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Reviewed, UniProtKB/Swiss-Prot P23906 (IRF2_MOUSE)

Last modified November 3, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Interferon regulatory factor 2
      Short name=IRF-2
Gene names
Name: Irf2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in cell cycle regulation through binding the site II (HiNF-M) promoter region of H4 and activating transcription during cell growth. Antagonizes IRF1 transcriptional activation.

Subunit structure

Interacts with BRD7, IRF2BP1 and IRF2BP2. Interacts with CREBBP in growing cells; the interaction acetylates IRF2 and regulates IRF2-dependent H4 promoter activity By similarity.

Subcellular location

Nucleus.

Induction

By viruses and IFN.

Post-translational modification

Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 is required for stimulation of H4 promoter activity By similarity.

The major sites of sumoylation are Lys-137 and Lys-293. Sumoylation by SUMO1 increases its transcriptional repressor activity on IRF1 and diminishes its ability to activate ISRE and H4 promoter By similarity.

Sequence similarities

Belongs to the IRF family.

Contains 1 tryptophan pentad repeat DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontranscription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Interferon regulatory factor 2
PRO_0000154550

Regions

DNA binding7 – 109103Tryptophan pentad repeat

Amino acid modifications

Modified residue751N6-acetyllysine By similarity
Modified residue781N6-acetyllysine By similarity
Cross-link137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Secondary structure

..................... 349
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23906-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 8738B082FB40FB11

FASTA34939,453
        10         20         30         40         50         60 
MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK DAPLFRNWAI 

        70         80         90        100        110        120 
HTGKHQPGID KPDPKTWKAN FRCAMNSLPD IEEVKDRSIK KGNNAFRVYR MLPLSERPSK 

       130        140        150        160        170        180 
KGKKPKTEKE ERVKHIKQEP VESSLGLSNG VSGFSPEYAV LTSAIKNEVD STVNIIVVGQ 

       190        200        210        220        230        240 
SHLDSNIEDQ EIVTNPPDIC QVVEVTTESD DQPVSMSELY PLQISPVSSY AESETTDSVA 

       250        260        270        280        290        300 
SDEENAEGRP HWRKRSIEGK QYLSNMGTRN TYLLPSMATF VTSNKPDLQV TIKEDSCPMP 

       310        320        330        340 
YNSSWPPFTD LPLPAPVTPT PSSSRPDRET RASVIKKTSD ITQARVKSC 

« Hide

References

[1]"Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes."
Harada H., Fujita T., Miyamoto M., Kimura Y., Maruyama M., Furia A., Miyata T., Taniguchi T.
Cell 58:729-739(1989) [PubMed: 2475256] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 108-120, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[3]"Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of the winged helix-turn-helix family."
Furui J., Uegaki K., Yamazaki T., Shirakawa M., Swindells M.B., Harada H., Taniguchi T., Kyogoku Y.
Structure 6:491-500(1998) [PubMed: 9562558] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-113.
[4]"Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences."
Fujii Y., Shimizu T., Kusumoto M., Kyogoku Y., Taniguchi T., Hakoshima T.
EMBO J. 18:5028-5041(1999) [PubMed: 10487755] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-113.
+Additional computationally mapped references.

Cross-references

Sequence databases

J03168 mRNA. Translation: AAA39333.1.
IPIIPI00138234.
RefSeqNP_032417.3.
UniGeneMm.1149

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IRFNMR-A2-113[»]
1IRGNMR-A2-113[»]
2IRFX-ray2.20G/H/I/J/K/L1-113[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP23906.

PTM databases

PhosphoSiteP23906.

Proteomic databases

PRIDEP23906.

Genome annotation databases

EnsemblENSMUST00000034041; ENSMUSP00000034041; ENSMUSG00000031627; Mus musculus. [Genome view]
GeneID16363.
KEGGmmu:16363.

Organism-specific databases

CTD16363.
MGIMGI:96591. Irf2.

Phylogenomic databases

HOGENOMP23906.
HOVERGENP23906.
OMAVTIKEES.

Gene expression databases

ArrayExpressP23906.
BgeeP23906.
CleanExMM_IRF2.
GenevestigatorP23906.
GermOnlineENSMUSG00000031627. Mus musculus.

Family and domain databases

InterProIPR017431. Interferon_regulatory_fac-1/2.
IPR019817. Interferon_regulatory_fac_CS.
IPR001346. Interferon_regulatory_factor.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF00605. IRF. 1 hit.
[Graphical view]
PIRSFPIRSF038196. IFN_RF1/2. 1 hit.
PRINTSPR00267. INTFRNREGFCT.
ProDomPD002355. IRF. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00348. IRF. 1 hit.
[Graphical view]
PROSITEPS00601. IRF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio289470.
SOURCESearch...

Entry information

Entry nameIRF2_MOUSE
AccessionPrimary (citable) accession number: P23906
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 3, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents