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Protein

Double-stranded RNA-specific editase 1

Gene

ADARB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi394Zinc1
Active sitei396Proton donor1
Binding sitei400Inositol hexakisphosphate1
Binding sitei401Inositol hexakisphosphate1
Metal bindingi451Zinc1
Metal bindingi556Zinc1
Binding sitei559Inositol hexakisphosphate1
Binding sitei562Inositol hexakisphosphate1
Binding sitei669Inositol hexakisphosphate1
Binding sitei702Inositol hexakisphosphate1
Binding sitei712Inositol hexakisphosphate1
Binding sitei730Inositol hexakisphosphate1

GO - Molecular functioni

  • double-stranded RNA adenosine deaminase activity Source: HGNC
  • double-stranded RNA binding Source: HGNC
  • metal ion binding Source: UniProtKB-KW
  • mRNA binding Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: HGNC

GO - Biological processi

  • adenosine to inosine editing Source: UniProtKB
  • base conversion or substitution editing Source: HGNC
  • defense response to virus Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • mRNA processing Source: UniProtKB-KW
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of viral genome replication Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • 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

BRENDAi3.5.4.37. 2681.
ReactomeiR-HSA-75102. C6 deamination of adenosine.
R-HSA-77042. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:226. ADARB1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi104.
OpenTargetsiENSG00000197381.
PharmGKBiPA24556.

Polymorphism and mutation databases

BioMutaiADARB1.
DMDMi2829669.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001717791 – 741Double-stranded RNA-specific editase 1Add BLAST741

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26PhosphoserineCombined sources1
Modified residuei149PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP78563.
MaxQBiP78563.
PaxDbiP78563.
PeptideAtlasiP78563.
PRIDEiP78563.

PTM databases

iPTMnetiP78563.
PhosphoSitePlusiP78563.

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

BgeeiENSG00000197381.
ExpressionAtlasiP78563. baseline and differential.
GenevisibleiP78563. HS.

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
PRKRAO755694EBI-12002366,EBI-713955
WWP2O003085EBI-2967304,EBI-743923

Protein-protein interaction databases

BioGridi106618. 25 interactors.
IntActiP78563. 16 interactors.
MINTiMINT-3023320.
STRINGi9606.ENSP00000353920.

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi313 – 315Combined sources3
Helixi320 – 338Combined sources19
Turni339 – 343Combined sources5
Helixi345 – 347Combined sources3
Beta strandi352 – 361Combined sources10
Helixi363 – 365Combined sources3
Beta strandi367 – 373Combined sources7
Beta strandi375 – 377Combined sources3
Helixi380 – 382Combined sources3
Beta strandi391 – 394Combined sources4
Helixi395 – 416Combined sources22
Helixi418 – 423Combined sources6
Beta strandi425 – 428Combined sources4
Beta strandi432 – 436Combined sources5
Beta strandi440 – 448Combined sources9
Helixi453 – 456Combined sources4
Turni515 – 518Combined sources4
Beta strandi521 – 524Combined sources4
Beta strandi529 – 532Combined sources4
Turni533 – 535Combined sources3
Helixi542 – 546Combined sources5
Beta strandi552 – 554Combined sources3
Helixi556 – 566Combined sources11
Helixi570 – 574Combined sources5
Beta strandi582 – 589Combined sources8
Helixi593 – 600Combined sources8
Helixi602 – 604Combined sources3
Beta strandi620 – 623Combined sources4
Beta strandi637 – 643Combined sources7
Beta strandi650 – 653Combined sources4
Turni654 – 657Combined sources4
Helixi669 – 680Combined sources12
Helixi685 – 687Combined sources3
Helixi698 – 703Combined sources6
Helixi706 – 721Combined sources16
Helixi732 – 735Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZY7X-ray1.70A/B299-741[»]
5ED1X-ray2.77A/D299-741[»]
5ED2X-ray2.95A/D299-741[»]
5HP2X-ray2.98A/D299-741[»]
5HP3X-ray3.09A/D299-741[»]
ProteinModelPortaliP78563.
SMRiP78563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78563.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 144DRBM 1PROSITE-ProRule annotationAdd BLAST67
Domaini231 – 298DRBM 2PROSITE-ProRule annotationAdd BLAST68
Domaini370 – 737A to I editasePROSITE-ProRule annotationAdd BLAST368

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni83 – 88Interaction with substrate RNABy similarity6
Regioni104 – 105Interaction with substrate RNABy similarity2
Regioni237 – 242Interaction with substrate RNABy similarity6
Regioni259Interaction with substrate RNABy similarity1

