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Q9NS39

- RED2_HUMAN

UniProt

Q9NS39 - RED2_HUMAN

Protein

Double-stranded RNA-specific editase B2

Gene

ADARB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Lacks editing activity. It prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. Capable of binding to dsRNA but also to ssRNA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi432 – 4321ZincPROSITE-ProRule annotation
    Active sitei434 – 4341Proton donorPROSITE-ProRule annotation
    Metal bindingi490 – 4901ZincPROSITE-ProRule annotation
    Metal bindingi555 – 5551ZincPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Double-stranded RNA-specific editase B2 (EC:3.5.-.-)
    Alternative name(s):
    RNA-dependent adenosine deaminase 3
    RNA-editing deaminase 2
    RNA-editing enzyme 2
    dsRNA adenosine deaminase B2
    Gene namesi
    Name:ADARB2
    Synonyms:ADAR3, RED2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:227. ADARB2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24557.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 739739Double-stranded RNA-specific editase B2PRO_0000171782Add
    BLAST

    Proteomic databases

    PaxDbiQ9NS39.
    PRIDEiQ9NS39.

    2D gel databases

    SWISS-2DPAGEQ9NS39.

    PTM databases

    PhosphoSiteiQ9NS39.

    Expressioni

    Tissue specificityi

    Brain specific. Expressed at higher levels in astrocytomas as compared to the normal brain tissue.2 Publications

    Gene expression databases

    ArrayExpressiQ9NS39.
    BgeeiQ9NS39.
    CleanExiHS_ADARB2.
    GenevestigatoriQ9NS39.

    Organism-specific databases

    HPAiHPA031332.
    HPA031333.

    Interactioni

    Protein-protein interaction databases

    BioGridi106619. 6 interactions.
    IntActiQ9NS39. 1 interaction.
    MINTiMINT-4728108.
    STRINGi9606.ENSP00000370713.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NS39.
    SMRiQ9NS39. Positions 124-341, 349-738.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 19167DRBM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini274 – 34168DRBM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini408 – 735328A to I editasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 3513R-domain (ssRNA-binding)Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG292433.
    HOGENOMiHOG000290164.
    HOVERGENiHBG003836.
    InParanoidiQ9NS39.
    KOiK13194.
    OMAiLFKEFEP.
    OrthoDBiEOG7VHSX4.
    PhylomeDBiQ9NS39.
    TreeFamiTF315806.

    Family and domain databases

    Gene3Di3.30.160.20. 2 hits.
    InterProiIPR002466. A_deamin.
    IPR014720. dsRNA-bd_dom.
    [Graphical view]
    PfamiPF02137. A_deamin. 1 hit.
    PF00035. dsrm. 2 hits.
    [Graphical view]
    SMARTiSM00552. ADEAMc. 1 hit.
    SM00358. DSRM. 2 hits.
    [Graphical view]
    PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
    PS50137. DS_RBD. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NS39-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVLGSGRG SGGLSSQLKC KSKRRRRRRS KRKDKVSILS TFLAPFKHLS    50
    PGITNTEDDD TLSTSSAEVK ENRNVGNLAA RPPPSGDRAR GGAPGAKRKR 100
    PLEEGNGGHL CKLQLVWKKL SWSVAPKNAL VQLHELRPGL QYRTVSQTGP 150
    VHAPVFAVAV EVNGLTFEGT GPTKKKAKMR AAELALRSFV QFPNACQAHL 200
    AMGGGPGPGT DFTSDQADFP DTLFQEFEPP APRPGLAGGR PGDAALLSAA 250
    YGRRRLLCRA LDLVGPTPAT PAAPGERNPV VLLNRLRAGL RYVCLAEPAE 300
    RRARSFVMAV SVDGRTFEGS GRSKKLARGQ AAQAALQELF DIQMPGHAPG 350
    RARRTPMPQE FADSISQLVT QKFREVTTDL TPMHARHKAL AGIVMTKGLD 400
    ARQAQVVALS SGTKCISGEH LSDQGLVVND CHAEVVARRA FLHFLYTQLE 450
    LHLSKRREDS ERSIFVRLKE GGYRLRENIL FHLYVSTSPC GDARLHSPYE 500
    ITTDLHSSKH LVRKFRGHLR TKIESGEGTV PVRGPSAVQT WDGVLLGEQL 550
    ITMSCTDKIA RWNVLGLQGA LLSHFVEPVY LQSIVVGSLH HTGHLARVMS 600
    HRMEGVGQLP ASYRHNRPLL SGVSDAEARQ PGKSPPFSMN WVVGSADLEI 650
    INATTGRRSC GGPSRLCKHV LSARWARLYG RLSTRTPSPG DTPSMYCEAK 700
    LGAHTYQSVK QQLFKAFQKA GLGTWVRKPP EQQQFLLTL 739
    Length:739
    Mass (Da):80,621
    Last modified:October 1, 2000 - v1
    Checksum:iA158A81D35894F79
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441A → T.
    Corresponds to variant rs3793733 [ dbSNP | Ensembl ].
    VAR_020438
    Natural varianti210 – 2101T → M in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035806
    Natural varianti512 – 5121V → I in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035807
    Natural varianti626 – 6261A → T.1 Publication
    Corresponds to variant rs2271275 [ dbSNP | Ensembl ].
    VAR_048726

