Jump to content
 







Main menu
   


Navigation  



Main page
Contents
Current events
Random article
About Wikipedia
Contact us
Donate
 




Contribute  



Help
Learn to edit
Community portal
Recent changes
Upload file
 








Search  

































Create account

Log in
 









Create account
 Log in
 




Pages for logged out editors learn more  



Contributions
Talk
 



















Contents

   



(Top)
 


1 Function  





2 Regulation  





3 Interactions  





4 See also  





5 References  





6 Further reading  





7 External links  














IRF1






Русский
Татарча / tatarça
Українська
 

Edit links
 









Article
Talk
 

















Read
Edit
View history
 








Tools
   


Actions  



Read
Edit
View history
 




General  



What links here
Related changes
Upload file
Special pages
Permanent link
Page information
Cite this page
Get shortened URL
Download QR code
Wikidata item
 




Print/export  



Download as PDF
Printable version
 




In other projects  



Wikimedia Commons
 
















Appearance
   

 






From Wikipedia, the free encyclopedia
 


IRF1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIRF1, IRF-1, MAR, interferon regulatory factor 1
External IDsOMIM: 147575; MGI: 96590; HomoloGene: 1658; GeneCards: IRF1; OMA:IRF1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002198

NM_001159393
NM_001159396
NM_008390

RefSeq (protein)

NP_002189
NP_001341853
NP_001341854

NP_001152865
NP_001152868
NP_032416

Location (UCSC)n/aChr 11: 53.66 – 53.67 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Interferon regulatory factor 1 is a protein that in humans is encoded by the IRF1 gene.[4][5]

Function

[edit]

Interferon regulatory factor 1 was the first member of the interferon regulatory transcription factor (IRF) family identified. Initially described as a transcription factor able to activate expression of the cytokine Interferon beta,[6] IRF-1 was subsequently shown to function as a transcriptional activator or repressor of a variety of target genes. IRF-1 regulates expression of target genes by binding to an interferon stimulated response element (ISRE) in their promoters. The IRF-1 protein binds to the ISRE via an N-terminal helix-turn-helix DNA binding domain,[7] which is highly conserved among all IRF proteins.

Beyond its function as a transcription factor, IRF-1 has also been shown to trans-activate the tumour suppressor protein p53 through the recruitment of its co-factor p300.[8]

IRF-1 has been shown to play roles in the immune response, regulating apoptosis, DNA damage and tumor suppression.[9]

Regulation

[edit]

It has been shown that the extreme C-terminus of IRF-1 regulates its ability to activate transcription, nanobodies targeting this domain (MF1) are able to increase IRF-1 activity.[10]

Interactions

[edit]

IRF1 has been shown to interact with:

See also

[edit]

