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P55265

- DSRAD_HUMAN

UniProt

P55265 - DSRAD_HUMAN

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Protein
Double-stranded RNA-specific adenosine deaminase
Gene
ADAR, ADAR1, DSRAD, G1P1, IFI4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication.10 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi910 – 9101Zinc By similarity
Active sitei912 – 9121Proton donor By similarity
Metal bindingi966 – 9661Zinc By similarity
Metal bindingi1036 – 10361Zinc By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi169 – 19527
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. double-stranded RNA adenosine deaminase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: IntAct

GO - Biological processi

  1. adenosine to inosine editing Source: UniProtKB
  2. base conversion or substitution editing Source: MGI
  3. cytokine-mediated signaling pathway Source: Reactome
  4. defense response to virus Source: UniProtKB-KW
  5. gene expression Source: Reactome
  6. gene silencing by RNA Source: UniProtKB-KW
  7. innate immune response Source: UniProtKB
  8. mRNA modification Source: Reactome
  9. mRNA processing Source: UniProtKB-KW
  10. negative regulation of apoptotic process Source: Ensembl
  11. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  12. positive regulation of viral genome replication Source: UniProtKB
  13. protein export from nucleus Source: UniProtKB
  14. protein import into nucleus Source: UniProtKB
  15. response to interferon-alpha Source: UniProtKB
  16. response to virus Source: UniProtKB
  17. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, mRNA processing, RNA-mediated gene silencing

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1231. C6 deamination of adenosine.
REACT_1966. Formation of editosomes by ADAR proteins.
REACT_25162. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Double-stranded RNA-specific adenosine deaminase (EC:3.5.4.37)
Short name:
DRADA
Alternative name(s):
136 kDa double-stranded RNA-binding protein
Short name:
p136
Interferon-inducible protein 4
Short name:
IFI-4
K88DSRBP
Gene namesi
Name:ADAR
Synonyms:ADAR1, DSRAD, G1P1, IFI4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:225. ADAR.

Subcellular locationi

Isoform 1 : Cytoplasm. Nucleus
Note: Shuttles between the cytoplasm and nucleus.3 Publications
Isoform 5 : Cytoplasm. Nucleus. Nucleusnucleolus
Note: Predominantly nuclear but can shuttle between nucleus and cytoplasm. TNPO1 can mediate its nuclear import whereas XPO1 can mediate its nuclear export.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleolus Source: UniProtKB-SubCell
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. supraspliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Dyschromatosis symmetrica hereditaria (DSH) [MIM:127400]: An autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed on the face and the dorsal parts of the hands and feet, that appear in infancy or early childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti923 – 9231L → P in DSH. 1 Publication
Corresponds to variant rs28936680 [ dbSNP | Ensembl ].
VAR_017604
Natural varianti966 – 9661C → F in DSH. 1 Publication
VAR_021729
Natural varianti1155 – 11551R → W in DSH. 1 Publication
VAR_026669
Natural varianti1165 – 11651F → S in DSH. 1 Publication
Corresponds to variant rs28936681 [ dbSNP | Ensembl ].
VAR_017605
Aicardi-Goutieres syndrome 6 (AGS6) [MIM:615010]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti193 – 1931P → A in AGS6. 1 Publication
VAR_069535
Natural varianti870 – 8701A → T in AGS6. 1 Publication
VAR_069536
Natural varianti872 – 8721I → T in AGS6. 1 Publication
VAR_069537
Natural varianti892 – 8921R → H in AGS6. 1 Publication
VAR_069538
Natural varianti999 – 9991K → N in AGS6. 1 Publication
VAR_069539
Natural varianti1007 – 10071G → R in AGS6. 1 Publication
VAR_069540
Natural varianti1112 – 11121Y → F in AGS6. 1 Publication
VAR_069541
Natural varianti1113 – 11131D → H in AGS6. 1 Publication
VAR_069542

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi418 – 4181K → R: Abolishes sumoylation. 1 Publication

