IRF1

Protein-coding gene in the species Homo sapiens
IRF1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1IF1

Identifiers
AliasesIRF1, IRF-1, MAR, interferon regulatory factor 1
External IDsOMIM: 147575 MGI: 96590 HomoloGene: 1658 GeneCards: IRF1
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[1]
Chromosome 11 (mouse)
Genomic location for IRF1
Genomic location for IRF1
Band11 B1.3|11 32.0 cMStart53,660,841 bp[1]
End53,669,200 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
    n/a
Top expressed in
  • jejunum

  • duodenum

  • corneal stroma

  • large intestine

  • spleen

  • colon

  • ileum

  • crypt of lieberkuhn of small intestine

  • right lung

  • right ventricle
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • sequence-specific DNA binding
  • DNA-binding transcription factor activity
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • protein binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • cytoplasm
  • cytosol
  • nucleoplasm
  • nucleus
Biological process
  • apoptotic process
  • regulation of CD8-positive, alpha-beta T cell proliferation
  • CD8-positive, alpha-beta T cell differentiation
  • regulation of innate immune response
  • negative regulation of regulatory T cell differentiation
  • regulation of transcription, DNA-templated
  • cellular response to interferon-beta
  • interferon-gamma-mediated signaling pathway
  • immune system process
  • regulation of adaptive immune response
  • blood coagulation
  • regulation of MyD88-dependent toll-like receptor signaling pathway
  • transcription by RNA polymerase II
  • transcription, DNA-templated
  • regulation of cell cycle
  • positive regulation of transcription, DNA-templated
  • cellular response to mechanical stimulus
  • defense response to virus
  • type I interferon signaling pathway
  • regulation of immune response
  • regulation of gene expression
  • innate immune response
  • negative regulation of transcription, DNA-templated
  • positive regulation of type I interferon production
  • positive regulation of transcription by RNA polymerase II
  • negative regulation of cell population proliferation
  • positive regulation of interferon-beta production
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3659

16362

Ensembl

ENSG00000125347

ENSMUSG00000018899

UniProt

P10914

P15314

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

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

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

IRF1 has been shown to interact with:

See also

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018899 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ 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.
  5. ^ 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.
  6. ^ 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.
  7. ^ 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.
  8. ^ 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.
  9. ^ "Entrez Gene: IRF1 interferon regulatory factor 1".
  10. ^ 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.
  11. ^ 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.
  12. ^ 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.
  13. ^ 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.
  14. ^ 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.
  15. ^ 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.
  16. ^ 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.
  17. ^ 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.
  18. ^ 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.
  19. ^ 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.
  20. ^ 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.
  21. ^ 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.
  22. ^ 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

  • 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.

External links

Wikimedia Commons has media related to Interferon regulatory factor 1 (IRF-1).

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

  • v
  • t
  • e
  • 1if1: INTERFERON REGULATORY FACTOR 1 (IRF-1) COMPLEX WITH DNA
    1if1: INTERFERON REGULATORY FACTOR 1 (IRF-1) COMPLEX WITH DNA
  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies
  • v
  • t
  • e
Ligand
Cytokine receptor
Janus kinase
Adaptor proteins
STAT
PIAS
SOCS
IRF