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Q96C10

- DHX58_HUMAN

UniProt

Q96C10 - DHX58_HUMAN

Protein

Probable ATP-dependent RNA helicase DHX58

Gene

DHX58

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to DDX58/RIG-I and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on DDX58/RIG-I signaling may involve the following mechanisms: competition with DDX58/RIG-I for binding to the viral RNA, binding to DDX58/RIG-I and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by DDX58/RIG-I and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate.10 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Zinc.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi556 – 5561Zinc
    Metal bindingi559 – 5591Zinc
    Metal bindingi612 – 6121Zinc
    Metal bindingi615 – 6151Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi24 – 318ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. innate immune response Source: UniProtKB-KW
    3. negative regulation of innate immune response Source: UniProtKB
    4. negative regulation of MDA-5 signaling pathway Source: UniProtKB
    5. negative regulation of RIG-I signaling pathway Source: UniProtKB
    6. negative regulation of type I interferon production Source: UniProtKB
    7. positive regulation of MDA-5 signaling pathway Source: UniProtKB
    8. positive regulation of RIG-I signaling pathway Source: UniProtKB
    9. positive regulation of type I interferon production Source: UniProtKB
    10. regulation of innate immune response Source: UniProtKB
    11. response to virus Source: UniProtKB
    12. 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_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DHX58 (EC:3.6.4.13)
    Alternative name(s):
    Probable ATP-dependent helicase LGP2
    Protein D11Lgp2 homolog
    RIG-I-like receptor 3
    Short name:
    RLR-3
    RIG-I-like receptor LGP2
    Short name:
    RLR
    Gene namesi
    Name:DHX58
    Synonyms:D11LGP2E, LGP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:29517. DHX58.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi634 – 6341K → E: Abolishes RNA binding. 2 Publications
    Mutagenesisi651 – 6511K → E: Abolishes RNA binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA162383566.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 678678Probable ATP-dependent RNA helicase DHX58PRO_0000102010Add
    BLAST

    Proteomic databases

    MaxQBiQ96C10.
    PaxDbiQ96C10.
    PRIDEiQ96C10.

    PTM databases

    PhosphoSiteiQ96C10.

    Expressioni

    Inductioni

    By interferon (IFN), virus infection, or intracellular dsRNA.

    Gene expression databases

    ArrayExpressiQ96C10.
    BgeeiQ96C10.
    CleanExiHS_DHX58.
    GenevestigatoriQ96C10.

    Organism-specific databases

    HPAiHPA018670.
    HPA019570.

    Interactioni

    Subunit structurei

    Monomer in the absence of dsRNA. Homodimer in the presence of dsRNA. Interacts with DDX58/RIG-I (via CARD domain), MAVS/IPS1 and DDX60. Found in a complex with DDX58/RIG-I and IFIH1/MDA5. Interacts (via helicase C-terminal domain) with non-structural protein V of Human parainfluenza 2 virus, Human parainfluenza 5 virus, measles virus, mumps virus, hendra virus and nipah virus.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGO2Q9UKV82EBI-744193,EBI-528269
    DHX30Q7L2E32EBI-744193,EBI-1211456
    DICER1Q9UPY32EBI-744193,EBI-395506
    EIF2AK2P195252EBI-744193,EBI-640775
    EIF6P565372EBI-744193,EBI-372243
    NKRFO152262EBI-744193,EBI-766011
    P/VP112072EBI-744193,EBI-6148694From a different organism.
    P/VP309272EBI-744193,EBI-6599165From a different organism.
    P/VQ9EMA92EBI-744193,EBI-6598728From a different organism.
    STAU2Q9NUL32EBI-744193,EBI-722938

    Protein-protein interaction databases

    BioGridi122553. 14 interactions.
    DIPiDIP-60792N.
    IntActiQ96C10. 18 interactions.
    MINTiMINT-1460040.
    STRINGi9606.ENSP00000251642.

    Structurei

    Secondary structure

    1
    678
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi549 – 5513
    Beta strandi553 – 5564
    Turni557 – 5593
    Beta strandi562 – 5654
    Helixi566 – 5683
    Beta strandi569 – 5724
    Turni573 – 5753
    Beta strandi576 – 5794
    Helixi582 – 5876
    Beta strandi588 – 5903
    Beta strandi592 – 5943
    Beta strandi597 – 5993
    Beta strandi602 – 61211
    Turni613 – 6153
    Beta strandi618 – 6258
    Beta strandi628 – 6336
    Helixi635 – 6373
    Beta strandi638 – 6425
    Beta strandi645 – 6473
    Helixi652 – 6543
    Beta strandi655 – 6573
    Helixi664 – 6718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RQANMR-A546-678[»]
    2W4RX-ray2.60A/B/C/D537-678[»]
    3EQTX-ray2.00A/B541-678[»]
    ProteinModelPortaliQ96C10.
    SMRiQ96C10. Positions 1-678.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96C10.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 188178Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini350 – 514165Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni476 – 678203Repressor domainAdd
    BLAST
    Regioni572 – 65584RNA-bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili489 – 54658Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi131 – 1344DECH box

    Domaini

    The repressor domain is capable of inhibiting dimerization and signaling of DDX58/RIG-I and also facilitates binding of dsRNA.

