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P78563

- RED1_HUMAN

UniProt

P78563 - RED1_HUMAN

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Protein

Double-stranded RNA-specific editase 1

Gene

ADARB1

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 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.3 Publications

Catalytic activityi

Adenine in double-stranded RNA + H2O = hypoxanthine in double-stranded RNA + NH3.2 Publications

Cofactori

1D-myo-inositol hexakisphosphateNote: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi394 – 3941Zinc
Active sitei396 – 3961Proton donor
Binding sitei400 – 4001Inositol hexakisphosphate
Binding sitei401 – 4011Inositol hexakisphosphate
Metal bindingi451 – 4511Zinc
Metal bindingi556 – 5561Zinc
Binding sitei559 – 5591Inositol hexakisphosphate
Binding sitei562 – 5621Inositol hexakisphosphate
Binding sitei669 – 6691Inositol hexakisphosphate
Binding sitei702 – 7021Inositol hexakisphosphate
Binding sitei712 – 7121Inositol hexakisphosphate
Binding sitei730 – 7301Inositol hexakisphosphate

GO - Molecular functioni

  1. adenosine deaminase activity Source: InterPro
  2. double-stranded RNA adenosine deaminase activity Source: HGNC
  3. double-stranded RNA binding Source: HGNC
  4. metal ion binding Source: UniProtKB-KW
  5. mRNA binding Source: BHF-UCL
  6. poly(A) RNA binding Source: UniProtKB
  7. RNA binding Source: HGNC

GO - Biological processi

  1. adenosine to inosine editing Source: UniProtKB
  2. base conversion or substitution editing Source: HGNC
  3. defense response to virus Source: UniProtKB-KW
  4. gene expression Source: Reactome
  5. innate immune response Source: UniProtKB-KW
  6. mRNA modification Source: Reactome
  7. mRNA processing Source: UniProtKB-KW
  8. negative regulation of cell migration Source: UniProtKB
  9. negative regulation of cell proliferation Source: UniProtKB
  10. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  11. positive regulation of viral genome replication Source: UniProtKB
  12. regulation of cell cycle Source: UniProtKB
  13. RNA processing Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, mRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1231. C6 deamination of adenosine.
REACT_1966. Formation of editosomes by ADAR proteins.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ADARB1
Synonyms:ADAR2, DRADA2, RED1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:226. ADARB1.

Subcellular locationi

Nucleus. Nucleusnucleolus
Note: Shuttles between nucleoli and the nucleoplasm.

GO - Cellular componenti

  1. nucleolus Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24556.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741Double-stranded RNA-specific editase 1PRO_0000171779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78563.
PaxDbiP78563.
PRIDEiP78563.

PTM databases

PhosphoSiteiP78563.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiP78563.
ExpressionAtlasiP78563. baseline and differential.
GenevestigatoriP78563.

Organism-specific databases

HPAiHPA018277.
HPA029645.

Interactioni

Subunit structurei

Homodimer. Homodimerization is essential for its catalytic activity. Can form heterodimers with isoform 5 of ADAR/ADAR1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIN1Q1352612EBI-2967304,EBI-714158
WWP2O003085EBI-2967304,EBI-743923

Protein-protein interaction databases

BioGridi106618. 19 interactions.
IntActiP78563. 3 interactions.
MINTiMINT-3023320.

