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P78563 (RED1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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=3.5.4.37
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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

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. Ref.12 Ref.16 Ref.19

Catalytic activity

Adenine in double-stranded RNA + H2O = hypoxanthine in double-stranded RNA + NH3. Ref.1 Ref.25

Cofactor

Binds 1 inositol hexakisphosphate (IP6) per subunit.

Subunit structure

Homodimer. Homodimerization is essential for its catalytic activity. Can form heterodimers with isoform 5 of ADAR/ADAR1. Ref.12

Subcellular location

Nucleus. Nucleusnucleolus. Note: Shuttles between nucleoli and the nucleoplasm. Ref.12 Ref.19

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. Ref.1 Ref.10 Ref.12

Sequence similarities

Contains 1 A to I editase domain.

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

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
mRNA processing
   Cellular componentNucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DomainRepeat
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Inferred from direct assay Ref.1. Source: HGNC

adenosine to inosine editing

Inferred from direct assay Ref.12Ref.19. Source: UniProtKB

base conversion or substitution editing

Inferred by curator Ref.1. Source: HGNC

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

gene expression

Traceable author statement. Source: Reactome

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA modification

Traceable author statement. Source: Reactome

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell migration

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of viral genome replication

Inferred from mutant phenotype Ref.19. Source: UniProtKB

regulation of cell cycle

Inferred from direct assay Ref.12. Source: UniProtKB

   Cellular_componentnucleolus

Inferred from direct assay Ref.12Ref.19. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 8995285. Source: HGNC

   Molecular_functionRNA binding

Inferred from direct assay Ref.3. Source: HGNC

adenosine deaminase activity

Inferred from electronic annotation. Source: InterPro

double-stranded RNA adenosine deaminase activity

Inferred from direct assay PubMed 8995285Ref.1. Source: HGNC

double-stranded RNA binding

Inferred from direct assay PubMed 8995285. Source: HGNC

mRNA binding

Traceable author statement Ref.1. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21847096. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative promoter usage and 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 → MKIPRMKTPCQPDRNSLRQSRNPQKYFAM
     466-505: Missing.
Isoform 5 (identifier: P78563-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGTFFSVMGRRYKRRRKKRSERKDRNSLRQSRNPQKYFAM
Note: Likely expressed from an alternative promoter. Contains a region highly similar to the so-called ssRNA-binding R-domain of ADARB2.

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.17

Natural variations

Alternative sequence11M → MKIPRMKTPCQPDRNSLRQS RNPQKYFAM in isoform 4.
VSP_019597
Alternative sequence11M → MGTFFSVMGRRYKRRRKKRS ERKDRNSLRQSRNPQKYFAM in isoform 5.
VSP_041421
Alternative sequence466 – 50540Missing in isoform 2 and isoform 4.
VSP_000865
Alternative sequence713 – 74129ARLFT…FSLTP → VH in isoform 3.
VSP_000866
Natural variant2241V → A. Ref.9
Corresponds to variant rs199697177 [ dbSNP | Ensembl ].
VAR_070931

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

........................................................... 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: BAB59C894273C4E8
Show »

FASTA72980,007
Isoform 5 [UniParc].

Checksum: B7637CEA1D2E19E6
Show »

