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Interferon beta (IFN-beta) (Fibroblast interferon)

 IFNB_HUMAN              Reviewed;         187 AA.
P01574; Q5VWC9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 194.
RecName: Full=Interferon beta;
Short=IFN-beta;
AltName: Full=Fibroblast interferon;
Flags: Precursor;
Name=IFNB1; Synonyms=IFB, IFNB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6164984; DOI=10.1093/nar/9.5.1045;
Lawn R.M., Adelman J., Franke A.E., Houck C.M., Gross M., Najarian R.,
Goeddel D.V.;
"Human fibroblast interferon gene lacks introns.";
Nucleic Acids Res. 9:1045-1052(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16593086; DOI=10.1073/pnas.78.9.5305;
Ohno S., Taniguchi T.;
"Structure of a chromosomal gene for human interferon beta.";
Proc. Natl. Acad. Sci. U.S.A. 78:5305-5309(1981).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6157601; DOI=10.1016/0378-1119(80)90138-9;
Taniguchi T., Ohno S., Fujii-Kuriyama Y., Muramatsu M.;
"The nucleotide sequence of human fibroblast interferon cDNA.";
Gene 10:11-15(1980).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6157094; DOI=10.1038/285542a0;
Derynck R., Content J., Declercq E., Volckaert G., Tavernier J.,
Devos R., Fiers W.;
"Isolation and structure of a human fibroblast interferon gene.";
Nature 285:542-547(1980).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6159580; DOI=10.1093/nar/8.13.2885;
Houghton M., Eaton M.A.W., Stewart A.G., Smith J.C., Doel S.M.,
Cartlin G.H., Lewis H.M., Patel T.P., Emtage J.S., Carey N.H.,
Porter A.G.;
"The complete amino acid sequence of human fibroblast interferon as
deduced using synthetic oligodeoxyribonucleotide primers of reverse
transcriptase.";
Nucleic Acids Res. 8:2885-2894(1980).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6159584; DOI=10.1093/nar/8.18.4057;
Goeddel D.V., Shepard H.M., Yelverton E., Leung D., Crea R., Sloma A.,
Pestka S.;
"Synthesis of human fibroblast interferon by E. coli.";
Nucleic Acids Res. 8:4057-4074(1980).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2414376; DOI=10.1089/jir.1985.5.521;
May L.T., Sehgal P.B.;
"On the relationship between human interferon alpha 1 and beta 1
genes.";
J. Interferon Res. 5:521-526(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-68.
PubMed=6159597; DOI=10.1093/nar/8.9.1913;
Houghton M., Stewart A.G., Doel S.M., Emtage J.S., Eaton M.A.W.,
Smith J.C., Patel T.P., Lewis H.M., Porter A.G., Birch J.R.,
Cartwright T., Carey N.H.;
"The amino-terminal sequence of human fibroblast interferon as deduced
from reverse transcripts obtained using synthetic oligonucleotide
primers.";
Nucleic Acids Res. 8:1913-1931(1980).
[13]
DISULFIDE BOND.
PubMed=6162107; DOI=10.1038/289606a0;
Wetzel R.;
"Assignment of the disulphide bonds of leukocyte interferon.";
Nature 289:606-607(1981).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 71-187, VARIANT TYR-162, AND
CHARACTERIZATION OF VARIANT TYR-162.
PubMed=6171735; DOI=10.1038/294563a0;
Shepard H.M., Leung D., Stebbing N., Goeddel D.V.;
"A single amino acid change in IFN-beta1 abolishes its antiviral
activity.";
Nature 294:563-565(1981).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=9342320; DOI=10.1073/pnas.94.22.11813;
Karpusas M., Nolte M., Benton C.B., Meier W., Lipscomb W.N., Goelz S.;
"The crystal structure of human interferon beta at 2.2-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 94:11813-11818(1997).
[16]
VARIANT [LARGE SCALE ANALYSIS] CYS-164.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Has antiviral, antibacterial and anticancer activities.
-!- SUBUNIT: Monomer. Signals mostly via binding to a IFNAR1-IFNAR2
heterodimeric receptor, but can also function with IFNAR1 alone
and independently of Jak-STAT pathways.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PHARMACEUTICAL: Available under the names Avonex (Biogen),
Betaseron (Berlex) and Rebif (Serono). Used in the treatment of
multiple sclerosis (MS). Betaseron is a slightly modified form of
IFNB1 with two residue substitutions.
-!- SIMILARITY: Belongs to the alpha/beta interferon family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Avonex; Note=Clinical information on Avonex;
URL="https://www.avonex.com";
-!- WEB RESOURCE: Name=Betaseron; Note=Clinical information on
Betaseron;
URL="https://www.betaseron.com";
-----------------------------------------------------------------------
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EMBL; V00534; CAA23795.1; -; Genomic_DNA.
EMBL; V00535; CAA23796.1; -; Genomic_DNA.
EMBL; V00546; CAA23807.1; -; mRNA.
EMBL; V00547; CAA23808.1; -; mRNA.
EMBL; M28622; AAA36040.1; -; mRNA.
EMBL; EF064725; ABK41908.1; -; Genomic_DNA.
EMBL; AB451323; BAG70137.1; -; mRNA.
EMBL; AB451452; BAG70266.1; -; mRNA.
EMBL; CH471071; EAW58625.1; -; Genomic_DNA.
EMBL; BC069314; AAH69314.1; -; mRNA.
EMBL; BC096150; AAH96150.1; -; mRNA.
