RED2_HUMAN
ID RED2_HUMAN Reviewed; 739 AA.
AC Q9NS39; B2RPJ5; Q5VUT6; Q5VW42;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Double-stranded RNA-specific editase B2;
DE EC=3.5.-.-;
DE AltName: Full=RNA-dependent adenosine deaminase 3;
DE AltName: Full=RNA-editing deaminase 2;
DE AltName: Full=RNA-editing enzyme 2;
DE AltName: Full=dsRNA adenosine deaminase B2;
GN Name=ADARB2; Synonyms=ADAR3, RED2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, REGION R-DOMAIN,
RP RNA-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=10836796; DOI=10.1017/s1355838200000170;
RA Chen C.-X., Cho D.S., Wang Q., Lai F., Carter K.C., Nishikura K.;
RT "A third member of the RNA-specific adenosine deaminase gene family, ADAR3,
RT contains both single- and double-stranded RNA binding domains.";
RL RNA 6:755-767(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-626.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=18178553; DOI=10.1074/jbc.m708316200;
RA Cenci C., Barzotti R., Galeano F., Corbelli S., Rota R., Massimi L.,
RA Di Rocco C., O'Connell M.A., Gallo A.;
RT "Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing
RT activity inhibits cell migration and proliferation.";
RL J. Biol. Chem. 283:7251-7260(2008).
RN [6]
RP REVIEW.
RX PubMed=22113393; DOI=10.1007/s12035-011-8220-2;
RA Orlandi C., Barbon A., Barlati S.;
RT "Activity regulation of adenosine deaminases acting on RNA (ADARs).";
RL Mol. Neurobiol. 45:61-75(2012).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-210 AND ILE-512.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Lacks editing activity. It prevents the binding of other ADAR
CC enzymes to targets in vitro, and decreases the efficiency of these
CC enzymes. Capable of binding to dsRNA but also to ssRNA.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NS39-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NS39-2; Sequence=VSP_056926, VSP_056927;
CC -!- TISSUE SPECIFICITY: Brain specific. Expressed at higher levels in
CC astrocytomas as compared to the normal brain tissue.
CC {ECO:0000269|PubMed:10836796, ECO:0000269|PubMed:18178553}.
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DR EMBL; AF034837; AAF78094.1; -; mRNA.
DR EMBL; AK055107; BAG51468.1; -; mRNA.
DR EMBL; AL442069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137477; AAI37478.1; -; mRNA.
DR EMBL; BC140852; AAI40853.1; -; mRNA.
DR CCDS; CCDS7058.1; -. [Q9NS39-1]
DR RefSeq; NP_061172.1; NM_018702.3. [Q9NS39-1]
DR AlphaFoldDB; Q9NS39; -.
DR SMR; Q9NS39; -.
DR BioGRID; 106619; 13.
DR IntAct; Q9NS39; 5.
DR STRING; 9606.ENSP00000370713; -.
DR iPTMnet; Q9NS39; -.
DR PhosphoSitePlus; Q9NS39; -.
DR BioMuta; ADARB2; -.
DR DMDM; 33112436; -.
DR SWISS-2DPAGE; Q9NS39; -.
DR EPD; Q9NS39; -.
DR MassIVE; Q9NS39; -.
DR PaxDb; Q9NS39; -.
DR PeptideAtlas; Q9NS39; -.
DR PRIDE; Q9NS39; -.
DR ProteomicsDB; 65520; -.
DR ProteomicsDB; 82477; -. [Q9NS39-1]
DR Antibodypedia; 23825; 37 antibodies from 17 providers.
DR DNASU; 105; -.
DR Ensembl; ENST00000381310.7; ENSP00000370711.3; ENSG00000185736.16. [Q9NS39-2]
DR Ensembl; ENST00000381312.6; ENSP00000370713.1; ENSG00000185736.16. [Q9NS39-1]
DR GeneID; 105; -.
DR KEGG; hsa:105; -.
DR MANE-Select; ENST00000381312.6; ENSP00000370713.1; NM_018702.4; NP_061172.1.
DR UCSC; uc001igm.5; human. [Q9NS39-1]
DR CTD; 105; -.
DR DisGeNET; 105; -.
DR GeneCards; ADARB2; -.
DR HGNC; HGNC:227; ADARB2.
DR HPA; ENSG00000185736; Tissue enriched (brain).
DR MIM; 602065; gene.
DR neXtProt; NX_Q9NS39; -.