FASTA78085,669

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"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] (ISOFORM 2), VARIANT ALA-224.
Tissue: Testis.
[10]"Novel exon of mammalian ADAR2 extends open reading frame."
Maas S., Gommans W.M.
PLoS ONE 4:E4225-E4225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-64 (ISOFORM 5), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY.
[11]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[12]"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: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Functions and regulation of RNA editing by ADAR deaminases."
Nishikura K.
Annu. Rev. Biochem. 79:321-349(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"Human BLCAP transcript: new editing events in normal and cancerous tissues."
Galeano F., Leroy A., Rossetti C., Gromova I., Gautier P., Keegan L.P., Massimi L., Di Rocco C., O'Connell M.A., Gallo A.
Int. J. Cancer 127:127-137(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"RNA editing catalyzed by ADAR1 and its function in mammalian cells."
Wang Q.
Biochemistry (Mosc.) 76:900-911(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[19]"ADAR2 editing enzyme is a novel human immunodeficiency virus-1 proviral factor."
Doria M., Tomaselli S., Neri F., Ciafre S.A., Farace M.G., Michienzi A., Gallo A.
J. Gen. Virol. 92:1228-1232(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]"Adenosine deaminases acting on RNA, RNA editing, and interferon action."
George C.X., Gan Z., Liu Y., Samuel C.E.
J. Interferon Cytokine Res. 31:99-117(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[21]"Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral."
Samuel C.E.
Virology 411:180-193(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[22]"A-to-I editing of protein coding and noncoding RNAs."
Mallela A., Nishikura K.
Crit. Rev. Biochem. Mol. Biol. 47:493-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[23]"ADAR proteins: structure and catalytic mechanism."
Goodman R.A., Macbeth M.R., Beal P.A.
Curr. Top. Microbiol. Immunol. 353:1-33(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[24]"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.
[25]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 299-741 IN COMPLEX WITH IP6, CATALYTIC ACTIVITY.
+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.
AL133499 Genomic DNA. No translation available.
AP001579 Genomic DNA. No translation available.
BX322560 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09357.1.
CH471079 Genomic DNA. Translation: EAX09359.1.
CH471079 Genomic DNA. Translation: EAX09360.1.
BC065545 mRNA. Translation: AAH65545.1.
FJ169506 mRNA. Translation: ACN49027.1.
CCDSCCDS33589.1. [P78563-1]
CCDS33590.1. [P78563-2]
CCDS42970.1. [P78563-3]
RefSeqNP_001103.1. NM_001112.3. [P78563-2]
NP_056648.1. NM_015833.3. [P78563-1]
NP_056649.1. NM_015834.3. [P78563-3]
XP_006724019.1. XM_006723956.1. [P78563-1]
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...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106618. 6 interactions.
IntActP78563. 3 interactions.
MINTMINT-3023320.

PTM databases

PhosphoSiteP78563.

Polymorphism databases

DMDM2829669.

Proteomic databases

MaxQBP78563.
PaxDbP78563.
PRIDEP78563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348831; ENSP00000015877; ENSG00000197381. [P78563-2]
ENST00000360697; ENSP00000353920; ENSG00000197381. [P78563-1]
ENST00000389861; ENSP00000374511; ENSG00000197381.
ENST00000389863; ENSP00000374513; ENSG00000197381. [P78563-3]
ENST00000492414; ENSP00000436367; ENSG00000197381. [P78563-2]
ENST00000496664; ENSP00000435381; ENSG00000197381. [P78563-1]
ENST00000539173; ENSP00000441897; ENSG00000197381. [P78563-1]
GeneID104.
KEGGhsa:104.
UCSCuc002zgr.2. human. [P78563-3]
uc002zgt.2. human. [P78563-2]
uc002zgy.2. human. [P78563-1]

Organism-specific databases

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

Phylogenomic databases

eggNOGNOG292433.
HOVERGENHBG003836.
InParanoidP78563.
KOK13194.
OMAFPDTLFN.
PhylomeDBP78563.
TreeFamTF315806.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP78563.
BgeeP78563.
GenevestigatorP78563.

Family and domain databases

Gene3D3.30.160.20. 2 hits.
InterProIPR002466. A_deamin.
IPR008996. Cytokine_IL1-like.
IPR014720. dsRNA-bd_dom.
IPR029484. GVQW.
[Graphical view]
PfamPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
PF13900. GVQW. 1 hit.
[Graphical view]
SMARTSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP78563.
GeneWikiADARB1.
GenomeRNAi104.
NextBio35482593.
PROP78563.
SOURCESearch...

Entry information

Entry nameRED1_HUMAN
AccessionPrimary (citable) accession number: P78563
Secondary accession number(s): A6NFK8 expand/collapse secondary AC list , A6NJ84, C3TTQ1, C3TTQ2, C9JUP4, G5E9B4, O00395, O00465, O00691, O00692, P78555, Q4AE79, Q6P0M9, Q8NFD1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 140 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 21

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