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O95786

- DDX58_HUMAN

UniProt

O95786 - DDX58_HUMAN

Protein

Probable ATP-dependent RNA helicase DDX58

Gene

DDX58

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (08 Nov 2005)
      Previous versions | rss
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    Functioni

    Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.13 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Zinc.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi810 – 8101Zinc
    Metal bindingi813 – 8131Zinc
    Metal bindingi864 – 8641Zinc
    Metal bindingi869 – 8691Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi264 – 2718ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. double-stranded DNA binding Source: Ensembl
    3. double-stranded RNA binding Source: UniProtKB
    4. helicase activity Source: UniProtKB-KW
    5. identical protein binding Source: IntAct
    6. protein binding Source: UniProtKB
    7. single-stranded RNA binding Source: UniProtKB
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cytoplasmic pattern recognition receptor signaling pathway in response to virus Source: UniProtKB
    2. detection of virus Source: BHF-UCL
    3. innate immune response Source: UniProtKB
    4. negative regulation of type I interferon production Source: Reactome
    5. positive regulation of defense response to virus by host Source: UniProtKB
    6. positive regulation of interferon-alpha production Source: UniProtKB
    7. positive regulation of interferon-beta production Source: UniProtKB
    8. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    9. positive regulation of transcription factor import into nucleus Source: BHF-UCL
    10. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. regulation of cell migration Source: UniProtKB
    12. regulation of type III interferon production Source: UniProtKB
    13. response to exogenous dsRNA Source: Ensembl
    14. response to virus Source: UniProtKB
    15. RIG-I signaling pathway Source: UniProtKB
    16. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX58 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 58
    RIG-I-like receptor 1
    Short name:
    RLR-1
    Retinoic acid-inducible gene 1 protein
    Short name:
    RIG-1
    Retinoic acid-inducible gene I protein
    Short name:
    RIG-I
    Gene namesi
    Name:DDX58
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:19102. DDX58.

    Subcellular locationi

    Cytoplasm. Cell projectionruffle membrane. Cytoplasmcytoskeleton. Cell junctiontight junction
    Note: Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. ruffle membrane Source: UniProtKB
    5. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551T → I: No IRF3 signaling activity; no effect on dsRNA binding. 1 Publication
    Mutagenesisi99 – 991K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
    Mutagenesisi154 – 1541K → R: Reduction of ubiquitination. Reduction of INFB induction. 1 Publication
    Mutagenesisi164 – 1641K → R: Reduction of ubiquitination. Reduction of INFB induction. 1 Publication
    Mutagenesisi169 – 1691K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
    Mutagenesisi172 – 1721K → R: Complete loss of ubiquitination; No interaction with MAVS/IPS1; No induction of IFN-beta. 2 Publications
    Mutagenesisi181 – 1811K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
    Mutagenesisi190 – 1901K → R: Little or no effect on ubiquitination of the 2 CARD domains.
    Mutagenesisi193 – 1931K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
    Mutagenesisi270 – 2701K → A: No IRF3 signaling activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA134994272.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 925925Probable ATP-dependent RNA helicase DDX58PRO_0000144093Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki154 – 154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki172 – 172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei770 – 7701Phosphothreonine; by CK21 Publication
    Modified residuei854 – 8541Phosphoserine; by CK21 Publication
    Modified residuei855 – 8551Phosphoserine; by CK21 Publication
    Modified residuei858 – 8581N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-770, Ser-854 and Ser-855 results in inhibition of its activity while dephosphorylation at these sites results in its activation.1 Publication
    ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response.3 Publications
    Sumoylated, probably by MUL1; inhibiting its polyubiquitination.2 Publications
    Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked ubiquitination. Lys-172 is the critical site for TRIM25-mediated ubiquitination, for MAVS/IPS1 binding and to induce anti-viral signal transduction. Lys-154, Lys-164 and Lys-172 are critical sites for RNF135-mediated ubiquitination. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'-and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO95786.
    PaxDbiO95786.
    PRIDEiO95786.

    PTM databases

    PhosphoSiteiO95786.

