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	MGI: 96591 HomoloGene: 1659 GeneCards: IRF2
Gene ontology Molecular function • transcription factor activity, sequence-specific DNA binding • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding • regulatory region DNA binding • DNA binding • RNA polymerase II regulatory region sequence-specific DNA binding • protein binding Cellular component • cytoplasm • cytosol • nucleus • focal adhesion • nucleoplasm Biological process • interferon-gamma-mediated signaling pathway • cell 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 Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3660	16363
Ensembl	ENSG00000168310	ENSMUSG00000031627
UniProt	P14316	P23906
RefSeq (mRNA)	NM_002199	NM_008391
RefSeq (protein)	NP_002190.2	NP_032417.3
Location (UCSC)	Chr 4: 184.39 – 184.47 Mb	Chr 8: 46.74 – 46.85 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Interferon regulatory factor 2 is a protein that in humans is encoded by the IRF2 gene.^[3]

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.^[4]

See also

• IRF1
• Interferon regulatory factors

Interactions

IRF2 has been shown to interact with BRD7,^[5] EP300^[6] and PCAF.^[6][7]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "Entrez Gene: IRF2 interferon regulatory factor 2".
5. 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.
6. 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.
7. 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. PMC 83974. 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, 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. 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. 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

• 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.