Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Double-stranded RNA-specific editase 1 (EC 3.5.4.37) (RNA-editing deaminase 1) (RNA-editing enzyme 1) (dsRNA adenosine deaminase)

 RED1_HUMAN              Reviewed;         741 AA.
P78563; A6NFK8; A6NJ84; C3TTQ1; C3TTQ2; C9JUP4; G5E9B4; O00395;
O00465; O00691; O00692; P78555; Q4AE77; Q4AE79; Q6P0M9; Q8NFA1;
Q8NFD1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
28-MAR-2018, entry version 173.
RecName: Full=Double-stranded RNA-specific editase 1;
EC=3.5.4.37;
AltName: Full=RNA-editing deaminase 1;
AltName: Full=RNA-editing enzyme 1;
AltName: Full=dsRNA adenosine deaminase;
Name=ADARB1; Synonyms=ADAR2, DRADA2, RED1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
CATALYTIC ACTIVITY.
TISSUE=Brain;
PubMed=9149227;
Gerber A., O'Connell M.A., Keller W.;
"Two forms of human double-stranded RNA-specific editase 1 (hRED1)
generated by the insertion of an Alu cassette.";
RNA 3:453-463(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fetal brain;
PubMed=9143496; DOI=10.1006/geno.1997.4655;
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; DOI=10.1128/MCB.17.5.2413;
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).
PubMed=9330641; DOI=10.1007/BF02679972;
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] (ISOFORMS 2 AND 4).
PubMed=12459255; DOI=10.1016/S0378-1119(02)01016-8;
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] (ISOFORMS 2 AND 6).
PubMed=16297572; DOI=10.1016/j.gene.2005.07.028;
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].
PubMed=10830953; DOI=10.1038/35012518;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ALA-224.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM 5), ALTERNATIVE PROMOTER
USAGE, AND TISSUE SPECIFICITY.
PubMed=19156214; DOI=10.1371/journal.pone.0004225;
Maas S., Gommans W.M.;
"Novel exon of mammalian ADAR2 extends open reading frame.";
PLoS ONE 4:E4225-E4225(2009).
[11]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[12]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18178553; DOI=10.1074/jbc.M708316200;
Cenci C., Barzotti R., Galeano F., Corbelli S., Rota R., Massimi L.,
Di Rocco C., O'Connell M.A., Gallo A.;
"Down-regulation of RNA editing in pediatric astrocytomas: ADAR2
editing activity inhibits cell migration and proliferation.";
J. Biol. Chem. 283:7251-7260(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
REVIEW.
PubMed=20192758; DOI=10.1146/annurev-biochem-060208-105251;
Nishikura K.;
"Functions and regulation of RNA editing by ADAR deaminases.";
Annu. Rev. Biochem. 79:321-349(2010).
[16]
FUNCTION.
PubMed=19908260; DOI=10.1002/ijc.25022;
Galeano F., Leroy A., Rossetti C., Gromova I., Gautier P.,
Keegan L.P., Massimi L., Di Rocco C., O'Connell M.A., Gallo A.;
"Human BLCAP transcript: new editing events in normal and cancerous
tissues.";
Int. J. Cancer 127:127-137(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
REVIEW.
PubMed=22022963; DOI=10.1134/S0006297911080050;
Wang Q.;
"RNA editing catalyzed by ADAR1 and its function in mammalian cells.";
Biochemistry (Mosc.) 76:900-911(2011).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21289159; DOI=10.1099/vir.0.028043-0;
Doria M., Tomaselli S., Neri F., Ciafre S.A., Farace M.G.,
Michienzi A., Gallo A.;
"ADAR2 editing enzyme is a novel human immunodeficiency virus-1
proviral factor.";
J. Gen. Virol. 92:1228-1232(2011).
[20]
REVIEW.
PubMed=21182352; DOI=10.1089/jir.2010.0097;
George C.X., Gan Z., Liu Y., Samuel C.E.;
"Adenosine deaminases acting on RNA, RNA editing, and interferon
action.";
J. Interferon Cytokine Res. 31:99-117(2011).
[21]
REVIEW.
PubMed=21211811; DOI=10.1016/j.virol.2010.12.004;
Samuel C.E.;
"Adenosine deaminases acting on RNA (ADARs) are both antiviral and
proviral.";
Virology 411:180-193(2011).
[22]
REVIEW.
PubMed=22988838; DOI=10.3109/10409238.2012.714350;
Mallela A., Nishikura K.;
"A-to-I editing of protein coding and noncoding RNAs.";
Crit. Rev. Biochem. Mol. Biol. 47:493-501(2012).
