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P10914

- IRF1_HUMAN

UniProt

P10914 - IRF1_HUMAN

Protein

Interferon regulatory factor 1

Gene

IRF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    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 include: 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.12 Publications

    Enzyme regulationi

    Activated by MYD88.By similarity

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    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_24938. TRAF6 mediated IRF7 activation.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    SignaLinkiP10914.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon regulatory factor 1
    Short name:
    IRF-1
    Gene namesi
    Name:IRF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6116. IRF1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nuclear chromatin Source: BHF-UCL
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81M → L in GASC; somatic mutation; produces a protein with markedly reduced transcriptional activity but unaltered DNA-binding activity. 1 Publication
    VAR_065134
    Natural varianti11 – 111W → R in GASC; the mutation abolishes DNA binding and transactivating activities. 1 Publication
    VAR_065135

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781K → R: Loss of acetylation. Partial loss of DNA-binding and transcriptional activity. 1 Publication
    Mutagenesisi275 – 2751K → R: Some loss of sumoylation. Partial inhibition of acetylation and activity. Abolishes sumoylation, diminished ubiquitination, higher resistance to degradation, and increased apoptotic activity; when associated with R-299. 1 Publication
    Mutagenesisi299 – 2991K → R: Large loss of sumoylation. Abolishes sumoylation, diminished ubiquitination, higher resistance to degradation, and increased apoptotic activity; when associated with R-275. 1 Publication

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi613659. phenotype.
    PharmGKBiPA29915.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 325325Interferon regulatory factor 1PRO_0000154545Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei78 – 781N6-acetyllysine1 Publication
    Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki299 – 299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Phosphorylated by CK2 and this positively regulates its activity.1 Publication
    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-275. Sumoylation is enhanced by PIAS3 By similarity. Desumoylated by SENP1 in tumor cells and appears to compete with ubiquitination on C-terminal sites.By similarity1 Publication
    Ubiquitinated. Appears to compete with sumoylation on C-terminal sites.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP10914.
    PRIDEiP10914.

    PTM databases

    PhosphoSiteiP10914.

    Expressioni

    Inductioni

    By viruses and interferon (IFN).

    Gene expression databases

    ArrayExpressiP10914.
    BgeeiP10914.
    CleanExiHS_IRF1.
    GenevestigatoriP10914.

    Organism-specific databases

    HPAiCAB011662.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Interacts with MYD88 and PIAS3 By similarity. Interacts with EP300.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E7P031293EBI-1055781,EBI-866453From a different organism.

    Protein-protein interaction databases

    BioGridi109867. 33 interactions.
    DIPiDIP-40988N.
    IntActiP10914. 4 interactions.
    MINTiMINT-123145.
    STRINGi9606.ENSP00000245414.

    Structurei

    3D structure databases

    ProteinModelPortaliP10914.
    SMRiP10914. Positions 7-111.
    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

    eggNOGiNOG42582.
    HOGENOMiHOG000037937.
    HOVERGENiHBG003455.
    InParanoidiP10914.
    KOiK09444.
    OMAiCKEEPEV.
    OrthoDBiEOG72ZCFD.
    PhylomeDBiP10914.
    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.

    P10914-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKH AAKHGWDINK    50
    DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN 100
    KGSSAVRVYR MLPPLTKNQR KERKSKSSRD AKSKAKRKSC GDSSPDTFSD 150
    GLSSSTLPDD HSSYTVPGYM QDLEVEQALT PALSPCAVSS TLPDWHIPVE 200
    VVPDSTSDLY NFQVSPMPST SEATTDEDEE GKLPEDIMKL LEQSEWQPTN 250
    VDGKGYLLNE PGVQPTSVYG DFSCKEEPEI DSPGGDIGLS LQRVFTDLKN 300
    MDATWLDSLL TPVRLPSIQA IPCAP 325
    Length:325
    Mass (Da):36,502
    Last modified:April 16, 2002 - v2
    Checksum:i2E06245A212D1541
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51R → W no nucleotide entry (PubMed:2726461)Curated
    Sequence conflicti5 – 51R → W no nucleotide entry (PubMed:3409321)Curated
    Sequence conflicti34 – 352FQ → LE no nucleotide entry (PubMed:2726461)Curated
    Sequence conflicti34 – 352FQ → LE no nucleotide entry (PubMed:3409321)Curated
    Sequence conflicti220 – 2201T → I no nucleotide entry (PubMed:2726461)Curated
    Sequence conflicti220 – 2201T → I no nucleotide entry (PubMed:3409321)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81M → L in GASC; somatic mutation; produces a protein with markedly reduced transcriptional activity but unaltered DNA-binding activity. 1 Publication
    VAR_065134
    Natural varianti11 – 111W → R in GASC; the mutation abolishes DNA binding and transactivating activities. 1 Publication
    VAR_065135