Keywords - Diseasei

Aicardi-Goutieres syndrome, Disease mutation

Organism-specific databases

MIMi127400. phenotype.
615010. phenotype.
Orphaneti51. Aicardi-Goutieres syndrome.
41. Dyschromatosis symmetrica hereditaria.
225154. Familial infantile bilateral striatal necrosis.
PharmGKBiPA24555.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12261226Double-stranded RNA-specific adenosine deaminase
PRO_0000171774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki418 – 418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei601 – 6011Phosphothreonine2 Publications
Modified residuei614 – 6141Phosphoserine1 Publication
Modified residuei808 – 8081Phosphothreonine5 Publications
Modified residuei823 – 8231Phosphoserine1 Publication
Modified residuei825 – 8251Phosphoserine3 Publications

Post-translational modificationi

Sumoylation reduces RNA-editing activity.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP55265.
PaxDbiP55265.
PRIDEiP55265.

PTM databases

PhosphoSiteiP55265.

Miscellaneous databases

PMAP-CutDBP55265.

Expressioni

Tissue specificityi

Ubiquitously expressed, highest levels were found in brain and lung. Isoform 5 is expressed at higher levels in astrocytomas as compared to normal brain tissue and expression increases strikingly with the severity of the tumor, being higher in the most aggressive tumors.1 Publication

Inductioni

Isoform 1 is induced by interferon alpha. Isoform 5 is constitutively expressed.1 Publication

Gene expression databases

ArrayExpressiP55265.
BgeeiP55265.
CleanExiHS_ADAR.
GenevestigatoriP55265.

Organism-specific databases

HPAiCAB056157.
HPA003890.

Interactioni

Subunit structurei

Homodimer. Homodimerization is essential for its catalytic activity. Isoform 5 can form heterodimers with ADARB1/ADAR2. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90. Binding to ILF3/NF90 up-regulates ILF3-mediated gene expression. Isoform 5 (via DRBM 3 domain) interacts with TNPO1. Isoform 5 (via DRBM domains) interacts with XPO5. Isoform 1 and isoform 5 can interact with EIF2AK2/PKR and UPF1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB83EBI-2462104,EBI-6858501From a different organism.
DICER1Q9UPY38EBI-6913210,EBI-395506
TARBP2Q156333EBI-6913210,EBI-978581

Protein-protein interaction databases

BioGridi106617. 34 interactions.
DIPiDIP-29310N.
IntActiP55265. 13 interactions.
MINTiMINT-4531596.
STRINGi9606.ENSP00000357459.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi127 – 1304
Helixi135 – 15016
Beta strandi152 – 1543
Helixi158 – 1658
Helixi169 – 18113
Beta strandi184 – 1929
Beta strandi194 – 1974
Helixi294 – 30916
Helixi315 – 3228
Helixi324 – 3263
Helixi327 – 33913
Beta strandi342 – 3465
Beta strandi348 – 3503
Beta strandi352 – 3554
Helixi357 – 3604
Turni361 – 3633
Helixi716 – 7249
Helixi727 – 73812
Beta strandi742 – 7498
Beta strandi758 – 7647
Beta strandi767 – 77610
Helixi777 – 79620

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QBJX-ray2.10A/B/C133-209[»]
1QGPNMR-A125-200[»]
1XMKX-ray0.97A294-366[»]
2ACJX-ray2.60A/B/C/D140-202[»]
2GXBX-ray2.25A/B140-202[»]
2L54NMR-A136-198[»]
2MDRNMR-A708-801[»]
3F21X-ray2.20A/B/C133-209[»]
3F22X-ray2.50A/B/C133-209[»]
3F23X-ray2.70A/B/C133-209[»]
3IRQX-ray2.80A/B/C/D140-202[»]
3IRRX-ray2.65A/B/C/D140-202[»]
ProteinModelPortaliP55265.
SMRiP55265. Positions 134-199, 294-366, 511-575, 612-681, 731-797.