[23]
REVIEW.
PubMed=21769729; DOI=10.1007/82_2011_144;
Goodman R.A., Macbeth M.R., Beal P.A.;
"ADAR proteins: structure and catalytic mechanism.";
Curr. Top. Microbiol. Immunol. 353:1-33(2012).
[24]
REVIEW.
PubMed=22113393; DOI=10.1007/s12035-011-8220-2;
Orlandi C., Barbon A., Barlati S.;
"Activity regulation of adenosine deaminases acting on RNA (ADARs).";
Mol. Neurobiol. 45:61-75(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 299-741 IN COMPLEX WITH IP6,
AND CATALYTIC ACTIVITY.
PubMed=16141067; DOI=10.1126/science.1113150;
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).
-!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine to
inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA
editing. This may affect gene expression and function in a number
of ways that include mRNA translation by changing codons and hence
the amino acid sequence of proteins; pre-mRNA splicing by altering
splice site recognition sequences; RNA stability by changing
sequences involved in nuclease recognition; genetic stability in
the case of RNA virus genomes by changing sequences during viral
RNA replication; and RNA structure-dependent activities such as
microRNA production or targeting or protein-RNA interactions. Can
edit both viral and cellular RNAs and can edit RNAs at multiple
sites (hyper-editing) or at specific sites (site-specific
editing). Its cellular RNA substrates include: bladder cancer-
associated protein (BLCAP), neurotransmitter receptors for
glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor
(GABRA3) and potassium voltage-gated channel (KCNA1). Site-
specific RNA editing of transcripts encoding these proteins
results in amino acid substitutions which consequently alter their
functional activities. Edits GRIA2 at both the Q/R and R/G sites
efficiently but converts the adenosine in hotspot1 much less
efficiently. Can exert a proviral effect towards human
immunodeficiency virus type 1 (HIV-1) and enhances its replication
via both an editing-dependent and editing-independent mechanism.
The former involves editing of adenosines in the 5'UTR while the
latter occurs via suppression of EIF2AK2/PKR activation and
function. Can inhibit cell proliferation and migration and can
stimulate exocytosis. {ECO:0000269|PubMed:18178553,
ECO:0000269|PubMed:19908260, ECO:0000269|PubMed:21289159}.
-!- CATALYTIC ACTIVITY: Adenine in double-stranded RNA + H(2)O =
hypoxanthine in double-stranded RNA + NH(3).
{ECO:0000269|PubMed:16141067, ECO:0000269|PubMed:9149227}.
-!- COFACTOR:
Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.;
-!- SUBUNIT: Homodimer. Homodimerization is essential for its
catalytic activity. Can form heterodimers with isoform 5 of
ADAR/ADAR1. {ECO:0000269|PubMed:16141067,
ECO:0000269|PubMed:18178553}.
-!- INTERACTION:
Q13526:PIN1; NbExp=12; IntAct=EBI-2967304, EBI-714158;
O75569:PRKRA; NbExp=4; IntAct=EBI-12002366, EBI-713955;
Q15633:TARBP2; NbExp=4; IntAct=EBI-12002366, EBI-978581;
O00308:WWP2; NbExp=5; IntAct=EBI-2967304, EBI-743923;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Note=Shuttles
between nucleoli and the nucleoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=RED1-L, DRADA2B;
IsoId=P78563-1; Sequence=Displayed;
Note=Alu insert from position 465 to 505. Has a lower catalytic
activity than isoform 2. May be produced at very low levels due
to a premature stop codon in the mRNA, leading to
nonsense-mediated mRNA decay.;
Name=2; Synonyms=ADAR2a, DRADA2A, RED1-S;
IsoId=P78563-2; Sequence=VSP_000865;
Note=Has a higher catalytic activity than isoform 1.;
Name=3; Synonyms=DRADA2C;
IsoId=P78563-3; Sequence=VSP_000866;
Name=4;
IsoId=P78563-4; Sequence=VSP_019597, VSP_000865;
Name=5; Synonyms=ADAR2R;
IsoId=P78563-5; Sequence=VSP_041421;
Note=Likely expressed from an alternative promoter. Contains a
region highly similar to the so-called ssRNA-binding R-domain of
ADARB2. {ECO:0000269|PubMed:19156214};
Name=6; Synonyms=ADAR2d;
IsoId=P78563-6; Sequence=VSP_000865, VSP_000866;
-!- TISSUE SPECIFICITY: Highly expressed in brain and heart and at
lower levels in placenta. Fair expression in lung, liver and
kidney. Detected in brain, heart, kidney, lung and liver (at
protein level). Isoform 5 is high expressed in hippocampus and
colon. Isoform 5 is expressed in pediatric astrocytomas and the
protein has a decreased RNA-editing activity. The decrease in RNA
editing correlates with the grade of malignancy of the tumors,
with the high grade tumors showing lower editing is seen.
