IRF2

Protein-coding gene in the species Homo sapiens
IRF2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1IRF, 1IRG, 2IRF

Identifiers
AliasesIRF2, IRF-2, interferon regulatory factor 2
External IDsOMIM: 147576 MGI: 96591 HomoloGene: 1659 GeneCards: IRF2
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for IRF2
Genomic location for IRF2
Band4q35.1Start184,385,702 bp[1]
End184,474,558 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for IRF2
Genomic location for IRF2
Band8|8 B1.1Start47,192,767 bp[2]
End47,300,493 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • blood

  • Achilles tendon

  • appendix

  • spleen

  • lymph node

  • rectum

  • left adrenal gland

  • bone marrow cells

  • gallbladder
Top expressed in
  • blood

  • left colon

  • spleen

  • left lobe of liver

  • thymus

  • duodenum

  • left lung lobe

  • superior frontal gyrus

  • lip

  • yolk sac
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • DNA binding
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding
  • protein binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • nucleus
  • focal adhesion
  • nucleoplasm
  • cytosol
Biological process
  • interferon-gamma-mediated signaling pathway
  • cell population proliferation
  • blood coagulation
  • regulation of transcription, DNA-templated
  • negative regulation of transcription by RNA polymerase II
  • type I interferon signaling pathway
  • transcription, DNA-templated
  • positive regulation of transcription by RNA polymerase II
  • transcription by RNA polymerase II
  • immune system process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3660

16363

Ensembl

ENSG00000168310

ENSMUSG00000031627

UniProt

P14316

P23906

RefSeq (mRNA)

NM_002199

NM_008391

RefSeq (protein)

NP_002190

NP_032417

Location (UCSC)Chr 4: 184.39 – 184.47 MbChr 8: 47.19 – 47.3 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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]

See also

Interactions

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000168310 – Ensembl, May 2017
  2. ^ a b c 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.
  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. S2CID 2033941.
  6. ^ "Entrez Gene: IRF2 interferon regulatory factor 2".
  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. S2CID 22932901.
  8. ^ a b 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.
  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.

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. 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. doi:10.1016/S0021-9258(17)37685-8. 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. Bibcode:1993Sci...259..971H. doi:10.1126/science.8438157. PMID 8438157. S2CID 41036818.
  • 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. S2CID 53166594.
  • 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. S2CID 34485265.
  • 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. S2CID 85574347.
  • 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. S2CID 22932901.
  • 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. S2CID 55595193.
  • 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 U.S. 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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  • 1irf: INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
    1irf: INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
  • 1irg: INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, 20 STRUCTURES
    1irg: INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, 20 STRUCTURES
  • 2irf: CRYSTAL STRUCTURE OF AN IRF-2/DNA COMPLEX.
    2irf: CRYSTAL STRUCTURE OF AN IRF-2/DNA COMPLEX.
  • v
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(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


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