ID INAR2_HUMAN Reviewed; 515 AA. AC P48551; A8KAJ4; D3DSE8; D3DSE9; Q15467; Q6FHD7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 24-JUL-2024, entry version 217. DE RecName: Full=Interferon alpha/beta receptor 2; DE Short=IFN-R-2; DE Short=IFN-alpha binding protein; DE Short=IFN-alpha/beta receptor 2; DE AltName: Full=Interferon alpha binding protein; DE AltName: Full=Type I interferon receptor 2; DE Flags: Precursor; GN Name=IFNAR2; Synonyms=IFNABR, IFNARB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, RP GLYCOSYLATION AT ASN-87 AND ASN-192, FUNCTION, SUBUNIT, INTERACTION WITH RP JAK1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT VAL-10. RC TISSUE=Monocyte; RX PubMed=8181059; DOI=10.1016/0092-8674(94)90154-6; RA Novick D., Cohen B., Rubinstein M.; RT "The human interferon alpha/beta receptor: characterization and molecular RT cloning."; RL Cell 77:391-400(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE RP SPECIFICITY. RC TISSUE=Lymphoblastoma; RX PubMed=7588638; DOI=10.1002/j.1460-2075.1995.tb00192.x; RA Lutfalla G., Holland S.J., Cinato E., Monneron D., Reboul J., Rogers N.C., RA Smith J.M., Stark G.R., Gardiner K., Mogensen K.E., Kerr I.M., Uze G.; RT "Mutant U5A cells are complemented by an interferon-alpha beta receptor RT subunit generated by alternative processing of a new member of a cytokine RT receptor gene cluster."; RL EMBO J. 14:5100-5108(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBUNIT. RC TISSUE=Myeloma; RX PubMed=7665574; DOI=10.1074/jbc.270.37.21606; RA Domanski P., Witte M., Kellum M., Rubinstein M., Hackett R., Pitha P., RA Colamonici O.R.; RT "Cloning and expression of a long form of the beta subunit of the RT interferon alpha beta receptor that is required for signaling."; RL J. Biol. Chem. 270:21606-21611(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PARTIAL PROTEIN SEQUENCE, FUNCTION, RP INTERACTION WITH JAK1, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, PHOSPHORYLATION, AND VARIANT VAL-10. RC TISSUE=Blood; RX PubMed=7759950; DOI=10.1002/jlb.57.5.712; RA Novick D., Cohen B., Tal N., Rubinstein M.; RT "Soluble and membrane-anchored forms of the human IFN-alpha/beta RT receptor."; RL J. Leukoc. Biol. 57:712-718(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-10. RC TISSUE=Blood; RA Cohen B., Kim S.H., Novick D., Rubinstein M.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-8; VAL-10 AND VAL-196. RG SeattleSNPs variation discovery resource; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP FUNCTION. RX PubMed=8798579; DOI=10.1074/jbc.271.39.23630; RA Platanias L.C., Uddin S., Domanski P., Colamonici O.R.; RT "Differences in interferon alpha and beta signaling. Interferon beta RT selectively induces the interaction of the alpha and betaL subunits of the RT type I interferon receptor."; RL J. Biol. Chem. 271:23630-23633(1996). RN [12] RP FUNCTION. RX PubMed=8969169; DOI=10.1074/jbc.271.52.33165; RA Croze E., Russell-Harde D., Wagner T.C., Pu H., Pfeffer L.M., Perez H.D.; RT "The human type I interferon receptor. Identification of the interferon RT beta-specific receptor-associated phosphoprotein."; RL J. Biol. Chem. 271:33165-33168(1996). RN [13] RP FUNCTION, AND INTERACTION WITH STAT1 AND STAT2. RX PubMed=9121453; DOI=10.1128/mcb.17.4.2048; RA Li X., Leung S., Kerr I.M., Stark G.R.; RT "Functional subdomains of STAT2 required for preassociation with the alpha RT interferon receptor and for signaling."; RL Mol. Cell. Biol. 17:2048-2056(1997). RN [14] RP INTERACTION WITH IFNAR1, AND FUNCTION. RX PubMed=10049744; DOI=10.1006/bbrc.1998.0105; RA Russell-Harde D., Wagner T.C., Perez H.D., Croze E.; RT "Formation of a uniquely stable type I interferon receptor complex by RT interferon beta is dependent upon particular interactions between RT interferon beta and its receptor and independent of tyrosine RT phosphorylation."; RL Biochem. Biophys. Res. Commun. 255:539-544(1999). RN [15] RP FUNCTION. RX PubMed=10556041; DOI=10.1006/jmbi.1999.3230; RA Piehler J., Schreiber G.; RT "Mutational and structural analysis of the binding interface between type I RT interferons and their receptor Ifnar2."; RL J. Mol. Biol. 294:223-237(1999). RN [16] RP FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, AND MUTAGENESIS OF RP TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512. RX PubMed=11682488; DOI=10.1074/jbc.m108928200; RA Wagner T.C., Velichko S., Vogel D., Rani M.R., Leung S., Ransohoff R.M., RA Stark G.R., Perez H.D., Croze E.; RT "Interferon signaling is dependent on specific tyrosines located within the RT intracellular domain of IFNAR2c. Expression of IFNAR2c tyrosine mutants in RT U5A cells."; RL J. Biol. Chem. 277:1493-1499(2002). RN [17] RP FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, AND MUTAGENESIS OF RP TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512. RX PubMed=12105218; DOI=10.1074/jbc.m204578200; RA Velichko S., Wagner T.C., Turkson J., Jove R., Croze E.; RT "STAT3 activation by type I interferons is dependent on specific tyrosines RT located in the cytoplasmic domain of interferon receptor chain 2c. RT Activation of multiple STATS proceeds through the redundant usage of two RT tyrosine residues."; RL J. Biol. Chem. 277:35635-35641(2002). RN [18] RP FUNCTION. RX PubMed=17517919; DOI=10.1096/fj.07-8585com; RA Kumaran J., Wei L., Kotra L.P., Fish E.N.; RT "A structural basis for interferon-alpha-receptor interactions."; RL FASEB J. 21:3288-3296(2007). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP STRUCTURE BY NMR OF 28-237, AND DISULFIDE BONDS. RX PubMed=12842042; DOI=10.1016/s0969-2126(03)00120-5; RA Chill J.H., Quadt S.R., Levy R., Schreiber G., Anglister J.; RT "The human type I interferon receptor: NMR structure reveals the molecular RT basis of ligand binding."; RL Structure 11:791-802(2003). RN [21] RP INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION, VARIANTS SER-8 AND VAL-10, RP AND CHARACTERIZATION OF VARIANT SER-8. RX PubMed=16757563; DOI=10.1073/pnas.0602800103; RA Frodsham A.J., Zhang L., Dumpis U., Taib N.A.M., Best S., Durham A., RA Hennig B.J.W., Hellier S., Knapp S., Wright M., Chiaramonte M., Bell J.I., RA Graves M., Whittle H.C., Thomas H.C., Thursz M.R., Hill A.V.S.; RT "Class II cytokine receptor gene cluster is a major locus for hepatitis B RT persistence."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9148-9153(2006). RN [22] RP INTERACTION WITH IFNAR1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025; RA Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S., Katlinski K., RA Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y., Greenberg R.A.; RT "A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon RT responses."; RL Cell Rep. 5:180-193(2013). RN [23] RP STRUCTURE BY NMR OF 28-239 IN COMPLEX WITH IFNA2, AND DISULFIDE BONDS. RX PubMed=17001036; DOI=10.1110/ps.062283006; RA Quadt-Akabayov S.R., Chill J.H., Levy R., Kessler N., Anglister J.; RT "Determination of the human type I interferon receptor binding site on RT human interferon-alpha2 by cross saturation and an NMR-based model of the RT complex."; RL Protein Sci. 15:2656-2668(2006). RN [24] RP STRUCTURE BY NMR OF 28-239 IN COMPLEX WITH IFNA2, AND DISULFIDE BONDS. RX PubMed=20496919; DOI=10.1021/bi100041f; RA Nudelman I., Akabayov S.R., Schnur E., Biron Z., Levy R., Xu Y., Yang D., RA Anglister J.; RT "Intermolecular interactions in a 44 kDa interferon-receptor complex RT detected by asymmetric reverse-protonation and two-dimensional NOESY."; RL Biochemistry 49:5117-5133(2010). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-436 IN COMPLEX WITH IFNAR1 AND RP IFNW1, FUNCTION, AND DISULFIDE BONDS. RX PubMed=21854986; DOI=10.1016/j.cell.2011.06.048; RA Thomas C., Moraga I., Levin D., Krutzik P.O., Podoplelova Y., Trejo A., RA Lee C., Yarden G., Vleck S.E., Glenn J.S., Nolan G.P., Piehler J., RA Schreiber G., Garcia K.C.; RT "Structural linkage between ligand discrimination and receptor activation RT by type I interferons."; RL Cell 146:621-632(2011). RN [26] RP STRUCTURE BY NMR OF 28-237, AND DISULFIDE BONDS. RX PubMed=21819146; DOI=10.1021/ja205480v; RA Nudelman I., Akabayov S.R., Scherf T., Anglister J.; RT "Observation of intermolecular interactions in large protein complexes by RT 2D-double difference nuclear Overhauser enhancement spectroscopy: RT application to the 44 kDa interferon-receptor complex."; RL J. Am. Chem. Soc. 133:14755-14764(2011). RN [27] RP INVOLVEMENT IN IMD45, AND FUNCTION. RX PubMed=26424569; DOI=10.1126/scitranslmed.aac4227; RA Duncan C.J., Mohamad S.M., Young D.F., Skelton A.J., Leahy T.R., RA Munday D.C., Butler K.M., Morfopoulou S., Brown J.R., Hubank M., RA Connell J., Gavin P.J., McMahon C., Dempsey E., Lynch N.E., Jacques T.S., RA Valappil M., Cant A.J., Breuer J., Engelhardt K.R., Randall R.E., RA Hambleton S.; RT "Human IFNAR2 deficiency: Lessons for antiviral immunity."; RL Sci. Transl. Med. 7:307RA154-307RA154(2015). RN [28] RP FUNCTION, INTERACTION WITH STAT2 AND USP18, AND REGION. RX PubMed=28165510; DOI=10.1038/nsmb.3378; RA Arimoto K.I., Loechte S., Stoner S.A., Burkart C., Zhang Y., Miyauchi S., RA Wilmes S., Fan J.B., Heinisch J.J., Li Z., Yan M., Pellegrini S., RA