ID IFNB_HUMAN Reviewed; 187 AA. AC P01574; Q5VWC9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 231. DE RecName: Full=Interferon beta {ECO:0000303|PubMed:16593086}; DE Short=IFN-beta {ECO:0000303|PubMed:16593086}; DE AltName: Full=Fibroblast interferon {ECO:0000303|PubMed:6157601}; DE Flags: Precursor; GN Name=IFNB1 {ECO:0000312|HGNC:HGNC:5434}; Synonyms=IFB, IFNB; 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]. RX PubMed=6157601; DOI=10.1016/0378-1119(80)90138-9; RA Taniguchi T., Ohno S., Fujii-Kuriyama Y., Muramatsu M.; RT "The nucleotide sequence of human fibroblast interferon cDNA."; RL Gene 10:11-15(1980). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=6157094; DOI=10.1038/285542a0; RA Derynck R., Content J., Declercq E., Volckaert G., Tavernier J., Devos R., RA Fiers W.; RT "Isolation and structure of a human fibroblast interferon gene."; RL Nature 285:542-547(1980). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6159584; DOI=10.1093/nar/8.18.4057; RA Goeddel D.V., Shepard H.M., Yelverton E., Leung D., Crea R., Sloma A., RA Pestka S.; RT "Synthesis of human fibroblast interferon by E. coli."; RL Nucleic Acids Res. 8:4057-4074(1980). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6164984; DOI=10.1093/nar/9.5.1045; RA Lawn R.M., Adelman J., Franke A.E., Houck C.M., Gross M., Najarian R., RA Goeddel D.V.; RT "Human fibroblast interferon gene lacks introns."; RL Nucleic Acids Res. 9:1045-1052(1981). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16593086; DOI=10.1073/pnas.78.9.5305; RA Ohno S., Taniguchi T.; RT "Structure of a chromosomal gene for human interferon beta."; RL Proc. Natl. Acad. Sci. U.S.A. 78:5305-5309(1981). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6159580; DOI=10.1093/nar/8.13.2885; RA Houghton M., Eaton M.A.W., Stewart A.G., Smith J.C., Doel S.M., RA Cartlin G.H., Lewis H.M., Patel T.P., Emtage J.S., Carey N.H., Porter A.G.; RT "The complete amino acid sequence of human fibroblast interferon as deduced RT using synthetic oligodeoxyribonucleotide primers of reverse RT transcriptase."; RL Nucleic Acids Res. 8:2885-2894(1980). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2414376; DOI=10.1089/jir.1985.5.521; RA May L.T., Sehgal P.B.; RT "On the relationship between human interferon alpha 1 and beta 1 genes."; RL J. Interferon Res. 5:521-526(1985). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., RA Nickerson D.A.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-68. RX PubMed=6159597; DOI=10.1093/nar/8.9.1913; RA Houghton M., Stewart A.G., Doel S.M., Emtage J.S., Eaton M.A.W., RA Smith J.C., Patel T.P., Lewis H.M., Porter A.G., Birch J.R., Cartwright T., RA Carey N.H.; RT "The amino-terminal sequence of human fibroblast interferon as deduced from RT reverse transcripts obtained using synthetic oligonucleotide primers."; RL Nucleic Acids Res. 8:1913-1931(1980). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-187, FUNCTION, VARIANT TYR-162, AND RP CHARACTERIZATION OF VARIANT TYR-162. RX PubMed=6171735; DOI=10.1038/294563a0; RA Shepard H.M., Leung D., Stebbing N., Goeddel D.V.; RT "A single amino acid change in IFN-beta1 abolishes its antiviral RT activity."; RL Nature 294:563-565(1981). RN [14] RP DISULFIDE BOND. RX PubMed=6162107; DOI=10.1038/289606a0; RA Wetzel R.; RT "Assignment of the disulphide bonds of leukocyte interferon."; RL Nature 289:606-607(1981). RN [15] RP PHARMACEUTICAL. RX PubMed=8469318; DOI=10.1212/wnl.43.4.655; RG The IFNB Multiple Sclerosis Study Group; RT "Interferon beta-1b is effective in relapsing-remitting multiple sclerosis. RT I. Clinical results of a multicenter, randomized, double-blind, placebo- RT controlled trial."; RL Neurology 43:655-661(1993). RN [16] RP PHARMACEUTICAL. RX PubMed=8469319; DOI=10.1212/wnl.43.4.662; RA Paty D.W., Li D.K.; RT "Interferon beta-1b is effective in relapsing-remitting