Biology:IFNAR2

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

Generic protein structure example

Interferon-alpha/beta receptor beta chain is a protein that in humans is encoded by the IFNAR2 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 interferons alpha and beta. Binding and activation of the receptor stimulates Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. Multiple transcript variants encoding at least two different isoforms have been found for this gene.

Interactions

IFNAR2 has been shown to interact with:

• GNB2L1,
• IFNA2,
• STAT1, and
• STAT2.

Further reading

• "Alpha-interferon and its effects on signal transduction pathways". J. Cell. Physiol. 202 (2): 323–35. 2005. doi:10.1002/jcp.20137. PMID 15389589. 
• "Three distinct loci on human chromosome 21 contribute to interferon-alpha/beta responsiveness". Somat. Cell Mol. Genet. 21 (2): 139–45. 1995. doi:10.1007/BF02255789. PMID 7570186. 
• "Mutant U5A cells are complemented by an interferon-alpha beta receptor subunit generated by alternative processing of a new member of a cytokine receptor gene cluster". EMBO J. 14 (20): 5100–8. 1995. doi:10.1002/j.1460-2075.1995.tb00192.x. PMID 7588638. 
• "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. 
• "Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor". J. Leukoc. Biol. 57 (5): 712–8. 1995. doi:10.1002/jlb.57.5.712. PMID 7759950. 
• "Differences in interferon alpha and beta signaling. Interferon beta selectively induces the interaction of the alpha and betaL subunits of the type I interferon receptor". J. Biol. Chem. 271 (39): 23630–3. 1996. doi:10.1074/jbc.271.39.23630. PMID 8798579. 
• "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. 1996. doi:10.1101/gr.6.9.791. PMID 8889548. 
• "The human type I interferon receptor. Identification of the interferon beta-specific receptor-associated phosphoprotein". J. Biol. Chem. 271 (52): 33165–8. 1996. doi:10.1074/jbc.271.52.33165. PMID 8969169. 
• "Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling". Mol. Cell. Biol. 17 (4): 2048–56. 1997. doi:10.1128/mcb.17.4.2048. PMID 9121453. 
• "Biophysical analysis of the interaction of human ifnar2 expressed in E. coli with IFNalpha2". J. Mol. Biol. 289 (1): 57–67. 1999. doi:10.1006/jmbi.1999.2726. PMID 10339405. 
• "Determination of residues involved in ligand binding and signal transmission in the human IFN-alpha receptor 2". J. Immunol. 163 (2): 766–73. 1999. PMID 10395669. 
• "The DNA sequence of human chromosome 21". Nature 405 (6784): 311–9. 2000. doi:10.1038/35012518. PMID 10830953. Bibcode: 2000Natur.405..311H. 
• "Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor". J. Immunol. 165 (9): 5127–32. 2000. doi:10.4049/jimmunol.165.9.5127. PMID 11046044. 
• "The WD motif-containing protein receptor for activated protein kinase C (RACK1) is required for recruitment and activation of signal transducer and activator of transcription 1 through the type I interferon receptor". J. Biol. Chem. 276 (25): 22948–53. 2001. doi:10.1074/jbc.M100087200. PMID 11301323. 
• "Stat2 binding to the interferon-alpha receptor 2 subunit is not required for interferon-alpha signaling". J. Biol. Chem. 277 (12): 9713–21. 2002. doi:10.1074/jbc.M111161200. PMID 11786546. 
• "The human interferon receptor: NMR-based modeling, mapping of the IFN-alpha 2 binding site, and observed ligand-induced tightening". Biochemistry 41 (11): 3575–85. 2002. doi:10.1021/bi011778f. PMID 11888273. 
• "STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c. Activation of multiple STATS proceeds through the redundant usage of two tyrosine residues". J. Biol. Chem. 277 (38): 35635–41. 2002. doi:10.1074/jbc.M204578200. PMID 12105218. 
• "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors". J. Immunol. 169 (3): 1302–8. 2002. doi:10.4049/jimmunol.169.3.1302. PMID 12133952. 
• "Loss of type I IFN receptors and impaired IFN responsiveness during terminal maturation of monocyte-derived human dendritic cells". J. Immunol. 169 (6): 3038–45. 2002. doi:10.4049/jimmunol.169.6.3038. PMID 12218119.