IRF1: Wikis


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Interferon regulatory factor 1

PDB rendering based on 1if1.
Available structures
Symbols IRF1; IRF-1; MAR
External IDs OMIM147575 MGI96590 HomoloGene1658 GeneCards: IRF1 Gene
RNA expression pattern
PBB GE IRF1 202531 at tn.png
More reference expression data
Species Human Mouse
Entrez 3659 16362
Ensembl ENSG00000125347 ENSMUSG00000018899
UniProt P10914 Q4FK18
RefSeq (mRNA) NM_002198 NM_008390
RefSeq (protein) NP_002189 NP_032416
Location (UCSC) Chr 5:
131.85 - 131.85 Mb
Chr 11:
53.61 - 53.62 Mb
PubMed search [1] [2]

Interferon regulatory factor 1 is a protein that in humans is encoded by the IRF1 gene.[1][2]

IRF1 encodes interferon regulatory factor 1, a member of the interferon regulatory transcription factor (IRF) family. IRF1 serves as an activator of interferons alpha and beta transcription, and in mouse it has been shown to be required for double-stranded RNA induction of these genes. IRF1 also functions as a transcription activator of genes induced by interferons alpha, beta, and gamma. Further, IRF1 has been shown to play roles in regulating apoptosis and tumor-suppression.[3]


See also


IRF1 has been shown to interact with IRF8,[4][5] STAT1[6], PCAF [7] and Foxp3.


  1. ^ Maruyama M, Fujita T, Taniguchi T (Jun 1989). "Sequence of a cDNA coding for human IRF-1". Nucleic Acids Res 17 (8): 3292. PMID 2726461.  
  2. ^ Itoh S, Harada H, Nakamura Y, White R, Taniguchi T (Nov 1991). "Assignment of the human interferon regulatory factor-1 (IRF1) gene to chromosome 5q23-q31". Genomics 10 (4): 1097–9. PMID 1680796.  
  3. ^ "Entrez Gene: IRF1 interferon regulatory factor 1".  
  4. ^ Schaper, F; Kirchhoff S, Posern G, Köster M, Oumard A, Sharf R, Levi B Z, Hauser H (Oct. 1998). "Functional domains of interferon regulatory factor I (IRF-1)". Biochem. J. (ENGLAND) 335 ( Pt 1): 147–57. ISSN 0264-6021. PMID 9742224.  
  5. ^ Sharf, R; Azriel A, Lejbkowicz F, Winograd S S, Ehrlich R, Levi B Z (Jun. 1995). "Functional domain analysis of interferon consensus sequence binding protein (ICSBP) and its association with interferon regulatory factors". J. Biol. Chem. (UNITED STATES) 270 (22): 13063–9. ISSN 0021-9258. PMID 7768900.  
  6. ^ Chatterjee-Kishore, M; van Den Akker F, Stark G R (Jul. 2000). "Adenovirus E1A down-regulates LMP2 transcription by interfering with the binding of stat1 to IRF1". J. Biol. Chem. (UNITED STATES) 275 (27): 20406–11. doi:10.1074/jbc.M001861200. ISSN 0021-9258. PMID 10764778.  
  7. ^ Masumi, A; Wang I M, Lefebvre B, Yang X J, Nakatani Y, Ozato K (Mar. 1999). "The histone acetylase PCAF is a phorbol-ester-inducible coactivator of the IRF family that confers enhanced interferon responsiveness". Mol. Cell. Biol. (UNITED STATES) 19 (3): 1810–20. ISSN 0270-7306. PMID 10022868.  

Further reading

  • Harada H, Taniguchi T, Tanaka N (1999). "The role of interferon regulatory factors in the interferon system and cell growth control.". Biochimie 80 (8-9): 641–50. doi:10.1016/S0300-9084(99)80017-0. PMID 9865486.  
  • Pitha PM, Au WC, Lowther W, et al. (1999). "Role of the interferon regulatory factors (IRFs) in virus-mediated signaling and regulation of cell growth.". Biochimie 80 (8-9): 651–8. doi:10.1016/S0300-9084(99)80018-2. PMID 9865487.  
  • Yu-Lee L (2002). "Stimulation of interferon regulatory factor-1 by prolactin.". Lupus 10 (10): 691–9. doi:10.1191/096120301717164921. PMID 11721695.  
  • Pine R (2002). "IRF and tuberculosis.". J. Interferon Cytokine Res. 22 (1): 15–25. doi:10.1089/107999002753452629. PMID 11846972.  
  • Romeo G, Fiorucci G, Chiantore MV, et al. (2002). "IRF-1 as a negative regulator of cell proliferation.". J. Interferon Cytokine Res. 22 (1): 39–47. doi:10.1089/107999002753452647. PMID 11846974.  
  • Cha Y, Sims SH, Romine MF, et al. (1992). "Human interferon regulatory factor 1: intron-exon organization.". DNA Cell Biol. 11 (8): 605–11. doi:10.1089/dna.1992.11.605. PMID 1382447.  
  • Harada H, Fujita T, Miyamoto M, et al. (1989). "Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes.". Cell 58 (4): 729–39. doi:10.1016/0092-8674(89)90107-4. PMID 2475256.  
  • Miyamoto M, Fujita T, Kimura Y, et al. (1988). "Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-beta gene regulatory elements.". Cell 54 (6): 903–13. doi:10.1016/S0092-8674(88)91307-4. PMID 3409321.  
  • Harada H, Takahashi E, Itoh S, et al. (1994). "Structure and regulation of the human interferon regulatory factor 1 (IRF-1) and IRF-2 genes: implications for a gene network in the interferon system.". Mol. Cell. Biol. 14 (2): 1500–9. PMID 7507207.  
  • Sharf R, Azriel A, Lejbkowicz F, et al. (1995). "Functional domain analysis of interferon consensus sequence binding protein (ICSBP) and its association with interferon regulatory factors.". J. Biol. Chem. 270 (22): 13063–9. doi:10.1074/jbc.270.22.13063. PMID 7768900.  
  • Willman CL, Sever CE, Pallavicini MG, et al. (1993). "Deletion of IRF-1, mapping to chromosome 5q31.1, in human leukemia and preleukemic myelodysplasia.". Science 259 (5097): 968–71. doi:10.1126/science.8438156. PMID 8438156.  
  • Drew PD, Franzoso G, Becker KG, et al. (1997). "NF kappa B and interferon regulatory factor 1 physically interact and synergistically induce major histocompatibility class I gene expression.". J. Interferon Cytokine Res. 15 (12): 1037–45. PMID 8746784.  
  • Ronco LV, Karpova AY, Vidal M, Howley PM (1998). "Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity.". Genes Dev. 12 (13): 2061–72. doi:10.1101/gad.12.13.2061. PMID 9649509.  
  • Nozawa H, Oda E, Ueda S, et al. (1998). "Functionally inactivating point mutation in the tumor-suppressor IRF-1 gene identified in human gastric cancer.". Int. J. Cancer 77 (4): 522–7. doi:10.1002/(SICI)1097-0215(19980812)77:4<522::AID-IJC8>3.0.CO;2-W. PMID 9679752.  
  • Schaper F, Kirchhoff S, Posern G, et al. (1998). "Functional domains of interferon regulatory factor I (IRF-1).". Biochem. J. 335 ( Pt 1): 147–57. PMID 9742224.  
  • Masumi A, Wang IM, Lefebvre B, et al. (1999). "The histone acetylase PCAF is a phorbol-ester-inducible coactivator of the IRF family that confers enhanced interferon responsiveness.". Mol. Cell. Biol. 19 (3): 1810–20. PMID 10022868.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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