multiple sclerosis. RT II. MRI analysis results of a multicenter, randomized, double-blind, RT placebo-controlled trial. UBC MS/MRI Study Group and the IFNB Multiple RT Sclerosis Study Group."; RL Neurology 43:662-667(1993). RN [17] RP FUNCTION. RX PubMed=7813427; DOI=10.1002/j.1460-2075.1994.tb06932.x; RA Abramovich C., Shulman L.M., Ratovitski E., Harroch S., Tovey M., Eid P., RA Revel M.; RT "Differential tyrosine phosphorylation of the IFNAR chain of the type I RT interferon receptor and of an associated surface protein in response to RT IFN-alpha and IFN-beta."; RL EMBO J. 13:5871-5877(1994). RN [18] RP FUNCTION. RX PubMed=8027027; DOI=10.1016/s0021-9258(17)32371-2; RA Platanias L.C., Uddin S., Colamonici O.R.; RT "Tyrosine phosphorylation of the alpha and beta subunits of the type I RT interferon receptor. Interferon-beta selectively induces tyrosine RT phosphorylation of an alpha subunit-associated protein."; RL J. Biol. Chem. 269:17761-17764(1994). RN [19] RP FUNCTION. 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 [20] 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 [21] 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 [22] RP PHARMACEUTICAL. RX PubMed=9345408; DOI=10.1177/135245859600100605; RA Goodkin D.E.; RT "Interferon beta treatment for multiple sclerosis: persisting questions."; RL Mult. Scler. 1:321-324(1996). RN [23] RP 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 [24] 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 [25] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, DISULFIDE BOND, AND RP GLYCOSYLATION AT ASN-101. RX PubMed=9342320; DOI=10.1073/pnas.94.22.11813; RA Karpusas M., Nolte M., Benton C.B., Meier W., Lipscomb W.N., Goelz S.; RT "The crystal structure of human interferon beta at 2.2-A resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 94:11813-11818(1997). RN [26] RP VARIANT [LARGE SCALE ANALYSIS] CYS-164. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Type I interferon cytokine that plays a key role in the CC innate immune response to infection, developing tumors and other CC inflammatory stimuli (PubMed:6157094, PubMed:6171735, PubMed:8027027, CC PubMed:7665574, PubMed:8969169, PubMed:10049744, PubMed:10556041). CC Signals via binding to high-affinity (IFNAR2) and low-affinity (IFNAR1) CC heterodimeric receptor, activating the canonical Jak-STAT signaling CC pathway resulting in transcriptional activation or repression of CC interferon-regulated genes that encode the effectors of the interferon CC response, such as antiviral proteins, regulators of cell proliferation CC and differentiation, and immunoregulatory proteins (PubMed:8027027, CC PubMed:7665574, PubMed:8969169, PubMed:10049744, PubMed:10556041). CC Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, CC but can also function with IFNAR1 alone and independently of Jak-STAT CC pathways (By similarity). Elicits a wide variety of responses, CC including antiviral and antibacterial activities, and can regulate the CC development of B-cells, myelopoiesis and lipopolysaccharide (LPS)- CC inducible production of tumor necrosis factor (By similarity). Plays a CC role in neuronal homeostasis by regulating dopamine turnover and CC protecting dopaminergic neurons: acts by promoting neuronal autophagy CC and alpha-synuclein clearance, thereby preventing dopaminergic neuron CC loss (By similarity). IFNB1 is more potent than interferon-alpha (IFN- CC alpha) in inducing the apoptotic and antiproliferative pathways CC required for control of tumor cell growth (By similarity). CC {ECO:0000250|UniProtKB:P01575, ECO:0000269|PubMed:10049744, CC ECO:0000269|PubMed:10556041, ECO:0000269|PubMed:6157094, CC ECO:0000269|PubMed:6171735, ECO:0000269|PubMed:7665574, CC ECO:0000269|PubMed:8027027, ECO:0000269|PubMed:8969169}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9342320}. CC -!