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Q14653

- IRF3_HUMAN

UniProt

Q14653 - IRF3_HUMAN

Protein

Interferon regulatory factor 3

Gene

IRF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which 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. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.

    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 bindingi5 – 111107IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: BHF-UCL
    2. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: BHF-UCL
    5. sequence-specific DNA binding transcription factor activity Source: InterPro
    6. transcription cofactor activity Source: ProtInc
    7. transcription regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. cellular response to dsRNA Source: Ensembl
    4. cytokine-mediated signaling pathway Source: Reactome
    5. defense response to virus Source: UniProtKB
    6. innate immune response Source: Reactome
    7. interferon-gamma-mediated signaling pathway Source: Reactome
    8. lipopolysaccharide-mediated signaling pathway Source: Ensembl
    9. macrophage apoptotic process Source: UniProtKB
    10. MDA-5 signaling pathway Source: UniProtKB
    11. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    12. negative regulation of defense response to virus by host Source: Ensembl
    13. negative regulation of interferon-beta biosynthetic process Source: Ensembl
    14. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    15. negative regulation of type I interferon production Source: Reactome
    16. positive regulation of cytokine secretion Source: Ensembl
    17. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    18. positive regulation of interferon-alpha production Source: UniProtKB
    19. positive regulation of interferon-beta production Source: UniProtKB
    20. positive regulation of type I interferon-mediated signaling pathway Source: Ensembl
    21. positive regulation of type I interferon production Source: Reactome
    22. response to exogenous dsRNA Source: Ensembl
    23. toll-like receptor 3 signaling pathway Source: Reactome
    24. toll-like receptor 4 signaling pathway Source: Reactome
    25. toll-like receptor signaling pathway Source: Reactome
    26. transcription from RNA polymerase II promoter Source: ProtInc
    27. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    28. type I interferon biosynthetic process Source: Ensembl
    29. type I interferon signaling pathway Source: Reactome
    30. viral process Source: UniProtKB-KW

    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_115831. ISG15 antiviral mechanism.
    REACT_118811. IRF3 mediated activation of type 1 IFN.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163993. IRF3-mediated induction of type I IFN.
    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_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon regulatory factor 3
    Short name:
    IRF-3
    Gene namesi
    Name:IRF3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6118. IRF3.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 782KR → NG: Abolishes nuclear localization.
    Mutagenesisi86 – 872RK → LQ: No effect on subcellular localization.
    Mutagenesisi139 – 1402IL → MM: Abolishes nuclear export.
    Mutagenesisi193 – 1931K → R: Highly diminished ISGylation; when associated with R-360 and R-366. 1 Publication
    Mutagenesisi360 – 3601K → R: Highly diminished ISGylation; when associated with R-193 and R-366. 1 Publication
    Mutagenesisi366 – 3661K → R: Highly diminished ISGylation; when associated with R-193 and R-360. 1 Publication
    Mutagenesisi385 – 3862SS → AA: Complete loss of viral infection induced phosphorylation. 1 Publication
    Mutagenesisi385 – 3851S → A, D or E: Complete loss of viral infection induced phosphorylation. 1 Publication
    Mutagenesisi386 – 3861S → A, D or E: Complete loss of viral infection induced phosphorylation. 2 Publications
    Mutagenesisi386 – 3861S → A: Abolishes dimerization after phosphorylation. 2 Publications
    Mutagenesisi396 – 40510SNSHPLSLTS → ANAHPLALAA: Complete loss of viral infection induced phosphorylation.
    Mutagenesisi396 – 40510SNSHPLSLTS → DNDHPLDLDD: Acts as a constitutively activated IRF3.
    Mutagenesisi396 – 3983SNS → ANA: Complete loss of viral infection induced phosphorylation.
    Mutagenesisi402 – 4054SLTS → ALAA: Complete loss of viral infection induced phosphorylation.

