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)

Q92985

- IRF7_HUMAN

UniProt

Q92985 - IRF7_HUMAN

Protein

Interferon regulatory factor 7

Gene

IRF7

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 138 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages.4 Publications

    Enzyme regulationi

    In the absence of viral infection, maintained as a monomer in an autoinhibited state and phosphorylation disrupts this autoinhibition leading to the liberation of the DNA-binding and dimerization activities and its nuclear localization where it can activate type I IFN and ISG genes.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi11 – 126116IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Source: UniProtKB
    4. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. cytokine-mediated signaling pathway Source: Reactome
    3. establishment of viral latency Source: UniProtKB
    4. immunoglobulin mediated immune response Source: Ensembl
    5. innate immune response Source: UniProtKB
    6. interferon-alpha production Source: UniProtKB
    7. interferon-beta production Source: UniProtKB
    8. interferon-gamma-mediated signaling pathway Source: Reactome
    9. MDA-5 signaling pathway Source: UniProtKB
    10. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    11. negative regulation of macrophage apoptotic process Source: UniProtKB
    12. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    13. positive regulation of interferon-alpha production Source: UniProtKB
    14. positive regulation of interferon-beta production Source: UniProtKB
    15. positive regulation of transcription, DNA-templated Source: UniProtKB
    16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    17. positive regulation of type I interferon-mediated signaling pathway Source: Ensembl
    18. positive regulation of type I interferon production Source: Reactome
    19. regulation of adaptive immune response Source: UniProtKB
    20. regulation of immune response Source: UniProtKB
    21. regulation of monocyte differentiation Source: UniProtKB
    22. regulation of MyD88-dependent toll-like receptor signaling pathway Source: UniProtKB
    23. regulation of MyD88-independent toll-like receptor signaling pathway Source: UniProtKB
    24. regulation of type I interferon production Source: UniProtKB
    25. response to virus Source: UniProtKB
    26. toll-like receptor 3 signaling pathway Source: Reactome
    27. toll-like receptor 4 signaling pathway Source: Reactome
    28. toll-like receptor 9 signaling pathway Source: Reactome
    29. toll-like receptor signaling pathway Source: Reactome
    30. transcription from RNA polymerase II promoter Source: ProtInc
    31. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    32. type I interferon biosynthetic process Source: Ensembl
    33. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

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

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25078. Interferon gamma signaling.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25162. Interferon alpha/beta signaling.
    SignaLinkiQ92985.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon regulatory factor 7
    Short name:
    IRF-7
    Gene namesi
    Name:IRF7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:6122. IRF7.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: The phosphorylated and active form accumulates selectively in the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. endosome membrane Source: Reactome
    4. nucleoplasm Source: Reactome
    5. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901G → T: Loss of acetylation, increased DNA-binding and activity; when associated with R-93. 2 Publications
    Mutagenesisi92 – 921K → R: Loss of acetylation, DNA-binding and activity. 2 Publications
    Mutagenesisi93 – 931T → R: Loss of acetylation, increased DNA-binding and activity; when associated with T-90. 2 Publications
    Mutagenesisi477 – 4793SLS → ALA: Complete loss of TBK1 and IKKE phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA29921.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 503503Interferon regulatory factor 7PRO_0000154562Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei92 – 921N6-acetyllysine; by KAT2A and KAT2B1 Publication
    Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki446 – 446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei477 – 4771Phosphoserine; by TBK1 and IKKE1 Publication
    Modified residuei479 – 4791Phosphoserine; by TBK1 and IKKE1 Publication

    Post-translational modificationi

    Acetylation inhibits its DNA-binding ability and activity.1 Publication
    In response to a viral infection, phosphorylated on Ser-477 and Ser-479 by TBK1 and IKBKE1. Phosphorylation, and subsequent activation is inhibited by vaccinia virus protein E3. In TLR7- and TLR9-mediated signaling pathway, phosphorylated by IRAK1.4 Publications
    TRAF6-mediated ubiquitination is required for IRF7 activation.By similarity
    Sumoylated by TRIM28, which inhibits its transactivation activity.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ92985.
    PaxDbiQ92985.
    PRIDEiQ92985.

    PTM databases

    PhosphoSiteiQ92985.

    Expressioni

    Tissue specificityi

    Expressed predominantly in spleen, thymus and peripheral blood leukocytes.

    Inductioni

    By type I interferon (IFN) and viruses.

    Gene expression databases

    ArrayExpressiQ92985.
    BgeeiQ92985.
    CleanExiHS_IRF7.
    GenevestigatoriQ92985.

    Organism-specific databases

    HPAiCAB017694.

    Interactioni

    Subunit structurei

    Monomer. Homodimer; phosphorylation-induced. Heterodimer with IRF3. Interacts with TICAM1 and TICAM2. Interacts with rotavirus A NSP1; this interaction leads to the proteasome-dependent degradation of IRF7. Interacts with Epstein-Barr virus LF2 and human herpes virus 8/HHV-8 proteins ORF45 and vIRF-1. Interacts with MYD88 AND TRAF6.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIPO001702EBI-968267,EBI-704197
    ARAFP103982EBI-968267,EBI-365961
    CCDC47Q96A332EBI-968267,EBI-720151
    CHUKO151114EBI-968267,EBI-81249
    IRAK1P516172EBI-968267,EBI-358664
    LTN1O948222EBI-968267,EBI-1044684
    ORF45F5HDE43EBI-968267,EBI-8843990From a different organism.
    PQ77M193EBI-968267,EBI-6149376From a different organism.
    PALD1Q9ULE62EBI-968267,EBI-3957166
    TBK1Q9UHD22EBI-968267,EBI-356402
    TLK2Q86UE82EBI-968267,EBI-1047967
    TRMT61BQ9BVS52EBI-968267,EBI-3197877

    Protein-protein interaction databases

    BioGridi109873. 42 interactions.
    DIPiDIP-34895N.
    IntActiQ92985. 24 interactions.
    MINTiMINT-1202972.
    STRINGi9606.ENSP00000329411.

    Structurei

    Secondary structure

    1
    503
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2411
    Beta strandi31 – 366
    Beta strandi39 – 435
    Helixi55 – 573
    Helixi58 – 669
    Helixi84 – 10219
    Beta strandi105 – 1128
    Beta strandi119 – 1257

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O61X-ray2.80A8-125[»]
    ProteinModelPortaliQ92985.
    SMRiQ92985. Positions 8-123, 289-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the IRF family.PROSITE-ProRule annotation
    Contains 1 IRF tryptophan pentad repeat DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG39245.
    HOGENOMiHOG000111812.
    HOVERGENiHBG105600.
    KOiK09447.
    OMAiGWKTNFR.
    PhylomeDBiQ92985.
    TreeFamiTF328512.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.60.200.10. 1 hit.
    InterProiIPR019817. Interferon_reg_fac_CS.
    IPR001346. Interferon_reg_fact_DNA-bd_dom.
    IPR019471. Interferon_reg_factor-3.
    IPR017855. SMAD_dom-like.
    IPR008984. SMAD_FHA_domain.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00605. IRF. 1 hit.
    PF10401. IRF-3. 1 hit.
    [Graphical view]
    PRINTSiPR00267. INTFRNREGFCT.
    SMARTiSM00348. IRF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    PROSITEiPS00601. IRF_1. 1 hit.
    PS51507. IRF_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q92985-1) [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

    MALAPERAAP RVLFGEWLLG EISSGCYEGL QWLDEARTCF RVPWKHFARK    50
    DLSEADARIF KAWAVARGRW PPSSRGGGPP PEAETAERAG WKTNFRCALR 100
    STRRFVMLRD NSGDPADPHK VYALSRELCW REGPGTDQTE AEAPAAVPPP 150
    QGGPPGPFLA HTHAGLQAPG PLPAPAGDKG DLLLQAVQQS CLADHLLTAS 200
    WGADPVPTKA PGEGQEGLPL TGACAGGPGL PAGELYGWAV ETTPSPGPQP 250
    AALTTGEAAA PESPHQAEPY LSPSPSACTA VQEPSPGALD VTIMYKGRTV 300
    LQKVVGHPSC TFLYGPPDPA VRATDPQQVA FPSPAELPDQ KQLRYTEELL 350
    RHVAPGLHLE LRGPQLWARR MGKCKVYWEV GGPPGSASPS TPACLLPRNC 400
    DTPIFDFRVF FQELVEFRAR QRRGSPRYTI YLGFGQDLSA GRPKEKSLVL 450
    VKLEPWLCRV HLEGTQREGV SSLDSSSLSL CLSSANSLYD DIECFLMELE 500
    QPA 503
    Length:503
    Mass (Da):54,278
    Last modified:October 17, 2006 - v2
    Checksum:i9863C147514652DE
    GO
    Isoform B (identifier: Q92985-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         228-256: Missing.

    Show »
    Length:474
    Mass (Da):51,459
    Checksum:iF98A7B630497BDD0
    GO
    Isoform C (identifier: Q92985-3) [UniParc]FASTAAdd to Basket

    Also known as: Gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         152-164: GGPPGPFLAHTHA → AQGSLLGSCTGGQ
         165-503: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:164
    Mass (Da):18,036
    Checksum:i6FC0146AD190006D
    GO
    Isoform D (identifier: Q92985-4) [UniParc]FASTAAdd to Basket

    Also known as: H

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MALAPE → MPVPERPAAGPDSPRPGTR

    Show »
    Length:516
    Mass (Da):55,635
    Checksum:i0A659B0BD1FE30F7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791K → E.2 Publications
    Corresponds to variant rs1061502 [ dbSNP | Ensembl ].
    VAR_027957
    Natural varianti204 – 2041D → N.
    Corresponds to variant rs41313489 [ dbSNP | Ensembl ].
    VAR_061273
    Natural varianti412 – 4121Q → R.1 Publication
    Corresponds to variant rs1131665 [ dbSNP | Ensembl ].
    VAR_034017

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MALAPE → MPVPERPAAGPDSPRPGTR in isoform D. 2 PublicationsVSP_002757
    Alternative sequencei152 – 16413GGPPG…AHTHA → AQGSLLGSCTGGQ in isoform C. 1 PublicationVSP_002758Add
    BLAST
    Alternative sequencei165 – 503339Missing in isoform C. 1 PublicationVSP_002759Add
    BLAST
    Alternative sequencei228 – 25629Missing in isoform B. 1 PublicationVSP_002760Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73036 mRNA. Translation: AAB17190.1.
    U53830 mRNA. Translation: AAB80686.1.
    U53831 mRNA. Translation: AAB80688.1.
    U53832 mRNA. Translation: AAB80690.1.
    U53832 mRNA. Translation: AAB80691.1.
    AF076494 mRNA. Translation: AAC70999.1.
    CH471158 Genomic DNA. Translation: EAX02360.1.
    BC136555 mRNA. Translation: AAI36556.1.
    CCDSiCCDS7703.1. [Q92985-1]
    CCDS7704.1. [Q92985-2]
    CCDS7705.1. [Q92985-4]
    RefSeqiNP_001563.2. NM_001572.3. [Q92985-1]
    NP_004020.1. NM_004029.2. [Q92985-2]
    NP_004022.2. NM_004031.2. [Q92985-4]
    XP_005252963.1. XM_005252906.1. [Q92985-4]
    XP_006725200.1. XM_006725137.1. [Q92985-4]
    UniGeneiHs.166120.

    Genome annotation databases

    EnsembliENST00000330243; ENSP00000329411; ENSG00000185507. [Q92985-4]
    ENST00000348655; ENSP00000331803; ENSG00000185507. [Q92985-2]
    ENST00000397566; ENSP00000380697; ENSG00000185507. [Q92985-4]
    ENST00000397570; ENSP00000380700; ENSG00000185507. [Q92985-2]
    ENST00000397574; ENSP00000380704; ENSG00000185507. [Q92985-1]
    ENST00000469048; ENSP00000434607; ENSG00000185507. [Q92985-3]
    ENST00000533182; ENSP00000433903; ENSG00000185507. [Q92985-3]
    GeneIDi3665.
    KEGGihsa:3665.
    UCSCiuc001lqg.3. human. [Q92985-4]
    uc001lqh.3. human. [Q92985-1]
    uc001lqi.3. human. [Q92985-2]

    Polymorphism databases

    DMDMi116242593.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73036 mRNA. Translation: AAB17190.1 .
    U53830 mRNA. Translation: AAB80686.1 .
    U53831 mRNA. Translation: AAB80688.1 .
    U53832 mRNA. Translation: AAB80690.1 .
    U53832 mRNA. Translation: AAB80691.1 .
    AF076494 mRNA. Translation: AAC70999.1 .
    CH471158 Genomic DNA. Translation: EAX02360.1 .
    BC136555 mRNA. Translation: AAI36556.1 .
    CCDSi CCDS7703.1. [Q92985-1 ]
    CCDS7704.1. [Q92985-2 ]
    CCDS7705.1. [Q92985-4 ]
    RefSeqi NP_001563.2. NM_001572.3. [Q92985-1 ]
    NP_004020.1. NM_004029.2. [Q92985-2 ]
    NP_004022.2. NM_004031.2. [Q92985-4 ]
    XP_005252963.1. XM_005252906.1. [Q92985-4 ]
    XP_006725200.1. XM_006725137.1. [Q92985-4 ]
    UniGenei Hs.166120.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O61 X-ray 2.80 A 8-125 [» ]
    ProteinModelPortali Q92985.
    SMRi Q92985. Positions 8-123, 289-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109873. 42 interactions.
    DIPi DIP-34895N.
    IntActi Q92985. 24 interactions.
    MINTi MINT-1202972.
    STRINGi 9606.ENSP00000329411.

    PTM databases

    PhosphoSitei Q92985.

    Polymorphism databases

    DMDMi 116242593.

    Proteomic databases

    MaxQBi Q92985.
    PaxDbi Q92985.
    PRIDEi Q92985.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330243 ; ENSP00000329411 ; ENSG00000185507 . [Q92985-4 ]
    ENST00000348655 ; ENSP00000331803 ; ENSG00000185507 . [Q92985-2 ]
    ENST00000397566 ; ENSP00000380697 ; ENSG00000185507 . [Q92985-4 ]
    ENST00000397570 ; ENSP00000380700 ; ENSG00000185507 . [Q92985-2 ]
    ENST00000397574 ; ENSP00000380704 ; ENSG00000185507 . [Q92985-1 ]
    ENST00000469048 ; ENSP00000434607 ; ENSG00000185507 . [Q92985-3 ]
    ENST00000533182 ; ENSP00000433903 ; ENSG00000185507 . [Q92985-3 ]
    GeneIDi 3665.
    KEGGi hsa:3665.
    UCSCi uc001lqg.3. human. [Q92985-4 ]
    uc001lqh.3. human. [Q92985-1 ]
    uc001lqi.3. human. [Q92985-2 ]

    Organism-specific databases

    CTDi 3665.
    GeneCardsi GC11M000602.
    HGNCi HGNC:6122. IRF7.
    HPAi CAB017694.
    MIMi 605047. gene.
    neXtProti NX_Q92985.
    PharmGKBi PA29921.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39245.
    HOGENOMi HOG000111812.
    HOVERGENi HBG105600.
    KOi K09447.
    OMAi GWKTNFR.
    PhylomeDBi Q92985.
    TreeFami TF328512.

    Enzyme and pathway databases

    Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25078. Interferon gamma signaling.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25162. Interferon alpha/beta signaling.
    SignaLinki Q92985.

    Miscellaneous databases

    ChiTaRSi IRF7. human.
    GeneWikii IRF7.
    GenomeRNAii 3665.
    NextBioi 14347.
    PROi Q92985.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92985.
    Bgeei Q92985.
    CleanExi HS_IRF7.
    Genevestigatori Q92985.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.60.200.10. 1 hit.
    InterProi IPR019817. Interferon_reg_fac_CS.
    IPR001346. Interferon_reg_fact_DNA-bd_dom.
    IPR019471. Interferon_reg_factor-3.
    IPR017855. SMAD_dom-like.
    IPR008984. SMAD_FHA_domain.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00605. IRF. 1 hit.
    PF10401. IRF-3. 1 hit.
    [Graphical view ]
    PRINTSi PR00267. INTFRNREGFCT.
    SMARTi SM00348. IRF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    PROSITEi PS00601. IRF_1. 1 hit.
    PS51507. IRF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Grossman A., Nicholl J., Antonio L., Luethy R., Suggs S., Sutherland G.R., Mak T.W.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT GLU-179.
      Tissue: Spleen.
    2. "IRF-7, a new interferon regulatory factor associated with Epstein-Barr virus latency."
      Zhang L., Pagano J.S.
      Mol. Cell. Biol. 17:5748-5757(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
    3. "Characterization of the interferon regulatory factor-7 and its potential role in the transcription activation of interferon A genes."
      Au W.-C., Moore P.A., LaFleur D.W., Tombal B., Pitha P.M.
      J. Biol. Chem. 273:29210-29217(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), VARIANTS GLU-179 AND ARG-412.
    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 D).
    6. "Phosphorylation-induced dimerization of interferon regulatory factor 7 unmasks DNA binding and a bipartite transactivation domain."
      Marie I.J., Smith E., Prakash A., Levy D.E.
      Mol. Cell. Biol. 20:8803-8814(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, SUBUNIT.
    7. "IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L protein."
      Smith E.J., Marie I.J., Prakash A., Garcia-Sastre A., Levy D.E.
      J. Biol. Chem. 276:8951-8957(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION OF PHOSPHORYLATION BY VACCINIA VIRUS PROTEIN E3.
    8. "HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators."
      Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A., Harrington W.J. Jr., Barber G.N., Hiscott J.
      Oncogene 20:800-811(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-8 PROTEIN VIRF1.
    9. "Acetylation of interferon regulatory factor-7 by p300/CREB-binding protein (CBP)-associated factor (PCAF) impairs its DNA binding."
      Caillaud A., Prakash A., Smith E., Masumi A., Hovanessian A.G., Levy D.E., Marie I.
      J. Biol. Chem. 277:49417-49421(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-92, MUTAGENESIS OF GLY-90; LYS-92 AND THR-93, PHOSPHORYLATION.
    10. Cited for: REVIEW ON FUNCTION.
    11. "A Kaposi's sarcoma-associated herpesviral protein inhibits virus-mediated induction of type I interferon by blocking IRF-7 phosphorylation and nuclear accumulation."
      Zhu F.X., King S.M., Smith E.J., Levy D.E., Yuan Y.
      Proc. Natl. Acad. Sci. U.S.A. 99:5573-5578(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-8 PROTEIN ORF45.
    12. "LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters TRAM and TRIF."
      Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A., Latz E., Monks B., Pitha P.M., Golenbock D.T.
      J. Exp. Med. 198:1043-1055(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM2.
    13. "Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways."
      Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.
      J. Biol. Chem. 279:15652-15661(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    14. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    15. "Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis virus infection and the role of viral ribonucleoprotein in the development of interferon antiviral immunity."
      tenOever B.R., Sharma S., Zou W., Sun Q., Grandvaux N., Julkunen I., Hemmi H., Yamamoto M., Akira S., Yeh W.C., Lin R., Hiscott J.
      J. Virol. 78:10636-10649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-477 AND SER-479 BY TBK1 AND IKKE, MUTAGENESIS OF 477-SER--SER-479.
    16. "Role of a transductional-transcriptional processor complex involving MyD88 and IRF-7 in Toll-like receptor signaling."
      Honda K., Yanai H., Mizutani T., Negishi H., Shimada N., Suzuki N., Ohba Y., Takaoka A., Yeh W.C., Taniguchi T.
      Proc. Natl. Acad. Sci. U.S.A. 101:15416-15421(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MYD88.
    17. "Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6."
      Kawai T., Sato S., Ishii K.J., Coban C., Hemmi H., Yamamoto M., Terai K., Matsuda M., Inoue J., Uematsu S., Takeuchi O., Akira S.
      Nat. Immunol. 5:1061-1068(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYD88 AND TRAF6.
    18. "Interleukin-1 receptor-associated kinase-1 plays an essential role for Toll-like receptor (TLR)7- and TLR9-mediated interferon-{alpha} induction."
      Uematsu S., Sato S., Yamamoto M., Hirotani T., Kato H., Takeshita F., Matsuda M., Coban C., Ishii K.J., Kawai T., Takeuchi O., Akira S.
      J. Exp. Med. 201:915-923(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY IRAK1.
    19. "Distinct functions of IRF-3 and IRF-7 in IFN-alpha gene regulation and control of anti-tumor activity in primary macrophages."
      Solis M., Goubau D., Romieu-Mourez R., Genin P., Civas A., Hiscott J.
      Biochem. Pharmacol. 72:1469-1476(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    20. "Type I interferon gene induction by the interferon regulatory factor family of transcription factors."
      Honda K., Takaoka A., Taniguchi T.
      Immunity 25:349-360(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    21. Erratum
      Honda K., Takaoka A., Taniguchi T.
      Immunity 25:849-849(2006)
    22. "IRF-7: new role in the regulation of genes involved in adaptive immunity."
      Sgarbanti M., Marsili G., Remoli A.L., Orsatti R., Battistini A.
      Ann. N. Y. Acad. Sci. 1095:325-333(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Rotavirus NSP1 inhibits expression of type I interferon by antagonizing the function of interferon regulatory factors IRF3, IRF5, and IRF7."
      Barro M., Patton J.T.
      J. Virol. 81:4473-4481(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROTAVIRUS A NSP1.
    24. Cited for: INTERACTION WITH EBV LF2.
    25. "Regulation of immunity and oncogenesis by the IRF transcription factor family."
      Savitsky D., Tamura T., Yanai H., Taniguchi T.
      Cancer Immunol. Immunother. 59:489-510(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    26. "IRF7: activation, regulation, modification and function."
      Ning S., Pagano J.S., Barber G.N.
      Genes Immun. 12:399-414(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    27. "Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7."
      Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H., Rauscher F.J. III, Ozato K., Zhu F.
      J. Immunol. 187:4754-4763(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-444 AND LYS-446 BY TRIM28.

    Entry informationi

    Entry nameiIRF7_HUMAN
    AccessioniPrimary (citable) accession number: Q92985
    Secondary accession number(s): B9EGL3
    , O00331, O00332, O00333, O75924, Q9UE79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 138 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 11
      Human chromosome 11: 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