{ECO:0000269|PubMed:18178553, ECO:0000269|PubMed:19156214,
ECO:0000269|PubMed:9149227}.
-!- SEQUENCE CAUTION:
Sequence=ACN49027.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U82120; AAB61686.1; -; mRNA.
EMBL; U82121; AAB61687.1; -; mRNA.
EMBL; X99227; CAA67611.1; -; mRNA.
EMBL; X99383; CAA67762.1; -; mRNA.
EMBL; U76420; AAC51240.1; -; mRNA.
EMBL; U76421; AAC51241.1; -; mRNA.
EMBL; U76422; AAC51242.1; -; mRNA.
EMBL; AF001042; AAB58300.1; -; mRNA.
EMBL; AF525422; AAM83100.1; -; mRNA.
EMBL; AF533142; AAM97654.1; -; mRNA.
EMBL; AY135659; AAN10291.1; -; mRNA.
EMBL; AB194370; BAE16326.1; -; mRNA.
EMBL; AB194371; BAE16327.1; -; mRNA.
EMBL; AB194372; BAE16328.1; -; mRNA.
EMBL; AB194373; BAE16329.1; -; mRNA.
EMBL; AL163301; CAB90493.1; -; Genomic_DNA.
EMBL; AL133499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX322560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09357.1; -; Genomic_DNA.
EMBL; CH471079; EAX09359.1; -; Genomic_DNA.
EMBL; CH471079; EAX09360.1; -; Genomic_DNA.
EMBL; BC065545; AAH65545.1; -; mRNA.
EMBL; FJ169506; ACN49027.1; ALT_INIT; mRNA.
CCDS; CCDS33589.1; -. [P78563-1]
CCDS; CCDS33590.1; -. [P78563-2]
CCDS; CCDS42970.1; -. [P78563-3]
RefSeq; NP_001103.1; NM_001112.3. [P78563-2]
RefSeq; NP_001153702.1; NM_001160230.1. [P78563-6]
RefSeq; NP_001333616.1; NM_001346687.1.
RefSeq; NP_001333617.1; NM_001346688.1. [P78563-6]
RefSeq; NP_056648.1; NM_015833.3. [P78563-1]
RefSeq; NP_056649.1; NM_015834.3. [P78563-3]
RefSeq; XP_016883736.1; XM_017028247.1. [P78563-1]
RefSeq; XP_016883737.1; XM_017028248.1. [P78563-1]
RefSeq; XP_016883738.1; XM_017028249.1. [P78563-1]
RefSeq; XP_016883739.1; XM_017028250.1. [P78563-1]
RefSeq; XP_016883740.1; XM_017028251.1. [P78563-1]
RefSeq; XP_016883743.1; XM_017028254.1. [P78563-3]
RefSeq; XP_016883744.1; XM_017028255.1. [P78563-2]
UniGene; Hs.474018; -.
PDB; 1ZY7; X-ray; 1.70 A; A/B=299-741.
PDB; 5ED1; X-ray; 2.77 A; A/D=299-741.
PDB; 5ED2; X-ray; 2.95 A; A/D=299-741.
PDB; 5HP2; X-ray; 2.98 A; A/D=299-741.
PDB; 5HP3; X-ray; 3.09 A; A/D=299-741.
PDBsum; 1ZY7; -.
PDBsum; 5ED1; -.
PDBsum; 5ED2; -.
PDBsum; 5HP2; -.
PDBsum; 5HP3; -.
ProteinModelPortal; P78563; -.
SMR; P78563; -.
BioGrid; 106618; 26.
IntAct; P78563; 20.
MINT; P78563; -.
STRING; 9606.ENSP00000353920; -.
iPTMnet; P78563; -.
PhosphoSitePlus; P78563; -.
BioMuta; ADARB1; -.
DMDM; 2829669; -.
EPD; P78563; -.
MaxQB; P78563; -.
PaxDb; P78563; -.
PeptideAtlas; P78563; -.
PRIDE; P78563; -.