    Organism-specific databases

    PharmGKBiPA29917.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Interferon regulatory factor 3PRO_0000154553Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Phosphothreonine1 Publication
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei75 – 751Phosphothreonine1 Publication
    Modified residuei97 – 971Phosphoserine1 Publication
    Modified residuei180 – 1801Phosphothreonine1 Publication
    Modified residuei188 – 1881Phosphoserine1 Publication
    Cross-linki193 – 193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
    Modified residuei237 – 2371Phosphothreonine1 Publication
    Modified residuei244 – 2441Phosphothreonine1 Publication
    Modified residuei253 – 2531Phosphothreonine1 Publication
    Disulfide bondi267 ↔ 2892 Publications
    Cross-linki360 – 360Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
    Cross-linki366 – 366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
    Modified residuei386 – 3861Phosphoserine; by TBK11 Publication
    Modified residuei396 – 3961Phosphoserine; by IKKE1 Publication
    Modified residuei398 – 3981Phosphoserine1 Publication
    Modified residuei404 – 4041Phosphothreonine1 Publication
    Modified residuei427 – 4271Phosphoserine1 Publication

    Post-translational modificationi

    Constitutively phosphorylated on many Ser/Thr residues. C-terminal serine/threonine cluster is phosphorylated in response of induction by IKBKE and TBK1. Phosphorylated at Ser-396 by IKBKE upon ssRNA viral infection. Ser-385 and Ser-386 may be specifically phosphorylated in response to induction. Phosphorylation at Ser-386 by TBK1 results in oligomerization. An alternate model propose that the five serine/threonine residues between 396 and 405 are phosphorylated in response to a viral infection. Phosphorylation, and subsequent activation of IRF3 is inhibited by vaccinia virus protein E3.2 Publications
    Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation. Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation.2 Publications
    ISGylated by HERC5 resulting in sustained IRF3 activation and in the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The phosphorylation state of IRF3 does not alter ISGylation.3 Publications

    Keywords - PTMi

    Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14653.
    PaxDbiQ14653.
    PeptideAtlasiQ14653.
    PRIDEiQ14653.

    PTM databases

    PhosphoSiteiQ14653.

    Expressioni

    Tissue specificityi

    Expressed constitutively in a variety of tissues.

    Gene expression databases

    ArrayExpressiQ14653.
    BgeeiQ14653.
    CleanExiHS_IRF3.
    GenevestigatoriQ14653.

    Organism-specific databases

    HPAiCAB013018.
    HPA004895.

    Interactioni

    Subunit structurei

    Monomer. Homodimer; phosphorylation-induced. Heterodimer with IRF7. Interacts with CREBBP. May interact with MAVS. Interacts with IKBKE and TBK1. Interacts with TICAM1 and TICAM2. Interacts with RBCK1. Interacts with TRIM21. Interacts with HERC5. InteractS with DDX3X (phosphorylated at 'Ser-102'); the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with rotavirus A NSP1 (via C-terminus); this interaction leads to the proteasome-dependent degradation of IRF3. Interacts with herpes virus 8/HHV-8 protein vIRF-1.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself9EBI-2650369,EBI-2650369
    CREBBPQ927934EBI-2650369,EBI-81215
    GRIP1Q9Y3R02EBI-2650369,EBI-5349621
    MAFBQ9Y5Q34EBI-2650369,EBI-3649340
    RB1P064002EBI-2650369,EBI-491274
    RBL1P287492EBI-2650369,EBI-971402
    SGTAO437653EBI-2650369,EBI-347996
    TBK1Q9UHD27EBI-2650369,EBI-356402

    Protein-protein interaction databases

    BioGridi109869. 45 interactions.
    DIPiDIP-41448N.
    IntActiQ14653. 26 interactions.
    MINTiMINT-253351.
    STRINGi9606.ENSP00000310127.

