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P15314

- IRF1_MOUSE

UniProt

P15314 - IRF1_MOUSE

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Protein
Interferon regulatory factor 1
Gene
Irf1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses. These include the regulation of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage. Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters. Its target genes for transcriptional activation activity are: genes involved in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA. Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53. Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells. Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development. Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells.6 Publications

Enzyme regulationi

Activated by MYD88.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi5 – 113109IRF tryptophan pentad repeat
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. CD8-positive, alpha-beta T cell differentiation Source: MGI
  2. apoptotic process Source: UniProtKB
  3. cell cycle arrest Source: UniProtKB
  4. cellular response to interferon-beta Source: Ensembl
  5. cellular response to mechanical stimulus Source: Ensembl
  6. defense response to virus Source: UniProtKB
  7. interferon-gamma-mediated signaling pathway Source: UniProtKB
  8. negative regulation of T-helper 2 cell differentiation Source: UniProtKB
  9. negative regulation of regulatory T cell differentiation Source: UniProtKB
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. positive regulation of T-helper 1 cell differentiation Source: UniProtKB
  12. positive regulation of interferon-beta production Source: UniProtKB
  13. positive regulation of interleukin-12 biosynthetic process Source: MGI
  14. positive regulation of natural killer cell differentiation Source: UniProtKB
  15. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  16. positive regulation of transcription, DNA-templated Source: UniProtKB
  17. positive regulation of type I interferon production Source: UniProtKB
  18. regulation of CD8-positive, alpha-beta T cell proliferation Source: UniProtKB
  19. regulation of MyD88-dependent toll-like receptor signaling pathway Source: UniProtKB
  20. regulation of adaptive immune response Source: UniProtKB
  21. regulation of gene expression Source: MGI
  22. regulation of innate immune response Source: UniProtKB
  23. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, 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 1
Short name:
IRF-1
Gene namesi
Name:Irf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:96590. Irf1.

Subcellular locationi

Nucleus. Cytoplasm
Note: MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nuclear chromatin Source: Ensembl
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Interferon regulatory factor 1
PRO_0000154546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781N6-acetyllysine By similarity
Cross-linki276 – 276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-linki300 – 300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Post-translational modificationi

Phosphorylated by CK2 and this positively regulates its activity By similarity.
Sumoylation represses the transcriptional activity and displays enhanced resistance to protein degradation. Inactivates the tumor suppressor activity. Elevated levels in tumor cells. Major site is Lys-276. Sumoylation is enhanced by PIAS3. Desumoylated by SENP1 in tumor cells and appears to compete with ubiquitination on C-terminal sites By similarity.2 Publications
Ubiquitinated. Appears to compete with sumoylation on C-terminal sites By similarity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP15314.

PTM databases

PhosphoSiteiP15314.

Expressioni

Inductioni

By viruses and IFN-gamma.

Gene expression databases

ArrayExpressiP15314.
BgeeiP15314.
CleanExiMM_IRF1.
GenevestigatoriP15314.

Interactioni

Subunit structurei

Monomer. Homodimer. Interacts with EP300 By similarity. Interacts with MYD88 and PIAS3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KEAP1Q141452EBI-6115486,EBI-751001From a different organism.
TRAF3Q131142EBI-6115486,EBI-357631From a different organism.

Protein-protein interaction databases

BioGridi200784. 6 interactions.
IntActiP15314. 5 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 209
Beta strandi21 – 255
Beta strandi29 – 346
Turni48 – 503
Beta strandi51 – 533
Helixi54 – 618
Helixi74 – 8714
Beta strandi89 – 935
Beta strandi100 – 1023
Beta strandi107 – 1093

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IF1X-ray3.00A/B1-113[»]
ProteinModelPortaliP15314.
SMRiP15314. Positions 7-111.

Miscellaneous databases

EvolutionaryTraceiP15314.

Family & Domainsi

Sequence similaritiesi

Belongs to the IRF family.

Phylogenomic databases

eggNOGiNOG42582.
HOGENOMiHOG000037937.
HOVERGENiHBG003455.
InParanoidiP15314.
KOiK09444.
OMAiCKEEPEV.
OrthoDBiEOG72ZCFD.
PhylomeDBiP15314.
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.

P15314-1 [UniParc]FASTAAdd to Basket

« Hide

MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKH AAKHGWDINK    50
DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN 100
KGSSAVRVYR MLPPLTRNQR KERKSKSSRD TKSKTKRKLC GDVSPDTFSD 150
GLSSSTLPDD HSSYTTQGYL GQDLDMERDI TPALSPCVVS SSLSEWHMQM 200
DIIPDSTTDL YNLQVSPMPS TSEAATDEDE EGKIAEDLMK LFEQSEWQPT 250
HIDGKGYLLN EPGTQLSSVY GDFSCKEEPE IDSPRGDIGI GIQHVFTEMK 300
NMDSIMWMDS LLGNSVRLPP SIQAIPCAP 329
Length:329
Mass (Da):37,319
Last modified:April 1, 1990 - v1
Checksum:i0E5DD23C0D977B34
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21065 mRNA. Translation: AAA39334.1.
BC003821 mRNA. Translation: AAH03821.1.
CCDSiCCDS24686.1.
PIRiA31595.
RefSeqiNP_001152868.1. NM_001159396.1.
NP_032416.1. NM_008390.2.
UniGeneiMm.105218.