Colland F., Piehler J., Zhang D.E.; RT "STAT2 is an essential adaptor in USP18-mediated suppression of type I RT interferon signaling."; RL Nat. Struct. Mol. Biol. 24:279-289(2017). RN [29] RP VARIANTS GLN-37; VAL-73; VAL-138; GLY-215; ARG-283; LEU-295; CYS-318; RP ASN-324; SER-346; SER-362; LEU-385 AND LEU-450, CHARACTERIZATION OF RP VARIANTS GLN-37; VAL-73; VAL-138; GLY-215; ARG-283; LEU-295; CYS-318; RP ASN-324; SER-346; SER-362; LEU-385 AND LEU-450, AND FUNCTION. RX PubMed=32972995; DOI=10.1126/science.abd4570; RG COVID-STORM Clinicians; RG COVID Clinicians; RG Imagine COVID Group; RG French COVID Cohort Study Group; RG CoV-Contact Cohort; RG Amsterdam UMC Covid-19 Biobank; RG COVID Human Genetic Effort; RG NIAID-USUHS/TAGC COVID Immunity Group; RA Zhang Q., Bastard P., Liu Z., Le Pen J., Moncada-Velez M., Chen J., RA Ogishi M., Sabli I.K.D., Hodeib S., Korol C., Rosain J., Bilguvar K., RA Ye J., Bolze A., Bigio B., Yang R., Arias A.A., Zhou Q., Zhang Y., RA Onodi F., Korniotis S., Karpf L., Philippot Q., Chbihi M., Bonnet-Madin L., RA Dorgham K., Smith N., Schneider W.M., Razooky B.S., Hoffmann H.H., RA Michailidis E., Moens L., Han J.E., Lorenzo L., Bizien L., Meade P., RA Neehus A.L., Ugurbil A.C., Corneau A., Kerner G., Zhang P., Rapaport F., RA Seeleuthner Y., Manry J., Masson C., Schmitt Y., Schlueter A., Le Voyer T., RA Khan T., Li J., Fellay J., Roussel L., Shahrooei M., Alosaimi M.F., RA Mansouri D., Al-Saud H., Al-Mulla F., Almourfi F., Al-Muhsen S.Z., RA Alsohime F., Al Turki S., Hasanato R., van de Beek D., Biondi A., RA Bettini L.R., D'Angio' M., Bonfanti P., Imberti L., Sottini A., Paghera S., RA Quiros-Roldan E., Rossi C., Oler A.J., Tompkins M.F., Alba C., RA Vandernoot I., Goffard J.C., Smits G., Migeotte I., Haerynck F., RA Soler-Palacin P., Martin-Nalda A., Colobran R., Morange P.E., Keles S., RA Coelkesen F., Ozcelik T., Yasar K.K., Senoglu S., Karabela S.N., RA Rodriguez-Gallego C., Novelli G., Hraiech S., Tandjaoui-Lambiotte Y., RA Duval X., Laouenan C., Snow A.L., Dalgard C.L., Milner J.D., Vinh D.C., RA Mogensen T.H., Marr N., Spaan A.N., Boisson B., Boisson-Dupuis S., RA Bustamante J., Puel A., Ciancanelli M.J., Meyts I., Maniatis T., RA Soumelis V., Amara A., Nussenzweig M., Garcia-Sastre A., Krammer F., RA Pujol A., Duffy D., Lifton R.P., Zhang S.Y., Gorochov G., Beziat V., RA Jouanguy E., Sancho-Shimizu V., Rice C.M., Abel L., Notarangelo L.D., RA Cobat A., Su H.C., Casanova J.L.; RT "Inborn errors of type I IFN immunity in patients with life-threatening RT COVID-19."; RL Science 370:0-0(2020). CC -!- FUNCTION: Together with IFNAR1, forms the heterodimeric receptor for CC type I interferons (including interferons alpha, beta, epsilon, omega CC and kappa) (PubMed:10049744, PubMed:10556041, PubMed:21854986, CC PubMed:26424569, PubMed:28165510, PubMed:32972995, PubMed:7665574, CC PubMed:7759950, PubMed:8181059, PubMed:8798579, PubMed:8969169). Type I CC interferon binding activates the JAK-STAT signaling cascade, resulting CC in transcriptional activation or repression of interferon-regulated CC genes that encode the effectors of the interferon response CC (PubMed:10049744, PubMed:17517919, PubMed:21854986, PubMed:26424569, CC PubMed:28165510, PubMed:32972995, PubMed:7665574, PubMed:7759950, CC PubMed:8181059, PubMed:8798579, PubMed:8969169). Mechanistically, type CC I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close CC proximity with one another, driving their associated Janus kinases CC (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross- CC phosphorylate one another (PubMed:10556041, PubMed:11682488, CC PubMed:12105218, PubMed:21854986, PubMed:32972995). The activated CC kinases phosphorylate specific tyrosine residues on the intracellular CC domains of IFNAR1 and IFNAR2, forming docking sites for the STAT CC transcription factors (STAT1, STAT2 and STAT) (PubMed:11682488, CC PubMed:12105218, PubMed:21854986, PubMed:32972995). STAT proteins are CC then phosphorylated by the JAKs, promoting their translocation into the CC nucleus to regulate expression of interferon-regulated genes CC (PubMed:12105218, PubMed:28165510, PubMed:9121453). CC {ECO:0000269|PubMed:10049744, ECO:0000269|PubMed:10556041, CC ECO:0000269|PubMed:11682488, ECO:0000269|PubMed:12105218, CC ECO:0000269|PubMed:17517919, ECO:0000269|PubMed:21854986, CC ECO:0000269|PubMed:26424569, ECO:0000269|PubMed:28165510, CC ECO:0000269|PubMed:32972995, ECO:0000269|PubMed:7665574, CC ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059, CC ECO:0000269|PubMed:8798579, ECO:0000269|PubMed:8969169, CC ECO:0000269|PubMed:9121453}. CC -!