Ensembl; ENST00000348831; ENSP00000015877; ENSG00000197381. [P78563-2]
Ensembl; ENST00000360697; ENSP00000353920; ENSG00000197381. [P78563-1]
Ensembl; ENST00000389863; ENSP00000374513; ENSG00000197381. [P78563-3]
Ensembl; ENST00000437626; ENSP00000414600; ENSG00000197381. [P78563-1]
Ensembl; ENST00000492414; ENSP00000436367; ENSG00000197381. [P78563-2]
Ensembl; ENST00000496664; ENSP00000435381; ENSG00000197381. [P78563-1]
Ensembl; ENST00000629643; ENSP00000486475; ENSG00000197381. [P78563-4]
GeneID; 104; -.
KEGG; hsa:104; -.
UCSC; uc002zgr.3; human. [P78563-1]
CTD; 104; -.
DisGeNET; 104; -.
EuPathDB; HostDB:ENSG00000197381.15; -.
GeneCards; ADARB1; -.
HGNC; HGNC:226; ADARB1.
HPA; HPA018277; -.
HPA; HPA029645; -.
MIM; 601218; gene.
neXtProt; NX_P78563; -.
OpenTargets; ENSG00000197381; -.
PharmGKB; PA24556; -.
eggNOG; KOG2777; Eukaryota.
eggNOG; ENOG410XT0Z; LUCA.
GeneTree; ENSGT00550000074412; -.
HOGENOM; HOG000213660; -.
HOVERGEN; HBG003836; -.
InParanoid; P78563; -.
KO; K13194; -.
OMA; DNVQFHL; -.
OrthoDB; EOG091G0MZP; -.
PhylomeDB; P78563; -.
TreeFam; TF315806; -.
BRENDA; 3.5.4.37; 2681.
Reactome; R-HSA-75102; C6 deamination of adenosine.
Reactome; R-HSA-77042; Formation of editosomes by ADAR proteins.
ChiTaRS; ADARB1; human.
EvolutionaryTrace; P78563; -.
GeneWiki; ADARB1; -.
GenomeRNAi; 104; -.
PRO; PR:P78563; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000197381; -.
ExpressionAtlas; P78563; baseline and differential.
Genevisible; P78563; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IDA:HGNC.
GO; GO:0003725; F:double-stranded RNA binding; IDA:HGNC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; TAS:BHF-UCL.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB.
GO; GO:0016553; P:base conversion or substitution editing; IC:HGNC.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0021610; P:facial nerve morphogenesis; IEA:Ensembl.
GO; GO:0021618; P:hypoglossal nerve morphogenesis; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0060384; P:innervation; IEA:Ensembl.
GO; GO:0061744; P:motor behavior; IEA:Ensembl.
GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0060415; P:muscle tissue morphogenesis; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:0006396; P:RNA processing; IDA:HGNC.
GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; IEA:Ensembl.
InterPro; IPR002466; A_deamin.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR008996; IL1/FGF.
Pfam; PF02137; A_deamin; 1.
Pfam; PF00035; dsrm; 2.
SMART; SM00552; ADEAMc; 1.
SMART; SM00358; DSRM; 2.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
PROSITE; PS50137; DS_RBD; 2.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Alternative splicing;
Antiviral defense; Complete proteome; Hydrolase; Immunity;
Innate immunity; Metal-binding; mRNA processing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding;
Zinc.
CHAIN 1 741 Double-stranded RNA-specific editase 1.
/FTId=PRO_0000171779.
DOMAIN 78 144 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 231 298 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 370 737 A to I editase. {ECO:0000255|PROSITE-
ProRule:PRU00240}.
REGION 83 88 Interaction with substrate RNA.
{ECO:0000250}.
REGION 104 105 Interaction with substrate RNA.
{ECO:0000250}.
REGION 237 242 Interaction with substrate RNA.
{ECO:0000250}.
REGION 259 259 Interaction with substrate RNA.
{ECO:0000250}.
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.
{ECO:0000244|PubMed:20068231}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1 M -> MKIPRMKTPCQPDRNSLRQSRNPQKYFAM (in
isoform 4).
{ECO:0000303|PubMed:12459255}.
/FTId=VSP_019597.
VAR_SEQ 1 1 M -> MASSTTPPLHMGTFFSVMGRRYKRRRKKRSERKDRN
SLRQSRNPQKYFAM (in isoform 5).
{ECO:0000303|PubMed:19156214}.
/FTId=VSP_041421.