    Expressioni

    Tissue specificityi

    Present in vascular smooth cells (at protein level).1 Publication

    Inductioni

    By bacterial lipopolysaccharides (LPS) in endothelial cells. By interferon (IFN).5 Publications

    Gene expression databases

    ArrayExpressiO95786.
    BgeeiO95786.
    CleanExiHS_DDX58.
    GenevestigatoriO95786.

    Organism-specific databases

    HPAiCAB012643.
    HPA047193.

    Interactioni

    Subunit structurei

    Monomer; maintained as a monomer in an autoinhibited state. Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts with MAVS/IPS1. Interacts with DHX58/LGP2, IKBKE, TBK1 and TMEM173/STING. Interacts (via CARD domain) with TRIM25 (via SPRY domain). Interacts with RNF135. Interacts with CYLD. Interacts with NLRC5; blocks the interaction of MAVS/IPS1 to DDX58. Interacts with SRC. Interacts with protein Z of Guanarito virus, Machupo virus, Junin arenavirus and Sabia virus. This interaction disrupts its interaction with MAVS/IPS1, impeding downstream IRF3 and NF-kappa-B activation and resulting in decreased IFN-beta induction. Interacts (via CARD domain) with Human respiratory syncytial virus A non-structural protein 2 (NS2) and this interaction disrupts its interaction with MAVS/IPS1, impeding downstream IRF3 activation. Interacts with Rotavirus A non-structural protein 1 (NSP1) and this interaction induces down-regulation of DDX58/RIG-I. Interacts with DDX60. Interacts with isoform 2 of ZC3HAV1 (via zinc-fingers) in an RNA-dependent manner.19 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-995350,EBI-995350
    1BP045432EBI-995350,EBI-3648048From a different organism.
    Casp12Q920D54EBI-995350,EBI-1374296From a different organism.
    CYLDQ9NQC72EBI-995350,EBI-2117940
    DDX3XO005712EBI-995350,EBI-353779
    MAVSQ7Z43412EBI-995350,EBI-995373
    NSSP216993EBI-995350,EBI-6693910From a different organism.
    STAT1P422244EBI-995350,EBI-1057697
    US11P044874EBI-995350,EBI-6150681From a different organism.
    WRNIP1Q96S552EBI-995350,EBI-2513471
    ZQ6IUF93EBI-995350,EBI-3647473From a different organism.
    ZQ6IVU53EBI-995350,EBI-3647294From a different organism.
    ZQ6UY622EBI-995350,EBI-3647496From a different organism.
    ZQ6UY713EBI-995350,EBI-3647448From a different organism.
    ZC3HAV1Q7Z2W43EBI-995350,EBI-922540
    ZC3HAV1Q7Z2W4-24EBI-995350,EBI-922559

    Protein-protein interaction databases

    BioGridi117121. 36 interactions.
    DIPiDIP-35444N.
    IntActiO95786. 19 interactions.
    MINTiMINT-2799116.
    STRINGi9606.ENSP00000369213.

