Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P78563

- RED1_HUMAN

UniProt

P78563 - RED1_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 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. protein binding Source: IntAct
    8. 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

    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

    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

    ArrayExpressiP78563.
    BgeeiP78563.
    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 – 33819
    Turni339 – 3435
    Helixi345 – 3473
    Beta strandi352 – 36110
    Helixi363 – 3653
    Beta strandi367 – 3737
    Helixi380 – 3823
    Helixi395 – 41622
    Helixi418 – 4236
    Beta strandi425 – 4284
    Beta strandi432 – 4365
    Beta strandi440 – 4489
    Helixi453 – 4564
    Beta strandi521 – 5244
    Helixi542 – 5465
    Beta strandi552 – 5543
    Helixi556 – 56611
    Helixi570 – 5745
    Beta strandi582 – 5898
    Helixi593 – 6008
    Helixi602 – 6043
    Beta strandi620 – 6234
    Beta strandi637 – 6437
    Beta strandi650 – 6534
    Turni654 – 6574
    Helixi669 – 68012
    Helixi685 – 6873
    Helixi698 – 7036
    Helixi706 – 72116
    Helixi732 – 7354

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG    50
    RKRPLEEGSN GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ 100
    TGPVHAPLFV MSVEVNGQVF EGSGPTKKKA KLHAAEKALR SFVQFPNASE 150
    AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF ETPDKAEPPF YVGSNGDDSF 200
    SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL NELRPGLKYD 250
    FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH 300
    LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK 350
    VLAGVVMTTG TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR 400
    RSLLRFLYTQ LELYLNNKDD QKRSIFQKSE RGGFRLKENV QFHLYISTSP 450
    CGDARIFSPH EPILEGSRSY TQAGVQWCNH GSLQPRPPGL LSDPSTSTFQ 500
    GAGTTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ TWDGVLQGER 550
    LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM 600
    YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDSAIE 650
    VINATTGKDE LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE 700
    SKLAAKEYQA AKARLFTAFI KAGLGAWVEK PTEQDQFSLT P 741

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 ]
    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.
    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

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

    Gene expression databases

    ArrayExpressi P78563.
    Bgeei P78563.
    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

    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: October 1, 2014
    This is version 142 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