References

[edit]
  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ Maruyama M, Fujita T, Taniguchi T (Jun 1989). "Sequence of a cDNA coding for human IRF-1". Nucleic Acids Res. 17 (8): 3292. doi:10.1093/nar/17.8.3292. PMC 317732. PMID 2726461.
  • ^ 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. doi:10.1016/0888-7543(91)90208-V. PMID 1680796.
  • ^ Miyamoto M, Fujita T, Kimura Y, Maruyama M, Harada H, Sudo Y, Miyata T, Taniguchi T (September 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. S2CID 35063951.
  • ^ Escalante CR, Yie J, Thanos D, Aggarwal AK (January 1998). "Structure of IRF-1 with bound DNA reveals determinants of interferon regulation". Nature. 391 (6662): 103–6. Bibcode:1998Natur.391..103E. doi:10.1038/34224. PMID 9422515. S2CID 4394514.
  • ^ Dornan D, Eckert M, Wallace M, Shimizu H, Ramsay E, Hupp TR, Ball KL (November 2004). "Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53". Mol. Cell. Biol. 24 (22): 10083–98. doi:10.1128/MCB.24.22.10083-10098.2004. PMC 525491. PMID 15509808.
  • ^ "Entrez Gene: IRF1 interferon regulatory factor 1".
  • ^ Möller A, Pion E, Narayan V, Ball KL (December 2010). "Intracellular activation of interferon regulatory factor-1 by nanobodies to the multifunctional (Mf1) domain". J. Biol. Chem. 285 (49): 38348–61. doi:10.1074/jbc.M110.149476. PMC 2992268. PMID 20817723.
  • ^ Narayan V, Pion E, Landré V, Müller P, Ball KL (October 2010). "Docking dependent ubiquitination of the interferon regulatory factor-1 tumour suppressor protein by the ubiquitin ligase CHIP". J Biol Chem. 286 (1): 607–19. doi:10.1074/jbc.M110.153122. PMC 3013021. PMID 20947504.
  • ^ Kular RK, Yehiely F, Kotlo KU, Cilensek ZM, Bedi R, Deiss LP (October 2009). "GAGE, an antiapoptotic protein binds and modulates the expression of nucleophosmin/B23 and interferon regulatory factor 1". J. Interferon Cytokine Res. 29 (10): 645–55. doi:10.1089/jir.2008.0099. PMID 19642896.
  • ^ Narayan V, Eckert M, Zylicz A, Zylicz M, Ball KL (September 2009). "Cooperative regulation of the interferon regulatory factor-1 tumor suppressor protein by core components of the molecular chaperone machinery". J Biol Chem. 284 (38): 25889–99. doi:10.1074/jbc.M109.019505. PMC 2757990. PMID 19502235.
  • ^ Schaper F, Kirchhoff S, Posern G, Köster M, Oumard A, Sharf R, Levi BZ, Hauser H (October 1998). "Functional domains of interferon regulatory factor I (IRF-1)". Biochem. J. 335 (1): 147–57. doi:10.1042/bj3350147. PMC 1219763. PMID 9742224.
  • ^ Sharf R, Azriel A, Lejbkowicz F, Winograd SS, Ehrlich R, Levi BZ (June 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.
  • ^ Umegaki N, Tamai K, Nakano H, Moritsugu R, Yamazaki T, Hanada K, Katayama I, Kaneda Y (June 2007). "Differential regulation of karyopherin alpha 2 expression by TGF-beta1 and IFN-gamma in normal human epidermal keratinocytes: evident contribution of KPNA2 for nuclear translocation of IRF-1". J. Invest. Dermatol. 127 (6): 1456–64. doi:10.1038/sj.jid.5700716. PMID 17255955.
  • ^ Negishi H, Fujita Y, Yanai H, Sakaguchi S, Ouyang X, Shinohara M, Takayanagi H, Ohba Y, Taniguchi T, Honda K (October 2006). "Evidence for licensing of IFN-gamma-induced IFN regulatory factor 1 transcription factor by MyD88 in Toll-like receptor-dependent gene induction program". Proc. Natl. Acad. Sci. U.S.A. 103 (41): 15136–41. Bibcode:2006PNAS..10315136N. doi:10.1073/pnas.0607181103. PMC 1586247. PMID 17018642.
  • ^ Masumi A, Wang IM, Lefebvre B, Yang XJ, Nakatani Y, Ozato K (March 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. doi:10.1128/MCB.19.3.1810. PMC 83974. PMID 10022868.
  • ^ Chatterjee-Kishore M, van Den Akker F, Stark GR (July 2000). "Adenovirus E1A down-regulates LMP2 transcription by interfering with the binding of stat1 to IRF1". J. Biol. Chem. 275 (27): 20406–11. doi:10.1074/jbc.M001861200. PMID 10764778.
  • ^ Sgarbanti M, Borsetti A, Moscufo N, Bellocchi MC, Ridolfi B, Nappi F, Marsili G, Marziali G, Coccia EM, Ensoli B, Battistini A (May 2002). "Modulation of human immunodeficiency virus 1 replication by interferon regulatory factors". J. Exp. Med. 195 (10): 1359–70. doi:10.1084/jem.20010753. PMC 2193759. PMID 12021315.
  • ^ Lee JH, Chun T, Park SY, Rho SB (September 2008). "Interferon regulatory factor-1 (IRF-1) regulates VEGF-induced angiogenesis in HUVECs". Biochim. Biophys. Acta. 1783 (9): 1654–62. doi:10.1016/j.bbamcr.2008.04.006. PMID 18472010.
  • ^ Gupta, M.; Rath, PC (2014). "Interferon regulatory factor-1 (IRF-1) interacts with regulated in development and DNA damage response 2 (REDD2) in the cytoplasm of mouse bone marrow cells". Int J Biol Macromol. 65: 41–50. doi:10.1016/j.ijbiomac.2014.01.005. PMID 24412152.
  • Further reading