    Structurei

    Secondary structure

    1
    925
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi97 – 10913
    Helixi111 – 1177
    Turni120 – 1234
    Helixi124 – 1274
    Turni128 – 1303
    Helixi133 – 14513
    Helixi148 – 16114
    Helixi166 – 17813
    Helixi182 – 1854
    Helixi245 – 25511
    Beta strandi260 – 2634
    Helixi270 – 28415
    Beta strandi293 – 2964
    Helixi300 – 31314
    Turni314 – 3185
    Beta strandi321 – 3244
    Beta strandi326 – 3283
    Beta strandi330 – 3323
    Helixi334 – 3396
    Beta strandi342 – 3465
    Helixi348 – 3569
    Helixi363 – 3653
    Beta strandi367 – 3726
    Helixi374 – 3763
    Beta strandi377 – 3815
    Helixi382 – 39514
    Beta strandi404 – 4107
    Helixi420 – 43314
    Beta strandi438 – 4403
    Helixi446 – 4527
    Beta strandi457 – 4626
    Helixi470 – 48920
    Helixi493 – 4953
    Beta strandi496 – 4983
    Beta strandi504 – 5063
    Helixi507 – 51812
    Helixi519 – 5213
    Helixi531 – 55727
    Helixi560 – 57516
    Helixi581 – 59111
    Helixi594 – 6029
    Helixi604 – 6063
    Helixi609 – 62214
    Beta strandi630 – 6334
    Helixi637 – 64913
    Helixi651 – 6533
    Beta strandi658 – 6603
    Beta strandi668 – 6703
    Helixi675 – 6839
    Beta strandi694 – 7007
    Helixi706 – 7083
    Beta strandi710 – 7167
    Helixi721 – 7277
    Beta strandi737 – 7437
    Helixi745 – 76824
    Helixi773 – 79321
    Beta strandi801 – 8044
    Beta strandi806 – 8105
    Turni811 – 8133
    Beta strandi816 – 8194
    Helixi820 – 8223
    Beta strandi823 – 8264
    Turni827 – 8293
    Beta strandi830 – 8334
    Helixi836 – 8394
    Beta strandi842 – 8465
    Beta strandi856 – 8649
    Turni867 – 8693
    Beta strandi872 – 8798
    Beta strandi882 – 8876
    Helixi889 – 8913
    Beta strandi892 – 8965
    Turni897 – 8993
    Beta strandi902 – 9043
    Turni908 – 9103
    Helixi920 – 9223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LWDNMR-A95-190[»]
    2LWENMR-A95-190[»]
    2QFBX-ray3.00A/B/C/D/E/F/G/H/I/J802-925[»]
    2QFDX-ray2.70A/B/C/D/E/F/G/H/I/J802-925[»]
    2RMJNMR-A792-925[»]
    2YKGX-ray2.50A230-925[»]
    3LRNX-ray2.60A/B803-923[»]
    3LRRX-ray2.15A/B803-923[»]
    3NCUX-ray2.55A/B792-925[»]
    3OG8X-ray2.40A/B802-925[»]
    3TMIX-ray2.90A232-925[»]
    3ZD6X-ray2.80A230-925[»]
    3ZD7X-ray2.50A230-925[»]
    4AY2X-ray2.80A239-925[»]
    4BPBX-ray2.58A230-925[»]
    4NQKX-ray3.70A/B/C/D1-200[»]
    ProteinModelPortaliO95786.
    SMRiO95786. Positions 1-188, 240-925.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95786.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8787CARD 1Add
    BLAST
    Domaini92 – 17281CARD 2Add
    BLAST
    Domaini251 – 430180Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini610 – 776167Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni218 – 925708Interaction with ZC3HAV1Add
    BLAST
    Regioni735 – 925191Repressor domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi372 – 3754DECH box

    Domaini

    The repressor domain controls homomultimerization and interaction with MAVS/IPS1. In the absence of viral infection, the protein is maintained as a monomer in an autoinhibited state with the CARD domains masked through intramolecular interactions mediated by the repressor domain. Upon binding to viral RNA in the presence of ATP, the repressor domain induces a conformational change exposing the CARD domain and promotes dimerization and CARD interactions with the adapter protein MAVS/IPS1 leading to the induction of downstream signaling.
    The helicase domain is responsible for dsRNA recognition.
    The 2 CARD domains are responsible for interaction with and signaling through MAVS/IPS1 and for association with the actin cytoskeleton.
    The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.

    Sequence similaritiesi

    Belongs to the helicase family. RLR subfamily.Curated
    Contains 2 CARD domains.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1111.
    HOGENOMiHOG000230911.
    HOVERGENiHBG052325.
    InParanoidiO95786.
    KOiK12646.
    OMAiKCKAFAC.
    PhylomeDBiO95786.
    TreeFamiTF330258.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR011029. DEATH-like_dom.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR021673. RIG-I_C-RD.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF11648. RIG-I_C-RD. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95786-1) [UniParc]FASTAAdd to Basket

