Reviewed,
UniProtKB/Swiss-Prot P23906 (IRF2_MOUSE)
Last modified
November 3, 2009.
Version 81.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Interferon regulatory factor 2 Short name=IRF-2 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 349 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| 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 process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Ligand | DNA-binding |
| Molecular function | Activator Repressor |
| PTM | Acetylation Isopeptide bond Ubl conjugation |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | transcription factor activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 349 | 349 | Interferon regulatory factor 2 | PRO_0000154550 | |||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||
| DNA binding | 7 – 109 | 103 | Tryptophan pentad repeat | ||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||
| Modified residue | 75 | 1 | N6-acetyllysine By similarity | ||||||||||||||||||||||||||
| Modified residue | 78 | 1 | N6-acetyllysine By similarity | ||||||||||||||||||||||||||
| Cross-link | 137 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity | |||||||||||||||||||||||||||
| Cross-link | 166 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity | |||||||||||||||||||||||||||
| Cross-link | 293 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity | |||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||
| Helix | 8 – 17 | 10 | |||||||||||||||||||||||||||
| Beta strand | 25 – 28 | 4 | |||||||||||||||||||||||||||
| Turn | 29 – 32 | 4 | |||||||||||||||||||||||||||
| Beta strand | 33 – 37 | 5 | |||||||||||||||||||||||||||
| Helix | 48 – 51 | 4 | |||||||||||||||||||||||||||
| Helix | 53 – 61 | 9 | |||||||||||||||||||||||||||
| Turn | 67 – 69 | 3 | |||||||||||||||||||||||||||
| Helix | 74 – 87 | 14 | |||||||||||||||||||||||||||
| Beta strand | 91 – 93 | 3 | |||||||||||||||||||||||||||
| Turn | 95 – 97 | 3 | |||||||||||||||||||||||||||
| Beta strand | 106 – 111 | 6 | |||||||||||||||||||||||||||
Sequences
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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. | |||||||||||||||||||||||||
| IPI | IPI00138234. | ||||||||||||||||||||||||
| RefSeq | NP_032417.3. | ||||||||||||||||||||||||
| UniGene | Mm.1149 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| |||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| STRING | P23906. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | P23906. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PRIDE | P23906. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENSMUST00000034041; ENSMUSP00000034041; ENSMUSG00000031627; Mus musculus. [Genome view] | ||||||||||||||||||||||||
| GeneID | 16363. | ||||||||||||||||||||||||
| KEGG | mmu:16363. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 16363. | ||||||||||||||||||||||||
| MGI | MGI:96591. Irf2. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P23906. | ||||||||||||||||||||||||
| HOVERGEN | P23906. | ||||||||||||||||||||||||
| OMA | VTIKEES. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P23906. | ||||||||||||||||||||||||
| Bgee | P23906. | ||||||||||||||||||||||||
| CleanEx | MM_IRF2. | ||||||||||||||||||||||||
| Genevestigator | P23906. | ||||||||||||||||||||||||
| GermOnline | ENSMUSG00000031627. Mus musculus. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR017431. Interferon_regulatory_fac-1/2. IPR019817. Interferon_regulatory_fac_CS. IPR001346. Interferon_regulatory_factor. IPR011991. Wing_hlx_DNA_bd. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00605. IRF. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PIRSF | PIRSF038196. IFN_RF1/2. 1 hit. | ||||||||||||||||||||||||
| PRINTS | PR00267. INTFRNREGFCT. | ||||||||||||||||||||||||
| ProDom | PD002355. IRF. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||||||||
| SMART | SM00348. IRF. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PROSITE | PS00601. IRF. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| NextBio | 289470. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | IRF2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P23906 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (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 |

Clusters with


