Double-stranded RNA-specific editase 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• adenosine in double-stranded RNA

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  + H⁺

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  + H₂O

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  = inosine in double-stranded RNA

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  + NH₄⁺

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  EC:3.5.4.37
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  Source: Rhea

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  adenosine in double-stranded RNA

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  AMP residue

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  +

  H⁺

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  +

  H₂O

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  =

  inosine in double-stranded RNA

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  IMP residue

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  +

  NH₄⁺

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  zoom

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• double-stranded RNA adenosine deaminase activity Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Structure and sequence determinants required for the RNA editing of ADAR2 substrates."
    Dawson T.R., Sansam C.L., Emeson R.B.
    J Biol Chem 279:4941-4951(2004) [PubMed] [Europe PMC] [Abstract]
  • Ref.1

    "A mammalian RNA editing enzyme."
    Melcher T., Maas S., Herb A., Sprengel R., Seeburg P.H., Higuchi M.
    Nature 379:460-464(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• double-stranded RNA binding Source: RGDInferred from direct assayⁱ
  • Ref.3

    "Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs."
    Stefl R., Xu M., Skrisovska L., Emeson R.B., Allain F.H.
    Structure 14:345-355(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: STRUCTURE BY NMR OF 74-301, FUNCTION, MUTAGENESIS OF LYS-128 AND LYS-281, RNA-BINDING.
• identical protein binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Dimerization of ADAR2 is mediated by the double-stranded RNA binding domain."
    Poulsen H., Jorgensen R., Heding A., Nielsen F.C., Bonven B., Egebjerg J.
    RNA 12:1350-1360(2006) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• RNA binding Source: RGDInferred from direct assayⁱ
  • "In vitro analysis of the binding of ADAR2 to the pre-mRNA encoding the GluR-B R/G site."
    Ohman M., Kallman A.M., Bass B.L.
    RNA 6:687-697(2000) [PubMed] [Europe PMC] [Abstract]
• tRNA-specific adenosine deaminase activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• adenosine to inosine editing Source: RGDInferred from direct assayⁱ
  • Ref.1

    "A mammalian RNA editing enzyme."
    Melcher T., Maas S., Herb A., Sprengel R., Seeburg P.H., Higuchi M.
    Nature 379:460-464(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• base conversion or substitution editing Source: RGDInferred from direct assayⁱ
  • "In vitro analysis of the binding of ADAR2 to the pre-mRNA encoding the GluR-B R/G site."
    Ohman M., Kallman A.M., Bass B.L.
    RNA 6:687-697(2000) [PubMed] [Europe PMC] [Abstract]
• brain development Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Developmental changes in expression and self-editing of adenosine deaminase type 2 pre-mRNA and mRNA in rat brain and cultured cortical neurons."
    Hang P.N., Tohda M., Matsumoto K.
    Neurosci Res 61:398-403(2008) [PubMed] [Europe PMC] [Abstract]
• facial nerve morphogenesis Source: RGD
• hypoglossal nerve morphogenesis Source: RGD
• innervation Source: RGD
• motor behavior Source: RGD
• motor neuron apoptotic process Source: RGD
• mRNA modification Source: RGDInferred from direct assayⁱ
  • "Structure and sequence determinants required for the RNA editing of ADAR2 substrates."
    Dawson T.R., Sansam C.L., Emeson R.B.
    J Biol Chem 279:4941-4951(2004) [PubMed] [Europe PMC] [Abstract]
• mRNA processing Source: UniProtKB-KW
• multicellular organism growth Source: RGD
• muscle tissue morphogenesis Source: RGD
• negative regulation of cell migration Source: UniProtKB
• negative regulation of cell population proliferation Source: UniProtKB
• negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
• neuromuscular process controlling posture Source: RGD
• neuromuscular synaptic transmission Source: RGD
• positive regulation of mRNA processing Source: RGDInferred from direct assayⁱ
  • "Regulation of alternative splicing by RNA editing."
    Rueter S.M., Dawson T.R., Emeson R.B.
    Nature 399:75-80(1999) [PubMed] [Europe PMC] [Abstract]
• positive regulation of viral genome replication Source: UniProtKB
• regulation of cell cycle Source: UniProtKB
• RNA processing Source: HGNC-UCL <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes."
    Keegan L.P., Leroy A., Sproul D., O'Connell M.A.
    Genome Biol 5:209-209(2004) [PubMed] [Europe PMC] [Abstract]
• spinal cord ventral commissure morphogenesis Source: RGD

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• identical protein binding Source: RGDInferred from physical interactionⁱ
  • "Dimerization of ADAR2 is mediated by the double-stranded RNA binding domain."
    Poulsen H., Jorgensen R., Heding A., Nielsen F.C., Bonven B., Egebjerg J.
    RNA 12:1350-1360(2006) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MDIEDEENMS SSSIDVKENR NLDNMPPKDS STPGPGEGIP LSNGGGGSTS 
        60         70         80         90        100
RKRPLEEGSN GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYMLLSQ 
       110        120        130        140        150
TGPVHAPLFV MSVEVNGQVF EGSGPTKKKA KLHAAEKALR SFVQFPNASE 
       160        170        180        190        200
AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF ETPDKSEPPF YVGSNGDDSF 
       210        220        230        240        250
SSSGDVSLSA SPVPASLTQP PLPIPPPFPP PSGKNPVMIL NELRPGLKYD 
       260        270        280        290        300
FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALATVFNLH 
       310        320        330        340        350
LDQTPSRQPV LSEGLQLHLP QVLADAVSRL VLGKFSDLTD NFSSPHARRK 
       360        370        380        390        400
VLSGVVMTTG TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR 
       410        420        430        440        450
RSLLRFLYAQ LELYLNNKED QKKSIFQKSE RGGFRLKDTV QFHLYISTSP 
       460        470        480        490        500
CGDARIFSPH EPVLEGMAPD SHQLTEPADR HPNRKARGQL RTKIESGEGT 
       510        520        530        540        550
IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG ALLSIFVEPI 
       560        570        580        590        600
YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR 
       610        620        630        640        650
QPGKAPNFSV NWTVGDTAIE VINATTGKDE LGRPSRLCKH ALYCRWMRVH 
       660        670        680        690        700
GKVPPHLLRT KITKPTTYHE SKLAAKEYQA AKARLFTAFI KAGLGAWVEK 
       710 
PTEQDQFSFT P                                           

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references