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14454 mRNA. Translation: CAA32624.1.
    L05072 Genomic DNA. Translation: AAA36043.1.
    BT019756 mRNA. Translation: AAV38561.1.
    BC009483 mRNA. Translation: AAH09483.1.
    CCDSiCCDS4155.1.
    PIRiB31595.
    I52998.
    RefSeqiNP_002189.1. NM_002198.2.
    UniGeneiHs.436061.

    Genome annotation databases

    EnsembliENST00000245414; ENSP00000245414; ENSG00000125347.
    ENST00000405885; ENSP00000384406; ENSG00000125347.
    GeneIDi3659.
    KEGGihsa:3659.
    UCSCiuc003kxa.2. human.

    Polymorphism databases

    DMDMi20178295.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14454 mRNA. Translation: CAA32624.1 .
    L05072 Genomic DNA. Translation: AAA36043.1 .
    BT019756 mRNA. Translation: AAV38561.1 .
    BC009483 mRNA. Translation: AAH09483.1 .
    CCDSi CCDS4155.1.
    PIRi B31595.
    I52998.
    RefSeqi NP_002189.1. NM_002198.2.
    UniGenei Hs.436061.

    3D structure databases

    ProteinModelPortali P10914.
    SMRi P10914. Positions 7-111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109867. 33 interactions.
    DIPi DIP-40988N.
    IntActi P10914. 4 interactions.
    MINTi MINT-123145.
    STRINGi 9606.ENSP00000245414.

    PTM databases

    PhosphoSitei P10914.

    Polymorphism databases

    DMDMi 20178295.

    Proteomic databases

    PaxDbi P10914.
    PRIDEi P10914.

    Protocols and materials databases

    DNASUi 3659.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245414 ; ENSP00000245414 ; ENSG00000125347 .
    ENST00000405885 ; ENSP00000384406 ; ENSG00000125347 .
    GeneIDi 3659.
    KEGGi hsa:3659.
    UCSCi uc003kxa.2. human.

    Organism-specific databases

    CTDi 3659.
    GeneCardsi GC05M131817.
    H-InvDB HIX0200727.
    HGNCi HGNC:6116. IRF1.
    HPAi CAB011662.
    MIMi 147575. gene.
    613659. phenotype.
    neXtProti NX_P10914.
    PharmGKBi PA29915.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42582.
    HOGENOMi HOG000037937.
    HOVERGENi HBG003455.
    InParanoidi P10914.
    KOi K09444.
    OMAi CKEEPEV.
    OrthoDBi EOG72ZCFD.
    PhylomeDBi P10914.
    TreeFami TF328512.

    Enzyme and pathway databases

    Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    SignaLinki P10914.