Miscellaneous databases

EvolutionaryTraceiP55265.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati133 – 20270DRADA 1
Add
BLAST
Repeati293 – 36068DRADA 2
Add
BLAST
Domaini503 – 57169DRBM 1
Add
BLAST
Domaini614 – 68269DRBM 2
Add
BLAST
Domaini726 – 79469DRBM 3
Add
BLAST
Domaini886 – 1221336A to I editase
Add
BLAST

Sequence similaritiesi

Contains 2 DRADA repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG292433.
HOVERGENiHBG067087.
KOiK12968.
OrthoDBiEOG7VHSX4.
PhylomeDBiP55265.
TreeFamiTF315806.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
3.30.160.20. 3 hits.
InterProiIPR002466. A_deamin.
IPR014720. dsRNA-bd_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view]
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1 (identifier: P55265-1) [UniParc]FASTAAdd to Basket

Also known as: ADAR-a, ADAR1L, p150

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.

« Hide

MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ     50
LPEAPVIGKQ TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR 100
SQGLQRGFQH PSPRGRSLPQ RGVDCLSSHF QELSIYQDQE QRILKFLEEL 150
GEGKATTAHD LSGKLGTPKK EINRVLYSLA KKGKLQKEAG TPPLWKIAVS 200
TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED LLEPFIAVSA 250
QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK 300
EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP 350
PIWHLTDKKR ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS 400
NNMVTTEKVE NGQEPVIKLE NRQEARPEPA RLKPPVHYNG PSKAGYVDFE 450
NGQWATDDIP DDLNSIRAAP GEFRAIMEMP SFYSHGLPRC SPYKKLTECQ 500
LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV INGREFPPAE 550
AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ 600
TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV 650
AVGAQTFPSV SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQPEGMISE 700
SLDNLESMMP NKVRKIGELV RYLNTNPVGG LLEYARSHGF AAEFKLVDQS 750
GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG KQEAADAALR VLIGENEKAE 800
RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF HDQIAMLSHR 850
CFNTLTNSFQ PSLLGRKILA AIIMKKDSED MGVVVSLGTG NRCVKGDSLS 900
LKGETVNDCH AEIISRRGFI RFLYSELMKY NSQTAKDSIF EPAKGGEKLQ 950
IKKTVSFHLY ISTAPCGDGA LFDKSCSDRA MESTESRHYP VFENPKQGKL 1000
RTKVENGEGT IPVESSDIVP TWDGIRLGER LRTMSCSDKI LRWNVLGLQG 1050
ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI CCRVTRDGSA FEDGLRHPFI 1100
VNHPKVGRVS IYDSKRQSGK TKETSVNWCL ADGYDLEILD GTRGTVDGPR 1150
NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK 1200
KGLKDMGYGN WISKPQEEKN FYLCPV 1226

Note: Produced by alternative promoter usage.

Length:1,226
Mass (Da):136,066
Last modified:November 30, 2010 - v4
Checksum:i9CE095D6F9C1BC79
GO
Isoform 2 (identifier: P55265-2) [UniParc]FASTAAdd to Basket

Also known as: ADAR-b

The sequence of this isoform differs from the canonical sequence as follows:
     807-832: Missing.

Note: Produced by alternative splicing of isoform 1.

Show »
Length:1,200
Mass (Da):133,274
Checksum:i4CB1B306DAC584FC
GO
Isoform 3 (identifier: P55265-3) [UniParc]FASTAAdd to Basket

Also known as: ADAR-c

The sequence of this isoform differs from the canonical sequence as follows:
     694-712: Missing.
     807-832: Missing.

Note: Produced by alternative splicing of isoform 1.

Show »
Length:1,181
Mass (Da):131,170
Checksum:i9764C8AB27BE118E
GO
Isoform 4 (identifier: P55265-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MNPRQ → MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPEEVQDP

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available. The N-terminus has been derived from EST and genomic sequences.

Show »
Length:1,269
Mass (Da):140,838
Checksum:iBB9B1DF19B8D3BC8
GO
Isoform 5 (identifier: P55265-5) [UniParc]FASTAAdd to Basket

Also known as: ADAR1S, p110

The sequence of this isoform differs from the canonical sequence as follows:
     1-295: Missing.

