IFNAR2

From Wikipedia, the free encyclopedia

Interferon (alpha, beta and omega) receptor 2

PDB rendering based on 1n6u.

Available structures: 1n6u, 1n6v, 2hym

Identifiers

Symbol(s)

IFNAR2; IFN-alpha-REC; IFN-R; IFNABR; IFNARB

External IDs

OMIM: 602376 MGI: 1098243 HomoloGene: 49242

Gene ontology
Molecular Function:	• receptor activity • interferon-alpha/beta receptor activity • protein binding
Cellular Component:	• extracellular region • plasma membrane • integral to plasma membrane
Biological Process:	• regulation of transcription from RNA polymerase II promoter • cell surface receptor linked signal transduction • JAK-STAT cascade • cell proliferation • response to virus

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000874 (mRNA)
NP_000865 (protein)

NM_010509 (mRNA)
NP_034639 (protein)

Location

Chr 21: 33.52 - 33.56 Mb

Chr 16: 91.26 - 91.29 Mb

Pubmed search

[1]

[2]

Interferon (alpha, beta and omega) receptor 2, also known as IFNAR2, is a human gene.

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.^[1]

[edit] References

^ Entrez Gene: IFNAR2 interferon (alpha, beta and omega) receptor 2.

[edit] Further reading

Caraglia M, Marra M, Pelaia G, et al. (2005). "Alpha-interferon and its effects on signal transduction pathways.". J. Cell. Physiol. 202 (2): 323–35. doi:10.1002/jcp.20137. PMID 15389589.
Raz R, Cheung K, Ling L, Levy DE (1995). "Three distinct loci on human chromosome 21 contribute to interferon-alpha/beta responsiveness.". Somat. Cell Mol. Genet. 21 (2): 139–45. PMID 7570186.
Lutfalla G, Holland SJ, Cinato E, et al. (1995). "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. PMID 7588638.
Domanski P, Witte M, Kellum M, et al. (1995). "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. PMID 7665574.
Novick D, Cohen B, Tal N, Rubinstein M (1995). "Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor.". J. Leukoc. Biol. 57 (5): 712–8. PMID 7759950.
Novick D, Cohen B, Rubinstein M (1994). "The human interferon alpha/beta receptor: characterization and molecular cloning.". Cell 77 (3): 391–400. PMID 8181059.
Platanias LC, Uddin S, Domanski P, Colamonici OR (1996). "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. PMID 8798579.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Croze E, Russell-Harde D, Wagner TC, et al. (1997). "The human type I interferon receptor. Identification of the interferon beta-specific receptor-associated phosphoprotein.". J. Biol. Chem. 271 (52): 33165–8. PMID 8969169.
Li X, Leung S, Kerr IM, Stark GR (1997). "Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling.". Mol. Cell. Biol. 17 (4): 2048–56. PMID 9121453.
Piehler J, Schreiber G (1999). "Biophysical analysis of the interaction of human ifnar2 expressed in E. coli with IFNalpha2.". J. Mol. Biol. 289 (1): 57–67. doi:10.1006/jmbi.1999.2726. PMID 10339405.
Chuntharapai A, Gibbs V, Lu J, et al. (1999). "Determination of residues involved in ligand binding and signal transmission in the human IFN-alpha receptor 2.". J. Immunol. 163 (2): 766–73. PMID 10395669.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
Croze E, Usacheva A, Asarnow D, et al. (2000). "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. PMID 11046044.
Usacheva A, Smith R, Minshall R, et al. (2001). "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. doi:10.1074/jbc.M100087200. PMID 11301323.
Nguyen VP, Saleh AZ, Arch AE, et al. (2002). "Stat2 binding to the interferon-alpha receptor 2 subunit is not required for interferon-alpha signaling.". J. Biol. Chem. 277 (12): 9713–21. doi:10.1074/jbc.M111161200. PMID 11786546.
Chill JH, Nivasch R, Levy R, et al. (2002). "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. PMID 11888273.
Velichko S, Wagner TC, Turkson J, et al. (2002). "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. doi:10.1074/jbc.M204578200. PMID 12105218.
Usacheva A, Kotenko S, Witte MM, Colamonici OR (2002). "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors.". J. Immunol. 169 (3): 1302–8. PMID 12133952.
Gauzzi MC, Canini I, Eid P, et al. (2002). "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. PMID 12218119.