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034837 mRNA. Translation: AAF78094.1.
    AL513304, AC026224, AL392083 Genomic DNA. Translation: CAH73405.1.
    AL392083, AC026224, AL513304 Genomic DNA. Translation: CAH72171.1.
    BC137477 mRNA. Translation: AAI37478.1.
    BC140852 mRNA. Translation: AAI40853.1.
    CCDSiCCDS7058.1.
    RefSeqiNP_061172.1. NM_018702.3.
    UniGeneiHs.586663.

    Genome annotation databases

    EnsembliENST00000381312; ENSP00000370713; ENSG00000185736.
    GeneIDi105.
    KEGGihsa:105.
    UCSCiuc009xhq.3. human.

    Polymorphism databases

    DMDMi33112436.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034837 mRNA. Translation: AAF78094.1 .
    AL513304 , AC026224 , AL392083 Genomic DNA. Translation: CAH73405.1 .
    AL392083 , AC026224 , AL513304 Genomic DNA. Translation: CAH72171.1 .
    BC137477 mRNA. Translation: AAI37478.1 .
    BC140852 mRNA. Translation: AAI40853.1 .
    CCDSi CCDS7058.1.
    RefSeqi NP_061172.1. NM_018702.3.
    UniGenei Hs.586663.

    3D structure databases

    ProteinModelPortali Q9NS39.
    SMRi Q9NS39. Positions 124-341, 349-738.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106619. 6 interactions.
    IntActi Q9NS39. 1 interaction.
    MINTi MINT-4728108.
    STRINGi 9606.ENSP00000370713.

    PTM databases

    PhosphoSitei Q9NS39.

    Polymorphism databases

    DMDMi 33112436.

    2D gel databases

    SWISS-2DPAGE Q9NS39.

    Proteomic databases

    PaxDbi Q9NS39.
    PRIDEi Q9NS39.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381312 ; ENSP00000370713 ; ENSG00000185736 .
    GeneIDi 105.
    KEGGi hsa:105.
    UCSCi uc009xhq.3. human.

    Organism-specific databases

    CTDi 105.
    GeneCardsi GC10M001219.
    HGNCi HGNC:227. ADARB2.
    HPAi HPA031332.
    HPA031333.
    MIMi 602065. gene.
    neXtProti NX_Q9NS39.
    PharmGKBi PA24557.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292433.
    HOGENOMi HOG000290164.
    HOVERGENi HBG003836.
    InParanoidi Q9NS39.
    KOi K13194.
    OMAi LFKEFEP.
    OrthoDBi EOG7VHSX4.
    PhylomeDBi Q9NS39.
    TreeFami TF315806.

    Miscellaneous databases

    ChiTaRSi ADARB2. human.
    GeneWikii ADARB2.
    GenomeRNAii 105.
    NextBioi 409.
    PROi Q9NS39.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NS39.
    Bgeei Q9NS39.
    CleanExi HS_ADARB2.
    Genevestigatori Q9NS39.

    Family and domain databases

    Gene3Di 3.30.160.20. 2 hits.
    InterProi IPR002466. A_deamin.
    IPR014720. dsRNA-bd_dom.
    [Graphical view ]
    Pfami PF02137. A_deamin. 1 hit.
    PF00035. dsrm. 2 hits.
    [Graphical view ]
    SMARTi SM00552. ADEAMc. 1 hit.
    SM00358. DSRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50141. A_DEAMIN_EDITASE. 1 hit.
    PS50137. DS_RBD. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains."
      Chen C.-X., Cho D.S., Wang Q., Lai F., Carter K.C., Nishikura K.
      RNA 6:755-767(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, REGION R-DOMAIN, RNA-BINDING, TISSUE SPECIFICITY.
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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], VARIANT THR-626.
    4. "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: TISSUE SPECIFICITY.
    5. "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.
    6. Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-210 AND ILE-512.

    Entry informationi

    Entry nameiRED2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NS39
    Secondary accession number(s): B2RPJ5, Q5VUT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3