Biology:IFNAR1

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Interferon-alpha/beta receptor alpha chain is a protein that in humans is encoded by the IFNAR1 gene.

Function

The protein encoded by this gene is a type I membrane protein that forms one of the two chains of a receptor for type I interferons, including interferon-alpha, -beta, and -lambda. Binding and activation of the receptor stimulates Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. The encoded protein also functions as an antiviral factor.

Interactions

IFNAR1 has been shown to interact with:

• PRMT1,
• STAT2, and
• Tyrosine kinase 2.

Further reading

• "Introns in sequence tags". Nature 357 (6377): 367–8. 1992. doi:10.1038/357367a0. PMID 1350660. Bibcode: 1992Natur.357..367B. 
• Qiujing Yu, Yuliya V Katlinskaya (2015). "DNA-Damage-Induced Type I Interferon Promotes Senescence and Inhibits Stem Cell Function". Cell Reports 11 (5): 785–797. doi:10.1016/j.celrep.2015.03.069. PMID 25921537. 
• "The structure of the human interferon alpha/beta receptor gene". J. Biol. Chem. 267 (4): 2802–9. 1992. doi:10.1016/S0021-9258(18)45950-9. PMID 1370833. 
• "Human interferon omega (omega) binds to the alpha/beta receptor". J. Biol. Chem. 266 (30): 19875–7. 1991. doi:10.1016/S0021-9258(18)54862-6. PMID 1834641. 
• "Assignment of the human interferon-alpha receptor gene to chromosome 21q22.1 by in situ hybridization". J. Interferon Res. 10 (5): 515–7. 1990. doi:10.1089/jir.1990.10.515. PMID 2148760. 
• "Genetic transfer of a functional human interferon alpha receptor into mouse cells: cloning and expression of its cDNA". Cell 60 (2): 225–34. 1990. doi:10.1016/0092-8674(90)90738-Z. PMID 2153461. 
• "Direct binding to and tyrosine phosphorylation of the alpha subunit of the type I interferon receptor by p135tyk2 tyrosine kinase". Mol. Cell. Biol. 14 (12): 8133–42. 1994. doi:10.1128/mcb.14.12.8133. PMID 7526154. 
• "Interaction of the transcriptional activator Stat-2 with the type I interferon receptor". J. Biol. Chem. 270 (42): 24627–30. 1995. doi:10.1074/jbc.270.42.24627. PMID 7559568. 
• "Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling". J. Biol. Chem. 270 (37): 21606–11. 1995. doi:10.1074/jbc.270.37.21606. PMID 7665574. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "Phosphorylated interferon-alpha receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein". EMBO J. 15 (5): 1064–74. 1996. doi:10.1002/j.1460-2075.1996.tb00444.x. PMID 8605876. 
• "Direct association of STAT3 with the IFNAR-1 chain of the human type I interferon receptor". J. Biol. Chem. 271 (14): 8057–61. 1996. doi:10.1074/jbc.271.14.8057. PMID 8626489. 
• "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J. 16 (2): 260–6. 1997. doi:10.1093/emboj/16.2.260. PMID 9029147. 
• "Post-translational up-regulation of the cell surface-associated alpha component of the human type I interferon receptor during differentiation of peripheral blood monocytes: role in the biological response to type I interferon". Eur. J. Immunol. 27 (5): 1075–81. 1997. doi:10.1002/eji.1830270506. PMID 9174595. 
• "Induction of cytokines by HIV-1 and its gp120 protein in human peripheral blood monocyte/macrophages and modulation of cytokine response during differentiation". J. Leukoc. Biol. 62 (1): 49–53. 1997. doi:10.1002/jlb.62.1.49. PMID 9225992. 
• "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• "Identification of amino acid residues critical for the Src-homology 2 domain-dependent docking of Stat2 to the interferon alpha receptor". J. Biol. Chem. 273 (31): 19495–501. 1998. doi:10.1074/jbc.273.31.19495. PMID 9677371. 
• "Specific contribution of Tyk2 JH regions to the binding and the expression of the interferon alpha/beta receptor component IFNAR1". J. Biol. Chem. 273 (38): 24723–9. 1998. doi:10.1074/jbc.273.38.24723. PMID 9733772. 
• "Catalytically active TYK2 is essential for interferon-beta-mediated phosphorylation of STAT3 and interferon-alpha receptor-1 (IFNAR-1) but not for activation of phosphoinositol 3-kinase". J. Biol. Chem. 274 (45): 32507–11. 1999. doi:10.1074/jbc.274.45.32507. PMID 10542297.