Genome annotation databases

EnsembliENSMUST00000019043; ENSMUSP00000019043; ENSMUSG00000018899.
ENSMUST00000108920; ENSMUSP00000104548; ENSMUSG00000018899.
GeneIDi16362.
KEGGimmu:16362.
UCSCiuc007iww.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21065 mRNA. Translation: AAA39334.1 .
BC003821 mRNA. Translation: AAH03821.1 .
CCDSi CCDS24686.1.
PIRi A31595.
RefSeqi NP_001152868.1. NM_001159396.1.
NP_032416.1. NM_008390.2.
UniGenei Mm.105218.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IF1 X-ray 3.00 A/B 1-113 [» ]
ProteinModelPortali P15314.
SMRi P15314. Positions 7-111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200784. 6 interactions.
IntActi P15314. 5 interactions.

PTM databases

PhosphoSitei P15314.

Proteomic databases

PRIDEi P15314.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019043 ; ENSMUSP00000019043 ; ENSMUSG00000018899 .
ENSMUST00000108920 ; ENSMUSP00000104548 ; ENSMUSG00000018899 .
GeneIDi 16362.
KEGGi mmu:16362.
UCSCi uc007iww.2. mouse.

Organism-specific databases

CTDi 3659.
MGIi MGI:96590. Irf1.

Phylogenomic databases

eggNOGi NOG42582.
HOGENOMi HOG000037937.
HOVERGENi HBG003455.
InParanoidi P15314.
KOi K09444.
OMAi CKEEPEV.
OrthoDBi EOG72ZCFD.
PhylomeDBi P15314.
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 P15314.
NextBioi 289466.
PROi P15314.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15314.
Bgeei P15314.
CleanExi MM_IRF1.
Genevestigatori P15314.

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

« Hide 'large scale' publications
  1. "Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-beta gene regulatory elements."
    Miyamoto M., Fujita T., Kimura Y., Maruyama M., Harada H., Sudo Y., Miyata T., Taniguchi T.
    Cell 54:903-913(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "Degradation of transcription factor IRF-1 by the ubiquitin-proteasome pathway. The C-terminal region governs the protein stability."
    Nakagawa K., Yokosawa H.
    Eur. J. Biochem. 267:1680-1686(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  4. "IRF family of transcription factors as regulators of host defense."
    Taniguchi T., Ogasawara K., Takaoka A., Tanaka N.
    Annu. Rev. Immunol. 19:623-655(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  5. "PIAS3 induces SUMO-1 modification and transcriptional repression of IRF-1."
    Nakagawa K., Yokosawa H.
    FEBS Lett. 530:204-208(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIAS3, SUMOYLATION, FUNCTION.
  6. Cited for: REVIEW ON FUNCTION.
  7. Cited for: REVIEW ON FUNCTION.
  8. "IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors."
    Honda K., Taniguchi T.
    Nat. Rev. Immunol. 6:644-658(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  9. "Evidence for licensing of IFN-gamma-induced IFN regulatory factor 1 transcription factor by MyD88 in Toll-like receptor-dependent gene induction program."
    Negishi H., Fujita Y., Yanai H., Sakaguchi S., Ouyang X., Shinohara M., Takayanagi H., Ohba Y., Taniguchi T., Honda K.
    Proc. Natl. Acad. Sci. U.S.A. 103:15136-15141(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYD88.
  10. "Ubc9-mediated sumoylation leads to transcriptional repression of IRF-1."
    Kim E.-J., Park J.-S., Um S.-J.
    Biochem. Biophys. Res. Commun. 377:952-956(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, FUNCTION.
  11. "IFN regulatory factor-1 negatively regulates CD4+ CD25+ regulatory T cell differentiation by repressing Foxp3 expression."
    Fragale A., Gabriele L., Stellacci E., Borghi P., Perrotti E., Ilari R., Lanciotti A., Remoli A.L., Venditti M., Belardelli F., Battistini A.
    J. Immunol. 181:1673-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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.
  13. "IFN regulatory factor-1 bypasses IFN-mediated antiviral effects through viperin gene induction."
    Stirnweiss A., Ksienzyk A., Klages K., Rand U., Grashoff M., Hauser H., Kroeger A.
    J. Immunol. 184:5179-5185(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Interferon regulatory factor-1 (IRF-1) shapes both innate and CD8(+) T cell immune responses against West Nile virus infection."
    Brien J.D., Daffis S., Lazear H.M., Cho H., Suthar M.S., Gale M. Jr., Diamond M.S.
    PLoS Pathog. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Structure of IRF-1 with bound DNA reveals determinants of interferon regulation."
    Escalante C.R., Yie J., Thanos D., Aggarwal A.K.
    Nature 391:103-106(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 7-111.

Entry informationi

Entry nameiIRF1_MOUSE
AccessioniPrimary (citable) accession number: P15314
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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