Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Interferon beta

Gene

Ifnb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has antiviral, antibacterial and anticancer activities.

GO - Molecular functioni

  • chloramphenicol O-acetyltransferase activity Source: MGI
  • cytokine activity Source: MGI
  • type I interferon receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Antiviral defense

Enzyme and pathway databases

ReactomeiR-MMU-909733. Interferon alpha/beta signaling.
R-MMU-912694. Regulation of IFNA signaling.
R-MMU-918233. TRAF3-dependent IRF activation pathway.
R-MMU-933541. TRAF6 mediated IRF7 activation.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon beta
Short name:
IFN-beta
Gene namesi
Name:Ifnb1
Synonyms:Ifb, Ifnb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:107657. Ifnb1.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 182161Interferon betaPRO_0000016403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphotyrosineBy similarity
Glycosylationi50 – 501N-linked (GlcNAc...)
Glycosylationi90 – 901N-linked (GlcNAc...)
Glycosylationi97 – 971N-linked (GlcNAc...)

Post-translational modificationi

This beta interferon does not have a disulfide bond.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01575.
PRIDEiP01575.

PTM databases

PhosphoSiteiP01575.
UniCarbKBiP01575.

Miscellaneous databases

PMAP-CutDBP01575.

Expressioni

Gene expression databases

BgeeiP01575.
CleanExiMM_IFNB1.
ExpressionAtlasiP01575. baseline and differential.
GenevisibleiP01575. MM.

Interactioni

Subunit structurei

Monomer. Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways.1 Publication

GO - Molecular functioni

  • cytokine activity Source: MGI
  • type I interferon receptor binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056720.

Structurei

Secondary structure

1
182
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 4320Combined sources
Helixi61 – 644Combined sources
Helixi69 – 8618Combined sources
Helixi92 – 943Combined sources
Helixi98 – 11821Combined sources
Helixi119 – 1224Combined sources
Helixi123 – 1297Combined sources
Helixi133 – 15119Combined sources
Turni152 – 1543Combined sources
Helixi156 – 17621Combined sources
Helixi177 – 1804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IFAX-ray2.60A24-181[»]
1WU3X-ray2.15I22-182[»]
2HIFmodel-A24-182[»]
3WCYX-ray2.90I22-182[»]
ProteinModelPortaliP01575.
SMRiP01575. Positions 22-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01575.

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha/beta interferon family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J0RY. Eukaryota.
ENOG41113EJ. LUCA.
HOGENOMiHOG000230501.
HOVERGENiHBG052086.
InParanoidiP01575.
KOiK05415.
OMAiNGRLEYC.
OrthoDBiEOG7J9VRD.
PhylomeDBiP01575.
TreeFamiTF336177.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000471. Interferon_alpha/beta/delta.
IPR015588. Interferon_beta.
[Graphical view]
PANTHERiPTHR11691. PTHR11691. 1 hit.
PTHR11691:SF40. PTHR11691:SF40. 1 hit.
PfamiPF00143. Interferon. 1 hit.
[Graphical view]
PRINTSiPR00266. INTERFERONAB.
SMARTiSM00076. IFabd. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00252. INTERFERON_A_B_D. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01575-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNRWILHAA FLLCFSTTAL SINYKQLQLQ ERTNIRKCQE LLEQLNGKIN
60 70 80 90 100
LTYRADFKIP MEMTEKMQKS YTAFAIQEML QNVFLVFRNN FSSTGWNETI
110 120 130 140 150
VVRLLDELHQ QTVFLKTVLE EKQEERLTWE MSSTALHLKS YYWRVQRYLK
160 170 180
LMKYNSYAWM VVRAEIFRNF LIIRRLTRNF QN
Length:182
Mass (Da):22,127
Last modified:July 21, 1986 - v1
Checksum:i8C4C32947FD1B917
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00020 mRNA. Translation: AAA37891.1.
X14455 Genomic DNA. Translation: CAA32625.1.
X14029 Genomic DNA. Translation: CAA32190.1.
CCDSiCCDS18318.1.
PIRiS02020. IVMSB.
RefSeqiNP_034640.1. NM_010510.1.
UniGeneiMm.1245.