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

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOGENOMiHOG000213660.
HOVERGENiHBG003836.
InParanoidiP78563.
KOiK13194.
OMAiFKMTVTI.
OrthoDBiEOG091G0MZP.
PhylomeDBiP78563.
TreeFamiTF315806.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
InterProiIPR002466. A_deamin.
IPR008996. Cytokine_IL1-like.
IPR014720. dsRBD_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

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: ADAR2a, DRADA2A, RED1-S

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
Also known as: ADAR2R

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MASSTTPPLHMGTFFSVMGRRYKRRRKKRSERKDRNSLRQSRNPQKYFAM

Note: Likely expressed from an alternative promoter. Contains a region highly similar to the so-called ssRNA-binding R-domain of ADARB2.1 Publication
Show »
Length:790
Mass (Da):86,692
Checksum:i5FE50BA398BA0CA0
GO
Isoform 6 (identifier: P78563-6) [UniParc]FASTAAdd to basket
Also known as: ADAR2d

The sequence of this isoform differs from the canonical sequence as follows:
     466-505: Missing.
     713-741: ARLFTAFIKAGLGAWVEKPTEQDQFSLTP → VH

Show »
Length:674
Mass (Da):73,665
Checksum:iE55004CC0C4A1EFB
GO

Sequence cautioni

The sequence ACN49027 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30G → A in AAB58300 (PubMed:9330641).Curated1
Sequence conflicti30G → A in AAM83100 (PubMed:12459255).Curated1
Sequence conflicti30G → A in AAM97654 (PubMed:12459255).Curated1
Sequence conflicti30G → A in AAN10291 (PubMed:12459255).Curated1
Sequence conflicti423R → E in AAB58300 (PubMed:9330641).Curated1
Sequence conflicti423R → E in AAM83100 (PubMed:12459255).Curated1
Sequence conflicti423R → E in AAM97654 (PubMed:12459255).Curated1
Sequence conflicti423R → E in AAN10291 (PubMed:12459255).Curated1
Sequence conflicti475V → L in AAM83100 (PubMed:12459255).Curated1
Sequence conflicti475V → L in AAN10291 (PubMed:12459255).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070931224V → A.1 PublicationCorresponds to variant rs199697177dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0195971M → MKIPRMKTPCQPDRNSLRQS RNPQKYFAM in isoform 4. 1 Publication1
Alternative sequenceiVSP_0414211M → MASSTTPPLHMGTFFSVMGR RYKRRRKKRSERKDRNSLRQ SRNPQKYFAM in isoform 5. 1 Publication1
Alternative sequenceiVSP_000865466 – 505Missing in isoform 2, isoform 4 and isoform 6. 6 PublicationsAdd BLAST40
Alternative sequenceiVSP_000866713 – 741ARLFT…FSLTP → VH in isoform 3 and isoform 6. 2 PublicationsAdd BLAST29

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.
AF533142 mRNA. Translation: AAM97654.1.
AY135659 mRNA. Translation: AAN10291.1.
AB194370 mRNA. Translation: BAE16326.1.
AB194371 mRNA. Translation: BAE16327.1.
AB194372 mRNA. Translation: BAE16328.1.
AB194373 mRNA. Translation: BAE16329.1.
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. Different initiation.
CCDSiCCDS33589.1. [P78563-1]
CCDS33590.1. [P78563-2]
CCDS42970.1. [P78563-3]
RefSeqiNP_001103.1. NM_001112.3. [P78563-2]
NP_001153702.1. NM_001160230.1. [P78563-6]
NP_056648.1. NM_015833.3. [P78563-1]
NP_056649.1. NM_015834.3. [P78563-3]
XP_016883736.1. XM_017028247.1. [P78563-1]
XP_016883737.1. XM_017028248.1. [P78563-1]
XP_016883738.1. XM_017028249.1. [P78563-1]
XP_016883739.1. XM_017028250.1. [P78563-1]
XP_016883740.1. XM_017028251.1. [P78563-1]
XP_016883743.1. XM_017028254.1. [P78563-3]
XP_016883744.1. XM_017028255.1. [P78563-2]
XP_016883745.1. XM_017028256.1. [P78563-6]
UniGeneiHs.474018.

