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UniProtKB/Swiss-Prot entry P78563


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RED1_HUMAN
Primary accession number P78563
Secondary accession numbers A6NFK8 A6NJ84 O00395 O00465 O00691 O00692 P78555 Q4AE79 Q8NFD1
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 89)
Name and origin of the protein
Protein name Double-stranded RNA-specific editase 1
Synonyms EC 3.5.-.-
dsRNA adenosine deaminase
RNA-editing deaminase 1
RNA-editing enzyme 1
Gene name
Name: ADARB1
Synonyms: ADAR2, DRADA2, RED1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
Gerber A., O'Connell M.A., Keller W.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fetal brain;
DOI=10.1006/geno.1997.4655; PubMed=9143496 [NCBI, ExPASy, EBI, Israel, Japan]
Mittaz L., Scott H.S., Rossier C., Seeburg P.H., Higuchi M., Antonarakis S.E.;
"Cloning of a human RNA editing deaminase (ADARB1) of glutamate receptors that maps to chromosome 21q22.3.";
Genomics 41:210-217(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=9111310 [NCBI, ExPASy, EBI, Israel, Japan]
Lai F., Chen C.-X., Carter K.C., Nishikura K.;
"Editing of glutamate receptor B subunit ion channel RNAs by four alternatively spliced DRADA2 double-stranded RNA adenosine deaminases.";
Mol. Cell. Biol. 17:2413-2424(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1007/BF02679972; PubMed=9330641 [NCBI, ExPASy, EBI, Israel, Japan]
Villard L., Tassone F., Haymowicz M., Welborn R., Gardiner K.;
"Map location, genomic organization and expression patterns of the human RED1 RNA editase.";
Somat. Cell Mol. Genet. 23:135-145(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
DOI=10.1016/S0378-1119(02)01016-8; PubMed=12459255 [NCBI, ExPASy, EBI, Israel, Japan]
Slavov D., Gardiner K.;
"Phylogenetic comparison of the pre-mRNA adenosine deaminase ADAR2 genes and transcripts: conservation and diversity in editing site sequence and alternative splicing patterns.";
Gene 299:83-94(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1016/j.gene.2005.07.028; PubMed=16297572 [NCBI, ExPASy, EBI, Israel, Japan]
Kawahara Y., Ito K., Ito M., Tsuji S., Kwak S.;
"Novel splice variants of human ADAR2 mRNA: skipping of the exon encoding the dsRNA-binding domains, and multiple C-terminal splice sites.";
Gene 363:193-201(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/35012518; PubMed=10830953 [NCBI, ExPASy, EBI, Israel, Japan]
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[9]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
DOI=10.1186/gb-2004-5-2-r8; PubMed=14759258 [NCBI, ExPASy, EBI, Israel, Japan]
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 299-741 IN COMPLEX WITH IP6.
DOI=10.1126/science.1113150; PubMed=16141067 [NCBI, ExPASy, EBI, Israel, Japan]
Macbeth M.R., Schubert H.L., Vandemark A.P., Lingam A.T., Hill C.P., Bass B.L.;
"Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing.";
Science 309:1534-1539(2005).
Comments
  • FUNCTION: Editing of the messenger RNAs for glutamate receptor (GluR) subunits by site-selective adenosine deamination. Edits both the GluR-B Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently.
  • COFACTOR: Binds 1 inositol hexakisphosphate (IP6) per subunit.
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
    Name1
    SynonymsRED1-L, DRADA2B
    Isoform IDP78563-1
    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsRED1-S, DRADA2A
    Isoform IDP78563-2
    Features which should be applied to build the isoform sequence: VSP_000865.
    Name3
    SynonymsDRADA2C
    Isoform IDP78563-3
    Features which should be applied to build the isoform sequence: VSP_000866.
    Name4
    Isoform IDP78563-4
    Features which should be applied to build the isoform sequence: VSP_019597, VSP_000865.
  • SIMILARITY: Contains 1 A to I editase domain.
  • SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U82120; AAB61686.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U82121; AAB61687.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X99227; CAA67611.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X99383; CAA67762.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U76420; AAC51240.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U76421; AAC51241.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U76422; AAC51242.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF001042; AAB58300.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525422; AAM83100.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY135659; AAN10291.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB194370; BAE16326.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB194371; BAE16327.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB194372; BAE16328.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL163301; CAB90493.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001579; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471079; EAX09359.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471079; EAX09360.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00020368; -.
IPI00184874; -.
IPI00334613; -.
IPI00477012; -.
RefSeq NP_001028221.1; -.
NP_001103.1; -.
NP_056648.1; -.
NP_056649.1; -.
UniGene Hs.474018
3D structure databases
PDB
1ZY7; X-ray; 1.70 A; A/B=299-741.[ExPASy / RCSB / EBI]
PDBsum 1ZY7; -.
SMR P78563; 74-146, 231-301.
ModBase P78563.
PTM databases
PhosphoSite P78563; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
Organism-specific databases
GeneCards GC21P045318; -.