DR OpenTargets; ENSG00000185736; -.
DR PharmGKB; PA24557; -.
DR VEuPathDB; HostDB:ENSG00000185736; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000157252; -.
DR HOGENOM; CLU_005382_3_1_1; -.
DR InParanoid; Q9NS39; -.
DR OMA; MYLHSII; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; Q9NS39; -.
DR TreeFam; TF315806; -.
DR PathwayCommons; Q9NS39; -.
DR SignaLink; Q9NS39; -.
DR BioGRID-ORCS; 105; 4 hits in 1068 CRISPR screens.
DR ChiTaRS; ADARB2; human.
DR GeneWiki; ADARB2; -.
DR GenomeRNAi; 105; -.
DR Pharos; Q9NS39; Tbio.
DR PRO; PR:Q9NS39; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NS39; protein.
DR Bgee; ENSG00000185736; Expressed in C1 segment of cervical spinal cord and 127 other tissues.
DR ExpressionAtlas; Q9NS39; baseline and differential.
DR Genevisible; Q9NS39; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0004000; F:adenosine deaminase activity; TAS:ProtInc.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; TAS:ProtInc.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0006382; P:adenosine to inosine editing; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR CDD; cd19896; DSRM_RED2_rpt1; 1.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR044460; ADAR3_DSRM_1.
DR InterPro; IPR014720; dsRBD_dom.
DR Pfam; PF02137; A_deamin; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Metal-binding; mRNA processing; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Zinc.
FT CHAIN 1..739
FT /note="Double-stranded RNA-specific editase B2"
FT /id="PRO_0000171782"
FT DOMAIN 125..191
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 274..341
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 408..735
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..35
FT /note="R-domain (ssRNA-binding)"
FT REGION 53..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 434
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT VAR_SEQ 1..69
FT /note="MASVLGSGRGSGGLSSQLKCKSKRRRRRRSKRKDKVSILSTFLAPFKHLSPG
FT ITNTEDDDTLSTSSAEV -> MGLWSPVPGNSVPRAPVMAGLGLGHSQGAPQGPHDGKT
FT DRSSGPGRRRTERTRLPGLLGGAPLTAGSPH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056926"
FT VAR_SEQ 70..560
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056927"
FT VARIANT 44
FT /note="A -> T (in dbSNP:rs3793733)"
FT /id="VAR_020438"
FT VARIANT 210
FT /note="T -> M (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035806"
FT VARIANT 512
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs138734198)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035807"
FT VARIANT 626
FT /note="A -> T (in dbSNP:rs2271275)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048726"
SQ SEQUENCE 739 AA; 80621 MW; A158A81D35894F79 CRC64;
MASVLGSGRG SGGLSSQLKC KSKRRRRRRS KRKDKVSILS TFLAPFKHLS PGITNTEDDD
TLSTSSAEVK ENRNVGNLAA RPPPSGDRAR GGAPGAKRKR PLEEGNGGHL CKLQLVWKKL
SWSVAPKNAL VQLHELRPGL QYRTVSQTGP VHAPVFAVAV EVNGLTFEGT GPTKKKAKMR
AAELALRSFV QFPNACQAHL AMGGGPGPGT DFTSDQADFP DTLFQEFEPP APRPGLAGGR
PGDAALLSAA YGRRRLLCRA LDLVGPTPAT PAAPGERNPV VLLNRLRAGL RYVCLAEPAE
RRARSFVMAV SVDGRTFEGS GRSKKLARGQ AAQAALQELF DIQMPGHAPG RARRTPMPQE
FADSISQLVT QKFREVTTDL TPMHARHKAL AGIVMTKGLD ARQAQVVALS SGTKCISGEH
LSDQGLVVND CHAEVVARRA FLHFLYTQLE LHLSKRREDS ERSIFVRLKE GGYRLRENIL
FHLYVSTSPC GDARLHSPYE ITTDLHSSKH LVRKFRGHLR TKIESGEGTV PVRGPSAVQT
WDGVLLGEQL ITMSCTDKIA RWNVLGLQGA LLSHFVEPVY LQSIVVGSLH HTGHLARVMS
HRMEGVGQLP ASYRHNRPLL SGVSDAEARQ PGKSPPFSMN WVVGSADLEI INATTGRRSC
GGPSRLCKHV LSARWARLYG RLSTRTPSPG DTPSMYCEAK LGAHTYQSVK QQLFKAFQKA
GLGTWVRKPP EQQQFLLTL