Genome annotation databases

EnsembliENST00000348831; ENSP00000015877; ENSG00000197381. [P78563-2]
ENST00000360697; ENSP00000353920; ENSG00000197381. [P78563-1]
ENST00000389863; ENSP00000374513; ENSG00000197381. [P78563-3]
ENST00000437626; ENSP00000414600; ENSG00000197381. [P78563-1]
ENST00000492414; ENSP00000436367; ENSG00000197381. [P78563-2]
ENST00000496664; ENSP00000435381; ENSG00000197381. [P78563-1]
ENST00000629643; ENSP00000486475; ENSG00000197381. [P78563-4]
GeneIDi104.
KEGGihsa:104.
UCSCiuc002zgr.3. human. [P78563-1]

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.
AF533142 mRNA. Translation: AAM97654.1.
AY135659 mRNA. Translation: AAN10291.1.
AB194370 mRNA. Translation: BAE16326.1.
AB194371 mRNA. Translation: BAE16327.1.
AB194372 mRNA. Translation: BAE16328.1.
AB194373 mRNA. Translation: BAE16329.1.
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. Different initiation.
CCDSiCCDS33589.1. [P78563-1]
CCDS33590.1. [P78563-2]
CCDS42970.1. [P78563-3]
RefSeqiNP_001103.1. NM_001112.3. [P78563-2]
NP_001153702.1. NM_001160230.1. [P78563-6]
NP_056648.1. NM_015833.3. [P78563-1]
NP_056649.1. NM_015834.3. [P78563-3]
XP_016883736.1. XM_017028247.1. [P78563-1]
XP_016883737.1. XM_017028248.1. [P78563-1]
XP_016883738.1. XM_017028249.1. [P78563-1]
XP_016883739.1. XM_017028250.1. [P78563-1]
XP_016883740.1. XM_017028251.1. [P78563-1]
XP_016883743.1. XM_017028254.1. [P78563-3]
XP_016883744.1. XM_017028255.1. [P78563-2]
XP_016883745.1. XM_017028256.1. [P78563-6]
UniGeneiHs.474018.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZY7X-ray1.70A/B299-741[»]
5ED1X-ray2.77A/D299-741[»]
5ED2X-ray2.95A/D299-741[»]
5HP2X-ray2.98A/D299-741[»]
5HP3X-ray3.09A/D299-741[»]
ProteinModelPortaliP78563.
SMRiP78563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106618. 25 interactors.
IntActiP78563. 16 interactors.
MINTiMINT-3023320.
STRINGi9606.ENSP00000353920.

PTM databases

iPTMnetiP78563.
PhosphoSitePlusiP78563.

Polymorphism and mutation databases

BioMutaiADARB1.
DMDMi2829669.

Proteomic databases

EPDiP78563.
MaxQBiP78563.
PaxDbiP78563.
PeptideAtlasiP78563.
PRIDEiP78563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348831; ENSP00000015877; ENSG00000197381. [P78563-2]
ENST00000360697; ENSP00000353920; ENSG00000197381. [P78563-1]
ENST00000389863; ENSP00000374513; ENSG00000197381. [P78563-3]
ENST00000437626; ENSP00000414600; ENSG00000197381. [P78563-1]
ENST00000492414; ENSP00000436367; ENSG00000197381. [P78563-2]
ENST00000496664; ENSP00000435381; ENSG00000197381. [P78563-1]
ENST00000629643; ENSP00000486475; ENSG00000197381. [P78563-4]
GeneIDi104.
KEGGihsa:104.
UCSCiuc002zgr.3. human. [P78563-1]

Organism-specific databases

CTDi104.
DisGeNETi104.
GeneCardsiADARB1.
HGNCiHGNC:226. ADARB1.
HPAiHPA018277.
HPA029645.
MIMi601218. gene.
neXtProtiNX_P78563.
OpenTargetsiENSG00000197381.
PharmGKBiPA24556.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOGENOMiHOG000213660.
HOVERGENiHBG003836.
InParanoidiP78563.
KOiK13194.
OMAiFKMTVTI.
OrthoDBiEOG091G0MZP.
PhylomeDBiP78563.
TreeFamiTF315806.

Enzyme and pathway databases

BRENDAi3.5.4.37. 2681.
ReactomeiR-HSA-75102. C6 deamination of adenosine.
R-HSA-77042. Formation of editosomes by ADAR proteins.

Miscellaneous databases

ChiTaRSiADARB1. human.
EvolutionaryTraceiP78563.
GeneWikiiADARB1.
GenomeRNAii104.
PROiP78563.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197381.
ExpressionAtlasiP78563. baseline and differential.
GenevisibleiP78563. HS.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
InterProiIPR002466. A_deamin.
IPR008996. Cytokine_IL1-like.
IPR014720. dsRBD_dom.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[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]
ProtoNetiSearch...

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, Q4AE77, Q4AE79, Q6P0M9, Q8NFA1, Q8NFD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.