- INTERACTION: CC P01574; P40855: PEX19; NbExp=3; IntAct=EBI-12383562, EBI-594747; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6157094}. CC -!- PHARMACEUTICAL: Alleviates the exacerbations of multiple sclerosis (MS) CC (PubMed:8469318, PubMed:8469319). Available under the names Avonex CC (Biogen), Betaseron (Berlex) and Rebif (Serono) (PubMed:9345408). CC Betaseron is a slightly modified form of IFNB1 with two residue CC substitutions (PubMed:9345408). {ECO:0000269|PubMed:8469318, CC ECO:0000269|PubMed:8469319, ECO:0000303|PubMed:9345408}. CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Avonex; Note=Clinical information on Avonex; CC URL="https://www.avonex.com"; CC -!- WEB RESOURCE: Name=Betaseron; Note=Clinical information on Betaseron; CC URL="https://www.betaseron.com"; 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; V00546; CAA23807.1; -; mRNA. DR EMBL; V00547; CAA23808.1; -; mRNA. DR EMBL; V00534; CAA23795.1; -; Genomic_DNA. DR EMBL; V00535; CAA23796.1; -; Genomic_DNA. DR EMBL; M28622; AAA36040.1; -; mRNA. DR EMBL; EF064725; ABK41908.1; -; Genomic_DNA. DR EMBL; AB451323; BAG70137.1; -; mRNA. DR EMBL; AB451452; BAG70266.1; -; mRNA. DR EMBL; CH471071; EAW58625.1; -; Genomic_DNA. DR EMBL; BC069314; AAH69314.1; -; mRNA. DR EMBL; BC096150; AAH96150.1; -; mRNA. DR EMBL; BC096151; AAH96151.1; -; mRNA. DR EMBL; BC096152; AAH96152.1; -; mRNA. DR EMBL; BC096153; AAH96153.1; -; mRNA. DR CCDS; CCDS6495.1; -. DR PIR; A93721; IVHUB1. DR RefSeq; NP_002167.1; NM_002176.3. DR PDB; 1AU1; X-ray; 2.20 A; A/B=22-187. DR PDBsum; 1AU1; -. DR AlphaFoldDB; P01574; -. DR SMR; P01574; -. DR BioGRID; 109678; 31. DR ComplexPortal; CPX-6007; Interferon beta receptor-ligand complex. DR CORUM; P01574; -. DR DIP; DIP-6018N; -. DR IntAct; P01574; 4. DR STRING; 9606.ENSP00000369581; -. DR ChEMBL; CHEMBL4630876; -. DR DrugBank; DB02379; Beta-D-Glucose. DR Allergome; 9875; Hom s IFN beta. DR GlyConnect; 291; 1 N-Linked glycan. DR GlyCosmos; P01574; 1 site, 2 glycans. DR GlyGen; P01574; 2 sites, 2 N-linked glycans (2 sites). DR iPTMnet; P01574; -. DR PhosphoSitePlus; P01574; -. DR BioMuta; IFNB1; -. DR DMDM; 124469; -. DR MassIVE; P01574; -. DR PaxDb; 9606-ENSP00000369581; -. DR PeptideAtlas; P01574; -. DR ProteomicsDB; 51388; -. DR TopDownProteomics; P01574; -. DR Antibodypedia; 3995; 1132 antibodies from 43 providers. DR DNASU; 3456; -. DR Ensembl; ENST00000380232.4; ENSP00000369581.2; ENSG00000171855.7. DR GeneID; 3456; -. DR KEGG; hsa:3456; -. DR MANE-Select; ENST00000380232.4; ENSP00000369581.2; NM_002176.4; NP_002167.1. DR UCSC; uc003zok.4; human. DR AGR; HGNC:5434; -. DR CTD; 3456; -. DR DisGeNET; 3456; -. DR GeneCards; IFNB1; -. DR HGNC; HGNC:5434; IFNB1. DR HPA; ENSG00000171855; Not detected. DR MIM; 147640; gene. DR neXtProt; NX_P01574; -. DR OpenTargets; ENSG00000171855; -. DR PharmGKB; PA29672; -. DR VEuPathDB; HostDB:ENSG00000171855; -. DR eggNOG; ENOG502SQGR; Eukaryota. DR GeneTree; ENSGT01000000214430; -. DR HOGENOM; CLU_109427_1_0_1; -. DR InParanoid; P01574; -. DR OMA; HWQKEHL; -. DR OrthoDB; 5358931at2759; -. DR PhylomeDB; P01574; -. DR TreeFam; TF336177; -. DR PathwayCommons; P01574; -. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR Reactome; R-HSA-912694; Regulation of IFNA/IFNB signaling. DR Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway. DR Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P01574; -. DR SIGNOR; P01574; -. DR BioGRID-ORCS; 3456; 9 hits in 1137 CRISPR screens. DR EvolutionaryTrace; P01574; -. DR GeneWiki; IFNB1; -. DR GenomeRNAi; 3456; -. DR Pharos; P01574; Tbio. DR PRO; PR:P01574; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P01574; Protein. DR Bgee; ENSG00000171855; Expressed in primordial germ cell in gonad and 8 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProt. DR GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IMP:AgBase. DR GO; GO:0005125; F:cytokine