Structurei

Secondary structure

1
741
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi320 – 33819Combined sources
Turni339 – 3435Combined sources
Helixi345 – 3473Combined sources
Beta strandi352 – 36110Combined sources
Helixi363 – 3653Combined sources
Beta strandi367 – 3737Combined sources
Helixi380 – 3823Combined sources
Helixi395 – 41622Combined sources
Helixi418 – 4236Combined sources
Beta strandi425 – 4284Combined sources
Beta strandi432 – 4365Combined sources
Beta strandi440 – 4489Combined sources
Helixi453 – 4564Combined sources
Beta strandi521 – 5244Combined sources
Helixi542 – 5465Combined sources
Beta strandi552 – 5543Combined sources
Helixi556 – 56611Combined sources
Helixi570 – 5745Combined sources
Beta strandi582 – 5898Combined sources
Helixi593 – 6008Combined sources
Helixi602 – 6043Combined sources
Beta strandi620 – 6234Combined sources
Beta strandi637 – 6437Combined sources
Beta strandi650 – 6534Combined sources
Turni654 – 6574Combined sources
Helixi669 – 68012Combined sources
Helixi685 – 6873Combined sources
Helixi698 – 7036Combined sources
Helixi706 – 72116Combined sources
Helixi732 – 7354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZY7X-ray1.70A/B299-741[»]
ProteinModelPortaliP78563.
SMRiP78563. Positions 74-301, 306-740.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78563.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 14467DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini231 – 29868DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini370 – 737368A to I editasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 886Interaction with substrate RNABy similarity
Regioni104 – 1052Interaction with substrate RNABy similarity
Regioni237 – 2426Interaction with substrate RNABy similarity
Regioni259 – 2591Interaction with substrate RNABy similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG292433.
GeneTreeiENSGT00550000074412.
HOVERGENiHBG003836.
InParanoidiP78563.
KOiK13194.
OMAiFPDTLFN.
PhylomeDBiP78563.
TreeFamiTF315806.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
InterProiIPR002466. A_deamin.
IPR008996. Cytokine_IL1-like.
IPR014720. dsRNA-bd_dom.
IPR029484. GVQW.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
PF13900. GVQW. 1 hit.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P78563-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG
60 70 80 90 100
RKRPLEEGSN GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ
110 120 130 140 150
TGPVHAPLFV MSVEVNGQVF EGSGPTKKKA KLHAAEKALR SFVQFPNASE
160 170 180 190 200
AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF ETPDKAEPPF YVGSNGDDSF
210 220 230 240 250
SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL NELRPGLKYD
260 270 280 290 300
FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH
310 320 330 340 350
LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK
360 370 380 390 400
VLAGVVMTTG TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR
410 420 430 440 450
RSLLRFLYTQ LELYLNNKDD QKRSIFQKSE RGGFRLKENV QFHLYISTSP
460 470 480 490 500
CGDARIFSPH EPILEGSRSY TQAGVQWCNH GSLQPRPPGL LSDPSTSTFQ
510 520 530 540 550
GAGTTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ TWDGVLQGER
560 570 580 590 600
LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM
610 620 630 640 650
YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDSAIE
660 670 680 690 700
VINATTGKDE LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE
710 720 730 740
SKLAAKEYQA AKARLFTAFI KAGLGAWVEK PTEQDQFSLT P

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.

Length:741
Mass (Da):80,763
Last modified:May 1, 1997 - v1
Checksum:i02B583414DD59C20
GO
Isoform 2 (identifier: P78563-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:701
Mass (Da):76,633
Checksum:i12D26888C1F131B6
GO
Isoform 3 (identifier: P78563-3) [UniParc]FASTAAdd to Basket

Also known as: DRADA2C

The sequence of this isoform differs from the canonical sequence as follows:
     713-741: ARLFTAFIKAGLGAWVEKPTEQDQFSLTP → VH

Show »
Length:714
Mass (Da):77,795
Checksum:i10F6C71FFB641CFE
GO
Isoform 4 (identifier: P78563-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKIPRMKTPCQPDRNSLRQSRNPQKYFAM
     466-505: Missing.

Show »
Length:729
Mass (Da):80,007
Checksum:iBAB59C894273C4E8
GO
Isoform 5 (identifier: P78563-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:780
Mass (Da):85,669
Checksum:iB7637CEA1D2E19E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301G → A in AAB58300. (PubMed:9330641)Curated
Sequence conflicti30 – 301G → A in AAM83100. (PubMed:12459255)Curated
Sequence conflicti30 – 301G → A in AAN10291. (PubMed:12459255)Curated
Sequence conflicti423 – 4231R → E in AAB58300. (PubMed:9330641)Curated
Sequence conflicti423 – 4231R → E in AAM83100. (PubMed:12459255)Curated
Sequence conflicti423 – 4231R → E in AAN10291. (PubMed:12459255)Curated
Sequence conflicti475 – 4751V → L in AAM83100. (PubMed:12459255)Curated
Sequence conflicti475 – 4751V → L in AAN10291. (PubMed:12459255)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241V → A.1 Publication
Corresponds to variant rs199697177 [ dbSNP | Ensembl ].
VAR_070931

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MKIPRMKTPCQPDRNSLRQS RNPQKYFAM in isoform 4. 1 PublicationVSP_019597
Alternative sequencei1 – 11M → MGTFFSVMGRRYKRRRKKRS ERKDRNSLRQSRNPQKYFAM in isoform 5. 1 PublicationVSP_041421
Alternative sequencei466 – 50540Missing in isoform 2 and isoform 4. 6 PublicationsVSP_000865Add
BLAST
Alternative sequencei713 – 74129ARLFT…FSLTP → VH in isoform 3. 1 PublicationVSP_000866Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33589.1. [P78563-1]
CCDS33590.1. [P78563-2]
CCDS42970.1. [P78563-3]
RefSeqiNP_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]
UniGeneiHs.474018.