VAR_SEQ 466 505 Missing (in isoform 2, isoform 4 and
isoform 6). {ECO:0000303|PubMed:12459255,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16297572,
ECO:0000303|PubMed:9111310,
ECO:0000303|PubMed:9143496,
ECO:0000303|PubMed:9149227}.
/FTId=VSP_000865.
VAR_SEQ 713 741 ARLFTAFIKAGLGAWVEKPTEQDQFSLTP -> VH (in
isoform 3 and isoform 6).
{ECO:0000303|PubMed:16297572,
ECO:0000303|PubMed:9111310}.
/FTId=VSP_000866.
VARIANT 224 224 V -> A (in dbSNP:rs199697177).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_070931.
CONFLICT 30 30 G -> A (in Ref. 4; AAB58300 and 5;
AAM83100/AAM97654/AAN10291).
{ECO:0000305}.
CONFLICT 423 423 R -> E (in Ref. 4; AAB58300 and 5;
AAM83100/AAM97654/AAN10291).
{ECO:0000305}.
CONFLICT 475 475 V -> L (in Ref. 5; AAM83100/AAN10291).
{ECO:0000305}.
STRAND 313 315 {ECO:0000244|PDB:5ED1}.
HELIX 320 338 {ECO:0000244|PDB:1ZY7}.
TURN 339 343 {ECO:0000244|PDB:1ZY7}.
HELIX 345 347 {ECO:0000244|PDB:1ZY7}.
STRAND 352 361 {ECO:0000244|PDB:1ZY7}.
HELIX 363 365 {ECO:0000244|PDB:1ZY7}.
STRAND 367 373 {ECO:0000244|PDB:1ZY7}.
STRAND 375 377 {ECO:0000244|PDB:5ED2}.
HELIX 380 382 {ECO:0000244|PDB:1ZY7}.
STRAND 391 394 {ECO:0000244|PDB:5ED2}.
HELIX 395 416 {ECO:0000244|PDB:1ZY7}.
HELIX 418 423 {ECO:0000244|PDB:1ZY7}.
STRAND 425 428 {ECO:0000244|PDB:1ZY7}.
STRAND 432 436 {ECO:0000244|PDB:1ZY7}.
STRAND 440 448 {ECO:0000244|PDB:1ZY7}.
HELIX 453 456 {ECO:0000244|PDB:1ZY7}.
TURN 515 518 {ECO:0000244|PDB:5ED1}.
STRAND 521 524 {ECO:0000244|PDB:1ZY7}.
STRAND 529 532 {ECO:0000244|PDB:5ED1}.
TURN 533 535 {ECO:0000244|PDB:5ED1}.
HELIX 542 546 {ECO:0000244|PDB:1ZY7}.
STRAND 552 554 {ECO:0000244|PDB:1ZY7}.
HELIX 556 566 {ECO:0000244|PDB:1ZY7}.
HELIX 570 574 {ECO:0000244|PDB:1ZY7}.
STRAND 582 589 {ECO:0000244|PDB:1ZY7}.
HELIX 593 600 {ECO:0000244|PDB:1ZY7}.
HELIX 602 604 {ECO:0000244|PDB:1ZY7}.
STRAND 620 623 {ECO:0000244|PDB:1ZY7}.
STRAND 637 643 {ECO:0000244|PDB:1ZY7}.
STRAND 650 653 {ECO:0000244|PDB:1ZY7}.
TURN 654 657 {ECO:0000244|PDB:1ZY7}.
HELIX 669 680 {ECO:0000244|PDB:1ZY7}.
HELIX 685 687 {ECO:0000244|PDB:1ZY7}.
HELIX 698 703 {ECO:0000244|PDB:1ZY7}.
HELIX 706 721 {ECO:0000244|PDB:1ZY7}.
HELIX 732 735 {ECO:0000244|PDB:1ZY7}.
