P01574 (IFNB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interferon beta
Short name=IFN-beta

Alternative name(s):
Fibroblast interferon

Gene names

Name:	IFNB1
Synonyms:	IFB, IFNB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has antiviral, antibacterial and anticancer activities.
Subunit structure	Monomer.
Subcellular location	Secreted.
Pharmaceutical use	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.
Sequence similarities	Belongs to the alpha/beta interferon family.

Ontologies

Keywords
Biological process	Antiviral defense
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Cytokine
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological process	B cell proliferation Non-traceable author statement. Source: UniProtKB activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome cellular response to exogenous dsRNA Inferred from mutant phenotype. Source: BHF-UCL defense response to virus Inferred from direct assay. Source: BHF-UCL induction of apoptosis Inferred from direct assay. Source: UniProtKB natural killer cell activation Non-traceable author statement. Source: UniProtKB negative regulation of T cell differentiation Inferred from direct assay. Source: UniProtKB negative regulation of T-helper 2 cell cytokine production Inferred from direct assay. Source: UniProtKB negative regulation of cell proliferation Non-traceable author statement. Source: UniProtKB negative regulation of viral genome replication Inferred from direct assay. Source: BHF-UCL negative regulation of viral transcription Inferred from direct assay. Source: BHF-UCL negative regulation of virion penetration into host cell Non-traceable author statement. Source: UniProtKB positive regulation of innate immune response Non-traceable author statement. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: BHF-UCL regulation of MHC class I biosynthetic process Non-traceable author statement. Source: UniProtKB regulation of type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytokine activity Inferred from electronic annotation. Source: UniProtKB-KW interferon-alpha/beta receptor binding Non-traceable author statement Ref.7. Source: UniProtKB transcription corepressor activity Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 187

166

Interferon beta

PRO_0000016400

Amino acid modifications

Modified residue

140

1

Phosphoserine Ref.12

Glycosylation

101

1

N-linked (GlcNAc...)

Disulfide bond

52 ↔ 162

Ref.10

Natural variations

Natural variant

162

1

C → Y in clone PF526, loss of ability to form the essential disulfide bond, loss of antiviral activity.

VAR_004016

Natural variant

164

1

W → C in a breast cancer sample; somatic mutation. Ref.14

VAR_036330

Secondary structure

1

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.

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.

187

Helix Strand Turn

Details...