    [edit]
    • 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, Juang YT, Schafer SL, Burysek L, Hiscott J, Moore PA (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. S2CID 13547888.
  • 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, Percario ZA, Vannucchi S, Affabris E (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, Kaufmann M, Deisseroth AB (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, Kimura Y, Maruyama M, Furia A, Miyata T, Taniguchi T (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. S2CID 2033941.
  • Miyamoto M, Fujita T, Kimura Y, Maruyama M, Harada H, Sudo Y, Miyata T, Taniguchi T (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. S2CID 35063951.
  • Harada H, Takahashi E, Itoh S, Harada K, Hori TA, Taniguchi T (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. doi:10.1128/MCB.14.2.1500. PMC 358505. PMID 7507207.
  • Sharf R, Azriel A, Lejbkowicz F, Winograd SS, Ehrlich R, Levi BZ (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, Harada H, Tanaka N, Slovak ML, Yamamoto H, Harada K, Meeker TC, List AF (1993). "Deletion of IRF-1, mapping to chromosome 5q31.1, in human leukemia and preleukemic myelodysplasia". Science. 259 (5097): 968–71. Bibcode:1993Sci...259..968W. doi:10.1126/science.8438156. PMID 8438156. S2CID 40142541.
  • Drew PD, Franzoso G, Becker KG, Bours V, Carlson LM, Siebenlist U, Ozato K (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. doi:10.1089/jir.1995.15.1037. 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. PMC 316980. PMID 9649509.
  • Nozawa H, Oda E, Ueda S, Tamura G, Maesawa C, Muto T, Taniguchi T, Tanaka N (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. S2CID 25951704.
  • Schaper F, Kirchhoff S, Posern G, Köster M, Oumard A, Sharf R, Levi BZ, Hauser H (1998). "Functional domains of interferon regulatory factor I (IRF-1)". Biochem. J. 335 (1): 147–57. doi:10.1042/bj3350147. PMC 1219763. PMID 9742224.
  • Masumi A, Wang IM, Lefebvre B, Yang XJ, Nakatani Y, Ozato K (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. doi:10.1128/MCB.19.3.1810. PMC 83974. PMID 10022868.
  • [edit]

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


    Retrieved from "https://en.wikipedia.org/w/index.php?title=IRF1&oldid=1190647751"

    Categories: 
    Human genes
    Transcription factors
    Genes mutated in mice
    Hidden categories: 
    Articles with short description
    Short description matches Wikidata
    Commons category link is on Wikidata
    Wikipedia articles incorporating text from the United States National Library of Medicine
     



    This page was last edited on 19 December 2023, at 02:43 (UTC).

    Text is available under the Creative Commons Attribution-ShareAlike License 4.0; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.



    Privacy policy

    About Wikipedia

    Disclaimers

    Contact Wikipedia

    Code of Conduct

    Developers

    Statistics

    Cookie statement

    Mobile view



    Wikimedia Foundation
    Powered by MediaWiki