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 1811
    Beta strandi25 – 273
    Beta strandi28 – 314
    Beta strandi33 – 375
    Beta strandi41 – 455
    Helixi49 – 513
    Helixi53 – 608
    Beta strandi66 – 694
    Helixi73 – 8513
    Beta strandi90 – 967
    Beta strandi100 – 1023
    Beta strandi104 – 1096
    Helixi191 – 1955
    Beta strandi202 – 2109
    Beta strandi213 – 2219
    Beta strandi226 – 2294
    Beta strandi239 – 2446
    Helixi248 – 2503
    Helixi255 – 26713
    Beta strandi272 – 2776
    Beta strandi280 – 2856
    Beta strandi287 – 2893
    Beta strandi291 – 2966
    Beta strandi308 – 3103
    Beta strandi313 – 3153
    Beta strandi317 – 3215
    Helixi322 – 33312
    Beta strandi343 – 3486
    Beta strandi354 – 3563
    Helixi357 – 3604
    Beta strandi363 – 3697
    Helixi370 – 38314
    Beta strandi389 – 3913
    Beta strandi401 – 4033
    Helixi405 – 41612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J2FX-ray2.30A/B175-427[»]
    1QWTX-ray2.10A/B173-427[»]
    1T2KX-ray3.00A/B1-112[»]
    1ZOQX-ray2.37A/B196-386[»]
    2O61X-ray2.80A9-111[»]
    2O6GX-ray3.10E/F/G/H1-123[»]
    2PI0X-ray2.31A/B/C/D1-113[»]
    3A77X-ray1.80A/B/C/D189-427[»]
    3QU6X-ray2.30A/B/C1-113[»]
    ProteinModelPortaliQ14653.
    SMRiQ14653. Positions 1-112, 189-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14653.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 360161Involved in HERC5 bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi139 – 14911Nuclear export signalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi151 – 19141Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG42868.
    HOGENOMiHOG000033705.
    HOVERGENiHBG105601.
    KOiK05411.
    OMAiCHTYWAV.
    OrthoDBiEOG7CCBR1.
    PhylomeDBiQ14653.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14653-1) [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

    MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED    50
    FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP 100
    HDPHKIYEFV NSGVGDFSQP DTSPDTNGGG STSDTQEDIL DELLGNMVLA 150
    PLPDPGPPSL AVAPEPCPQP LRSPSLDNPT PFPNLGPSEN PLKRLLVPGE 200
    EWEFEVTAFY RGRQVFQQTI SCPEGLRLVG SEVGDRTLPG WPVTLPDPGM 250
    SLTDRGVMSY VRHVLSCLGG GLALWRAGQW LWAQRLGHCH TYWAVSEELL 300
    PNSGHGPDGE VPKDKEGGVF DLGPFIVDLI TFTEGSGRSP RYALWFCVGE 350
    SWPQDQPWTK RLVMVKVVPT CLRALVEMAR VGGASSLENT VDLHISNSHP 400
    LSLTSDQYKA YLQDLVEGMD FQGPGES 427
    Length:427
    Mass (Da):47,219
    Last modified:November 1, 1997 - v1
    Checksum:iF536676FA78B0110
    GO
    Isoform 2 (identifier: Q14653-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         201-327: Missing.

    Show »
    Length:300
    Mass (Da):33,170
    Checksum:i1195BFBBA65C2DCE
    GO
    Isoform 3 (identifier: Q14653-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-146: Missing.
         201-327: Missing.

    Show »
    Length:154
    Mass (Da):16,730
    Checksum:i7A327E1716F74231
    GO
    Isoform 4 (identifier: Q14653-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         328-427: DLITFTEGSG...GMDFQGPGES → GSWAPRSDYL...NPPVPHHLNQ

    Note: No experimental confirmation available.

    Show »
    Length:452
    Mass (Da):49,134
    Checksum:i96B059A029751B64
    GO
    Isoform 5 (identifier: Q14653-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         56-104: AWAEATGAYV...DRSKDPHDPH → ELGTFPSQTP...SQIRDPQAWL
         105-427: Missing.