    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

    MTTEQRRSLQ AFQDYIRKTL DPTYILSYMA PWFREEEVQY IQAEKNNKGP    50
    MEAATLFLKF LLELQEEGWF RGFLDALDHA GYSGLYEAIE SWDFKKIEKL 100
    EEYRLLLKRL QPEFKTRIIP TDIISDLSEC LINQECEEIL QICSTKGMMA 150
    GAEKLVECLL RSDKENWPKT LKLALEKERN KFSELWIVEK GIKDVETEDL 200
    EDKMETSDIQ IFYQEDPECQ NLSENSCPPS EVSDTNLYSP FKPRNYQLEL 250
    ALPAMKGKNT IICAPTGCGK TFVSLLICEH HLKKFPQGQK GKVVFFANQI 300
    PVYEQQKSVF SKYFERHGYR VTGISGATAE NVPVEQIVEN NDIIILTPQI 350
    LVNNLKKGTI PSLSIFTLMI FDECHNTSKQ HPYNMIMFNY LDQKLGGSSG 400
    PLPQVIGLTA SVGVGDAKNT DEALDYICKL CASLDASVIA TVKHNLEELE 450
    QVVYKPQKFF RKVESRISDK FKYIIAQLMR DTESLAKRIC KDLENLSQIQ 500
    NREFGTQKYE QWIVTVQKAC MVFQMPDKDE ESRICKALFL YTSHLRKYND 550
    ALIISEHARM KDALDYLKDF FSNVRAAGFD EIEQDLTQRF EEKLQELESV 600
    SRDPSNENPK LEDLCFILQE EYHLNPETIT ILFVKTRALV DALKNWIEGN 650
    PKLSFLKPGI LTGRGKTNQN TGMTLPAQKC ILDAFKASGD HNILIATSVA 700
    DEGIDIAQCN LVILYEYVGN VIKMIQTRGR GRARGSKCFL LTSNAGVIEK 750
    EQINMYKEKM MNDSILRLQT WDEAVFREKI LHIQTHEKFI RDSQEKPKPV 800
    PDKENKKLLC RKCKALACYT ADVRVIEECH YTVLGDAFKE CFVSRPHPKP 850
    KQFSSFEKRA KIFCARQNCS HDWGIHVKYK TFEIPVIKIE SFVVEDIATG 900
    VQTLYSKWKD FHFEKIPFDP AEMSK 925
    Length:925
    Mass (Da):106,600
    Last modified:November 8, 2005 - v2
    Checksum:iBF0D501C395BAE25
    GO
    Isoform 2 (identifier: O95786-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         36-80: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:880
    Mass (Da):101,377
    Checksum:i4B1603B6F2F37A66
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71R → C.1 Publication
    Corresponds to variant rs10813831 [ dbSNP | Ensembl ].
    VAR_023747
    Natural varianti580 – 5801D → E.2 Publications
    Corresponds to variant rs17217280 [ dbSNP | Ensembl ].
    VAR_023748

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei36 – 8045Missing in isoform 2. 1 PublicationVSP_016054Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038963 mRNA. Translation: AAD19826.1.
    AL353671, AL161783 Genomic DNA. Translation: CAH71251.1.
    AL161783, AL353671 Genomic DNA. Translation: CAH72600.1.
    CH471071 Genomic DNA. Translation: EAW58548.1.
    BC132786 mRNA. Translation: AAI32787.1.
    BC136610 mRNA. Translation: AAI36611.1.
    BX647917 mRNA. Translation: CAI46068.1.
    AL137608 mRNA. Translation: CAB70840.1.
    CCDSiCCDS6526.1. [O95786-1]
    PIRiT46312.
    RefSeqiNP_055129.2. NM_014314.3. [O95786-1]
    UniGeneiHs.190622.