- FUNCTION: [Isoform 3]: Potent inhibitor of type I IFN receptor CC activity. {ECO:0000269|PubMed:7759950}. CC -!- SUBUNIT: Heterodimer with IFNAR1; forming the receptor for type I CC interferon (PubMed:10049744, PubMed:21854986, PubMed:24075985, CC PubMed:7665574, PubMed:8181059). Interacts with JAK1 (PubMed:7759950, CC PubMed:8181059). Interacts with the transcriptional factors STAT1 and CC STAT2 (PubMed:28165510, PubMed:9121453). Interacts with USP18; CC indirectly via STAT2, it negatively regulates the assembly of the CC ternary interferon-IFNAR1-IFNAR2 complex and therefore type I CC interferon signaling (PubMed:28165510). {ECO:0000269|PubMed:10049744, CC ECO:0000269|PubMed:17001036, ECO:0000269|PubMed:20496919, CC ECO:0000269|PubMed:21854986, ECO:0000269|PubMed:24075985, CC ECO:0000269|PubMed:28165510, ECO:0000269|PubMed:7665574, CC ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059, CC ECO:0000269|PubMed:9121453}. CC -!- INTERACTION: CC P48551; Q92793: CREBBP; NbExp=4; IntAct=EBI-958408, EBI-81215; CC P48551; P01563: IFNA2; NbExp=2; IntAct=EBI-958408, EBI-4394394; CC P48551; Q00978: IRF9; NbExp=6; IntAct=EBI-958408, EBI-626526; CC P48551; P23458: JAK1; NbExp=3; IntAct=EBI-958408, EBI-1383438; CC P48551; P63244: RACK1; NbExp=4; IntAct=EBI-958408, EBI-296739; CC P48551; P42224: STAT1; NbExp=2; IntAct=EBI-958408, EBI-1057697; CC P48551; P52630: STAT2; NbExp=4; IntAct=EBI-958408, EBI-1546963; CC P48551; Q9UMW8: USP18; NbExp=4; IntAct=EBI-958408, EBI-356206; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane CC {ECO:0000269|PubMed:7665574}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:7665574}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane CC {ECO:0000269|PubMed:7665574, ECO:0000269|PubMed:7759950, CC ECO:0000269|PubMed:8181059}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:7665574}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted CC {ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Long form beta {ECO:0000303|PubMed:7665574}, IFNaR2-2, CC IFNaR2-1b; CC IsoId=P48551-1; Sequence=Displayed; CC Name=2; Synonyms=Short form beta {ECO:0000303|PubMed:7665574}, CC IFNaR2-1, IFNaR2-1a; CC IsoId=P48551-2; Sequence=VSP_001738, VSP_001739; CC Name=3; Synonyms=IFNaR2-3, IFNaR2-2a, P40 {ECO:0000303|PubMed:8181059}; CC IsoId=P48551-3; Sequence=VSP_001736, VSP_001737; CC -!- TISSUE SPECIFICITY: Isoform 3 is detected in the urine (at protein CC level) (PubMed:7759950, PubMed:8181059). Expressed in blood cells. CC Expressed in lymphoblastoid and fibrosarcoma cell lines. CC {ECO:0000269|PubMed:7588638, ECO:0000269|PubMed:7759950, CC ECO:0000269|PubMed:8181059}. CC -!- PTM: Phosphorylated on tyrosine residues upon interferon binding. CC Phosphorylation at Tyr-337 or Tyr-512 are sufficient to mediate CC interferon dependent activation of STAT1, STAT2 and STAT3 leading to CC antiproliferative effects on many different cell types. CC {ECO:0000269|PubMed:11682488, ECO:0000269|PubMed:12105218, CC ECO:0000269|PubMed:7759950}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8181059}. CC -!- POLYMORPHISM: Genetic variations in IFNAR2 influence susceptibility to CC hepatitis B virus (HBV) infection [MIM:610424]. CC -!- DISEASE: Immunodeficiency 45 (IMD45) [MIM:616669]: An autosomal CC recessive disorder characterized by increased susceptibility to viral CC infection due to impaired antiviral immunity, resulting in infection- CC associated encephalopathy. Affected individuals are at risk for CC developing fatal encephalitis after routine measles/mumps/rubella (MMR) CC vaccination. {ECO:0000269|PubMed:26424569}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 3]: Soluble receptor. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the type II cytokine receptor family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/ifnar2/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X77722; CAA54785.1; -; mRNA. DR EMBL; L42243; AAB46417.1; -; Genomic_DNA. DR EMBL; L42238; AAB46417.1; JOINED; Genomic_DNA. DR EMBL; L42239; AAB46417.1; JOINED; Genomic_DNA. DR EMBL; L42240; AAB46417.1; JOINED; Genomic_DNA. DR EMBL; L42323; AAB46417.1; JOINED; Genomic_DNA. DR EMBL; L42241; AAB46417.1; JOINED; Genomic_DNA. DR EMBL; L42242; AAB46417.1; JOINED; Genomic_DNA. DR EMBL; L42243; AAB46418.1; -; Genomic_DNA. DR EMBL; L42238; AAB46418.1; JOINED; Genomic_DNA. DR EMBL; L42239; AAB46418.1; JOINED; Genomic_DNA. DR EMBL; L42240; AAB46418.1; JOINED; Genomic_DNA. DR EMBL; L42323; AAB46418.1; JOINED; Genomic_DNA. DR EMBL; L42241; AAB46418.1; JOINED; Genomic_DNA. DR EMBL; L42243; AAB46419.1; -; Genomic_DNA. DR EMBL; L42238; AAB46419.1; JOINED; Genomic_DNA. DR EMBL; L42239; AAB46419.1; JOINED; Genomic_DNA. DR EMBL; L42240; AAB46419.1; JOINED; Genomic_DNA. DR EMBL; L42323; AAB46419.1; JOINED; Genomic_DNA. DR EMBL; L42241; AAB46419.1; JOINED; Genomic_DNA. DR EMBL; L42242; AAB46419.1; JOINED; Genomic_DNA. DR EMBL; L41942; AAB46413.1; -; mRNA. DR EMBL; L41943; AAB46414.1; -; mRNA. DR EMBL; L41944; AAB46415.1; -; mRNA. DR EMBL; U29584; AAC50202.1; -; mRNA. DR EMBL; X89814; CAA61940.1; -; mRNA. DR EMBL; X89772; CAA61914.1; -; mRNA. DR EMBL; AY740397; AAU21038.1; -; Genomic_DNA. DR EMBL; AK293059; BAF85748.1; -; mRNA. DR EMBL; CR541817; CAG46616.1; -; mRNA. DR EMBL; AP000292; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000293; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000294; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000295; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09842.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09843.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09844.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09846.1; -; Genomic_DNA. DR CCDS; CCDS13621.1; -. [P48551-1] DR CCDS; CCDS13622.1; -. [P48551-2] DR CCDS; CCDS74782.1; -. [P48551-3] DR PIR; I39073; I39073. DR PIR; S59501; S59501. DR RefSeq; NP_000865.2; NM_000874.4. [P48551-2] DR RefSeq; NP_001276054.1; NM_001289125.1. [P48551-1] DR RefSeq; NP_001276055.1; NM_001289126.1. [P48551-3] DR RefSeq; NP_001276057.1; NM_001289128.1. [P48551-3] DR RefSeq; NP_997467.1; NM_207584.2. [P48551-2] DR RefSeq; NP_997468.1; NM_207585.2. [P48551-1] DR PDB; 1N6U; NMR; -; A=28-237. DR PDB; 1N6V; NMR; -; A=28-237. DR PDB; 2HYM; NMR; -; A=28-237. DR PDB; 2KZ1; NMR; -; B=28-237. DR PDB; 2LAG; NMR; -; B=28-237. DR PDB; 3S8W; X-ray; 2.60 A; A/B/C=131-232. DR PDB; 3S9D; X-ray; 2.00 A; B/D=37-232. DR PDB; 3SE3; X-ray; 4.00 A; C=34-232. DR PDB; 3SE4; X-ray; 3.50 A; C=34-232. DR PDBsum; 1N6U; -. DR PDBsum; 1N6V; -. DR PDBsum; 2HYM; -. DR PDBsum; 2KZ1; -. DR PDBsum; 2LAG; -. DR PDBsum; 3S8W; -. DR PDBsum; 3S9D; -. DR PDBsum; 3SE3; -. DR PDBsum; 3SE4; -. DR AlphaFoldDB; P48551; -. DR BMRB; P48551; -. DR SMR; P48551; -. DR BioGRID; 109677; 30. DR ComplexPortal; CPX-5995; Interferon alpha receptor-ligand complex, IFNA2 variant. DR ComplexPortal; CPX-5996; Interferon alpha receptor-ligand complex, IFNA1 variant. DR ComplexPortal; CPX-5997; Interferon alpha receptor-ligand complex, IFNA7 variant. DR ComplexPortal; CPX-5998; Interferon alpha receptor-ligand complex, IFNA4 variant. DR ComplexPortal; CPX-5999; Interferon alpha receptor-ligand complex, IFNA5 variant. DR ComplexPortal; CPX-6000; Interferon alpha receptor-ligand complex, IFNA6 variant. DR ComplexPortal; CPX-6001; Interferon alpha receptor-ligand complex, IFNA8 variant. DR ComplexPortal; CPX-6002; Interferon alpha receptor-ligand complex, IFNA10 variant. DR ComplexPortal; CPX-6003; Interferon alpha receptor-ligand complex, IFNA14 variant. DR ComplexPortal; CPX-6004; Interferon alpha receptor-ligand complex, IFNA16 variant. DR ComplexPortal; CPX-6005; Interferon alpha receptor-ligand complex, IFNA17 variant. DR ComplexPortal; CPX-6006; Interferon alpha receptor-ligand complex, IFNA21 variant. DR ComplexPortal; CPX-6007; Interferon beta receptor-ligand complex. DR ComplexPortal; CPX-6008; Interferon epsilon receptor-ligand complex. DR ComplexPortal; CPX-6009; Interferon kappa receptor-ligand complex. DR ComplexPortal; CPX-6010; Interferon omega receptor-ligand complex. DR CORUM; P48551; -. DR DIP; DIP-945N; -. DR IntAct; P48551; 16. DR MINT; P48551; -. DR STRING; 9606.ENSP00000343957; -. DR ChEMBL; CHEMBL2364170; -. DR DrugBank; DB05472; Human interferon omega-1. DR DrugBank; DB00034; Interferon alfa-2a. DR DrugBank; DB00105; Interferon alfa-2b. DR DrugBank; DB00011; Interferon alfa-n1. DR DrugBank; DB00018; Interferon alfa-n3. DR DrugBank; DB00069; Interferon alfacon-1. DR DrugBank; DB00060; Interferon beta-1a. DR DrugBank; DB00068; Interferon beta-1b. DR DrugBank; DB06152; Nylidrin. DR DrugBank; DB00008; Peginterferon alfa-2a. DR DrugBank; DB00022; Peginterferon alfa-2b. DR DrugBank; DB15119; Ropeginterferon alfa-2b. DR DrugCentral; P48551; -. DR GlyConnect; 2051; 4 N-Linked glycans (1 site). DR GlyCosmos; P48551; 5 sites, 8 glycans. DR GlyGen; P48551; 6 sites, 8 N-linked glycans (1 site). DR iPTMnet; P48551; -. DR PhosphoSitePlus; P48551; -. DR BioMuta; IFNAR2; -. DR DMDM; 1352466; -. DR jPOST; P48551; -. DR MassIVE; P48551; -. DR PaxDb; 9606-ENSP00000343957; -. DR PeptideAtlas; P48551; -. DR ProteomicsDB; 55905; -. [P48551-1] DR ProteomicsDB; 55906; -. [P48551-2] DR ProteomicsDB; 