Genome annotation databases

EnsembliENST00000348831; ENSP00000015877; ENSG00000197381. [P78563-2]
ENST00000360697; ENSP00000353920; ENSG00000197381. [P78563-1]
ENST00000389861; ENSP00000374511; ENSG00000197381. [P78563-4]
ENST00000389863; ENSP00000374513; ENSG00000197381. [P78563-3]
ENST00000437626; ENSP00000414600; ENSG00000197381. [P78563-1]
ENST00000492414; ENSP00000436367; ENSG00000197381. [P78563-2]
ENST00000496664; ENSP00000435381; ENSG00000197381. [P78563-1]
GeneIDi104.
KEGGihsa:104.
UCSCiuc002zgr.2. human. [P78563-3]
uc002zgt.2. human. [P78563-2]
uc002zgy.2. human. [P78563-1]

Polymorphism databases

DMDMi2829669.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS33589.1. [P78563-1 ]
CCDS33590.1. [P78563-2 ]
CCDS42970.1. [P78563-3 ]
RefSeqi NP_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 ]
UniGenei Hs.474018.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZY7 X-ray 1.70 A/B 299-741 [» ]
ProteinModelPortali P78563.
SMRi P78563. Positions 74-301, 306-740.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106618. 19 interactions.
IntActi P78563. 3 interactions.
MINTi MINT-3023320.

PTM databases

PhosphoSitei P78563.

Polymorphism databases

DMDMi 2829669.

Proteomic databases

MaxQBi P78563.
PaxDbi P78563.
PRIDEi P78563.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000348831 ; ENSP00000015877 ; ENSG00000197381 . [P78563-2 ]
ENST00000360697 ; ENSP00000353920 ; ENSG00000197381 . [P78563-1 ]
ENST00000389861 ; ENSP00000374511 ; ENSG00000197381 . [P78563-4 ]
ENST00000389863 ; ENSP00000374513 ; ENSG00000197381 . [P78563-3 ]
ENST00000437626 ; ENSP00000414600 ; ENSG00000197381 . [P78563-1 ]
ENST00000492414 ; ENSP00000436367 ; ENSG00000197381 . [P78563-2 ]
ENST00000496664 ; ENSP00000435381 ; ENSG00000197381 . [P78563-1 ]
GeneIDi 104.
KEGGi hsa:104.
UCSCi uc002zgr.2. human. [P78563-3 ]
uc002zgt.2. human. [P78563-2 ]
uc002zgy.2. human. [P78563-1 ]

Organism-specific databases

CTDi 104.
GeneCardsi GC21P046493.
HGNCi HGNC:226. ADARB1.
HPAi HPA018277.
HPA029645.
MIMi 601218. gene.
neXtProti NX_P78563.
PharmGKBi PA24556.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292433.
GeneTreei ENSGT00550000074412.
HOVERGENi HBG003836.
InParanoidi P78563.
KOi K13194.
OMAi FPDTLFN.
PhylomeDBi P78563.
TreeFami TF315806.

Enzyme and pathway databases

Reactomei REACT_1231. C6 deamination of adenosine.
REACT_1966. Formation of editosomes by ADAR proteins.

Miscellaneous databases

ChiTaRSi ADARB1. human.
EvolutionaryTracei P78563.
GeneWikii ADARB1.
GenomeRNAii 104.
NextBioi 35482593.
PROi P78563.
SOURCEi Search...

Gene expression databases

Bgeei P78563.
ExpressionAtlasi P78563. baseline and differential.
Genevestigatori P78563.

Family and domain databases

Gene3Di 3.30.160.20. 2 hits.
InterProi IPR002466. A_deamin.
IPR008996. Cytokine_IL1-like.
IPR014720. dsRNA-bd_dom.
IPR029484. GVQW.
[Graphical view ]
Pfami PF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
PF13900. GVQW. 1 hit.
[Graphical view ]
SMARTi SM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view ]
SUPFAMi SSF50353. SSF50353. 1 hit.
PROSITEi PS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiRED1_HUMAN
AccessioniPrimary (citable) accession number: P78563
Secondary accession number(s): A6NFK8
, A6NJ84, C3TTQ1, C3TTQ2, C9JUP4, G5E9B4, O00395, O00465, O00691, O00692, P78555, Q4AE79, Q6P0M9, Q8NFD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 26, 2014
This is version 144 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: 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