199, 294-366, 511-575, 612-681, 731-797.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106617. 34 interactions.
    DIPi DIP-29310N.
    IntActi P55265. 13 interactions.
    MINTi MINT-4531596.
    STRINGi 9606.ENSP00000357459.

    PTM databases

    PhosphoSitei P55265.

    Polymorphism databases

    DMDMi 313104303.

    Proteomic databases

    MaxQBi P55265.
    PaxDbi P55265.
    PRIDEi P55265.

    Protocols and materials databases

    DNASUi 103.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368471 ; ENSP00000357456 ; ENSG00000160710 . [P55265-5 ]
    ENST00000368474 ; ENSP00000357459 ; ENSG00000160710 . [P55265-1 ]
    GeneIDi 103.
    KEGGi hsa:103.
    UCSCi uc001ffh.3. human. [P55265-1 ]
    uc001ffi.3. human. [P55265-2 ]
    uc001ffj.3. human. [P55265-3 ]

    Organism-specific databases

    CTDi 103.
    GeneCardsi GC01M154554.
    HGNCi HGNC:225. ADAR.
    HPAi CAB056157.
    HPA003890.
    MIMi 127400. phenotype.
    146920. gene.
    615010. phenotype.
    neXtProti NX_P55265.
    Orphaneti 51. Aicardi-Goutieres syndrome.
    41. Dyschromatosis symmetrica hereditaria.
    225154. Familial infantile bilateral striatal necrosis.
    PharmGKBi PA24555.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292433.
    HOVERGENi HBG067087.
    KOi K12968.
    OrthoDBi EOG7VHSX4.
    PhylomeDBi P55265.
    TreeFami TF315806.

    Enzyme and pathway databases

    Reactomei REACT_1231. C6 deamination of adenosine.
    REACT_1966. Formation of editosomes by ADAR proteins.
    REACT_25162. Interferon alpha/beta signaling.

    Miscellaneous databases

    ChiTaRSi ADAR. human.
    EvolutionaryTracei P55265.
    GeneWikii ADAR.
    GenomeRNAii 103.
    NextBioi 389.
    PMAP-CutDB P55265.
    PROi P55265.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55265.
    Bgeei P55265.
    CleanExi HS_ADAR.
    Genevestigatori P55265.

    Family and domain databases

    Gene3Di 1.10.10.10. 2 hits.
    3.30.160.20. 3 hits.
    InterProi IPR002466. A_deamin.
    IPR014720. dsRNA-bd_dom.
    IPR000607. dsRNA_A_deaminase.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF02137. A_deamin. 1 hit.
    PF00035. dsrm. 3 hits.
    PF02295. z-alpha. 2 hits.
    [Graphical view ]
    SMARTi SM00552. ADEAMc. 1 hit.
    SM00358. DSRM. 3 hits.
    SM00550. Zalpha. 2 hits.
    [Graphical view ]
    PROSITEi PS50141. A_DEAMIN_EDITASE. 1 hit.
    PS50139. DRADA_REPEAT. 2 hits.
    PS50137. DS_RBD. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. 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. 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiDSRAD_HUMAN
    AccessioniPrimary (citable) accession number: P55265
    Secondary accession number(s): B1AQQ9
    , B1AQR0, D3DV76, O15223, O43859, O43860, Q9BYM3, Q9BYM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 161 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3