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P78563 (RED1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Double-stranded RNA-specific editase 1
EC=3.5.-.-
Alternative name(s):
RNA-editing deaminase 1
RNA-editing enzyme 1
dsRNA adenosine deaminase
Gene names
Name:ADARB1
Synonyms:ADAR2, DRADA2, RED1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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.

Tissue specificity

Highly expressed in brain and heart and at lower levels in placenta. Fair expression in lung, liver and kikney. Detected in brain, heart, kidney, lung and liver (at protein level). Isoform 5 is high expressed in hippocampus and colon. Ref.1 Ref.9

Sequence similarities

Contains 1 A to I editase domain.

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

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P78563-1)

Also known as: RED1-L; DRADA2B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
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.
Isoform 2 (identifier: P78563-2)

Also known as: RED1-S; DRADA2A;

The sequence of this isoform differs from the canonical sequence as follows:
     466-505: Missing.
Note: Has a higher catalytic activity than isoform 1.
Isoform 3 (identifier: P78563-3)

Also known as: DRADA2C;

The sequence of this isoform differs from the canonical sequence as follows:
     713-741: ARLFTAFIKAGLGAWVEKPTEQDQFSLTP → VH
Isoform 4 (identifier: P78563-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKIPRMKTPCQPDRNSLRQSRNPQKYFA
     466-505: Missing.
Isoform 5 (identifier: P78563-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGTFFSVMGRRYKRRRKKRSERKDRNSLRQSRNPQKYFAM
     26-741: Missing.
Note: Incomplete sequence. Alternative 5'exon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 741741Double-stranded RNA-specific editase 1
PRO_0000171779

Regions

Domain78 – 14467DRBM 1
Domain231 – 29868DRBM 2
Domain370 – 737368A to I editase
Region83 – 886Interaction with substrate RNA By similarity
Region104 – 1052Interaction with substrate RNA By similarity
Region237 – 2426Interaction with substrate RNA By similarity
Region2591Interaction with substrate RNA By similarity

Sites

Active site3961Proton donor
Metal binding3941Zinc
Metal binding4511Zinc
Metal binding5561Zinc
Binding site4001Inositol hexakisphosphate
Binding site4011Inositol hexakisphosphate
Binding site5591Inositol hexakisphosphate
Binding site5621Inositol hexakisphosphate
Binding site6691Inositol hexakisphosphate
Binding site7021Inositol hexakisphosphate
Binding site7121Inositol hexakisphosphate
Binding site7301Inositol hexakisphosphate

Amino acid modifications

Modified residue261Phosphoserine Ref.11 Ref.12

Natural variations

Alternative sequence11M → MKIPRMKTPCQPDRNSLRQS RNPQKYFA in isoform 4.
VSP_019597
Alternative sequence11M → MGTFFSVMGRRYKRRRKKRS ERKDRNSLRQSRNPQKYFAM in isoform 5.
VSP_041421
Alternative sequence26 – 741716Missing in isoform 5.
VSP_041422
Alternative sequence466 – 50540Missing in isoform 2 and isoform 4.
VSP_000865
Alternative sequence713 – 74129ARLFT…FSLTP → VH in isoform 3.
VSP_000866

Experimental info

Sequence conflict301G → A in AAB58300. Ref.4
Sequence conflict301G → A in AAM83100. Ref.5
Sequence conflict301G → A in AAN10291. Ref.5
Sequence conflict4231R → E in AAB58300. Ref.4
Sequence conflict4231R → E in AAM83100. Ref.5
Sequence conflict4231R → E in AAN10291. Ref.5
Sequence conflict4751V → L in AAM83100. Ref.5
Sequence conflict4751V → L in AAN10291. Ref.5

Secondary structure

1 ........................................................... 741
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RED1-L) (DRADA2B) [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 02B583414DD59C20

FASTA74180,763
        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

« Hide

Isoform 2 (RED1-S) (DRADA2A) [UniParc].

Checksum: 12D26888C1F131B6
Show »

FASTA70176,633
Isoform 3 (DRADA2C) [UniParc].

Checksum: 10F6C71FFB641CFE
Show »

FASTA71477,795
Isoform 4 [UniParc].

Checksum: F1C025263B9D3F3F
Show »

FASTA72879,876
Isoform 5 [UniParc].