Note: Produced by alternative promoter usage.

Show »
Length:931
Mass (Da):103,642
Checksum:i113B63CF165097FC
GO

Sequence cautioni

The sequence CAE45853.1 differs from that shown. Reason: Erroneous termination at position 1227. Translated as stop.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001R → G.6 Publications
Corresponds to variant rs1466731 [ dbSNP | Ensembl ].
VAR_048725
Natural varianti193 – 1931P → A in AGS6. 1 Publication
VAR_069535
Natural varianti384 – 3841K → R.4 Publications
Corresponds to variant rs2229857 [ dbSNP | Ensembl ].
VAR_017240
Natural varianti587 – 5871Y → C.
Corresponds to variant rs17843865 [ dbSNP | Ensembl ].
VAR_024407
Natural varianti806 – 8061E → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035805
Natural varianti870 – 8701A → T in AGS6. 1 Publication
VAR_069536
Natural varianti872 – 8721I → T in AGS6. 1 Publication
VAR_069537
Natural varianti892 – 8921R → H in AGS6. 1 Publication
VAR_069538
Natural varianti923 – 9231L → P in DSH. 1 Publication
Corresponds to variant rs28936680 [ dbSNP | Ensembl ].
VAR_017604
Natural varianti966 – 9661C → F in DSH. 1 Publication
VAR_021729
Natural varianti999 – 9991K → N in AGS6. 1 Publication
VAR_069539
Natural varianti1007 – 10071G → R in AGS6. 1 Publication
VAR_069540
Natural varianti1112 – 11121Y → F in AGS6. 1 Publication
VAR_069541
Natural varianti1113 – 11131D → H in AGS6. 1 Publication
VAR_069542
Natural varianti1155 – 11551R → W in DSH. 1 Publication
VAR_026669
Natural varianti1165 – 11651F → S in DSH. 1 Publication
Corresponds to variant rs28936681 [ dbSNP | Ensembl ].
VAR_017605

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 295295Missing in isoform 5.
VSP_019235Add
BLAST
Alternative sequencei1 – 55MNPRQ → MMSPICDQTIDSRLKVEKAT WWGRVGGGSRPHWQPPGVRP CPEEVQDP in isoform 4.
VSP_008872
Alternative sequencei694 – 71219Missing in isoform 3.
VSP_008873Add
BLAST
Alternative sequencei807 – 83226Missing in isoform 2 and isoform 3.
VSP_008874Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531E → G in CAA55968. 1 Publication
Sequence conflicti245 – 2451F → L in CAE45853. 1 Publication
Sequence conflicti482 – 4821F → L in CAE45853. 1 Publication
Sequence conflicti873 – 8731I → V in CAE45853. 1 Publication
Sequence conflicti1093 – 10931D → G in CAE45853. 1 Publication
Sequence conflicti1184 – 11841E → K in CAA55967. 1 Publication
Sequence conflicti1184 – 11841E → K in CAA55968. 1 Publication
Sequence conflicti1184 – 11841E → K in CAA67169. 1 Publication
Sequence conflicti1184 – 11841E → K in CAA67170. 1 Publication
Isoform 4 (identifier: P55265-4)
Sequence conflicti13 – 131R → G in CAE45853. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10439 mRNA. Translation: AAB06697.1.
U75503
, U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97116.1.
U75503
, U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97117.1.
U75503
, U75489, U75490, U75491, U75492, U75493, U75494, U75495, U75496, U75497, U75498, U75499, U75500, U75501, U75502 Genomic DNA. Translation: AAB97118.1.
U18121 mRNA. Translation: AAC13782.1.
X79448 mRNA. Translation: CAA55967.1.
X79449 mRNA. Translation: CAA55968.1.
X98559 mRNA. Translation: CAA67169.1.
X98559 mRNA. Translation: CAA67170.1.
BX538232 mRNA. Translation: CAD98075.1.
BX640741 mRNA. Translation: CAE45853.1. Sequence problems.
AL606500, AL592078, AL691488 Genomic DNA. Translation: CAH71907.1.
AL606500, AL592078, AL691488 Genomic DNA. Translation: CAH71908.1.
AL592078, AL606500, AL691488 Genomic DNA. Translation: CAI16183.1.
AL592078, AL606500, AL691488 Genomic DNA. Translation: CAI16185.1.
AL691488, AL592078, AL606500 Genomic DNA. Translation: CAI17375.1.
AL691488, AL592078, AL606500 Genomic DNA. Translation: CAI17376.1.
CH471121 Genomic DNA. Translation: EAW53183.1.
CH471121 Genomic DNA. Translation: EAW53187.1.
BC038227 mRNA. Translation: AAH38227.1.
CCDSiCCDS1071.1. [P55265-1]
CCDS30879.1. [P55265-5]
PIRiS65593.
RefSeqiNP_001020278.1. NM_001025107.2. [P55265-5]
NP_001102.2. NM_001111.4.
NP_001180424.1. NM_001193495.1. [P55265-5]
NP_056655.2. NM_015840.3.
NP_056656.2. NM_015841.3.
XP_006711174.1. XM_006711111.1. [P55265-5]
XP_006711175.1. XM_006711112.1. [P55265-5]
XP_006711176.1. XM_006711113.1. [P55265-5]
UniGeneiHs.12341.