    Genome annotation databases

    EnsembliENST00000379883; ENSP00000369213; ENSG00000107201. [O95786-1]
    GeneIDi23586.
    KEGGihsa:23586.
    UCSCiuc003zra.3. human. [O95786-1]
    uc010mjk.1. human. [O95786-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038963 mRNA. Translation: AAD19826.1 .
    AL353671 , AL161783 Genomic DNA. Translation: CAH71251.1 .
    AL161783 , AL353671 Genomic DNA. Translation: CAH72600.1 .
    CH471071 Genomic DNA. Translation: EAW58548.1 .
    BC132786 mRNA. Translation: AAI32787.1 .
    BC136610 mRNA. Translation: AAI36611.1 .
    BX647917 mRNA. Translation: CAI46068.1 .
    AL137608 mRNA. Translation: CAB70840.1 .
    CCDSi CCDS6526.1. [O95786-1 ]
    PIRi T46312.
    RefSeqi NP_055129.2. NM_014314.3. [O95786-1 ]
    UniGenei Hs.190622.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LWD NMR - A 95-190 [» ]
    2LWE NMR - A 95-190 [» ]
    2QFB X-ray 3.00 A/B/C/D/E/F/G/H/I/J 802-925 [» ]
    2QFD X-ray 2.70 A/B/C/D/E/F/G/H/I/J 802-925 [» ]
    2RMJ NMR - A 792-925 [» ]
    2YKG X-ray 2.50 A 230-925 [» ]
    3LRN X-ray 2.60 A/B 803-923 [» ]
    3LRR X-ray 2.15 A/B 803-923 [» ]
    3NCU X-ray 2.55 A/B 792-925 [» ]
    3OG8 X-ray 2.40 A/B 802-925 [» ]
    3TMI X-ray 2.90 A 232-925 [» ]
    3ZD6 X-ray 2.80 A 230-925 [» ]
    3ZD7 X-ray 2.50 A 230-925 [» ]
    4AY2 X-ray 2.80 A 239-925 [» ]
    4BPB X-ray 2.58 A 230-925 [» ]
    4NQK X-ray 3.70 A/B/C/D 1-200 [» ]
    ProteinModelPortali O95786.
    SMRi O95786. Positions 1-188, 240-925.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117121. 36 interactions.
    DIPi DIP-35444N.
    IntActi O95786. 19 interactions.
    MINTi MINT-2799116.
    STRINGi 9606.ENSP00000369213.

    PTM databases

    PhosphoSitei O95786.

    Proteomic databases

    MaxQBi O95786.
    PaxDbi O95786.
    PRIDEi O95786.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379883 ; ENSP00000369213 ; ENSG00000107201 . [O95786-1 ]
    GeneIDi 23586.
    KEGGi hsa:23586.
    UCSCi uc003zra.3. human. [O95786-1 ]
    uc010mjk.1. human. [O95786-2 ]

    Organism-specific databases

    CTDi 23586.
    GeneCardsi GC09M032447.
    HGNCi HGNC:19102. DDX58.
    HPAi CAB012643.
    HPA047193.
    MIMi 609631. gene.
    neXtProti NX_O95786.
    PharmGKBi PA134994272.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1111.
    HOGENOMi HOG000230911.
    HOVERGENi HBG052325.
    InParanoidi O95786.
    KOi K12646.
    OMAi KCKAFAC.
    PhylomeDBi O95786.
    TreeFami TF330258.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Miscellaneous databases