Checksum: F931D8FC8850764D
Show »

FASTA647,778

References

« Hide 'large scale' references
[1]"Two forms of human double-stranded RNA-specific editase 1 (hRED1) generated by the insertion of an Alu cassette."
Gerber A., O'Connell M.A., Keller W.
RNA 3:453-463(1997) [PubMed: 9149227] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, CATALYTIC ACTIVITY.
Tissue: Brain.
[2]"Cloning of a human RNA editing deaminase (ADARB1) of glutamate receptors that maps to chromosome 21q22.3."
Mittaz L., Scott H.S., Rossier C., Seeburg P.H., Higuchi M., Antonarakis S.E.
Genomics 41:210-217(1997) [PubMed: 9143496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Fetal brain.
[3]"Editing of glutamate receptor B subunit ion channel RNAs by four alternatively spliced DRADA2 double-stranded RNA adenosine deaminases."
Lai F., Chen C.-X., Carter K.C., Nishikura K.
Mol. Cell. Biol. 17:2413-2424(1997) [PubMed: 9111310] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[4]"Map location, genomic organization and expression patterns of the human RED1 RNA editase."
Villard L., Tassone F., Haymowicz M., Welborn R., Gardiner K.
Somat. Cell Mol. Genet. 23:135-145(1997) [PubMed: 9330641] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Phylogenetic comparison of the pre-mRNA adenosine deaminase ADAR2 genes and transcripts: conservation and diversity in editing site sequence and alternative splicing patterns."
Slavov D., Gardiner K.
Gene 299:83-94(2002) [PubMed: 12459255] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[6]"Novel splice variants of human ADAR2 mRNA: skipping of the exon encoding the dsRNA-binding domains, and multiple C-terminal splice sites."
Kawahara Y., Ito K., Ito M., Tsuji S., Kwak S.
Gene 363:193-201(2005) [PubMed: 16297572] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]"The DNA sequence of human chromosome 21."
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. expand/collapse author list , 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.
Nature 405:311-319(2000) [PubMed: 10830953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"Novel exon of mammalian ADAR2 extends open reading frame."
Maas S., Gommans W.M.
PLoS ONE 4:E4225-E4225(2009) [PubMed: 19156214] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY.
[10]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed: 14759258] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[11]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing."
Macbeth M.R., Schubert H.L., Vandemark A.P., Lingam A.T., Hill C.P., Bass B.L.
Science 309:1534-1539(2005) [PubMed: 16141067] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 299-741 IN COMPLEX WITH IP6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U82120 mRNA. Translation: AAB61686.1.
U82121 mRNA. Translation: AAB61687.1.
X99227 mRNA. Translation: CAA67611.1.
X99383 mRNA. Translation: CAA67762.1.
U76420 mRNA. Translation: AAC51240.1.
U76421 mRNA. Translation: AAC51241.1.
U76422 mRNA. Translation: AAC51242.1.
AF001042 mRNA. Translation: AAB58300.1.
AF525422 mRNA. Translation: AAM83100.1.
AY135659 mRNA. Translation: AAN10291.1.
AB194370 mRNA. Translation: BAE16326.1.
AB194371 mRNA. Translation: BAE16327.1.
AB194372 mRNA. Translation: BAE16328.1.
AL163301 Genomic DNA. Translation: CAB90493.1.
AP001579 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09359.1.
CH471079 Genomic DNA. Translation: EAX09360.1.
FJ169505 mRNA. Translation: ACN49026.1.
IPIIPI00020368.
IPI00184874.
IPI00334613.
IPI00477012.
IPI01019091.
RefSeqNP_001103.1. NM_001112.3.
NP_056648.1. NM_015833.3.
NP_056649.1. NM_015834.3.
UniGeneHs.474018.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZY7X-ray1.70A/B299-741[»]
ProteinModelPortalP78563.
SMRP78563. Positions 74-301, 306-740.
ModBaseSearch...

Protein-protein interaction databases

IntActP78563. 1 interaction.
STRINGP78563.

PTM databases

PhosphoSiteP78563.

Polymorphism databases

DMDM2829669.

Proteomic databases

PRIDEP78563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360697; ENSP00000353920; ENSG00000197381.
GeneID104.
KEGGhsa:104.
UCSCuc002zgr.2. human.
uc002zgt.2. human.
uc002zgy.2. human.

Organism-specific databases

CTD104.
GeneCardsGC21P046493.
HGNCHGNC:226. ADARB1.
HPAHPA018277.
HPA029645.
MIM601218. gene.
neXtProtNX_P78563.
PharmGKBPA24556.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292433.
GeneTreeENSGT00550000074412.
HOVERGENHBG003836.
InParanoidP78563.
KOK13194.
OMADEENMSS.

Enzyme and pathway databases

ReactomeREACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP78563.
BgeeP78563.
GenevestigatorP78563.
GermOnlineENSG00000197381. Homo sapiens.

Family and domain databases

Gene3DG3DSA:3.30.160.20. dsRNA-bd-like. 2 hits.
InterProIPR002466. A_deamin.
IPR008996. Cytokine_IL1-like.
IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like.
[Graphical view]
PfamPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[Graphical view]
SMARTSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
SUPFAMSSF50353. Cytok_IL1_like. 1 hit.
PROSITEPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP78563.
NextBio399.
SOURCESearch...

Entry information

Entry nameRED1_HUMAN
AccessionPrimary (citable) accession number: P78563
Secondary accession number(s): A6NFK8 expand/collapse secondary AC list , A6NJ84, C3TTQ1, O00395, O00465, O00691, O00692, P78555, Q4AE79, Q8NFD1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: May 16, 2012
This is version 118 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

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents