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Q8R5F7

- IFIH1_MOUSE

UniProt

Q8R5F7 - IFIH1_MOUSE

Protein

Interferon-induced helicase C domain-containing protein 1

Gene

Ifih1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      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 mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length). 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. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and theiler's murine encephalomyelitis virus (TMEV). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines.5 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Zinc.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei208 – 2092Cleavage
    Sitei216 – 2172Cleavage
    Sitei251 – 2522Cleavage
    Metal bindingi907 – 9071ZincBy similarity
    Metal bindingi910 – 9101ZincBy similarity
    Metal bindingi962 – 9621ZincBy similarity
    Metal bindingi964 – 9641ZincBy similarity

    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: MGI
    6. ribonucleoprotein complex binding Source: Ensembl
    7. single-stranded RNA binding Source: UniProtKB
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. innate immune response Source: UniProtKB
    3. positive regulation of interferon-alpha production Source: UniProtKB
    4. positive regulation of interferon-beta production Source: UniProtKB
    5. protein sumoylation Source: UniProtKB
    6. regulation of apoptotic process Source: InterPro
    7. response to virus Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Antiviral defense, Immunity, Innate immunity

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon-induced helicase C domain-containing protein 1 (EC:3.6.4.13)
    Alternative name(s):
    Helicase with 2 CARD domains
    Short name:
    Helicard
    Interferon induced with helicase C domain protein 1
    Melanoma differentiation-associated protein 5
    Short name:
    MDA-5
    RIG-I-like receptor 2
    Short name:
    RLR-2
    Gene namesi
    Name:Ifih1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1918836. Ifih1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus Curated
    Note: May be found in the nucleus, during apoptosis.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10251025Interferon-induced helicase C domain-containing protein 1PRO_0000102013Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei645 – 6451Phosphoserine1 Publication
    Modified residuei648 – 6481Phosphoserine1 Publication

    Post-translational modificationi

    During apoptosis, processed into 3 cleavage products. The helicase-containing fragment, once liberated from the CARD domains, translocate from the cytoplasm to the nucleus. The processed protein significantly sensitizes cells to DNA degradation.1 Publication
    Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta By similarity.By similarity
    Ubiquitinated. USP17L2/USP17-dependent deubiquitination positively regulates the receptor By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8R5F7.
    PaxDbiQ8R5F7.
    PRIDEiQ8R5F7.

    PTM databases

    PhosphoSiteiQ8R5F7.

    Expressioni

    Tissue specificityi

    Expression is prominent in lung, liver, kidney, heart and spleen (at protein level). Widely expressed at low level.1 Publication

    Inductioni

    By interferon (IFN).

    Gene expression databases

    ArrayExpressiQ8R5F7.
    BgeeiQ8R5F7.
    CleanExiMM_IFIH1.
    GenevestigatoriQ8R5F7.

    Interactioni

    Subunit structurei

    Monomer in the absence of ligands and homodimerizes in the presence of dsRNA ligands. Can assemble into helical or linear polymeric filaments on long dsRNA. Interacts with MAVS/IPS1. Interacts with V protein of Sendai virus. Binding to paramyxoviruses V proteins prevents IFN-beta induction, and the further establishment of an antiviral state By similarity. Interacts with PCBP2 By similarity. Interacts with NLRC5 By similarity. Interacts with PIAS2-beta By similarity. Interacts with DDX60 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi214799. 1 interaction.
    DIPiDIP-60085N.
    IntActiQ8R5F7. 1 interaction.
    MINTiMINT-4118007.

    Structurei

    Secondary structure

    1
    1025
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi550 – 56516
    Helixi577 – 59317
    Helixi596 – 61722
    Helixi620 – 64021
    Helixi671 – 69121
    Helixi694 – 6963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TS9X-ray2.00A545-697[»]
    ProteinModelPortaliQ8R5F7.
    SMRiQ8R5F7. Positions 8-199, 300-1025.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 9791CARD 1Add
    BLAST
    Domaini110 – 19081CARD 2Add
    BLAST
    Domaini317 – 510194Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini700 – 872173Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    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.
    GeneTreeiENSGT00510000046789.
    HOVERGENiHBG106019.
    InParanoidiA2AUY7.
    KOiK12647.
    OMAiKCGQAWG.
    OrthoDBiEOG7RV9FC.
    PhylomeDBiQ8R5F7.
    TreeFamiTF330258.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR021673. RIG-I_C-RD.
    [Graphical view]
    PfamiPF00619. CARD. 1 hit.
    PF00271. 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]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF52540. SSF52540. 2 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: Q8R5F7-1) [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

