IFNB_HUMAN
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 03-AUG-2022, entry version 222.
DE RecName: Full=Interferon beta;
DE Short=IFN-beta;
DE AltName: Full=Fibroblast interferon;
DE Flags: Precursor;
GN Name=IFNB1; 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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [5]
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 [6]
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 [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 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 [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-187, VARIANT TYR-162, AND CHARACTERIZATION
RP 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
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 [16]
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: Has antiviral, antibacterial and anticancer activities.
CC -!- SUBUNIT: Monomer. Signals mostly via binding to a IFNAR1-IFNAR2
CC heterodimeric receptor, but can also function with IFNAR1 alone and
CC independently of Jak-STAT pathways.
CC -!- INTERACTION:
CC P01574; P40855: PEX19; NbExp=3; IntAct=EBI-12383562, EBI-594747;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PHARMACEUTICAL: Available under the names Avonex (Biogen), Betaseron
CC (Berlex) and Rebif (Serono). Used in the treatment of multiple
CC sclerosis (MS). Betaseron is a slightly modified form of IFNB1 with two
CC residue substitutions.
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";
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DR EMBL; V00534; CAA23795.1; -; Genomic_DNA.
DR EMBL; V00535; CAA23796.1; -; Genomic_DNA.
DR EMBL; V00546; CAA23807.1; -; mRNA.
DR EMBL; V00547; CAA23808.1; -; mRNA.
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; 26.
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 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; P01574; -.
DR PeptideAtlas; P01574; -.
DR PRIDE; P01574; -.
DR ProteomicsDB; 51388; -.
DR TopDownProteomics; P01574; -.
DR Antibodypedia; 3995; 1010 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 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; 1358010at2759; -.
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; 8 hits in 1063 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 bone element and 7 other tissues.
DR Genevisible; P01574; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IMP:AgBase.
DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
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:BHF-UCL.
DR GO; GO:0098586; P:cellular response to virus; IEP:ARUK-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; TAS:BHF-UCL.
DR GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
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: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:2001235; P:positive regulation of apoptotic signaling pathway; IDA: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: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 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 InterPro; IPR015588; Interferon_beta.
DR PANTHER; PTHR11691; PTHR11691; 1.
DR PANTHER; PTHR11691:SF68; PTHR11691:SF68; 1.
DR Pfam; PF00143; Interferon; 1.
DR PRINTS; PR00266; INTERFERONAB.
DR SMART; SM00076; IFabd; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00252; INTERFERON_A_B_D; 1.
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 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 DISULFID 52..162
FT /evidence="ECO:0000269|PubMed:6162107"
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