    ChiTaRSi DDX58. human.
    EvolutionaryTracei O95786.
    GeneWikii RIG-I.
    GenomeRNAii 23586.
    NextBioi 46208.
    PROi O95786.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95786.
    Bgeei O95786.
    CleanExi HS_DDX58.
    Genevestigatori O95786.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR011029. DEATH-like_dom.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR021673. RIG-I_C-RD.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF11648. RIG-I_C-RD. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RIG-I, a human homolog gene of RNA helicase, is induced by retinoic acid during the differentiation of acute promyelocytic leukemia cell."
      Sun Y.-W.
      Thesis (1997), Shanghai Institute of Hematology, China
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-580.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-580, INDUCTION.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-748 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-925 (ISOFORMS 1/2), VARIANT CYS-7.
      Tissue: Skin and Testis.
    7. "Retinoic acid-inducible gene-I is induced by interferon-gamma and regulates the expression of interferon-gamma stimulated gene 15 in MCF-7 cells."
      Cui X.-F., Imaizumi T., Yoshida H., Borden E.C., Satoh K.
      Biochem. Cell Biol. 82:401-405(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, SUBCELLULAR LOCATION.
    8. "Expression of retinoic acid-inducible gene-I in vascular smooth muscle cells stimulated with interferon-gamma."
      Imaizumi T., Yagihashi N., Hatakeyama M., Yamashita K., Ishikawa A., Taima K., Yoshida H., Inoue I., Fujita T., Yagihashi S., Satoh K.
      Life Sci. 75:1171-1180(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    9. "The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses."
      Yoneyama M., Kikuchi M., Natsukawa T., Shinobu N., Imaizumi T., Miyagishi M., Taira K., Akira S., Fujita T.
      Nat. Immunol. 5:730-737(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, MUTAGENESIS OF LYS-270, SUBCELLULAR LOCATION, BINDING TO DOUBLE-STRANDED RNA, FUNCTION.
    10. "Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3."
      Seth R.B., Sun L., Ea C.-K., Chen Z.J.
      Cell 122:669-682(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAVS/IPS1.
    11. "SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways."
      Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B.
      EMBO J. 24:4018-4028(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKBKE AND TBK1.
    12. "Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I."
      Sumpter R. Jr., Loo Y.-M., Foy E., Li K., Yoneyama M., Fujita T., Lemon S.M., Gale M. Jr.
      J. Virol. 79:2689-2699(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, MUTAGENESIS OF THR-55 AND LYS-270, BINDING TO DOUBLE-STRANDED RNA, FUNCTION.
    13. "VISA is an adapter protein required for virus-triggered IFN-beta Signaling."
      Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.
      Mol. Cell 19:727-740(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAVS/IPS1.
    14. "IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction."
      Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S.
      Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAVS/IPS1.
    15. "Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways."
      Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.
      Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ISGYLATION.
    16. "TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity."
      Gack M.U., Shin Y.C., Joo C.H., Urano T., Liang C., Sun L., Takeuchi O., Akira S., Chen Z., Inoue S., Jung J.U.
      Nature 446:916-920(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM25, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF LYS-99; LYS-169; LYS-172; LYS-181 AND LYS-193.
    17. "Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2."
      Saito T., Hirai R., Loo Y.-M., Owen D., Johnson C.L., Sinha S.C., Akira S., Fujita T., Gale M. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 104:582-587(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, REPRESSOR DOMAIN, INTERACTION WITH DHX58.
    18. Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH CYLD.
    19. "Negative feedback regulation of RIG-I-mediated antiviral signaling by interferon-induced ISG15 conjugation."
      Kim M.J., Hwang S.Y., Imaizumi T., Yoo J.Y.
      J. Virol. 82:1474-1483(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION.
    20. "STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling."
      Ishikawa H., Barber G.N.
      Nature 455:674-678(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM173.
    21. "RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway."
      Chiu Y.-H., Macmillan J.B., Chen Z.J.
      Cell 138:576-591(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus."
      Schlee M., Roth A., Hornung V., Hagmann C.A., Wimmenauer V., Barchet W., Coch C., Janke M., Mihailovic A., Wardle G., Juranek S., Kato H., Kawai T., Poeck H., Fitzgerald K.A., Takeuchi O., Akira S., Tuschl T.
      , Latz E., Ludwig J., Hartmann G.
      Immunity 31:25-34(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Riplet/RNF135, a RING finger protein, ubiquitinates RIG-I to promote interferon-beta induction during the early phase of viral infection."
      Oshiumi H., Matsumoto M., Hatakeyama S., Seya T.
      J. Biol. Chem. 284:807-817(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH RNF135.
    24. "Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions."
      Mukherjee A., Morosky S.A., Shen L., Weber C.R., Turner J.R., Kim K.S., Wang T., Coyne C.B.
      J. Biol. Chem. 284:6486-6494(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    25. "Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2."
      Bamming D., Horvath C.M.
      J. Biol. Chem. 284:9700-9712(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling."
      Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.
      J. Biol. Chem. 284:19122-19131(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRC.
    27. "Human respiratory syncytial virus nonstructural protein NS2 antagonizes the activation of beta interferon transcription by interacting with RIG-I."
      Ling Z., Tran K.C., Teng M.N.
      J. Virol. 83:3734-3742(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRSV PROTEIN NS2.
    28. "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate."
      Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A., Hornung V.
      Nat. Immunol. 10:1065-1072(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "REUL is a novel E3 ubiquitin ligase and stimulator of retinoic-acid-inducible gene-I."
      Gao D., Yang Y.K., Wang R.P., Zhou X., Diao F.C., Li M.D., Zhai Z.H., Jiang Z.F., Chen D.Y.
      PLoS ONE 4:E5760-E5760(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-154; LYS-164 AND LYS-172, INTERACTION WITH RNF135, MUTAGENESIS OF LYS-154; LYS-164 AND LYS-172.
    30. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-858, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways."
      Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P., Zheng S., Chen Z.J., Wang R.F.
      Cell 141:483-496(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NLRC5.
    32. "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
      Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
      Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP17L2.
    33. "Function and regulation of retinoic acid-inducible gene-I."
      Matsumiya T., Stafforini D.M.
      Crit. Rev. Immunol. 30:489-513(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    34. "Z proteins of New World arenaviruses bind RIG-I and interfere with type I interferon induction."
      Fan L., Briese T., Lipkin W.I.
      J. Virol. 84:1785-1791(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEW WORLD ARENAVIRUSES PROTEIN Z.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Immune signaling by RIG-I-like receptors."
      Loo Y.M., Gale M. Jr.
      Immunity 34:680-692(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    37. "RIG-I-like receptors: cytoplasmic sensors for non-self RNA."
      Kato H., Takahasi K., Fujita T.
      Immunol. Rev. 243:91-98(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    38. "Innate immune responses in human monocyte-derived dendritic cells are highly dependent on the size and the 5' phosphorylation of RNA molecules."
      Jiang M., Osterlund P., Sarin L.P., Poranen M.M., Bamford D.H., Guo D., Julkunen I.
      J. Immunol. 187:1713-1721(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    39. "IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging MAVS and TBK1."
      Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.
      J. Immunol. 187:2559-2568(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT3.
    40. Cited for: REVIEW ON FUNCTION.
    41. "Phosphorylation of RIG-I by casein kinase II inhibits its antiviral response."
      Sun Z., Ren H., Liu Y., Teeling J.L., Gu J.
      J. Virol. 85:1036-1047(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-770; SER-854 AND SER-855.
    42. "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling."
      Miyashita M., Oshiumi H., Matsumoto M., Seya T.
      Mol. Cell. Biol. 31:3802-3819(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX60.
    43. Cited for: INTERACTION WITH ZC3HAV1, SUBCELLULAR LOCATION.
    44. "Rotavirus nonstructural protein 1 antagonizes innate immune response by interacting with retinoic acid inducible gene I."
      Qin L., Ren L., Zhou Z., Lei X., Chen L., Xue Q., Liu X., Wang J., Hung T.
      Virol. J. 8:526-526(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROTAVIRUS PROTEIN NSP1.
    45. "Sensing of viral nucleic acids by RIG-I: from translocation to translation."
      Schmidt A., Rothenfusser S., Hopfner K.P.
      Eur. J. Cell Biol. 91:78-85(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    46. Cited for: SUMOYLATION BY MUL1.
    47. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 802-925 IN COMPLEX WITH ZINC IONS.
    48. "Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses."
      Takahasi K., Yoneyama M., Nishihori T., Hirai R., Kumeta H., Narita R., Gale M. Jr., Inagaki F., Fujita T.
      Mol. Cell 29:428-440(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 792-925.

    Entry informationi

    Entry nameiDDX58_HUMAN
    AccessioniPrimary (citable) accession number: O95786
    Secondary accession number(s): A2RU81
    , Q5HYE1, Q5VYT1, Q9NT04
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 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 9
      Human chromosome 9: 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