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1111.
    HOGENOMiHOG000230992.
    HOVERGENiHBG106019.
    InParanoidiQ96C10.
    KOiK12649.
    OMAiENPKLEM.
    PhylomeDBiQ96C10.
    TreeFamiTF330258.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR021673. RIG-I_C-RD.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF04851. ResIII. 1 hit.
    PF11648. RIG-I_C-RD. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96C10-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELRSYQWEV IMPALEGKNI IIWLPTGAGK TRAAAYVAKR HLETVDGAKV    50
    VVLVNRVHLV TQHGEEFRRM LDGRWTVTTL SGDMGPRAGF GHLARCHDLL 100
    ICTAELLQMA LTSPEEEEHV ELTVFSLIVV DECHHTHKDT VYNVIMSQYL 150
    ELKLQRAQPL PQVLGLTASP GTGGASKLDG AINHVLQLCA NLDTWCIMSP 200
    QNCCPQLQEH SQQPCKQYNL CHRRSQDPFG DLLKKLMDQI HDHLEMPELS 250
    RKFGTQMYEQ QVVKLSEAAA LAGLQEQRVY ALHLRRYNDA LLIHDTVRAV 300
    DALAALQDFY HREHVTKTQI LCAERRLLAL FDDRKNELAH LATHGPENPK 350
    LEMLEKILQR QFSSSNSPRG IIFTRTRQSA HSLLLWLQQQ QGLQTVDIRA 400
    QLLIGAGNSS QSTHMTQRDQ QEVIQKFQDG TLNLLVATSV AEEGLDIPHC 450
    NVVVRYGLLT NEISMVQARG RARADQSVYA FVATEGSREL KRELINEALE 500
    TLMEQAVAAV QKMDQAEYQA KIRDLQQAAL TKRAAQAAQR ENQRQQFPVE 550
    HVQLLCINCM VAVGHGSDLR KVEGTHHVNV NPNFSNYYNV SRDPVVINKV 600
    FKDWKPGGVI SCRNCGEVWG LQMIYKSVKL PVLKVRSMLL ETPQGRIQAK 650
    KWSRVPFSVP DFDFLQHCAE NLSDLSLD 678
    Length:678
    Mass (Da):76,613
    Last modified:December 1, 2001 - v1
    Checksum:i859E1749C7313D06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti473 – 4731R → W in BAB13818. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761T → A.
    Corresponds to variant rs34891485 [ dbSNP | Ensembl ].
    VAR_049336
    Natural varianti95 – 951R → Q.
    Corresponds to variant rs35118457 [ dbSNP | Ensembl ].
    VAR_049337
    Natural varianti425 – 4251Q → R.
    Corresponds to variant rs2074158 [ dbSNP | Ensembl ].
    VAR_019394
    Natural varianti523 – 5231R → Q.
    Corresponds to variant rs2074160 [ dbSNP | Ensembl ].
    VAR_019395

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK021416 mRNA. Translation: BAB13818.1.
    BC014949 mRNA. Translation: AAH14949.1.
    CCDSiCCDS11416.1.
    RefSeqiNP_077024.2. NM_024119.2.
    UniGeneiHs.55918.

    Genome annotation databases

    EnsembliENST00000251642; ENSP00000251642; ENSG00000108771.
    GeneIDi79132.
    KEGGihsa:79132.
    UCSCiuc002hyw.3. human.

    Polymorphism databases

    DMDMi50401123.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK021416 mRNA. Translation: BAB13818.1 .
    BC014949 mRNA. Translation: AAH14949.1 .
    CCDSi CCDS11416.1.
    RefSeqi NP_077024.2. NM_024119.2.
    UniGenei Hs.55918.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RQA NMR - A 546-678 [» ]
    2W4R X-ray 2.60 A/B/C/D 537-678 [» ]
    3EQT X-ray 2.00 A/B 541-678 [» ]
    ProteinModelPortali Q96C10.
    SMRi Q96C10. Positions 1-678.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122553. 14 interactions.
    DIPi DIP-60792N.
    IntActi Q96C10. 18 interactions.
    MINTi MINT-1460040.
    STRINGi 9606.ENSP00000251642.

    PTM databases

    PhosphoSitei Q96C10.

    Polymorphism databases

    DMDMi 50401123.

    Proteomic databases

    MaxQBi Q96C10.
    PaxDbi Q96C10.
    PRIDEi Q96C10.

    Protocols and materials databases

    DNASUi 79132.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251642 ; ENSP00000251642 ; ENSG00000108771 .
    GeneIDi 79132.
    KEGGi hsa:79132.
    UCSCi uc002hyw.3. human.

    Organism-specific databases

    CTDi 79132.
    GeneCardsi GC17M040255.
    HGNCi HGNC:29517. DHX58.
    HPAi HPA018670.
    HPA019570.
    MIMi 608588. gene.
    neXtProti NX_Q96C10.
    PharmGKBi PA162383566.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1111.
    HOGENOMi HOG000230992.
    HOVERGENi HBG106019.
    InParanoidi Q96C10.
    KOi K12649.
    OMAi ENPKLEM.
    PhylomeDBi Q96C10.
    TreeFami TF330258.

    Enzyme and pathway databases

    Reactomei REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Miscellaneous databases

    ChiTaRSi DHX58. human.
    EvolutionaryTracei Q96C10.
    GeneWikii LGP2.
    GenomeRNAii 79132.
    NextBioi 67993.
    PROi Q96C10.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96C10.
    Bgeei Q96C10.
    CleanExi HS_DHX58.
    Genevestigatori Q96C10.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR021673. RIG-I_C-RD.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF04851. ResIII. 1 hit.
    PF11648. RIG-I_C-RD. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.
    2. "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].
      Tissue: Colon.
    3. "Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity."
      Yoneyama M., Kikuchi M., Matsumoto K., Imaizumi T., Miyagishi M., Taira K., Foy E., Loo Y.-M., Gale M. Jr., Akira S., Yonehara S., Kato A., Fujita T.
      J. Immunol. 175:2851-2858(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2."
      Komuro A., Horvath C.M.
      J. Virol. 80:12332-12342(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAVS/IPS1 AND DDX58/RIG-I.
    5. "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, INTERACTION WITH DDX58/RIG-I.
    6. "Regulation of interferon production by RIG-I and LGP2: a lesson in self-control."
      Vitour D., Meurs E.F.
      Sci. STKE 2007:PE20-PE20(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    7. "Structure and function of LGP2, a DEX(D/H) helicase that regulates the innate immunity response."
      Murali A., Li X., Ranjith-Kumar C.T., Bhardwaj K., Holzenburg A., Li P., Kao C.C.
      J. Biol. Chem. 283:15825-15833(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    8. "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.
    9. "A shared interface mediates paramyxovirus interference with antiviral RNA helicases MDA5 and LGP2."
      Parisien J.P., Bamming D., Komuro A., Ramachandran A., Rodriguez J.J., Barber G., Wojahn R.D., Horvath C.M.
      J. Virol. 83:7252-7260(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARAMYXOVIRUSES NON-STRUCTURAL PROTEIN V.
    10. "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.
    11. "RIG-I/MDA5/MAVS are required to signal a protective IFN response in rotavirus-infected intestinal epithelium."
      Broquet A.H., Hirata Y., McAllister C.S., Kagnoff M.F.
      J. Immunol. 186:1618-1626(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Ambivalent role of the innate immune response in rabies virus pathogenesis."
      Chopy D., Pothlichet J., Lafage M., Megret F., Fiette L., Si-Tahar M., Lafon M.
      J. Virol. 85:6657-6668(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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.
    14. "Regulation of RLR-mediated innate immune signaling--it is all about keeping the balance."
      Eisenaecher K., Krug A.
      Eur. J. Cell Biol. 91:36-47(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    15. "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.
    16. "The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA."
      Li X., Ranjith-Kumar C.T., Brooks M.T., Dharmaiah S., Herr A.B., Kao C., Li P.
      J. Biol. Chem. 284:13881-13891(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 541-678 IN COMPLEX WITH RNA, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-634 AND LYS-651, ZINC-BINDING SITES.
    17. "Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors."
      Takahasi K., Kumeta H., Tsuduki N., Narita R., Shigemoto T., Hirai R., Yoneyama M., Horiuchi M., Ogura K., Fujita T., Inagaki F.
      J. Biol. Chem. 284:17465-17474(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 546-678, FUNCTION, SUBCELLULAR LOCATION.
    18. "The regulatory domain of the RIG-I family ATPase LGP2 senses double-stranded RNA."
      Pippig D.A., Hellmuth J.C., Cui S., Kirchhofer A., Lammens K., Lammens A., Schmidt A., Rothenfusser S., Hopfner K.-P.
      Nucleic Acids Res. 37:2014-2025(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 537-678, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-634, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiDHX58_HUMAN
    AccessioniPrimary (citable) accession number: Q96C10
    Secondary accession number(s): Q9HAM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 107 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 17
      Human chromosome 17: 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