EMBL; BC096151; AAH96151.1; -; mRNA.
EMBL; BC096152; AAH96152.1; -; mRNA.
EMBL; BC096153; AAH96153.1; -; mRNA.
CCDS; CCDS6495.1; -.
PIR; A93721; IVHUB1.
RefSeq; NP_002167.1; NM_002176.3.
UniGene; Hs.93177; -.
PDB; 1AU1; X-ray; 2.20 A; A/B=22-187.
PDBsum; 1AU1; -.
ProteinModelPortal; P01574; -.
SMR; P01574; -.
BioGrid; 109678; 2.
CORUM; P01574; -.
DIP; DIP-6018N; -.
IntAct; P01574; 1.
STRING; 9606.ENSP00000369581; -.
DrugBank; DB02379; Beta-D-Glucose.
Allergome; 9875; Hom s IFN beta.
iPTMnet; P01574; -.
PhosphoSitePlus; P01574; -.
UniCarbKB; P01574; -.
BioMuta; IFNB1; -.
DMDM; 124469; -.
PaxDb; P01574; -.
PeptideAtlas; P01574; -.
PRIDE; P01574; -.
TopDownProteomics; P01574; -.
Ensembl; ENST00000380232; ENSP00000369581; ENSG00000171855.
GeneID; 3456; -.
KEGG; hsa:3456; -.
UCSC; uc003zok.4; human.
CTD; 3456; -.
DisGeNET; 3456; -.
EuPathDB; HostDB:ENSG00000171855.6; -.
GeneCards; IFNB1; -.
HGNC; HGNC:5434; IFNB1.
HPA; CAB009386; -.
MIM; 147640; gene.
neXtProt; NX_P01574; -.
OpenTargets; ENSG00000171855; -.
PharmGKB; PA29672; -.
eggNOG; ENOG410J0RY; Eukaryota.
eggNOG; ENOG41113EJ; LUCA.
GeneTree; ENSGT00760000119150; -.
HOGENOM; HOG000230501; -.
HOVERGEN; HBG052086; -.
InParanoid; P01574; -.
KO; K05415; -.
OMA; SSTGWNE; -.
OrthoDB; EOG091G0V76; -.
PhylomeDB; P01574; -.
TreeFam; TF336177; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-912694; Regulation of IFNA signaling.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P01574; -.
SIGNOR; P01574; -.
EvolutionaryTrace; P01574; -.
GeneWiki; IFNB1; -.
GenomeRNAi; 3456; -.
PMAP-CutDB; P01574; -.
PRO; PR:P01574; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000171855; -.
CleanEx; HS_IFNB1; -.
Genevisible; P01574; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IMP:AgBase.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0005132; F:type I interferon receptor binding; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:Ensembl.
GO; GO:0002312; P:B cell activation involved in immune response; IMP:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
GO; GO:0042100; P:B cell proliferation; IBA:GO_Central.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071360; P:cellular response to exogenous dsRNA; TAS:BHF-UCL.
GO; GO:0035458; P:cellular response to interferon-beta; IDA:BHF-UCL.
GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; TAS:BHF-UCL.
GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
GO; GO:0030101; P:natural killer cell activation; NAS:UniProtKB.
GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central.
GO; GO:0045581; P:negative regulation of T cell differentiation; IDA:UniProtKB.
GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0045089; P:positive regulation of innate immune response; NAS:UniProtKB.
GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045343; P:regulation of MHC class I biosynthetic process; NAS:UniProtKB.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
GO; GO:0009615; P:response to virus; NAS:UniProtKB.
GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
GO; GO:0060337; P:type I interferon signaling pathway; IDA:BHF-UCL.
CDD; cd00095; IFab; 1.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000471; Interferon_alpha/beta/delta.
InterPro; IPR015588; Interferon_beta.
PANTHER; PTHR11691; PTHR11691; 1.
PANTHER; PTHR11691:SF43; PTHR11691:SF43; 1.
Pfam; PF00143; Interferon; 1.
PRINTS; PR00266; INTERFERONAB.
SMART; SM00076; IFabd; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00252; INTERFERON_A_B_D; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Complete proteome; Cytokine;
Disulfide bond; Glycoprotein; Pharmaceutical; Phosphoprotein;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 21
CHAIN 22 187 Interferon beta.
/FTId=PRO_0000016400.
MOD_RES 24 24 Phosphotyrosine.
{ECO:0000250|UniProtKB:P70499}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
DISULFID 52 162 {ECO:0000269|PubMed:6162107}.
VARIANT 162 162 C -> Y (variant found in a clone obtained
from a fibroblast cell line; does not
form the essential disulfide bond;
results in loss of antiviral activity).
{ECO:0000269|PubMed:6171735}.
/FTId=VAR_004016.
VARIANT 164 164 W -> C (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036330.
HELIX 24 42 {ECO:0000244|PDB:1AU1}.
HELIX 51 55 {ECO:0000244|PDB:1AU1}.
HELIX 63 67 {ECO:0000244|PDB:1AU1}.
HELIX 73 91 {ECO:0000244|PDB:1AU1}.
HELIX 96 98 {ECO:0000244|PDB:1AU1}.
HELIX 102 127 {ECO:0000244|PDB:1AU1}.
TURN 137 139 {ECO:0000244|PDB:1AU1}.
HELIX 140 156 {ECO:0000244|PDB:1AU1}.
TURN 157 159 {ECO:0000244|PDB:1AU1}.
HELIX 161 182 {ECO:0000244|PDB:1AU1}.
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


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