IRF2

IRF2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1IRF, 1IRG, 2IRF
Identifiers
Aliases	IRF2, IRF-2, interferon regulatory factor 2
External IDs	OMIM: 147576 MGI: 96591 HomoloGene: 1659 GeneCards: IRF2
Gene location (Human)
Chr.	Chromosome 4 (human)[1]
End	184,474,580 bp[1]
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)[2]
End	46,847,458 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity; • GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific; • DNA binding; • RNA polymerase II regulatory region sequence-specific DNA binding; • GO:0001948 protein binding; • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific;
Cellular component	• cell nucleus; • focal adhesion; • nucleoplasm; • cytosol;
Biological process	• interferon-gamma-mediated signaling pathway; • cellular proliferation; • blood coagulation; • regulation of transcription, DNA-templated; • negative regulation of transcription from RNA polymerase II promoter; • type I interferon signaling pathway; • transcription, DNA-templated; • positive regulation of transcription from RNA polymerase II promoter; • transcription from RNA polymerase II promoter; • immune system process;
	Sources:Amigo / QuickGO
Orthologs
	3660
	16363
	ENSG00000168310
	ENSMUSG00000031627
	P14316
	P23906
	NM_002199
	NM_008391
	NP_002190
	NP_032417
	Wikidata
View/Edit Human	View/Edit Mouse

Interferon regulatory factor 2 is a protein that in humans is encoded by the IRF2 gene.[5]

Function

IRF2 encodes interferon regulatory factor 2, a member of the interferon regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of interferons alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4.[6]

Interactions

IRF2 has been shown to interact with BRD7,[7] EP300[8] and PCAF.[8][9]

References

GRCh38: Ensembl release 89: ENSG00000168310 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000031627 - Ensembl, May 2017
"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.
Harada H, Fujita T, Miyamoto M, Kimura Y, Maruyama M, Furia A, Miyata T, Taniguchi T (September 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.
"Entrez Gene: IRF2 interferon regulatory factor 2".
Staal A, Enserink JM, Stein JL, Stein GS, van Wijnen AJ (November 2000). "Molecular characterization of celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2". J. Cell. Physiol. 185 (2): 269–79. doi:10.1002/1097-4652(200011)185:2<269::AID-JCP12>3.0.CO;2-L. PMID 11025449.
Masumi A, Ozato K (June 2001). "Coactivator p300 acetylates the interferon regulatory factor-2 in U937 cells following phorbol ester treatment". J. Biol. Chem. 276 (24): 20973–80. doi:10.1074/jbc.M101707200. PMID 11304541.
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.

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.
Itoh S, Harada H, Fujita T, Mimura T, Taniguchi T (1989). "Sequence of a cDNA coding for human IRF-2". Nucleic Acids Res. 17 (20): 8372. doi:10.1093/nar/17.20.8372. PMC 334978. PMID 2813069.
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.
Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
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.
Cha Y, Deisseroth AB (1994). "Human interferon regulatory factor 2 gene. Intron-exon organization and functional analysis of 5'-flanking region". J. Biol. Chem. 269 (7): 5279–87. PMID 8106512.
Harada H, Kitagawa M, Tanaka N, Yamamoto H, Harada K, Ishihara M, Taniguchi T (1993). "Anti-oncogenic and oncogenic potentials of interferon regulatory factors-1 and -2". Science. 259 (5097): 971–4. doi:10.1126/science.8438157. PMID 8438157.
Drew PD, Franzoso G, Carlson LM, Biddison WE, Siebenlist U, Ozato K (1996). "Interferon regulatory factor-2 physically interacts with NF-kappa B in vitro and inhibits NF-kappa B induction of major histocompatibility class I and beta 2-microglobulin gene expression in transfected human neuroblastoma cells". J. Neuroimmunol. 63 (2): 157–62. doi:10.1016/0165-5728(95)00140-9. PMID 8550813.
Birnbaum MJ, van Zundert B, Vaughan PS, Whitmarsh AJ, van Wijnen AJ, Davis RJ, Stein GS, Stein JL (1997). "Phosphorylation of the oncogenic transcription factor interferon regulatory factor 2 (IRF2) in vitro and in vivo". J. Cell. Biochem. 66 (2): 175–83. doi:10.1002/(SICI)1097-4644(19970801)66:2<175::AID-JCB5>3.0.CO;2-N. PMID 9213219.
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.
Li W, Nagineni CN, Hooks JJ, Chepelinsky AB, Egwuagu CE (1999). "Interferon-gamma signaling in human retinal pigment epithelial cells mediated by STAT1, ICSBP, and IRF-1 transcription factors". Invest. Ophthalmol. Vis. Sci. 40 (5): 976–82. PMID 10102295.
Whitney LW, Becker KG, Tresser NJ, Caballero-Ramos CI, Munson PJ, Prabhu VV, Trent JM, McFarland HF, Biddison WE (1999). "Analysis of gene expression in multiple sclerosis lesions using cDNA microarrays". Ann. Neurol. 46 (3): 425–8. doi:10.1002/1531-8249(199909)46:3<425::AID-ANA22>3.0.CO;2-O. PMID 10482277.
Mild GC, Schmahl GE, Shayan P, Niemeyer CM (2000). "Expression of interferon regulatory factor 1 and 2 in hematopoietic cells of children with juvenile myelomonocytic leukemia". Leuk. Lymphoma. 35 (5–6): 507–11. doi:10.1080/10428199909169615. PMID 10609788.
Staal A, Enserink JM, Stein JL, Stein GS, van Wijnen AJ (2000). "Molecular characterization of celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2". J. Cell. Physiol. 185 (2): 269–79. doi:10.1002/1097-4652(200011)185:2<269::AID-JCP12>3.0.CO;2-L. PMID 11025449.
Larrea E, Alberdi A, Castelruiz Y, Boya P, Civeira MP, Prieto J (2001). "Expression of interferon-alpha subtypes in peripheral mononuclear cells from patients with chronic hepatitis C: a role for interferon-alpha5". J. Viral Hepat. 8 (2): 103–10. doi:10.1046/j.1365-2893.2001.00273.x. PMID 11264730.
Masumi A, Ozato K (2001). "Coactivator p300 acetylates the interferon regulatory factor-2 in U937 cells following phorbol ester treatment". J. Biol. Chem. 276 (24): 20973–80. doi:10.1074/jbc.M101707200. PMID 11304541.

External links

Media related to Interferon regulatory factor-2, IRF-2 at Wikimedia Commons
IRF2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

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

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000168310 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000031627 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2475256-5] Harada H, Fujita T, Miyamoto M, Kimura Y, Maruyama M, Furia A, Miyata T, Taniguchi T (September 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.

[6] "Entrez Gene: IRF2 interferon regulatory factor 2".

[pmid11025449-7] Staal A, Enserink JM, Stein JL, Stein GS, van Wijnen AJ (November 2000). "Molecular characterization of celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2". J. Cell. Physiol. 185 (2): 269–79. doi:10.1002/1097-4652(200011)185:2<269::AID-JCP12>3.0.CO;2-L. PMID 11025449.

[pmid11304541-8] Masumi A, Ozato K (June 2001). "Coactivator p300 acetylates the interferon regulatory factor-2 in U937 cells following phorbol ester treatment". J. Biol. Chem. 276 (24): 20973–80. doi:10.1074/jbc.M101707200. PMID 11304541.

[pmid10022868-9] 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.

IRF2

Function

See also

Interactions

References

Further reading

External links