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P55265

- DSRAD_HUMAN

UniProt

P55265 - DSRAD_HUMAN

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Protein

Double-stranded RNA-specific adenosine deaminase

Gene

ADAR

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 – 9101ZincPROSITE-ProRule annotation
Active sitei912 – 9121Proton donorPROSITE-ProRule annotation
Metal bindingi966 – 9661ZincPROSITE-ProRule annotation
Metal bindingi1036 – 10361ZincPROSITE-ProRule annotation

Regions

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

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. innate immune response Source: UniProtKB
  7. in utero embryonic development Source: Ensembl
  8. miRNA loading onto RISC involved in gene silencing by miRNA Source: MGI
  9. mRNA modification Source: Reactome
  10. mRNA processing Source: UniProtKB-KW
  11. negative regulation of apoptotic process Source: Ensembl
  12. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  13. negative regulation of viral genome replication Source: Ensembl
  14. positive regulation of viral genome replication Source: UniProtKB
  15. pre-miRNA processing Source: MGI
  16. protein export from nucleus Source: UniProtKB
  17. protein import into nucleus Source: UniProtKB
  18. response to interferon-alpha Source: UniProtKB
  19. response to virus Source: UniProtKB
  20. 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.
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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: UniProtKB
  3. nucleolus Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. 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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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 deaminasePRO_0000171774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki418 – 418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
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

BgeeiP55265.
CleanExiHS_ADAR.
ExpressionAtlasiP55265. baseline and differential.
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 UPF1.8 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. 37 interactions.
DIPiDIP-29310N.
IntActiP55265. 13 interactions.
MINTiMINT-4531596.
STRINGi9606.ENSP00000357459.

Structurei

Secondary structure

1
1226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi127 – 1304Combined sources
Helixi135 – 15016Combined sources
Beta strandi152 – 1543Combined sources
Helixi158 – 1658Combined sources
Helixi169 – 18113Combined sources
Beta strandi184 – 1929Combined sources
Beta strandi194 – 1974Combined sources
Helixi294 – 30916Combined sources
Helixi315 – 3228Combined sources
Helixi324 – 3263Combined sources
Helixi327 – 33913Combined sources
Beta strandi342 – 3465Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3554Combined sources
Helixi357 – 3604Combined sources
Turni361 – 3633Combined sources
Helixi716 – 7249Combined sources
Helixi727 – 73812Combined sources
Beta strandi742 – 7498Combined sources
Beta strandi758 – 7647Combined sources
Beta strandi767 – 77610Combined sources
Helixi777 – 79620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 503-572, 614-683, 708-801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55265.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 A to I editase domain.PROSITE-ProRule annotation
Contains 2 DRADA repeats.PROSITE-ProRule annotation
Contains 3 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG292433.
GeneTreeiENSGT00550000074412.
HOVERGENiHBG067087.
InParanoidiP55265.
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

        10         20         30         40         50
MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ
60 70 80 90 100
LPEAPVIGKQ TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR
110 120 130 140 150
SQGLQRGFQH PSPRGRSLPQ RGVDCLSSHF QELSIYQDQE QRILKFLEEL
160 170 180 190 200
GEGKATTAHD LSGKLGTPKK EINRVLYSLA KKGKLQKEAG TPPLWKIAVS
210 220 230 240 250
TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED LLEPFIAVSA
260 270 280 290 300
QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK
310 320 330 340 350
EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP
360 370 380 390 400
PIWHLTDKKR ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS
410 420 430 440 450
NNMVTTEKVE NGQEPVIKLE NRQEARPEPA RLKPPVHYNG PSKAGYVDFE
460 470 480 490 500
NGQWATDDIP DDLNSIRAAP GEFRAIMEMP SFYSHGLPRC SPYKKLTECQ
510 520 530 540 550
LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV INGREFPPAE
560 570 580 590 600
AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ
610 620 630 640 650
TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV
660 670 680 690 700
AVGAQTFPSV SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQPEGMISE
710 720 730 740 750
SLDNLESMMP NKVRKIGELV RYLNTNPVGG LLEYARSHGF AAEFKLVDQS
760 770 780 790 800
GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG KQEAADAALR VLIGENEKAE
810 820 830 840 850
RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF HDQIAMLSHR
860 870 880 890 900
CFNTLTNSFQ PSLLGRKILA AIIMKKDSED MGVVVSLGTG NRCVKGDSLS
910 920 930 940 950
LKGETVNDCH AEIISRRGFI RFLYSELMKY NSQTAKDSIF EPAKGGEKLQ
960 970 980 990 1000
IKKTVSFHLY ISTAPCGDGA LFDKSCSDRA MESTESRHYP VFENPKQGKL
1010 1020 1030 1040 1050
RTKVENGEGT IPVESSDIVP TWDGIRLGER LRTMSCSDKI LRWNVLGLQG
1060 1070 1080 1090 1100
ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI CCRVTRDGSA FEDGLRHPFI
1110 1120 1130 1140 1150
VNHPKVGRVS IYDSKRQSGK TKETSVNWCL ADGYDLEILD GTRGTVDGPR
1160 1170 1180 1190 1200
NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK
1210 1220
KGLKDMGYGN WISKPQEEKN FYLCPV

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.Curated

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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531E → G in CAA55968. 1 PublicationCurated
Sequence conflicti245 – 2451F → L in CAE45853. (PubMed:17974005)Curated
Sequence conflicti482 – 4821F → L in CAE45853. (PubMed:17974005)Curated
Sequence conflicti873 – 8731I → V in CAE45853. (PubMed:17974005)Curated
Sequence conflicti1093 – 10931D → G in CAE45853. (PubMed:17974005)Curated
Sequence conflicti1184 – 11841E → K in CAA55967. 1 PublicationCurated
Sequence conflicti1184 – 11841E → K in CAA55968. 1 PublicationCurated
Sequence conflicti1184 – 11841E → K in CAA67169. 1 PublicationCurated
Sequence conflicti1184 – 11841E → K in CAA67170. 1 PublicationCurated
Isoform 4 (identifier: P55265-4)
Sequence conflicti13 – 131R → G in CAE45853. (PubMed:17974005)Curated

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. 1 PublicationVSP_019235Add
BLAST
Alternative sequencei1 – 55MNPRQ → MMSPICDQTIDSRLKVEKAT WWGRVGGGSRPHWQPPGVRP CPEEVQDP in isoform 4. 1 PublicationVSP_008872
Alternative sequencei694 – 71219Missing in isoform 3. CuratedVSP_008873Add
BLAST
Alternative sequencei807 – 83226Missing in isoform 2 and isoform 3. CuratedVSP_008874Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 503-572, 614-683, 708-801.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106617. 37 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.
GeneTreei ENSGT00550000074412.
HOVERGENi HBG067087.
InParanoidi P55265.
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

Bgeei P55265.
CleanExi HS_ADAR.
ExpressionAtlasi P55265. baseline and differential.
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: October 29, 2014
This is version 162 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