Genome annotation databases

EnsembliENST00000368471; ENSP00000357456; ENSG00000160710. [P55265-5]
ENST00000368474; ENSP00000357459; ENSG00000160710. [P55265-1]
GeneIDi103.
KEGGihsa:103.
UCSCiuc001ffh.3. human. [P55265-1]
uc001ffi.3. human. [P55265-2]
uc001ffj.3. human. [P55265-3]

Polymorphism databases

DMDMi313104303.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10439 mRNA. Translation: AAB06697.1 .
U75503
, U75489 , U75490 , U75491 , U75492 , U75493 , U75494 , U75495 , U75496 , U75497 , U75498 , U75499 , U75500 , U75501 , U75502 Genomic DNA. Translation: AAB97116.1 .
U75503
, U75489 , U75490 , U75491 , U75492 , U75493 , U75494 , U75495 , U75496 , U75497 , U75498 , U75499 , U75500 , U75501 , U75502 Genomic DNA. Translation: AAB97117.1 .
U75503
, U75489 , U75490 , U75491 , U75492 , U75493 , U75494 , U75495 , U75496 , U75497 , U75498 , U75499 , U75500 , U75501 , U75502 Genomic DNA. Translation: AAB97118.1 .
U18121 mRNA. Translation: AAC13782.1 .
X79448 mRNA. Translation: CAA55967.1 .
X79449 mRNA. Translation: CAA55968.1 .
X98559 mRNA. Translation: CAA67169.1 .
X98559 mRNA. Translation: CAA67170.1 .
BX538232 mRNA. Translation: CAD98075.1 .
BX640741 mRNA. Translation: CAE45853.1 . Sequence problems.
AL606500 , AL592078 , AL691488 Genomic DNA. Translation: CAH71907.1 .
AL606500 , AL592078 , AL691488 Genomic DNA. Translation: CAH71908.1 .
AL592078 , AL606500 , AL691488 Genomic DNA. Translation: CAI16183.1 .
AL592078 , AL606500 , AL691488 Genomic DNA. Translation: CAI16185.1 .
AL691488 , AL592078 , AL606500 Genomic DNA. Translation: CAI17375.1 .
AL691488 , AL592078 , AL606500 Genomic DNA. Translation: CAI17376.1 .
CH471121 Genomic DNA. Translation: EAW53183.1 .
CH471121 Genomic DNA. Translation: EAW53187.1 .
BC038227 mRNA. Translation: AAH38227.1 .
CCDSi CCDS1071.1. [P55265-1 ]
CCDS30879.1. [P55265-5 ]
PIRi S65593.
RefSeqi NP_001020278.1. NM_001025107.2. [P55265-5 ]
NP_001102.2. NM_001111.4.
NP_001180424.1. NM_001193495.1. [P55265-5 ]
NP_056655.2. NM_015840.3.
NP_056656.2. NM_015841.3.
XP_006711174.1. XM_006711111.1. [P55265-5 ]
XP_006711175.1. XM_006711112.1. [P55265-5 ]
XP_006711176.1. XM_006711113.1. [P55265-5 ]
UniGenei Hs.12341.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QBJ X-ray 2.10 A/B/C 133-209 [» ]
1QGP NMR - A 125-200 [» ]
1XMK X-ray 0.97 A 294-366 [» ]
2ACJ X-ray 2.60 A/B/C/D 140-202 [» ]
2GXB X-ray 2.25 A/B 140-202 [» ]
2L54 NMR - A 136-198 [» ]
2MDR NMR - A 708-801 [» ]
3F21 X-ray 2.20 A/B/C 133-209 [» ]
3F22 X-ray 2.50 A/B/C 133-209 [» ]
3F23 X-ray 2.70 A/B/C 133-209 [» ]
3IRQ X-ray 2.80 A/B/C/D 140-202 [» ]
3IRR X-ray 2.65 A/B/C/D 140-202 [» ]
ProteinModelPortali P55265.
SMRi P55265. Positions 134-199, 294-366, 511-575, 612-681, 731-797.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106617. 34 interactions.
DIPi DIP-29310N.
IntActi P55265. 13 interactions.
MINTi MINT-4531596.
STRINGi 9606.ENSP00000357459.