55907; -. [P48551-3] DR Antibodypedia; 34938; 461 antibodies from 36 providers. DR DNASU; 3455; -. DR Ensembl; ENST00000342101.7; ENSP00000343289.3; ENSG00000159110.22. [P48551-3] DR Ensembl; ENST00000342136.9; ENSP00000343957.5; ENSG00000159110.22. [P48551-1] DR Ensembl; ENST00000382264.7; ENSP00000371699.3; ENSG00000159110.22. [P48551-2] DR Ensembl; ENST00000404220.7; ENSP00000384309.2; ENSG00000159110.22. [P48551-2] DR Ensembl; ENST00000683941.1; ENSP00000508013.1; ENSG00000159110.22. [P48551-1] DR GeneID; 3455; -. DR KEGG; hsa:3455; -. DR MANE-Select; ENST00000342136.9; ENSP00000343957.5; NM_001289125.3; NP_001276054.1. DR UCSC; uc002yrb.5; human. [P48551-1] DR AGR; HGNC:5433; -. DR CTD; 3455; -. DR DisGeNET; 3455; -. DR GeneCards; IFNAR2; -. DR HGNC; HGNC:5433; IFNAR2. DR HPA; ENSG00000159110; Low tissue specificity. DR MalaCards; IFNAR2; -. DR MIM; 602376; gene. DR MIM; 610424; phenotype. DR MIM; 616669; phenotype. DR neXtProt; NX_P48551; -. DR OpenTargets; ENSG00000159110; -. DR Orphanet; 431166; Primary immunodeficiency with post-measles-mumps-rubella vaccine viral infection. DR PharmGKB; PA29671; -. DR VEuPathDB; HostDB:ENSG00000159110; -. DR eggNOG; ENOG502S60E; Eukaryota. DR GeneTree; ENSGT00510000049322; -. DR HOGENOM; CLU_072607_0_0_1; -. DR InParanoid; P48551; -. DR OMA; PSAECPW; -. DR OrthoDB; 4258084at2759; -. DR PhylomeDB; P48551; -. DR TreeFam; TF335897; -. DR PathwayCommons; P48551; -. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. [P48551-2] DR Reactome; R-HSA-912694; Regulation of IFNA/IFNB signaling. [P48551-2] DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. [P48551-2] DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. [P48551-2] DR Reactome; R-HSA-9833109; Evasion by RSV of host interferon responses. [P48551-2] DR SignaLink; P48551; -. DR SIGNOR; P48551; -. DR BioGRID-ORCS; 3455; 23 hits in 1179 CRISPR screens. DR ChiTaRS; IFNAR2; human. DR EvolutionaryTrace; P48551; -. DR GeneWiki; IFNAR2; -. DR GenomeRNAi; 3455; -. DR Pharos; P48551; Tclin. DR PRO; PR:P48551; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P48551; Protein. DR Bgee; ENSG00000159110; Expressed in blood and 196 other cell types or tissues. DR ExpressionAtlas; P48551; baseline and differential. DR GO; GO:0005576; C:extracellular region; TAS:ProtInc. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0019955; F:cytokine binding; IPI:UniProtKB. DR GO; GO:0042018; F:interleukin-22 receptor activity; IBA:GO_Central. DR GO; GO:0008269; F:JAK pathway signal transduction adaptor activity; TAS:UniProt. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0019962; F:type I interferon binding; IPI:UniProtKB. DR GO; GO:0004905; F:type I interferon receptor activity; IDA:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0007259; P:cell surface receptor signaling pathway via JAK-STAT; IDA:UniProtKB. DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:UniProt. DR GO; GO:0098586; P:cellular response to virus; NAS:ComplexPortal. DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB. DR GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB. DR GO; GO:0035456; P:response to interferon-beta; IDA:UniProtKB. DR GO; GO:0009615; P:response to virus; TAS:ProtInc. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IDA:UniProtKB. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR015373; Interferon/interleukin_rcp_dom. DR InterPro; IPR050650; Type-II_Cytokine-TF_Rcpt. DR PANTHER; PTHR20859:SF84; INTERFERON ALPHA_BETA RECEPTOR 2; 1. DR PANTHER; PTHR20859; INTERFERON/INTERLEUKIN RECEPTOR; 1. DR Pfam; PF09294; Interfer-bind; 1. DR Pfam; PF01108; Tissue_fac; 1. DR SUPFAM; SSF49265; Fibronectin type III; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Secreted; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..26 FT CHAIN 27..515 FT /note="Interferon alpha/beta receptor 2" FT /id="PRO_0000011006" FT TOPO_DOM 27..243 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 244..264 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 265..515 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 318..418 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 418..444 FT /note="Mediates interaction with STAT2 (and required for FT the recruitment of USP18)" FT /evidence="ECO:0000269|PubMed:28165510" FT REGION 455..515 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 466..497 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 337 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 467 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35664" FT MOD_RES 512 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT CARBOHYD 