SEQUENCE 741 AA; 80763 MW; 02B583414DD59C20 CRC64;
MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG RKRPLEEGSN
GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ TGPVHAPLFV MSVEVNGQVF
EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF
ETPDKAEPPF YVGSNGDDSF SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL
NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH
LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK VLAGVVMTTG
TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYTQ LELYLNNKDD
QKRSIFQKSE RGGFRLKENV QFHLYISTSP CGDARIFSPH EPILEGSRSY TQAGVQWCNH
GSLQPRPPGL LSDPSTSTFQ GAGTTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ
TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM
YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDSAIE VINATTGKDE
LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE SKLAAKEYQA AKARLFTAFI
KAGLGAWVEK PTEQDQFSLT P


Related products :

Catalog number Product name Quantity
EIAAB34198 Adar3,Adarb2,Double-stranded RNA-specific editase B2,dsRNA adenosine deaminase B2,Mouse,Mus musculus,Red2,RNA-dependent adenosine deaminase 3,RNA-editing deaminase 2,RNA-editing enzyme 2
EIAAB34199 Adar3,Adarb2,Double-stranded RNA-specific editase B2,dsRNA adenosine deaminase B2,Rat,Rattus norvegicus,Red2,RNA-dependent adenosine deaminase 3,RNA-editing deaminase 2,RNA-editing enzyme 2
EIAAB34200 ADAR3,ADARB2,Double-stranded RNA-specific editase B2,dsRNA adenosine deaminase B2,Homo sapiens,Human,RED2,RNA-dependent adenosine deaminase 3,RNA-editing deaminase 2,RNA-editing enzyme 2
EIAAB34197 Adarb1,Double-stranded RNA-specific editase 1,dsRNA adenosine deaminase,Rat,Rattus norvegicus,Red1,RNA-editing deaminase 1,RNA-editing enzyme 1
EIAAB34196 Adar2,Adarb1,Double-stranded RNA-specific editase 1,dsRNA adenosine deaminase,Mouse,Mus musculus,Red1,RNA-editing deaminase 1,RNA-editing enzyme 1
EIAAB34195 ADAR2,ADARB1,Double-stranded RNA-specific editase 1,DRADA2,dsRNA adenosine deaminase,Homo sapiens,Human,RED1,RNA-editing deaminase 1,RNA-editing enzyme 1
25-654 ADARB2 is a member of the double-stranded RNA adenosine deaminase family of RNA-editing enzymes and may play a regulatory role in RNA editing. This gene encodes a member of the double-stranded RNA ade 0.05 mg
EIAAB11980 Adar,Double-stranded RNA-specific adenosine deaminase,DRADA,Mouse,Mus musculus,RNA adenosine deaminase 1
DSRAD_RAT Rat ELISA Kit FOR Double-stranded RNA-specific adenosine deaminase 96T
CSB-RP007744h Recombinant human Double-stranded RNA-specific adenosine deaminase 500ug
CSB-EL001324RA Rat Double-stranded RNA-specific adenosine deaminase(ADAR) ELISA kit 96T
EIAAB11979 136 kDa double-stranded RNA-binding protein,ADAR,ADAR1,Double-stranded RNA-specific adenosine deaminase,DRADA,DSRAD,G1P1,Homo sapiens,Human,IFI4,IFI-4,Interferon-inducible protein 4,K88DSRBP,p136
CSB-EL001324HU Human Double-stranded RNA-specific adenosine deaminase(ADAR) ELISA kit 96T
PE007744h Recombinant human Double-stranded RNA-specific adenosine deaminase protein 50ug
CSB-EL001324MO Mouse Double-stranded RNA-specific adenosine deaminase(ADAR) ELISA kit 96T
PE007744h Recombinant human Double-stranded RNA-specific adenosine deaminase protein 200ug
PE007744h Recombinant human Double-stranded RNA-specific adenosine deaminase protein 5mg
PE007744h Recombinant human Double-stranded RNA-specific adenosine deaminase protein 1mg
CSB-EL001324RA Rat Double-stranded RNA-specific adenosine deaminase(ADAR) ELISA kit SpeciesRat 96T
CSB-EL001324MO Mouse Double-stranded RNA-specific adenosine deaminase(ADAR) ELISA kit SpeciesMouse 96T
CSB-RP007744h Recombinant human Double-stranded RNA-specific adenosine deaminase Source: E.coli 1mg
CSB-RP007744h Recombinant human Double-stranded RNA-specific adenosine deaminase Source: E.coli 200ug
CSB-EL001324HU Human Double-stranded RNA-specific adenosine deaminase(ADAR) ELISA kit SpeciesHuman 96T
29-405 ADAT1 is a member of the ADAR (adenosine deaminase acting on RNA) family. Using site-specific adenosine modification, the family participates in the pre-mRNA editing of nuclear transcripts. ADAT1, tRN 0.1 mg
29-406 ADAT1 is a member of the ADAR (adenosine deaminase acting on RNA) family. Using site-specific adenosine modification, the family participates in the pre-mRNA editing of nuclear transcripts. ADAT1, tRN 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur