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P23906

- IRF2_MOUSE

UniProt

P23906 - IRF2_MOUSE

Protein

Interferon regulatory factor 2

Gene

Irf2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in cell cycle regulation through binding the site II (HiNF-M) promoter region of H4 and activating transcription during cell growth. Antagonizes IRF1 transcriptional activation.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi5 – 113109IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. regulatory region DNA binding Source: InterPro
    2. sequence-specific DNA binding transcription factor activity Source: InterPro

    GO - Biological processi

    1. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_198660. Interferon gamma signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon regulatory factor 2
    Short name:
    IRF-2
    Gene namesi
    Name:Irf2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:96591. Irf2.

    Subcellular locationi

    GO - Cellular componenti

    1. focal adhesion Source: Ensembl
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 349349Interferon regulatory factor 2PRO_0000154550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751N6-acetyllysineBy similarity
    Modified residuei78 – 781N6-acetyllysineBy similarity
    Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki166 – 166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 is required for stimulation of H4 promoter activity By similarity.By similarity
    The major sites of sumoylation are Lys-137 and Lys-293. Sumoylation with SUMO1 increases its transcriptional repressor activity on IRF1 and diminishes its ability to activate ISRE and H4 promoter By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiP23906.
    PRIDEiP23906.

    PTM databases

    PhosphoSiteiP23906.

    Expressioni

    Inductioni

    By viruses and IFN.

    Gene expression databases

    ArrayExpressiP23906.
    BgeeiP23906.
    CleanExiMM_IRF2.
    GenevestigatoriP23906.

    Interactioni

    Subunit structurei

    Interacts with BRD7, IRF2BP1 and IRF2BP2. Interacts with CREBBP in growing cells; the interaction acetylates IRF2 and regulates IRF2-dependent H4 promoter activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi200785. 1 interaction.
    IntActiP23906. 1 interaction.
    MINTiMINT-4098768.

    Structurei

    Secondary structure

    1
    349
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 1710
    Beta strandi25 – 284
    Turni29 – 324
    Beta strandi33 – 375
    Beta strandi43 – 475
    Helixi48 – 514
    Helixi53 – 619
    Turni67 – 693
    Helixi74 – 8714
    Beta strandi91 – 933
    Turni95 – 973
    Beta strandi98 – 1003
    Beta strandi106 – 1116

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRFNMR-A2-113[»]
    1IRGNMR-A2-113[»]
    2IRFX-ray2.20G/H/I/J/K/L1-113[»]
    ProteinModelPortaliP23906.
    SMRiP23906. Positions 5-113.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23906.

    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

    eggNOGiNOG41436.
    HOGENOMiHOG000037937.
    HOVERGENiHBG003455.
    InParanoidiP23906.
    KOiK10153.
    OMAiSWPPFPD.
    OrthoDBiEOG72ZCFD.
    PhylomeDBiP23906.
    TreeFamiTF328512.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR017431. Interferon_reg_fac-1/2.
    IPR019817. Interferon_reg_fac_CS.
    IPR001346. Interferon_reg_fact_DNA-bd_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00605. IRF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038196. IFN_RF1/2. 1 hit.
    PRINTSiPR00267. INTFRNREGFCT.
    SMARTiSM00348. IRF. 1 hit.
    [Graphical view]
    PROSITEiPS00601. IRF_1. 1 hit.
    PS51507. IRF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23906-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK    50
    DAPLFRNWAI HTGKHQPGID KPDPKTWKAN FRCAMNSLPD IEEVKDRSIK 100
    KGNNAFRVYR MLPLSERPSK KGKKPKTEKE ERVKHIKQEP VESSLGLSNG 150
    VSGFSPEYAV LTSAIKNEVD STVNIIVVGQ SHLDSNIEDQ EIVTNPPDIC 200
    QVVEVTTESD DQPVSMSELY PLQISPVSSY AESETTDSVA SDEENAEGRP 250
    HWRKRSIEGK QYLSNMGTRN TYLLPSMATF VTSNKPDLQV TIKEDSCPMP 300
    YNSSWPPFTD LPLPAPVTPT PSSSRPDRET RASVIKKTSD ITQARVKSC 349
    Length:349
    Mass (Da):39,453
    Last modified:November 1, 1991 - v1
    Checksum:i8738B082FB40FB11
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03168 mRNA. Translation: AAA39333.1.
    CCDSiCCDS22295.1.
    RefSeqiNP_032417.3. NM_008391.4.
    XP_006509351.1. XM_006509288.1.
    XP_006509352.1. XM_006509289.1.
    UniGeneiMm.1149.

    Genome annotation databases

    EnsembliENSMUST00000034041; ENSMUSP00000034041; ENSMUSG00000031627.
    GeneIDi16363.
    KEGGimmu:16363.
    UCSCiuc009lqo.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03168 mRNA. Translation: AAA39333.1 .
    CCDSi CCDS22295.1.
    RefSeqi NP_032417.3. NM_008391.4.
    XP_006509351.1. XM_006509288.1.
    XP_006509352.1. XM_006509289.1.
    UniGenei Mm.1149.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IRF NMR - A 2-113 [» ]
    1IRG NMR - A 2-113 [» ]
    2IRF X-ray 2.20 G/H/I/J/K/L 1-113 [» ]
    ProteinModelPortali P23906.
    SMRi P23906. Positions 5-113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200785. 1 interaction.
    IntActi P23906. 1 interaction.
    MINTi MINT-4098768.

    PTM databases

    PhosphoSitei P23906.

    Proteomic databases

    PaxDbi P23906.
    PRIDEi P23906.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034041 ; ENSMUSP00000034041 ; ENSMUSG00000031627 .
    GeneIDi 16363.
    KEGGi mmu:16363.
    UCSCi uc009lqo.2. mouse.

    Organism-specific databases

    CTDi 3660.
    MGIi MGI:96591. Irf2.

    Phylogenomic databases

    eggNOGi NOG41436.
    HOGENOMi HOG000037937.
    HOVERGENi HBG003455.
    InParanoidi P23906.
    KOi K10153.
    OMAi SWPPFPD.
    OrthoDBi EOG72ZCFD.
    PhylomeDBi P23906.
    TreeFami TF328512.

    Enzyme and pathway databases

    Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_198660. Interferon gamma signaling.

    Miscellaneous databases

    EvolutionaryTracei P23906.
    NextBioi 289470.
    PROi P23906.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23906.
    Bgeei P23906.
    CleanExi MM_IRF2.
    Genevestigatori P23906.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR017431. Interferon_reg_fac-1/2.
    IPR019817. Interferon_reg_fac_CS.
    IPR001346. Interferon_reg_fact_DNA-bd_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00605. IRF. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038196. IFN_RF1/2. 1 hit.
    PRINTSi PR00267. INTFRNREGFCT.
    SMARTi SM00348. IRF. 1 hit.
    [Graphical view ]
    PROSITEi PS00601. IRF_1. 1 hit.
    PS51507. IRF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes."
      Harada H., Fujita T., Miyamoto M., Kimura Y., Maruyama M., Furia A., Miyata T., Taniguchi T.
      Cell 58:729-739(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 108-120, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    3. "Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of the winged helix-turn-helix family."
      Furui J., Uegaki K., Yamazaki T., Shirakawa M., Swindells M.B., Harada H., Taniguchi T., Kyogoku Y.
      Structure 6:491-500(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-113.
    4. "Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences."
      Fujii Y., Shimizu T., Kusumoto M., Kyogoku Y., Taniguchi T., Hakoshima T.
      EMBO J. 18:5028-5041(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-113.

    Entry informationi

    Entry nameiIRF2_MOUSE
    AccessioniPrimary (citable) accession number: P23906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 125 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, Direct protein sequencing, 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