Q9NS39 (RED2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	739 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Does not act on glutamate receptor or on serotonin receptor subtype 2C. Capable of binding to dsRNA but also to ssRNA.
Subcellular location	Nucleus.
Tissue specificity	Brain specific. Ref.1
Sequence similarities	Contains 1 A to I editase domain. Contains 2 DRBM (double-stranded RNA-binding) domains.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	adenosine deaminase activity Traceable author statement. Source: ProtInc double-stranded RNA binding Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded RNA binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 739	739	Double-stranded RNA-specific editase B2		PRO_0000171782
Regions
	Domain	125 – 191	67	DRBM 1
	Domain	274 – 341	68	DRBM 2
	Domain	408 – 735	328	A to I editase
Sites
	Active site	434	1	Proton donor By similarity
	Metal binding	432	1	Zinc By similarity
	Metal binding	490	1	Zinc By similarity
	Metal binding	555	1	Zinc By similarity
Natural variations
	Natural variant	44	1	A → T. Corresponds to variant rs3793733 [ dbSNP | Ensembl ].		VAR_020438
	Natural variant	210	1	T → M in a colorectal cancer sample; somatic mutation. Ref.4		VAR_035806
	Natural variant	512	1	V → I in a colorectal cancer sample; somatic mutation. Ref.4		VAR_035807
	Natural variant	626	1	A → T. Ref.3 Corresponds to variant rs2271275 [ dbSNP | Ensembl ].		VAR_048726

Sequences

	Sequence		Length	Mass (Da)
	Q9NS39 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: A158A81D35894F79	FASTA	739	80,621
	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

References

	« Hide 'large scale' referencesShow '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: 10836796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, 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. , 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: 15164054] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-626.
[4]	"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. , 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: 16959974] [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.
IPI	IPI00033017.
RefSeq	NP_061172.1. NM_018702.3.
UniGene	Hs.586663. Hs.657984. Hs.730397.
3D structure databases
ProteinModelPortal	Q9NS39.
SMR	Q9NS39. Positions 121-738.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NS39. 1 interaction.
STRING	Q9NS39.
Polymorphism databases
DMDM	33112436.
2D gel databases
SWISS-2DPAGE	Q9NS39.
Proteomic databases
PRIDE	Q9NS39.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381312; ENSP00000370713; ENSG00000185736.
GeneID	105.
KEGG	hsa:105.
UCSC	uc009xhq.1. human.
Organism-specific databases
CTD	105.
GeneCards	GC10M001219.
H-InvDB	HIX0008591.
HGNC	HGNC:227. ADARB2.
HPA	HPA031332. HPA031333.
MIM	602065. gene.
neXtProt	NX_Q9NS39.
PharmGKB	PA24557.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06535.
GeneTree	ENSGT00550000074412.
HOGENOM	HBG314788.
HOVERGEN	HBG003836.
InParanoid	Q9NS39.
OMA	PNACQAH.
OrthoDB	EOG46143H.
PhylomeDB	Q9NS39.
Gene expression databases
ArrayExpress	Q9NS39.
Bgee	Q9NS39.
CleanEx	HS_ADARB2.
Genevestigator	Q9NS39.
GermOnline	ENSG00000185736. Homo sapiens.
Family and domain databases
InterPro	IPR002466. A_deamin. IPR001159. Ds-RNA-bd. IPR014720. dsRNA-bd-like. [Graphical view]
Gene3D	G3DSA:3.30.160.20. dsRNA-bd-like. 2 hits.
KO	K13194.
Pfam	PF02137. A_deamin. 1 hit. PF00035. dsrm. 2 hits. [Graphical view]
SMART	SM00552. ADEAMc. 1 hit. SM00358. DSRM. 2 hits. [Graphical view]
PROSITE	PS50141. A_DEAMIN_EDITASE. 1 hit. PS50137. DS_RBD. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	409.
SOURCE	Search...

Entry information

Entry name

RED2_HUMAN

Accession

Primary (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:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.