58 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 87 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8181059" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 188 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 192 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:8181059" FT DISULFID 39..122 FT /evidence="ECO:0000269|PubMed:17001036, FT ECO:0000269|PubMed:20496919, ECO:0000269|PubMed:21819146, FT ECO:0000269|PubMed:21854986, ECO:0007744|PDB:1N6U, FT ECO:0007744|PDB:1N6V, ECO:0007744|PDB:2HYM, FT ECO:0007744|PDB:2KZ1, ECO:0007744|PDB:2LAG, FT ECO:0007744|PDB:3S9D, ECO:0007744|PDB:3SE3, FT ECO:0007744|PDB:3SE4" FT DISULFID 85..93 FT /evidence="ECO:0000269|PubMed:17001036, FT ECO:0000269|PubMed:20496919, ECO:0000269|PubMed:21819146, FT ECO:0000269|PubMed:21854986, ECO:0007744|PDB:1N6U, FT ECO:0007744|PDB:1N6V, ECO:0007744|PDB:2HYM, FT ECO:0007744|PDB:2KZ1, ECO:0007744|PDB:2LAG, FT ECO:0007744|PDB:3S9D, ECO:0007744|PDB:3SE3, FT ECO:0007744|PDB:3SE4" FT DISULFID 207..227 FT /evidence="ECO:0000269|PubMed:17001036, FT ECO:0000269|PubMed:20496919, ECO:0000269|PubMed:21819146, FT ECO:0000269|PubMed:21854986, ECO:0007744|PDB:1N6U, FT ECO:0007744|PDB:1N6V, ECO:0007744|PDB:2HYM, FT ECO:0007744|PDB:2KZ1, ECO:0007744|PDB:2LAG, FT ECO:0007744|PDB:3S8W, ECO:0007744|PDB:3S9D, FT ECO:0007744|PDB:3SE3, ECO:0007744|PDB:3SE4" FT VAR_SEQ 238..239 FT /note="SA -> FS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7588638, FT ECO:0000303|PubMed:7759950" FT /id="VSP_001736" FT VAR_SEQ 240..515 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7588638, FT ECO:0000303|PubMed:7759950" FT /id="VSP_001737" FT VAR_SEQ 281..331 FT /note="NFHNFLAWPFPNLPPLEAMDMVEVIYINRKKKVWDYNYDDESDSDTEAAPR FT -> RQGLAKGWNAVAIHRCSHNALQSETPELKQSSCLSFPSSWDYKRASLCPSD (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:7588638, FT ECO:0000303|PubMed:8181059, ECO:0000303|Ref.8" FT /id="VSP_001738" FT VAR_SEQ 332..515 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7588638, FT ECO:0000303|PubMed:8181059, ECO:0000303|Ref.8" FT /id="VSP_001739" FT VARIANT 8 FT /note="F -> S (risk factor for HVB infection; lower cell FT surface levels; lower induction of MHC class 1 expression FT by INF-alpha; dbSNP:rs2229207)" FT /evidence="ECO:0000269|PubMed:16757563, ECO:0000269|Ref.6" FT /id="VAR_020521" FT VARIANT 10 FT /note="F -> V (in dbSNP:rs1051393)" FT /evidence="ECO:0000269|PubMed:16757563, FT ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059, FT ECO:0000269|Ref.5, ECO:0000269|Ref.6" FT /id="VAR_020522" FT VARIANT 37 FT /note="E -> Q (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs201003373)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084099" FT VARIANT 73 FT /note="M -> V (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs142850110)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084100" FT VARIANT 138 FT /note="E -> V (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084101" FT VARIANT 196 FT /note="I -> V (in dbSNP:rs17860223)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_020523" FT VARIANT 215 FT /note="S -> G (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs747605798)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084102" FT VARIANT 283 FT /note="H -> R (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs763508005)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084103" FT VARIANT 295 FT /note="P -> L (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs759744926)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084104" FT VARIANT 318 FT /note="Y -> C (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs756571542)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084105" FT VARIANT 324 FT /note="S -> N (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs201411274)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084106" FT VARIANT 346 FT /note="P -> S (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs148519830)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084107" FT VARIANT 362 FT /note="P -> S (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs1441207963)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084108" FT VARIANT 385 FT /note="P -> L (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs1231284605)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084109" FT VARIANT 450 FT /note="S -> L (no effect on activation of STAT1 upon IFNA2 FT or IFNG binding; dbSNP:rs866733383)" FT /evidence="ECO:0000269|PubMed:32972995" FT /id="VAR_084110" FT MUTAGEN 269 FT /note="Y->F: Does not inhibit STAT1, STAT2 and STAT3 FT activation by IFN. Inhibits