activity; IDA:UniProtKB. DR GO; GO:0005126; F:cytokine receptor binding; IDA:UniProtKB. DR GO; GO:0005132; F:type I interferon receptor binding; IBA:GO_Central. DR GO; GO:0002250; P:adaptive immune response; IBA:GO_Central. DR GO; GO:0002312; P:B cell activation involved in immune response; IMP:UniProtKB. DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central. DR GO; GO:0042100; P:B cell proliferation; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0071360; P:cellular response to exogenous dsRNA; TAS:BHF-UCL. DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:UniProtKB. DR GO; GO:0098586; P:cellular response to virus; IEP:ARUK-UCL. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProt. DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB. DR GO; GO:0006959; P:humoral immune response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IDA:UniProt. DR GO; GO:0030101; P:natural killer cell activation; NAS:UniProtKB. DR GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central. DR GO; GO:0140123; P:negative regulation of Lewy body formation; ISS:UniProtKB. DR GO; GO:0045581; P:negative regulation of T cell differentiation; IDA:UniProtKB. DR GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IDA:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL. DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB. DR GO; GO:0045089; P:positive regulation of innate immune response; NAS:UniProtKB. DR GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:UniProtKB. DR GO; GO:0045343; P:regulation of MHC class I biosynthetic process; NAS:UniProtKB. DR GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI. DR GO; GO:0009615; P:response to virus; NAS:UniProtKB. DR GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IDA:BHF-UCL. DR CDD; cd00095; IFab; 1. DR Gene3D; 1.20.1250.10; -; 1. DR InterPro; IPR009079; 4_helix_cytokine-like_core. DR InterPro; IPR000471; Interferon_alpha/beta/delta. DR PANTHER; PTHR11691:SF72; INTERFERON BETA; 1. DR PANTHER; PTHR11691; TYPE I INTERFERON; 1. DR Pfam; PF00143; Interferon; 1. DR PRINTS; PR00266; INTERFERONAB. DR SMART; SM00076; IFabd; 1. DR SUPFAM; SSF47266; 4-helical cytokines; 1. DR PROSITE; PS00252; INTERFERON_A_B_D; 1. DR Genevisible; P01574; HS. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; Cytokine; Disulfide bond; Glycoprotein; KW Pharmaceutical; Phosphoprotein; Reference proteome; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..187 FT /note="Interferon beta" FT /id="PRO_0000016400" FT MOD_RES 24 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P70499" FT CARBOHYD 101 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:9342320" FT DISULFID 52..162 FT /evidence="ECO:0000269|PubMed:6162107, FT ECO:0000269|PubMed:9342320" FT VARIANT 162 FT /note="C -> Y (variant found in a clone obtained from a FT fibroblast cell line; does not form the essential disulfide FT bond; results in loss of antiviral activity)" FT /evidence="ECO:0000269|PubMed:6171735" FT /id="VAR_004016" FT VARIANT 164 FT /note="W -> C (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036330" FT HELIX 24..42 FT /evidence="ECO:0007829|PDB:1AU1" FT HELIX 51..55 FT /evidence="ECO:0007829|PDB:1AU1" FT HELIX 63..67 FT /evidence="ECO:0007829|PDB:1AU1" FT HELIX 73..91 FT /evidence="ECO:0007829|PDB:1AU1" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:1AU1" FT HELIX 102..127 FT /evidence="ECO:0007829|PDB:1AU1" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:1AU1" FT HELIX 140..156 FT /evidence="ECO:0007829|PDB:1AU1" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:1AU1" FT HELIX 161..182 FT /evidence="ECO:0007829|PDB:1AU1" SQ SEQUENCE 187 AA; 22294 MW; 0B013D4087723CEC CRC64; MTNKCLLQIA LLLCFSTTAL SMSYNLLGFL QRSSNFQCQK LLWQLNGRLE YCLKDRMNFD IPEEIKQLQQ FQKEDAALTI YEMLQNIFAI FRQDSSSTGW NETIVENLLA NVYHQINHLK TVLEEKLEKE DFTRGKLMSS LHLKRYYGRI LHYLKAKEYS HCAWTIVRVE ILRNFYFINR LTGYLRN //