PTM databases

PhosphoSitei P55265.

Polymorphism databases

DMDMi 313104303.

Proteomic databases

MaxQBi P55265.
PaxDbi P55265.
PRIDEi P55265.

Protocols and materials databases

DNASUi 103.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368471 ; ENSP00000357456 ; ENSG00000160710 . [P55265-5 ]
ENST00000368474 ; ENSP00000357459 ; ENSG00000160710 . [P55265-1 ]
GeneIDi 103.
KEGGi hsa:103.
UCSCi uc001ffh.3. human. [P55265-1 ]
uc001ffi.3. human. [P55265-2 ]
uc001ffj.3. human. [P55265-3 ]

Organism-specific databases

CTDi 103.
GeneCardsi GC01M154554.
HGNCi HGNC:225. ADAR.
HPAi CAB056157.
HPA003890.
MIMi 127400. phenotype.
146920. gene.
615010. phenotype.
neXtProti NX_P55265.
Orphaneti 51. Aicardi-Goutieres syndrome.
41. Dyschromatosis symmetrica hereditaria.
225154. Familial infantile bilateral striatal necrosis.
PharmGKBi PA24555.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292433.
HOVERGENi HBG067087.
KOi K12968.
OrthoDBi EOG7VHSX4.
PhylomeDBi P55265.
TreeFami TF315806.

Enzyme and pathway databases

Reactomei REACT_1231. C6 deamination of adenosine.
REACT_1966. Formation of editosomes by ADAR proteins.
REACT_25162. Interferon alpha/beta signaling.

Miscellaneous databases

ChiTaRSi ADAR. human.
EvolutionaryTracei P55265.
GeneWikii ADAR.
GenomeRNAii 103.
NextBioi 389.
PMAP-CutDB P55265.
PROi P55265.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55265.
Bgeei P55265.
CleanExi HS_ADAR.
Genevestigatori P55265.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
3.30.160.20. 3 hits.
InterProi IPR002466. A_deamin.
IPR014720. dsRNA-bd_dom.
IPR000607. dsRNA_A_deaminase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF02137. A_deamin. 1 hit.
PF00035. dsrm. 3 hits.
PF02295. z-alpha. 2 hits.
[Graphical view ]
SMARTi SM00552. ADEAMc. 1 hit.
SM00358. DSRM. 3 hits.
SM00550. Zalpha. 2 hits.
[Graphical view ]
PROSITEi PS50141. A_DEAMIN_EDITASE. 1 hit.
PS50139. DRADA_REPEAT. 2 hits.
PS50137. DS_RBD. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing."
    Kim U., Wang Y., Sanford T., Zeng Y., Nishikura K.
    Proc. Natl. Acad. Sci. U.S.A. 91:11457-11461(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT GLY-100.
  2. "Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase."
    Patterson J.B., Samuel C.E.
    Mol. Cell. Biol. 15:5376-5388(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-100 AND ARG-384.
    Tissue: Kidney.
  3. "Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase."
    Liu Y., George C.X., Patterson J.B., Samuel C.E.
    J. Biol. Chem. 272:4419-4428(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), VARIANTS GLY-100 AND ARG-384.
    Tissue: Placenta.
  4. "The gene coding for the interferon-inducible human dsRNA adenosine deaminase is transcribed into several messengers specifying different proteins."
    Deblandre G., Marinx O., Nols C., Defrance P., Berr P., Huez G., Caput D.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), VARIANTS GLY-100 AND ARG-384.
    Tissue: Cervix carcinoma.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS GLY-100 AND ARG-384.
    Tissue: Amygdala and Fetal kidney.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1), VARIANT GLY-100.
    Tissue: Lymph.
  9. "Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible."
    George C.X., Samuel C.E.
    Proc. Natl. Acad. Sci. U.S.A. 96:4621-4626(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE PROMOTER USAGE, INDUCTION.
  10. "Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNA."
    Cho D.-S.C., Yang W., Lee J.T., Shiekhattar R., Murray J.M., Nishikura K.
    J. Biol. Chem. 278:17093-17102(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION.
  11. Cited for: SUBCELLULAR LOCATION.
  12. "ADAR1 RNA deaminase limits short interfering RNA efficacy in mammalian cells."
    Yang W., Wang Q., Howell K.L., Lee J.T., Cho D.-S.C., Murray J.M., Nishikura K.
    J. Biol. Chem. 280:3946-3953(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "New antiviral pathway that mediates hepatitis C virus replicon interferon sensitivity through ADAR1."
    Taylor D.R., Puig M., Darnell M.E., Mihalik K., Feinstone S.M.
    J. Virol. 79:6291-6298(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: SUMOYLATION AT LYS-418, MUTAGENESIS OF LYS-418.
  15. "ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing."
    Nie Y., Ding L., Kao P.N., Braun R., Yang J.-H.
    Mol. Cell. Biol. 25:6956-6963(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ILF2 AND ILF3.
  16. "The large form of ADAR 1 is responsible for enhanced hepatitis delta virus RNA editing in interferon-alpha-stimulated host cells."
    Hartwig D., Schuette C., Warnecke J., Dorn I., Hennig H., Kirchner H., Schlenke P.
    J. Viral Hepat. 13:150-157(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus infection."
    Nie Y., Hammond G.L., Yang J.H.
    J. Virol. 81:917-923(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
  20. "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: ALTERNATIVE SPLICING, SUBUNIT, TISSUE SPECIFICITY.
  21. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-614; SER-823 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact in the cell nucleus."
    Agranat L., Raitskin O., Sperling J., Sperling R.
    Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UPF1, SUBCELLULAR LOCATION.
  24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR."
    Toth A.M., Li Z., Cattaneo R., Samuel C.E.
    J. Biol. Chem. 284:29350-29356(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "ADAR1 interacts with PKR during human immunodeficiency virus infection of lymphocytes and contributes to viral replication."
    Clerzius G., Gelinas J.F., Daher A., Bonnet M., Meurs E.F., Gatignol A.
    J. Virol. 83:10119-10128(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
  27. "RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1."
    Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., Jantsch M.F.
    Mol. Cell. Biol. 29:1487-1497(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TNFO1 AND XPO1.
  28. "Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates viral infection."
    Doria M., Neri F., Gallo A., Farace M.G., Michienzi A.
    Nucleic Acids Res. 37:5848-5858(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601 AND THR-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  30. "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.
  31. Cited for: FUNCTION.
  32. "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 THR-808 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "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.
  35. "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.
  36. "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.
  37. "Enhancement of replication of RNA viruses by ADAR1 via RNA editing and inhibition of RNA-activated protein kinase."
    Gelinas J.F., Clerzius G., Shaw E., Gatignol A.
    J. Virol. 85:8460-8466(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  38. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "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.
  40. "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.
  41. Cited for: REVIEW.
  42. "Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction of interferon by measles virus."
    Li Z., Okonski K.M., Samuel C.E.
    J. Virol. 86:3787-3794(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  43. "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.
  44. "Crystal structure of the Z alpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA."
    Schwartz T., Rould M.A., Lowenhaupt K., Herbert A., Rich A.
    Science 284:1841-1845(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-209 IN COMPLEX WITH Z-DNA.
  45. "The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA."
    Schade M., Turner C.J., Kuehne R., Schmieder P., Lowenhaupt K., Herbert A., Rich A., Oschkinat H.
    Proc. Natl. Acad. Sci. U.S.A. 96:12465-12470(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 125-201 IN COMPLEX WITH Z-DNA AND ALONE.
  46. "Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are involved in dyschromatosis symmetrica hereditaria."
    Miyamura Y., Suzuki T., Kono M., Inagaki K., Ito S., Suzuki N., Tomita Y.
    Am. J. Hum. Genet. 73:693-699(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DSH PRO-923 AND SER-1165.
  47. "Seven novel mutations of the ADAR gene in Chinese families and sporadic patients with dyschromatosis symmetrica hereditaria (DSH)."
    Zhang X.-J., He P.-P., Li M., He C.-D., Yan K.-L., Cui Y., Yang S., Zhang K.-Y., Gao M., Chen J.-J., Li C.-R., Jin L., Chen H.-D., Xu S.-J., Huang W.
    Hum. Mutat. 23:629-630(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DSH PHE-966.
  48. "A new arginine substitution mutation of DSRAD gene in a Chinese family with dyschromatosis symmetrica hereditaria."
    Li C.-R., Li M., Ma H.-J., Luo D., Yang L.-J., Wang D.-G., Zhu X.-H., Yue X.-Z., Chen W.-Q., Zhu W.-Y.
    J. Dermatol. Sci. 37:95-99(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DSH TRP-1155.
  49. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-806.
  50. "Mutations in ADAR1 cause Aicardi-Goutieres syndrome associated with a type I interferon signature."
    Rice G.I., Kasher P.R., Forte G.M., Mannion N.M., Greenwood S.M., Szynkiewicz M., Dickerson J.E., Bhaskar S.S., Zampini M., Briggs T.A., Jenkinson E.M., Bacino C.A., Battini R., Bertini E., Brogan P.A., Brueton L.A., Carpanelli M., De Laet C.
    , de Lonlay P., del Toro M., Desguerre I., Fazzi E., Garcia-Cazorla A., Heiberg A., Kawaguchi M., Kumar R., Lin J.P., Lourenco C.M., Male A.M., Marques W. Jr., Mignot C., Olivieri I., Orcesi S., Prabhakar P., Rasmussen M., Robinson R.A., Rozenberg F., Schmidt J.L., Steindl K., Tan T.Y., van der Merwe W.G., Vanderver A., Vassallo G., Wakeling E.L., Wassmer E., Whittaker E., Livingston J.H., Lebon P., Suzuki T., McLaughlin P.J., Keegan L.P., O'Connell M.A., Lovell S.C., Crow Y.J.
    Nat. Genet. 44:1243-1248(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AGS6 ALA-193; THR-870; THR-872; HIS-892; ASN-999; ARG-1007; PHE-1112 AND HIS-1113.

Entry informationi

Entry nameiDSRAD_HUMAN
AccessioniPrimary (citable) accession number: P55265
Secondary accession number(s): B1AQQ9
, B1AQR0, D3DV76, O15223, O43859, O43860, Q9BYM3, Q9BYM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 160 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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