    Show »
    Length:104
    Mass (Da):12,330
    Checksum:i7DA489EFD316732D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti196 – 1961L → F in BAG37040. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961R → Q.
    Corresponds to variant rs968457 [ dbSNP | Ensembl ].
    VAR_011901
    Natural varianti107 – 1071Y → F.
    Corresponds to variant rs34745118 [ dbSNP | Ensembl ].
    VAR_049643
    Natural varianti377 – 3771E → K.
    Corresponds to variant rs1049486 [ dbSNP | Ensembl ].
    VAR_011902
    Natural varianti427 – 4271S → T.2 Publications
    Corresponds to variant rs7251 [ dbSNP | Ensembl ].
    VAR_011903

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 146146Missing in isoform 3. 1 PublicationVSP_046911Add
    BLAST
    Alternative sequencei56 – 10449AWAEA…PHDPH → ELGTFPSQTPLRTPMVEAVL LIPRKTFWMSYWVTWCWPHS QIRDPQAWL in isoform 5. 1 PublicationVSP_047690Add
    BLAST
    Alternative sequencei105 – 427323Missing in isoform 5. 1 PublicationVSP_047691Add
    BLAST
    Alternative sequencei201 – 327127Missing in isoform 2 and isoform 3. 1 PublicationVSP_043319Add
    BLAST
    Alternative sequencei328 – 427100DLITF…GPGES → GSWAPRSDYLHGRKRTLTTL CPLVLCGGVMAPGPAVDQEA RDGQGCAHVPQGLGRNGPGR GCLLPGEYCGPAHFQQPPTL PHLRPVQGLPAGLGGGHGFP GPWGELSPRSSWCASNPPVP HHLNQ in isoform 4. 1 PublicationVSP_046912Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z56281 mRNA. Translation: CAA91227.1.
    AB102884 mRNA. Translation: BAD89413.1.
    AB102886 mRNA. Translation: BAD89415.1.
    AB102887 mRNA. Translation: BAD89416.1.
    AK292027 mRNA. Translation: BAF84716.1.
    AK314421 mRNA. Translation: BAG37040.1.
    AC011495 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52510.1.
    BC000660 mRNA. Translation: AAH00660.1.
    BC071721 mRNA. Translation: AAH71721.1.
    U86636 Genomic DNA. Translation: AAC68818.1.
    CCDSiCCDS12775.1. [Q14653-1]
    CCDS56099.1. [Q14653-2]
    CCDS59407.1. [Q14653-3]
    CCDS59409.1. [Q14653-4]
    RefSeqiNP_001184051.1. NM_001197122.1. [Q14653-4]
    NP_001184052.1. NM_001197123.1.
    NP_001184053.1. NM_001197124.1. [Q14653-2]
    NP_001184054.1. NM_001197125.1.
    NP_001184055.1. NM_001197126.1.
    NP_001184056.1. NM_001197127.1. [Q14653-3]
    NP_001184057.1. NM_001197128.1. [Q14653-3]
    NP_001562.1. NM_001571.5. [Q14653-1]
    XP_006723260.1. XM_006723197.1. [Q14653-4]
    XP_006723261.1. XM_006723198.1. [Q14653-4]
    XP_006723262.1. XM_006723199.1. [Q14653-1]
    UniGeneiHs.289052.
    Hs.731922.
    Hs.75254.

    Genome annotation databases

    EnsembliENST00000309877; ENSP00000310127; ENSG00000126456. [Q14653-1]
    ENST00000377135; ENSP00000366339; ENSG00000126456. [Q14653-2]
    ENST00000377139; ENSP00000366344; ENSG00000126456. [Q14653-1]
    ENST00000442265; ENSP00000400378; ENSG00000126456. [Q14653-5]
    ENST00000596765; ENSP00000470512; ENSG00000126456. [Q14653-3]
    ENST00000597198; ENSP00000469113; ENSG00000126456. [Q14653-1]
    ENST00000599223; ENSP00000471358; ENSG00000126456. [Q14653-2]
    ENST00000600022; ENSP00000472700; ENSG00000126456. [Q14653-3]
    ENST00000601291; ENSP00000471896; ENSG00000126456. [Q14653-4]
    GeneIDi3661.
    KEGGihsa:3661.
    UCSCiuc002pot.2. human. [Q14653-2]
    uc002pou.3. human. [Q14653-1]
    uc002pow.3. human.

    Polymorphism databases

    DMDMi2497442.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z56281 mRNA. Translation: CAA91227.1 .
    AB102884 mRNA. Translation: BAD89413.1 .
    AB102886 mRNA. Translation: BAD89415.1 .
    AB102887 mRNA. Translation: BAD89416.1 .
    AK292027 mRNA. Translation: BAF84716.1 .
    AK314421 mRNA. Translation: BAG37040.1 .
    AC011495 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52510.1 .
    BC000660 mRNA. Translation: AAH00660.1 .
    BC071721 mRNA. Translation: AAH71721.1 .
    U86636 Genomic DNA. Translation: AAC68818.1 .
    CCDSi CCDS12775.1. [Q14653-1 ]
    CCDS56099.1. [Q14653-2 ]
    CCDS59407.1. [Q14653-3 ]
    CCDS59409.1. [Q14653-4 ]
    RefSeqi NP_001184051.1. NM_001197122.1. [Q14653-4 ]
    NP_001184052.1. NM_001197123.1.
    NP_001184053.1. NM_001197124.1. [Q14653-2 ]
    NP_001184054.1. NM_001197125.1.
    NP_001184055.1. NM_001197126.1.
    NP_001184056.1. NM_001197127.1. [Q14653-3 ]
    NP_001184057.1. NM_001197128.1. [Q14653-3 ]
    NP_001562.1. NM_001571.5. [Q14653-1 ]
    XP_006723260.1. XM_006723197.1. [Q14653-4 ]
    XP_006723261.1. XM_006723198.1. [Q14653-4 ]
    XP_006723262.1. XM_006723199.1. [Q14653-1 ]
    UniGenei Hs.289052.
    Hs.731922.
    Hs.75254.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J2F X-ray 2.30 A/B 175-427 [» ]
    1QWT X-ray 2.10 A/B 173-427 [» ]
    1T2K X-ray 3.00 A/B 1-112 [» ]
    1ZOQ X-ray 2.37 A/B 196-386 [» ]
    2O61 X-ray 2.80 A 9-111 [» ]
    2O6G X-ray 3.10 E/F/G/H 1-123 [» ]
    2PI0 X-ray 2.31 A/B/C/D 1-113 [» ]
    3A77 X-ray 1.80 A/B/C/D 189-427 [» ]
    3QU6 X-ray 2.30 A/B/C 1-113 [» ]
    ProteinModelPortali Q14653.
    SMRi Q14653. Positions 1-112, 189-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109869. 45 interactions.
    DIPi DIP-41448N.
    IntActi Q14653. 26 interactions.
    MINTi MINT-253351.
    STRINGi 9606.ENSP00000310127.

    PTM databases

    PhosphoSitei Q14653.

    Polymorphism databases

    DMDMi 2497442.

    Proteomic databases

    MaxQBi Q14653.
    PaxDbi Q14653.
    PeptideAtlasi Q14653.
    PRIDEi Q14653.

    Protocols and materials databases

    DNASUi 3661.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309877 ; ENSP00000310127 ; ENSG00000126456 . [Q14653-1 ]
    ENST00000377135 ; ENSP00000366339 ; ENSG00000126456 . [Q14653-2 ]
    ENST00000377139 ; ENSP00000366344 ; ENSG00000126456 . [Q14653-1 ]
    ENST00000442265 ; ENSP00000400378 ; ENSG00000126456 . [Q14653-5 ]
    ENST00000596765 ; ENSP00000470512 ; ENSG00000126456 . [Q14653-3 ]
    ENST00000597198 ; ENSP00000469113 ; ENSG00000126456 . [Q14653-1 ]
    ENST00000599223 ; ENSP00000471358 ; ENSG00000126456 . [Q14653-2 ]
    ENST00000600022 ; ENSP00000472700 ; ENSG00000126456 . [Q14653-3 ]
    ENST00000601291 ; ENSP00000471896 ; ENSG00000126456 . [Q14653-4 ]
    GeneIDi 3661.
    KEGGi hsa:3661.
    UCSCi uc002pot.2. human. [Q14653-2 ]
    uc002pou.3. human. [Q14653-1 ]
    uc002pow.3. human.

    Organism-specific databases

    CTDi 3661.
    GeneCardsi GC19M050162.
    HGNCi HGNC:6118. IRF3.
    HPAi CAB013018.
    HPA004895.
    MIMi 603734. gene.
    neXtProti NX_Q14653.
    PharmGKBi PA29917.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42868.
    HOGENOMi HOG000033705.
    HOVERGENi HBG105601.
    KOi K05411.
    OMAi CHTYWAV.
    OrthoDBi EOG7CCBR1.
    PhylomeDBi Q14653.
    TreeFami TF328512.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_118811. IRF3 mediated activation of type 1 IFN.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163993. IRF3-mediated induction of type I IFN.
    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_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.

    Miscellaneous databases

    ChiTaRSi IRF3. human.
    EvolutionaryTracei Q14653.
    GeneWikii IRF3.
    GenomeRNAii 3661.
    NextBioi 14319.
    PROi Q14653.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14653.
    Bgeei Q14653.
    CleanExi HS_IRF3.
    Genevestigatori Q14653.

    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. "Identification of a member of the interferon regulatory factor family that binds to the interferon-stimulated response element and activates expression of interferon-induced genes."
      Au W.W.-C., Moore P.P.A., Lowther W.W., Juang Y.-T., Pitha P.M.
      Proc. Natl. Acad. Sci. U.S.A. 92:11657-11661(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    2. "IRF3 mRNA, nirs splice variants."
      Tabata Y., Sameshima E., Hayashi A., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
    3. "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] (ISOFORM 1), VARIANT THR-427.
      Tissue: Spleen.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-427.
    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] (ISOFORMS 1 AND 4).
      Tissue: Eye and Kidney.
    7. "Mapping of human interferon regulatory factor 3 (IRF3) to chromosome 19q13.3-13.4 by an intragenic polymorphic marker."
      Bellingham J., Gregory-Evans K., Gregory-Evans C.Y.
      Ann. Hum. Genet. 62:231-234(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-413.
    8. "Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation."
      Lin R., Heylbroeck C., Pitha P.M., Hiscott J.
      Mol. Cell. Biol. 18:2986-2996(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 385-SER-SER-386 AND 396-SER--SER-405.
    9. "Analyses of virus-induced homomeric and heteromeric protein associations between IRF-3 and coactivator CBP/p300."
      Suhara W., Yoneyama M., Iwamura T., Yoshimura S., Tamura K., Namiki H., Aimoto S., Fujita T.
      J. Biochem. 128:301-307(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-385 AND SER-386.
    10. "Regulated nuclear-cytoplasmic localization of interferon regulatory factor 3, a subunit of double-stranded RNA-activated factor 1."
      Kumar K.P., McBride K.M., Weaver B.K., Dingwall C., Reich N.C.
      Mol. Cell. Biol. 20:4159-4168(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 77-LYS-ARG-78; 86-ARG-LYS-87 AND 139-ILE-LEU-140.
    11. "Identification of distinct signaling pathways leading to the phosphorylation of interferon regulatory factor 3."
      Servant M.J., ten Oever B., LePage C., Conti L., Gessani S., Julkunen I., Lin R., Hiscott J.
      J. Biol. Chem. 276:355-363(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    12. "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.
    13. "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.
    14. Cited for: REVIEW.
    15. "A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling."
      Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K., Akira S.
      J. Immunol. 169:6668-6672(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    16. "Interferon regulatory factor 3 is a cellular partner of rotavirus NSP1."
      Graff J.W., Mitzel D.N., Weisend C.M., Flenniken M.L., Hardy M.E.
      J. Virol. 76:9545-9550(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROTAVIRUS A NSP1.
    17. "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.
    18. "Triggering the interferon antiviral response through an IKK-related pathway."
      Sharma S., tenOever B.R., Grandvaux N., Zhou G.-P., Lin R., Hiscott J.
      Science 300:1148-1151(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    19. "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.
    20. "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.
    21. "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: INTERACTION WITH MAVS.
    22. "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.
    23. "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.
    24. Erratum
      Honda K., Takaoka A., Taniguchi T.
      Immunity 25:849-849(2006)
    25. "Negative feedback regulation of cellular antiviral signaling by RBCK1-mediated degradation of IRF3."
      Zhang M., Tian Y., Wang R.P., Gao D., Zhang Y., Diao F.C., Chen D.Y., Zhai Z.H., Shu H.B.
      Cell Res. 18:1096-1104(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH RBCK1.
    26. "The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3."
      Higgs R., Ni Gabhann J., Ben Larbi N., Breen E.P., Fitzgerald K.A., Jefferies C.A.
      J. Immunol. 181:1780-1786(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM21, POLYUBIQUITINATION.
    27. "Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1."
      Prins K.C., Cardenas W.B., Basler C.F.
      J. Virol. 83:3069-3077(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY IKBKE AND TBK1.
    28. "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.
    29. "Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification."
      Shi H.X., Yang K., Liu X., Liu X.Y., Wei B., Shan Y.F., Zhu L.H., Wang C.
      Mol. Cell. Biol. 30:2424-2436(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION AT LYS-193; LYS-360 AND LYS-366, MUTAGENESIS OF LYS-193; LYS-360 AND LYS-366, INTERACTION WITH HERC5.
    30. "Human DEAD box helicase 3 couples IkappaB kinase epsilon to interferon regulatory factor 3 activation."
      Gu L., Fullam A., Brennan R., Schroder M.
      Mol. Cell. Biol. 33:2004-2015(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX3X AND IKBKE, PHOSPHORYLATION AT SER-396.
    31. "Structural insights into the functions of TBK1 in innate antimicrobial immunity."
      Shu C., Sankaran B., Chaton C.T., Herr A.B., Mishra A., Peng J., Li P.
      Structure 21:1137-1148(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-3; SER-14; THR-75; SER-97; THR-180; SER-188; THR-237; THR-244; THR-253; SER-398; THR-404 AND SER-427, PHOSPHORYLATION AT SER-386 BY TBK1, MUTAGENESIS OF SER-386.
    32. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-427, DISULFIDE BOND.
    33. "Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation."
      Qin B.Y., Liu C., Lam S.S., Srinath H., Delston R., Correia J.J., Derynck R., Lin K.
      Nat. Struct. Biol. 10:913-921(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 173-427, DISULFIDE BOND.
    34. "Crystal structure of ATF-2/c-Jun and IRF-3 bound to the interferon-beta enhancer."
      Panne D., Maniatis T., Harrison S.C.
      EMBO J. 23:4384-4393(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-112.
    35. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 173-394.

    Entry informationi

    Entry nameiIRF3_HUMAN
    AccessioniPrimary (citable) accession number: Q14653
    Secondary accession number(s): A8K7L2
    , B2RAZ3, Q5FBY1, Q5FBY2, Q5FBY4, Q7Z5G6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 141 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 19
      Human chromosome 19: 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