Genome annotation databases

EnsembliENSMUST00000055671; ENSMUSP00000056720; ENSMUSG00000048806.
GeneIDi15977.
KEGGimmu:15977.
UCSCiuc008tmz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00020 mRNA. Translation: AAA37891.1.
X14455 Genomic DNA. Translation: CAA32625.1.
X14029 Genomic DNA. Translation: CAA32190.1.
CCDSiCCDS18318.1.
PIRiS02020. IVMSB.
RefSeqiNP_034640.1. NM_010510.1.
UniGeneiMm.1245.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IFAX-ray2.60A24-181[»]
1WU3X-ray2.15I22-182[»]
2HIFmodel-A24-182[»]
3WCYX-ray2.90I22-182[»]
ProteinModelPortaliP01575.
SMRiP01575. Positions 22-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056720.

PTM databases

PhosphoSiteiP01575.
UniCarbKBiP01575.

Proteomic databases

PaxDbiP01575.
PRIDEiP01575.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055671; ENSMUSP00000056720; ENSMUSG00000048806.
GeneIDi15977.
KEGGimmu:15977.
UCSCiuc008tmz.1. mouse.

Organism-specific databases

CTDi3456.
MGIiMGI:107657. Ifnb1.

Phylogenomic databases

eggNOGiENOG410J0RY. Eukaryota.
ENOG41113EJ. LUCA.
HOGENOMiHOG000230501.
HOVERGENiHBG052086.
InParanoidiP01575.
KOiK05415.
OMAiNGRLEYC.
OrthoDBiEOG7J9VRD.
PhylomeDBiP01575.
TreeFamiTF336177.

Enzyme and pathway databases

ReactomeiR-MMU-909733. Interferon alpha/beta signaling.
R-MMU-912694. Regulation of IFNA signaling.
R-MMU-918233. TRAF3-dependent IRF activation pathway.
R-MMU-933541. TRAF6 mediated IRF7 activation.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP01575.
NextBioi288756.
PMAP-CutDBP01575.
PROiP01575.
SOURCEiSearch...

Gene expression databases

BgeeiP01575.
CleanExiMM_IFNB1.
ExpressionAtlasiP01575. baseline and differential.
GenevisibleiP01575. MM.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000471. Interferon_alpha/beta/delta.
IPR015588. Interferon_beta.
[Graphical view]
PANTHERiPTHR11691. PTHR11691. 1 hit.
PTHR11691:SF40. PTHR11691:SF40. 1 hit.
PfamiPF00143. Interferon. 1 hit.
[Graphical view]
PRINTSiPR00266. INTERFERONAB.
SMARTiSM00076. IFabd. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00252. INTERFERON_A_B_D. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure and expression of a cloned cDNA for mouse interferon-beta."
    Higashi Y., Sokawa Y., Watanabe Y., Kawade Y., Ohno S., Takaoka C., Taniguchi T.
    J. Biol. Chem. 258:9522-9529(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Nucleotide sequence of the mouse interferon-beta gene."
    Kuga T., Fujita T., Taniguchi T.
    Nucleic Acids Res. 17:3291-3291(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure and characterization of a murine chromosomal fragment containing the interferon beta gene."
    Vodjdani G., Coulombel C., Doly J.
    J. Mol. Biol. 204:221-231(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Purification and carbohydrate structure of natural murine interferon-beta."
    Civas A., Fournet B., Coulombel C., le Roscouet D., Honvault A., Petek F., Montreuil J., Doly J.
    Eur. J. Biochem. 173:311-316(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES.
  5. "Three-dimensional structure of recombinant murine interferon-beta."
    Senda T., Matsuda S., Kurihara H., Nakamura K.T., Kawano G., Shimizu H., Mizuno H., Mitsui Y.
    Proc. Jpn. Acad., B, Phys. Biol. Sci. 66:77-80(1990)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
  6. "Three-dimensional crystal structure of recombinant murine interferon-beta."
    Senda T., Shimazu T., Matsuda S., Kawano G., Shimizu H., Nakamura K.T., Mitsui Y.
    EMBO J. 11:3193-3201(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  7. "Refined crystal structure of recombinant murine interferon-beta at 2.15-A resolution."
    Senda T., Saitoh S., Mitsui Y.
    J. Mol. Biol. 253:187-207(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-182 IN COMPLEX WITH IFNAR1, SUBUNIT.

Entry informationi

Entry nameiIFNB_MOUSE
AccessioniPrimary (citable) accession number: P01575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.