HGNC HGNC:226; ADARB1.
GenAtlas ADARB1.
HPA HPA018277; -.
MIM 601218; gene. [NCBI / EBI]
PharmGKB PA24556; -.
Gene expression databases
ArrayExpress P78563; -.
Bgee P78563; -.
GermOnline ENSG00000197381; Homo sapiens.
Ontologies
GO
GO:0005622; Cellular component: intracellular (inferred from electronic annotation from InterPro).
GO:0004000; Molecular function: adenosine deaminase activity (inferred from electronic annotation from InterPro).
GO:0003725; Molecular function: double-stranded RNA binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006397; Biological process: mRNA processing (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002466; A_deamin.
IPR001159; Ds-RNA_bd.
IPR014720; dsRNA-bd-like.
Graphical view of domain structure.
Gene3D G3DSA:3.30.160.20; dsRNA-bd-like; 2.
Pfam PF02137; A_deamin; 1.
PF00035; dsrm; 2.
Pfam graphical view of domain structure.
SMART SM00552; ADEAMc; 1.
SM00358; DSRM; 2.
SMART graphical view of domain structure.
PROSITE PS50141; A_DEAMIN_EDITASE; 1.
PS50137; DS_RBD; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P78563; -.
Genome annotation databases
Ensembl ENSG00000197381; Homo sapiens. [Contig view]
GeneID 104; -.
KEGG hsa:104; -.
Phylogenomic databases
HOVERGEN P78563; -.
OMA P78563; PPLYTLN.
Other
NextBio 399; -.
SOURCE ADARB1; Homo sapiens.
ProtoNet P78563.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Hydrolase; Metal-binding; mRNA processing; Phosphoprotein; Repeat; RNA-binding; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   741  741     Double-stranded RNA-specific editase 1. PRO_0000171779
DOMAIN   78   144  67     DRBM 1. 
DOMAIN   231   298  68     DRBM 2. 
DOMAIN   370   737  368     A to I editase. 
ACT_SITE   396   396        Proton donor. 
METAL   394   394        Zinc. 
METAL   451   451        Zinc. 
METAL   556   556        Zinc. 
BINDING   400   400        Inositol hexakisphosphate. 
BINDING   401   401        Inositol hexakisphosphate. 
BINDING   559   559        Inositol hexakisphosphate. 
BINDING   562   562        Inositol hexakisphosphate. 
BINDING   669   669        Inositol hexakisphosphate. 
BINDING   702   702        Inositol hexakisphosphate. 
BINDING   712   712        Inositol hexakisphosphate. 
BINDING   730   730        Inositol hexakisphosphate. 
MOD_RES   26    26        Phosphoserine. 
VAR_SEQ   1     1        M -> MKIPRMKTPCQPDRNSLRQSRNPQKYFA (in isoform 4). VSP_019597
VAR_SEQ   466   505        Missing (in isoform 2 and isoform 4). VSP_000865
VAR_SEQ   713   741        ARLFTAFIKAGLGAWVEKPTEQDQFSLTP -> VH (in isoform 3). VSP_000866
CONFLICT   30    30        G -> A (in Ref. 4; AAB58300 and 5; AAM83100/AAN10291). 
CONFLICT   423   423        R -> E (in Ref. 4; AAB58300 and 5; AAM83100/AAN10291). 
CONFLICT   475   475        V -> L (in Ref. 5; AAM83100/AAN10291). 
HELIX   320   338  19      
TURN   339   343  5      
HELIX   345   347  3      
STRAND   352   361  10      
HELIX   363   365  3      
STRAND   367   373  7      
HELIX   380   382  3      
HELIX   395   416  22      
HELIX   418   423  6      
STRAND   425   428  4      
STRAND   432   436  5      
STRAND   440   448  9      
HELIX   453   456  4      
STRAND   521   524  4      
HELIX   542   546  5      
STRAND   552   554  3      
HELIX   556   566  11      
HELIX   570   574  5      
STRAND   582   589  8      
HELIX   593   600  8      
HELIX   602   604  3      
STRAND   620   623  4      
STRAND   637   643  7      
STRAND   650   653  4      
TURN   654   657  4      
HELIX   669   680  12      
HELIX   685   687  3      
HELIX   698   703  6      
HELIX   706   721  16      
HELIX   732   735  4      
Sequence information
Length: 741 AA [This is the length of the unprocessed precursor] Molecular weight: 80763 Da [This is the MW of the unprocessed precursor] CRC64: 02B583414DD59C20 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG RKRPLEEGSN 

        70         80         90        100        110        120 
GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ TGPVHAPLFV MSVEVNGQVF 

       130        140        150        160        170        180 
EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF 

       190        200        210        220        230        240 
ETPDKAEPPF YVGSNGDDSF SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL 

       250        260        270        280        290        300 
NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH 

       310        320        330        340        350        360 
LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK VLAGVVMTTG 

       370        380        390        400        410        420 
TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYTQ LELYLNNKDD 

       430        440        450        460        470        480 
QKRSIFQKSE RGGFRLKENV QFHLYISTSP CGDARIFSPH EPILEGSRSY TQAGVQWCNH 

       490        500        510        520        530        540 
GSLQPRPPGL LSDPSTSTFQ GAGTTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ 

       550        560        570        580        590        600 
TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM 

       610        620        630        640        650        660 
YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDSAIE VINATTGKDE 

       670        680        690        700        710        720 
LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE SKLAAKEYQA AKARLFTAFI 

       730        740 
KAGLGAWVEK PTEQDQFSLT P 

P78563 in FASTA format

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