Helix

24 – 42

19

Helix

51 – 55

5

Helix

63 – 67

5

Helix

73 – 91

19

Helix

96 – 98

3

Helix

102 – 127

26

Turn

137 – 139

3

Helix

140 – 156

17

Turn

157 – 159

3

Helix

161 – 182

22

Sequences

	Sequence		Length	Mass (Da)
	P01574 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0B013D4087723CEC	FASTA	187	22,294
	10 20 30 40 50 60 MTNKCLLQIA LLLCFSTTAL SMSYNLLGFL QRSSNFQCQK LLWQLNGRLE YCLKDRMNFD 70 80 90 100 110 120 IPEEIKQLQQ FQKEDAALTI YEMLQNIFAI FRQDSSSTGW NETIVENLLA NVYHQINHLK 130 140 150 160 170 180 TVLEEKLEKE DFTRGKLMSS LHLKRYYGRI LHYLKAKEYS HCAWTIVRVE ILRNFYFINR LTGYLRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human fibroblast interferon gene lacks introns." Lawn R.M., Adelman J., Franke A.E., Houck C.M., Gross M., Najarian R., Goeddel D.V. Nucleic Acids Res. 9:1045-1052(1981) [PubMed: 6164984] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structure of a chromosomal gene for human interferon beta." Ohno S., Taniguchi T. Proc. Natl. Acad. Sci. U.S.A. 78:5305-5309(1981) [PubMed: 16593086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of human fibroblast interferon cDNA." Taniguchi T., Ohno S., Fujii-Kuriyama Y., Muramatsu M. Gene 10:11-15(1980) [PubMed: 6157601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Isolation and structure of a human fibroblast interferon gene." Derynck R., Content J., Declercq E., Volckaert G., Tavernier J., Devos R., Fiers W. Nature 285:542-547(1980) [PubMed: 6157094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The complete amino acid sequence of human fibroblast interferon as deduced using synthetic oligodeoxyribonucleotide primers of reverse transcriptase." 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. Nucleic Acids Res. 8:2885-2894(1980) [PubMed: 6159580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Synthesis of human fibroblast interferon by E. coli." Goeddel D.V., Shepard H.M., Yelverton E., Leung D., Crea R., Sloma A., Pestka S. Nucleic Acids Res. 8:4057-4074(1980) [PubMed: 6159584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"On the relationship between human interferon alpha 1 and beta 1 genes." May L.T., Sehgal P.B. J. Interferon Res. 5:521-526(1985) [PubMed: 2414376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"The amino-terminal sequence of human fibroblast interferon as deduced from reverse transcripts obtained using synthetic oligonucleotide primers." 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. Nucleic Acids Res. 8:1913-1931(1980) [PubMed: 6159597] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-68.
[10]	"Assignment of the disulphide bonds of leukocyte interferon." Wetzel R. Nature 289:606-607(1981) [PubMed: 6162107] [Abstract] Cited for: DISULFIDE BOND.
[11]	"A single amino acid change in IFN-beta1 abolishes its antiviral activity." Shepard H.M., Leung D., Stebbing N., Goeddel D.V. Nature 294:563-565(1981) [PubMed: 6171735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 71-187 (VARIANT CLONE PF526).
[12]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"The crystal structure of human interferon beta at 2.2-A resolution." Karpusas M., Nolte M., Benton C.B., Meier W., Lipscomb W.N., Goelz S. Proc. Natl. Acad. Sci. U.S.A. 94:11813-11818(1997) [PubMed: 9342320] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[14]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-164.
+	Additional computationally mapped references.

Web resources

Avonex

Clinical information on Avonex

Betaseron

Clinical information on Betaseron

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00534 Genomic DNA. Translation: CAA23795.1.
V00535 Genomic DNA. Translation: CAA23796.1.
V00546 mRNA. Translation: CAA23807.1.
V00547 mRNA. Translation: CAA23808.1.
M28622 mRNA. Translation: AAA36040.1.
BC069314 mRNA. Translation: AAH69314.1.

IPI

IPI00003088.

PIR

IVHUB1. A93721.

RefSeq

NP_002167.1. NM_002176.2.

UniGene

Hs.93177.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AU1	X-ray	2.20	A/B	22-187	[»]

ProteinModelPortal

P01574.

SMR

P01574. Positions 22-187.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6018N.

STRING

P01574.

PTM databases

PhosphoSite

P01574.

Polymorphism databases

DMDM

124469.

Proteomic databases

PRIDE

P01574.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380232; ENSP00000369581; ENSG00000171855.

GeneID

3456.

KEGG

hsa:3456.

UCSC

uc003zok.1. human.

Organism-specific databases

CTD

3456.

GeneCards

GC09M021077.

H-InvDB

HIX0034856.

HGNC

HGNC:5434. IFNB1.

HPA

CAB009386.

MIM

147640. gene.

neXtProt

NX_P01574.

PharmGKB

PA29672.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18223.

HOGENOM

HBG126445.

HOVERGEN

HBG052086.

InParanoid

P01574.

OMA

SSTGWNE.

OrthoDB

EOG4Q84ZV.

PhylomeDB

P01574.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P01574.

CleanEx

HS_IFNB1.

Genevestigator

P01574.

GermOnline

ENSG00000171855. Homo sapiens.

Family and domain databases

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000471. Interferon_alpha/beta/delta.
IPR015588. Interferon_beta.
[Graphical view]

Gene3D

G3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.

KO

K05415.

PANTHER

PTHR11691:SF7. IFNb. 1 hit.
PTHR11691. Interferon_abd. 1 hit.

Pfam

PF00143. Interferon. 1 hit.
[Graphical view]

PRINTS

PR00266. INTERFERONAB.

SMART

SM00076. IFabd. 1 hit.
[Graphical view]

SUPFAM

SSF47266. 4_helix_cytokine. 1 hit.

PROSITE

PS00252. INTERFERON_A_B_D. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00060. Interferon beta-1a.
DB00068. Interferon beta-1b.

NextBio

13618.

PMAP-CutDB

P01574.

SOURCE

Search...

Entry information

Entry name

IFNB_HUMAN

Accession

Primary (citable) accession number: P01574

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.