ID:INAR2_HUMAN DESCRIPTION: RecName: Full=Interferon alpha/beta receptor 2; Short=IFN-R-2; Short=IFN-alpha binding protein; Short=IFN-alpha/beta receptor 2; AltName: Full=Interferon alpha binding protein; AltName: Full=Type I interferon receptor 2; Flags: Precursor; FUNCTION: Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity. SUBUNIT: Heterodimer with IFNAR1; in presence of interferon alpha and/or beta ligands forms the type I interferon receptor. Isoform 1 interacts with the transcriptional factors STAT1 and STAT2. Interacts with JAK1. INTERACTION: Q92793:CREBBP; NbExp=4; IntAct=EBI-958408, EBI-81215; P63244:GNB2L1; NbExp=4; IntAct=EBI-958408, EBI-296739; Q00978:IRF9; NbExp=6; IntAct=EBI-958408, EBI-626526; P52630:STAT2; NbExp=2; IntAct=EBI-958408, EBI-1546963; SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Isoform 2: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Isoform 3: Secreted. TISSUE SPECIFICITY: Isoform 3 is detected in the urine (at protein level). Expressed in blood cells. Expressed in lymphoblastoid and fibrosarcoma cell lines. PTM: Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-337 or Tyr-512 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types. PTM: Glycosylated. POLYMORPHISM: Genetic variations in IFNAR2 influence susceptibility to hepatitis B virus (HBV) infection [MIM:610424]. SIMILARITY: Belongs to the type II cytokine receptor family. WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ifnar2/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P48551
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0004905 type I interferon receptor activity GO:0005515 protein binding GO:0019901 protein kinase binding GO:0019962 type I interferon binding
Biological Process: GO:0007166 cell surface receptor signaling pathway GO:0007259 JAK-STAT cascade GO:0009615 response to virus GO:0035455 response to interferon-alpha GO:0035456 response to interferon-beta GO:0051607 defense response to virus GO:0060337 type I interferon signaling pathway GO:0060338 regulation of type I interferon-mediated signaling pathway