STAT1, STAT2 and STAT3 FT activation by IFN; when associated with F-306; F-316; F- FT 318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-306; F-316; FT F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-306; F-316; FT F-318 and F-337." FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT MUTAGEN 306 FT /note="Y->F: Does not inhibit STAT1, STAT2 and STAT3 FT activation by IFN. Inhibits STAT1, STAT2 and STAT3 FT activation by IFN; when associated with F-269; F-316; F- FT 318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-269; F-316; FT F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-512. Does FT not inhibit STAT1, STAT2 and STAT3 activation by IFN; when FT associated with F-269; F-316; F-318 and F-337." FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT MUTAGEN 316 FT /note="Y->F: Does not inhibit STAT1, STAT2 and STAT3 FT activation by IFN. Inhibits STAT1, STAT2 and STAT3 FT activation by IFN; when associated with F-269; F-306; F- FT 318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-269; F-306; FT F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-512. Does FT not inhibit STAT1, STAT2 and STAT3 activation by IFN; when FT associated with F-269; F-306; F-318 and F-337." FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT MUTAGEN 318 FT /note="Y->F: Does not inhibit STAT1, STAT2 and STAT3 FT activation by IFN. Inhibits STAT1, STAT2 and STAT3 FT activation by IFN; when associated with F-269; F-306; F- FT 316; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-269; F-306; FT F-316; F-411 and F-512. Does not inhibit STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-512. Does FT not inhibit STAT1, STAT2 and STAT3 activation by IFN; when FT associated with F-269; F-306; F-316 and F-337." FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT MUTAGEN 337 FT /note="Y->F: Does not inhibit STAT1, STAT2 and STAT3 FT activation by IFN. Inhibits STAT1, STAT2 and STAT3 FT activation by IFN; when associated with F-269; F-306; F- FT 316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 FT and STAT3 activation by IFN; when associated with F-512. FT Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; FT when associated with F-269; F-306; F-316 and F-318." FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT MUTAGEN 411 FT /note="Y->F: Does not inhibit STAT1, STAT2 and STAT3 FT activation by IFN. Inhibits STAT1, STAT2 and STAT3 FT activation by IFN; when associated with F-269; F-306; F- FT 316; F-318; F-337 and F-512. Inhibits STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-269; F-306; FT F-316; F-318 and F-512. Does not inhibit STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-512." FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT MUTAGEN 512 FT /note="Y->F: Does not inhibit STAT1, STAT2 and STAT3 FT activation by IFN. Inhibits STAT1, STAT2 and STAT3 FT activation by IFN; when associated with F-269; F-306; F- FT 316; F-318; F-337 and F-411. Inhibits STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-269; F-306; FT F-316; F-318 and F-411. Does not inhibit STAT1, STAT2 and FT STAT3 activation by IFN; when associated with F-411." FT /evidence="ECO:0000269|PubMed:11682488, FT ECO:0000269|PubMed:12105218" FT CONFLICT 151 FT /note="M -> V (in Ref. 3; AAC50202)" FT /evidence="ECO:0000305" FT STRAND 40..46 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:1N6U" FT STRAND 65..75 FT /evidence="ECO:0007829|PDB:3S9D" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:3S9D" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 119..126 FT /evidence="ECO:0007829|PDB:3S9D" FT HELIX 128..131 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:3S9D" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1N6U" FT STRAND 167..174 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:3S8W" FT STRAND 191..197 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 205..213 FT /evidence="ECO:0007829|PDB:3S9D" FT STRAND 226..229 FT /evidence="ECO:0007829|PDB:3S9D" SQ SEQUENCE 515 AA; 57759 MW; 4D7730D93AA739F4 CRC64; MLLSQNAFIF RSLNLVLMVY ISLVFGISYD SPDYTDESCT FKISLRNFRS ILSWELKNHS IVPTHYTLLY TIMSKPEDLK VVKNCANTTR SFCDLTDEWR STHEAYVTVL EGFSGNTTLF SCSHNFWLAI DMSFEPPEFE IVGFTNHINV MVKFPSIVEE ELQFDLSLVI EEQSEGIVKK HKPEIKGNMS GNFTYIIDKL IPNTNYCVSV YLEHSDEQAV IKSPLKCTLL PPGQESESAE SAKIGGIITV FLIALVLTST IVTLKWIGYI CLRNSLPKVL NFHNFLAWPF PNLPPLEAMD MVEVIYINRK KKVWDYNYDD ESDSDTEAAP RTSGGGYTMH GLTVRPLGQA SATSTESQLI DPESEEEPDL PEVDVELPTM PKDSPQQLEL LSGPCERRKS PLQDPFPEED YSSTEGSGGR ITFNVDLNSV FLRVLDDEDS DDLEAPLMLS SHLEEMVDPE DPDNVQSNHL LASGEGTQPT FPSPSSEGLW SEDAPSDQSD TSESDVDLGD GYIMR //