    Miscellaneous databases

    GeneWikii IRF1.
    GenomeRNAii 3659.
    NextBioi 14311.
    PROi P10914.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10914.
    Bgeei P10914.
    CleanExi HS_IRF1.
    Genevestigatori P10914.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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 [GENOMIC DNA].
    3. "Human interferon regulatory factor 1: intron-exon organization."
      Cha Y., Sims S.H., Romine M.F., Kaufmann M., Deisseroth A.B.
      DNA Cell Biol. 11:605-611(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Tissue: Pancreas.
    6. "Deletion of IRF-1, mapping to chromosome 5q31.1, in human leukemia and preleukemic myelodysplasia."
      Willman C.L., Sever C.E., Pallavicini M.G., Harada H., Tanaka N., Slovak M.L., Yamamoto H., Harada K., Meeker T.C., List A.F., Taniguchi T.
      Science 259:968-971(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN LEUKEMIAS.
    7. "A role for casein kinase II phosphorylation in the regulation of IRF-1 transcriptional activity."
      Lin R., Hiscott J.
      Mol. Cell. Biochem. 191:169-180(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    8. "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.
    9. Cited for: REVIEW ON FUNCTION.
    10. Cited for: REVIEW ON FUNCTION.
    11. "Interferon regulatory factor 1 (IRF-1) and IRF-2 distinctively up-regulate gene expression and production of interleukin-7 in human intestinal epithelial cells."
      Oshima S., Nakamura T., Namiki S., Okada E., Tsuchiya K., Okamoto R., Yamazaki M., Yokota T., Aida M., Yamaguchi Y., Kanai T., Handa H., Watanabe M.
      Mol. Cell. Biol. 24:6298-6310(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53."
      Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R., Ball K.L.
      Mol. Cell. Biol. 24:10083-10098(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EP300.
    13. "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.
    14. "Central role of interferon regulatory factor-1 (IRF-1) in controlling retinoic acid inducible gene-I (RIG-I) expression."
      Su Z.Z., Sarkar D., Emdad L., Barral P.M., Fisher P.B.
      J. Cell. Physiol. 213:502-510(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "RNA interference of interferon regulatory factor-1 gene expression in THP-1 cell line leads to Toll-like receptor-4 overexpression/activation as well as up-modulation of annexin-II."
      Maratheftis C.I., Giannouli S., Spachidou M.P., Panayotou G., Voulgarelis M.
      Neoplasia 9:1012-1020(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Elevated level of SUMOylated IRF-1 in tumor cells interferes with IRF-1-mediated apoptosis."
      Park J., Kim K., Lee E.-J., Seo Y.-J., Lim S.-N., Park K., Rho S.B., Lee S.-H., Lee J.-H.
      Proc. Natl. Acad. Sci. U.S.A. 104:17028-17033(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-275 AND LYS-299, UBIQUITINATION AT LYS-275 AND LYS-299, FUNCTION, MUTAGENESIS OF LYS-275 AND LYS-299.
    17. "IRF-1 promotes apoptosis in p53-damaged basal-type human mammary epithelial cells: a model for early basal-type mammary carcinogenesis."
      Bowie M.L., Ibarra C., Seewalt V.L.
      Adv. Exp. Med. Biol. 617:367-374(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "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.
    19. "Type I interferons and interferon regulatory factors regulate TNF-related apoptosis-inducing ligand (TRAIL) in HIV-1-infected macrophages."
      Huang Y., Walstrom A., Zhang L., Zhao Y., Cui M., Ye L., Zheng J.C.
      PLoS ONE 4:E5397-E5397(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "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.
    21. "IRF-1 transcriptionally upregulates PUMA, which mediates the mitochondrial apoptotic pathway in IRF-1-induced apoptosis in cancer cells."
      Gao J., Senthil M., Ren B., Yan J., Xing Q., Yu J., Zhang L., Yim J.H.
      Cell Death Differ. 17:699-709(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Human papillomavirus type 16 E5 protein induces expression of beta interferon through interferon regulatory factor 1 in human keratinocytes."
      Muto V., Stellacci E., Lamberti A.G., Perrotti E., Carrabba A., Matera G., Sgarbanti M., Battistini A., Liberto M.C., Foca A.
      J. Virol. 85:5070-5080(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Interferon regulatory factor 1 (IRF-1) induces p21(WAF1/CIP1) dependent cell cycle arrest and p21(WAF1/CIP1) independent modulation of survivin in cancer cells."
      Armstrong M.J., Stang M.T., Liu Y., Gao J., Ren B., Zuckerbraun B.S., Mahidhara R.S., Xing Q., Pizzoferrato E., Yim J.H.
      Cancer Lett. 319:56-65(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "Interferon regulatory factor 1 transactivates the expression of human DNA polymerase eta in response to the carcinogen N-methyl-N'-nitro-N-nitrosoguanidine."
      Qi H., Zhu H., Lou M., Fan Y., Liu H., Shen J., Li Z., Lv X., Shan J., Zhu L., Chin Y.E., Shao J.
      J. Biol. Chem. 287:12622-12633(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-78, MUTAGENESIS OF LYS-78.
    25. "Functionally inactivating point mutation in the tumor-suppressor IRF-1 gene identified in human gastric cancer."
      Nozawa H., Oda E., Ueda S., Tamura G., Maesawa C., Muto T., Taniguchi T., Tanaka N.
      Int. J. Cancer 77:522-527(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GASC LEU-8, CHARACTERIZATION OF VARIANT GASC LEU-8.
    26. "Interferon regulatory factor 1 tryptophan 11 to arginine point mutation abolishes DNA binding."
      Eason D.D., Shepherd A.T., Blanck G.
      Biochim. Biophys. Acta 1446:140-144(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GASC ARG-11.

    Entry informationi

    Entry nameiIRF1_HUMAN
    AccessioniPrimary (citable) accession number: P10914
    Secondary accession number(s): Q96GG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 140 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

    Miscellaneous

    Deletion or rearrangement of IRF1 are found in preleukemic myelodysplastic syndrome (MDS) and acute myelogenous leukemia (AML).

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3