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Q9NS39 (RED2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ADARB2
Synonyms:ADAR3, RED2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Nucleus.

Tissue specificity

Brain specific. Expressed at higher levels in astrocytomas as compared to the normal brain tissue. Ref.1 Ref.4

Sequence similarities

Contains 1 A to I editase domain.

Contains 2 DRBM (double-stranded RNA-binding) domains.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionadenosine deaminase activity

Traceable author statement Ref.1. Source: ProtInc

double-stranded RNA binding

Traceable author statement Ref.1. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

single-stranded RNA binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 739739Double-stranded RNA-specific editase B2
PRO_0000171782

Regions

Domain125 – 19167DRBM 1
Domain274 – 34168DRBM 2
Domain408 – 735328A to I editase
Region23 – 3513R-domain (ssRNA-binding)

Sites

Active site4341Proton donor By similarity
Metal binding4321Zinc By similarity
Metal binding4901Zinc By similarity
Metal binding5551Zinc By similarity

Natural variations

Natural variant441A → T.
Corresponds to variant rs3793733 [ dbSNP | Ensembl ].
VAR_020438
Natural variant2101T → M in a colorectal cancer sample; somatic mutation. Ref.6
VAR_035806
Natural variant5121V → I in a colorectal cancer sample; somatic mutation. Ref.6
VAR_035807
Natural variant6261A → T. Ref.3
Corresponds to variant rs2271275 [ dbSNP | Ensembl ].
VAR_048726

Sequences

Sequence LengthMass (Da)Tools
Q9NS39 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A158A81D35894F79

FASTA73980,621
        10         20         30         40         50         60 
MASVLGSGRG SGGLSSQLKC KSKRRRRRRS KRKDKVSILS TFLAPFKHLS PGITNTEDDD 

        70         80         90        100        110        120 
TLSTSSAEVK ENRNVGNLAA RPPPSGDRAR GGAPGAKRKR PLEEGNGGHL CKLQLVWKKL 

       130        140        150        160        170        180 
SWSVAPKNAL VQLHELRPGL QYRTVSQTGP VHAPVFAVAV EVNGLTFEGT GPTKKKAKMR 

       190        200        210        220        230        240 
AAELALRSFV QFPNACQAHL AMGGGPGPGT DFTSDQADFP DTLFQEFEPP APRPGLAGGR 

       250        260        270        280        290        300 
PGDAALLSAA YGRRRLLCRA LDLVGPTPAT PAAPGERNPV VLLNRLRAGL RYVCLAEPAE 

       310        320        330        340        350        360 
RRARSFVMAV SVDGRTFEGS GRSKKLARGQ AAQAALQELF DIQMPGHAPG RARRTPMPQE 

       370        380        390        400        410        420 
FADSISQLVT QKFREVTTDL TPMHARHKAL AGIVMTKGLD ARQAQVVALS SGTKCISGEH 

       430        440        450        460        470        480 
LSDQGLVVND CHAEVVARRA FLHFLYTQLE LHLSKRREDS ERSIFVRLKE GGYRLRENIL 

       490        500        510        520        530        540 
FHLYVSTSPC GDARLHSPYE ITTDLHSSKH LVRKFRGHLR TKIESGEGTV PVRGPSAVQT 

       550        560        570        580        590        600 
WDGVLLGEQL ITMSCTDKIA RWNVLGLQGA LLSHFVEPVY LQSIVVGSLH HTGHLARVMS 

       610        620        630        640        650        660 
HRMEGVGQLP ASYRHNRPLL SGVSDAEARQ PGKSPPFSMN WVVGSADLEI INATTGRRSC 

       670        680        690        700        710        720 
GGPSRLCKHV LSARWARLYG RLSTRTPSPG DTPSMYCEAK LGAHTYQSVK QQLFKAFQKA 

       730 
GLGTWVRKPP EQQQFLLTL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-210 AND ILE-512.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_061172.1. NM_018702.3.
UniGeneHs.586663.

3D structure databases

ProteinModelPortalQ9NS39.
SMRQ9NS39. Positions 124-341, 349-738.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106619. 1 interaction.
IntActQ9NS39. 1 interaction.
MINTMINT-4728108.
STRING9606.ENSP00000370713.

PTM databases

PhosphoSiteQ9NS39.

Polymorphism databases

DMDM33112436.

2D gel databases

SWISS-2DPAGEQ9NS39.

Proteomic databases

PaxDbQ9NS39.
PRIDEQ9NS39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381312; ENSP00000370713; ENSG00000185736.
GeneID105.
KEGGhsa:105.
UCSCuc009xhq.3. human.

Organism-specific databases

CTD105.
GeneCardsGC10M001219.
HGNCHGNC:227. ADARB2.
HPAHPA031332.
HPA031333.
MIM602065. gene.
neXtProtNX_Q9NS39.
PharmGKBPA24557.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292433.
HOGENOMHOG000290164.
HOVERGENHBG003836.
InParanoidQ9NS39.
KOK13194.
OMALFKEFEP.
OrthoDBEOG7VHSX4.
PhylomeDBQ9NS39.
TreeFamTF315806.

Gene expression databases

ArrayExpressQ9NS39.
BgeeQ9NS39.
CleanExHS_ADARB2.
GenevestigatorQ9NS39.

Family and domain databases

Gene3D3.30.160.20. 2 hits.
InterProIPR002466. A_deamin.
IPR014720. dsRNA-bd_dom.
[Graphical view]
PfamPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[Graphical view]
SMARTSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
PROSITEPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADARB2. human.
GeneWikiADARB2.
GenomeRNAi105.
NextBio409.
PROQ9NS39.
SOURCESearch...

Entry information

Entry nameRED2_HUMAN
AccessionPrimary (citable) accession number: Q9NS39
Secondary accession number(s): B2RPJ5, Q5VUT6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM