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Q92985

- IRF7_HUMAN

UniProt

Q92985 - IRF7_HUMAN

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Protein

Interferon regulatory factor 7

Gene

IRF7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Source: UniProtKB
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi92 – 921K → R: Loss of acetylation, DNA-binding and activity. 1 Publication
Mutagenesisi93 – 931T → R: Loss of acetylation, increased DNA-binding and activity; when associated with T-90. 1 Publication
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

BgeeiQ92985.
CleanExiHS_IRF7.
ExpressionAtlasiQ92985. baseline and differential.
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. 43 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.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000111812.
HOVERGENiHBG105600.
InParanoidiQ92985.
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

        10         20         30         40         50
MALAPERAAP RVLFGEWLLG EISSGCYEGL QWLDEARTCF RVPWKHFARK
60 70 80 90 100
DLSEADARIF KAWAVARGRW PPSSRGGGPP PEAETAERAG WKTNFRCALR
110 120 130 140 150
STRRFVMLRD NSGDPADPHK VYALSRELCW REGPGTDQTE AEAPAAVPPP
160 170 180 190 200
QGGPPGPFLA HTHAGLQAPG PLPAPAGDKG DLLLQAVQQS CLADHLLTAS
210 220 230 240 250
WGADPVPTKA PGEGQEGLPL TGACAGGPGL PAGELYGWAV ETTPSPGPQP
260 270 280 290 300
AALTTGEAAA PESPHQAEPY LSPSPSACTA VQEPSPGALD VTIMYKGRTV
310 320 330 340 350
LQKVVGHPSC TFLYGPPDPA VRATDPQQVA FPSPAELPDQ KQLRYTEELL
360 370 380 390 400
RHVAPGLHLE LRGPQLWARR MGKCKVYWEV GGPPGSASPS TPACLLPRNC
410 420 430 440 450
DTPIFDFRVF FQELVEFRAR QRRGSPRYTI YLGFGQDLSA GRPKEKSLVL
460 470 480 490 500
VKLEPWLCRV HLEGTQREGV SSLDSSSLSL CLSSANSLYD DIECFLMELE

QPA
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]
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. 43 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 ]
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.
GeneTreei ENSGT00760000119093.
HOGENOMi HOG000111812.
HOVERGENi HBG105600.
InParanoidi Q92985.
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

Bgeei Q92985.
CleanExi HS_IRF7.
ExpressionAtlasi Q92985. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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