    MSIVCSAEDS FRNLILFFRP RLKMYIQVEP VLDHLIFLSA ETKEQILKKI     50
    NTCGNTSAAE LLLSTLEQGQ WPLGWTQMFV EALEHSGNPL AARYVKPTLT 100
    DLPSPSSETA HDECLHLLTL LQPTLVDKLL INDVLDTCFE KGLLTVEDRN 150
    RISAAGNSGN ESGVRELLRR IVQKENWFST FLDVLRQTGN DALFQELTGG 200
    GCPEDNTDLA NSSHRDGPAA NECLLPAVDE SSLETEAWNV DDILPEASCT 250
    DSSVTTESDT SLAEGSVSCF DESLGHNSNM GRDSGTMGSD SDESVIQTKR 300
    VSPEPELQLR PYQMEVAQPA LDGKNIIICL PTGSGKTRVA VYITKDHLDK 350
    KKQASESGKV IVLVNKVMLA EQLFRKEFNP YLKKWYRIIG LSGDTQLKIS 400
    FPEVVKSYDV IISTAQILEN SLLNLESGDD DGVQLSDFSL IIIDECHHTN 450
    KEAVYNNIMR RYLKQKLRNN DLKKQNKPAI PLPQILGLTA SPGVGAAKKQ 500
    SEAEKHILNI CANLDAFTIK TVKENLGQLK HQIKEPCKKF VIADDTRENP 550
    FKEKLLEIMA SIQTYCQKSP MSDFGTQHYE QWAIQMEKKA AKDGNRKDRV 600
    CAEHLRKYNE ALQINDTIRM IDAYSHLETF YTDEKEKKFA VLNDSDKSDD 650
    EASSCNDQLK GDVKKSLKLD ETDEFLMNLF FDNKKMLKKL AENPKYENEK 700
    LIKLRNTILE QFTRSEESSR GIIFTKTRQS TYALSQWIME NAKFAEVGVK 750
    AHHLIGAGHS SEVKPMTQTE QKEVISKFRT GEINLLIATT VAEEGLDIKE 800
    CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVTSSGSGV TEREIVNDFR 850
    EKMMYKAINR VQNMKPEEYA HKILELQVQS ILEKKMKVKR SIAKQYNDNP 900
    SLITLLCKNC SMLVCSGENI HVIEKMHHVN MTPEFKGLYI VRENKALQKK 950
    FADYQTNGEI ICKCGQAWGT MMVHKGLDLP CLKIRNFVVN FKNNSPKKQY 1000
    KKWVELPIRF PDLDYSEYCL YSDED 1025
    Length:1,025
    Mass (Da):115,971
    Last modified:June 1, 2002 - v1
    Checksum:i708FCAC690C9F6D8
    GO
    Isoform 2 (identifier: Q8R5F7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         207-255: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:976
    Mass (Da):110,842
    Checksum:iB9F6D84C207F1031
    GO

    Sequence cautioni

    The sequence AAH25508.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001T → I in AAH80200. (PubMed:15489334)Curated
    Sequence conflicti339 – 3391V → E in BAE31652. (PubMed:16141072)Curated
    Sequence conflicti412 – 4143IST → TRP in AAH25508. (PubMed:15489334)Curated
    Sequence conflicti624 – 6241Y → H in AAH25508. (PubMed:15489334)Curated
    Sequence conflicti629 – 6291T → A in AAM21359. (PubMed:11805321)Curated
    Sequence conflicti647 – 6471K → E in AAH25508. (PubMed:15489334)Curated
    Sequence conflicti647 – 6471K → E in AAH04031. (PubMed:15489334)Curated
    Sequence conflicti647 – 6471K → E in AAH80200. (PubMed:15489334)Curated
    Sequence conflicti889 – 8891K → E in BAB31303. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei207 – 25549Missing in isoform 2. 1 PublicationVSP_013339Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY075132 mRNA. Translation: AAL77205.1.
    AF374384 mRNA. Translation: AAM21359.1.
    AK018602 mRNA. Translation: BAB31303.2.
    AK037057 mRNA. Translation: BAC29687.2.
    AK040519 mRNA. Translation: BAC30614.1.
    AK153018 mRNA. Translation: BAE31652.1.
    AL929246 Genomic DNA. Translation: CAM21790.1.
    BC004031 mRNA. Translation: AAH04031.1.
    BC019605 mRNA. Translation: AAH19605.1.
    BC025508 mRNA. Translation: AAH25508.1. Different initiation.
    BC080200 mRNA. Translation: AAH80200.1.
    CCDSiCCDS16068.1. [Q8R5F7-1]
    CCDS50594.1. [Q8R5F7-2]
    RefSeqiNP_001157949.1. NM_001164477.1. [Q8R5F7-2]
    NP_082111.2. NM_027835.3. [Q8R5F7-1]
    UniGeneiMm.136224.

    Genome annotation databases

    EnsembliENSMUST00000028259; ENSMUSP00000028259; ENSMUSG00000026896. [Q8R5F7-1]
    ENSMUST00000112459; ENSMUSP00000108078; ENSMUSG00000026896. [Q8R5F7-2]
    GeneIDi71586.
    KEGGimmu:71586.
    UCSCiuc008jvm.2. mouse. [Q8R5F7-1]
    uc012bvy.1. mouse. [Q8R5F7-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY075132 mRNA. Translation: AAL77205.1 .
    AF374384 mRNA. Translation: AAM21359.1 .
    AK018602 mRNA. Translation: BAB31303.2 .
    AK037057 mRNA. Translation: BAC29687.2 .
    AK040519 mRNA. Translation: BAC30614.1 .
    AK153018 mRNA. Translation: BAE31652.1 .
    AL929246 Genomic DNA. Translation: CAM21790.1 .
    BC004031 mRNA. Translation: AAH04031.1 .
    BC019605 mRNA. Translation: AAH19605.1 .
    BC025508 mRNA. Translation: AAH25508.1 . Different initiation.
    BC080200 mRNA. Translation: AAH80200.1 .
    CCDSi CCDS16068.1. [Q8R5F7-1 ]
    CCDS50594.1. [Q8R5F7-2 ]
    RefSeqi NP_001157949.1. NM_001164477.1. [Q8R5F7-2 ]
    NP_082111.2. NM_027835.3. [Q8R5F7-1 ]
    UniGenei Mm.136224.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3TS9 X-ray 2.00 A 545-697 [» ]
    ProteinModelPortali Q8R5F7.
    SMRi Q8R5F7. Positions 8-199, 300-1025.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 214799. 1 interaction.
    DIPi DIP-60085N.
    IntActi Q8R5F7. 1 interaction.
    MINTi MINT-4118007.

    PTM databases

    PhosphoSitei Q8R5F7.

    Proteomic databases

    MaxQBi Q8R5F7.
    PaxDbi Q8R5F7.
    PRIDEi Q8R5F7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028259 ; ENSMUSP00000028259 ; ENSMUSG00000026896 . [Q8R5F7-1 ]
    ENSMUST00000112459 ; ENSMUSP00000108078 ; ENSMUSG00000026896 . [Q8R5F7-2 ]
    GeneIDi 71586.
    KEGGi mmu:71586.
    UCSCi uc008jvm.2. mouse. [Q8R5F7-1 ]
    uc012bvy.1. mouse. [Q8R5F7-2 ]

    Organism-specific databases

    CTDi 64135.
    MGIi MGI:1918836. Ifih1.

    Phylogenomic databases

    eggNOGi COG1111.
    GeneTreei ENSGT00510000046789.
    HOVERGENi HBG106019.
    InParanoidi A2AUY7.
    KOi K12647.
    OMAi KCGQAWG.
    OrthoDBi EOG7RV9FC.
    PhylomeDBi Q8R5F7.
    TreeFami TF330258.

    Enzyme and pathway databases

    Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Miscellaneous databases

    NextBioi 334053.
    PROi Q8R5F7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8R5F7.
    Bgeei Q8R5F7.
    CleanExi MM_IFIH1.
    Genevestigatori Q8R5F7.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR021673. RIG-I_C-RD.
    [Graphical view ]
    Pfami PF00619. CARD. 1 hit.
    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 SSF47986. SSF47986. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation."
      Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J.
      Curr. Biol. 12:838-843(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CLEAVAGE SITES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. Erratum
      Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J.
      Curr. Biol. 12:1633-1633(2002)
    3. "mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties."
      Kang D.-C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M., Fisher P.B.
      Proc. Natl. Acad. Sci. U.S.A. 99:637-642(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Bone marrow, Cecum, Thymus and Vagina.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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).
      Strain: FVB/N.
      Tissue: Mammary gland.
    7. Cited for: FUNCTION.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. Cited for: FUNCTION.
    10. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Activation of MDA5 requires higher-order RNA structures generated during virus infection."
      Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O., Akira S., Way M., Schiavo G., Reis e Sousa C.
      J. Virol. 83:10761-10769(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "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.
    13. "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.
    14. Cited for: REVIEW ON FUNCTION.
    15. "2 methylate or not 2 methylate: viral evasion of the type I interferon response."
      Garcia-Sastre A.
      Nat. Immunol. 12:114-115(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    16. "Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5."
      Zuest R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., Szretter K.J., Baker S.C., Barchet W., Diamond M.S., Siddell S.G., Ludewig B., Thiel V.
      Nat. Immunol. 12:137-143(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA."
      Berke I.C., Modis Y.
      EMBO J. 31:1714-1726(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 545-697, SUBUNIT.

    Entry informationi

    Entry nameiIFIH1_MOUSE
    AccessioniPrimary (citable) accession number: Q8R5F7
    Secondary accession number(s): A2AUY7
    , Q3U6S2, Q68EM4, Q8BYC9, Q8BZ01, Q8K5C7, Q8R144, Q8VE79, Q99KS4, Q9D2Z5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3