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Protein

Interferon regulatory factor 2

Gene

Irf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi5 – 113109IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_311354. TRAF6 mediated IRF7 activation.
REACT_349056. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon regulatory factor 2
Short name:
IRF-2
Gene namesi
Name:Irf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96591. Irf2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Interferon regulatory factor 2PRO_0000154550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei78 – 781N6-acetyllysineBy similarity
Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki166 – 166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei225 – 2251PhosphoserineBy similarity
Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 is required for stimulation of H4 promoter activity (By similarity).By similarity
The major sites of sumoylation are Lys-137 and Lys-293. Sumoylation with SUMO1 increases its transcriptional repressor activity on IRF1 and diminishes its ability to activate ISRE and H4 promoter (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP23906.
PRIDEiP23906.

PTM databases

PhosphoSiteiP23906.

Expressioni

Inductioni

By viruses and IFN.

Gene expression databases

BgeeiP23906.
CleanExiMM_IRF2.
ExpressionAtlasiP23906. baseline and differential.
GenevisibleiP23906. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi200785. 1 interaction.
IntActiP23906. 1 interaction.
MINTiMINT-4098768.
STRINGi10090.ENSMUSP00000034041.

Structurei

Secondary structure

1
349
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1710Combined sources
Beta strandi25 – 284Combined sources
Turni29 – 324Combined sources
Beta strandi33 – 375Combined sources
Beta strandi43 – 475Combined sources
Helixi48 – 514Combined sources
Helixi53 – 619Combined sources
Turni67 – 693Combined sources
Helixi74 – 8714Combined sources
Beta strandi91 – 933Combined sources
Turni95 – 973Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi106 – 1116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRFNMR-A2-113[»]
1IRGNMR-A2-113[»]
2IRFX-ray2.20G/H/I/J/K/L1-113[»]
ProteinModelPortaliP23906.
SMRiP23906. Positions 5-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23906.

Family & Domainsi

Sequence similaritiesi

Belongs to the IRF family.PROSITE-ProRule annotation
Contains 1 IRF tryptophan pentad repeat DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG41436.
HOGENOMiHOG000037937.
HOVERGENiHBG003455.
InParanoidiP23906.
KOiK10153.
OMAiSWPPFPD.
OrthoDBiEOG72ZCFD.
PhylomeDBiP23906.
TreeFamiTF328512.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR017431. Interferon_reg_fac-1/2.
IPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00605. IRF. 1 hit.
[Graphical view]
PIRSFiPIRSF038196. IFN_RF1/2. 1 hit.
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
[Graphical view]
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23906-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK
60 70 80 90 100
DAPLFRNWAI HTGKHQPGID KPDPKTWKAN FRCAMNSLPD IEEVKDRSIK
110 120 130 140 150
KGNNAFRVYR MLPLSERPSK KGKKPKTEKE ERVKHIKQEP VESSLGLSNG
160 170 180 190 200
VSGFSPEYAV LTSAIKNEVD STVNIIVVGQ SHLDSNIEDQ EIVTNPPDIC
210 220 230 240 250
QVVEVTTESD DQPVSMSELY PLQISPVSSY AESETTDSVA SDEENAEGRP
260 270 280 290 300
HWRKRSIEGK QYLSNMGTRN TYLLPSMATF VTSNKPDLQV TIKEDSCPMP
310 320 330 340
YNSSWPPFTD LPLPAPVTPT PSSSRPDRET RASVIKKTSD ITQARVKSC
Length:349
Mass (Da):39,453
Last modified:November 1, 1991 - v1
Checksum:i8738B082FB40FB11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03168 mRNA. Translation: AAA39333.1.
CCDSiCCDS22295.1.
RefSeqiNP_032417.3. NM_008391.4.
XP_006509351.1. XM_006509288.2.
XP_006509352.1. XM_006509289.2.
UniGeneiMm.1149.

Genome annotation databases

EnsembliENSMUST00000034041; ENSMUSP00000034041; ENSMUSG00000031627.
GeneIDi16363.
KEGGimmu:16363.
UCSCiuc009lqo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03168 mRNA. Translation: AAA39333.1.
CCDSiCCDS22295.1.
RefSeqiNP_032417.3. NM_008391.4.
XP_006509351.1. XM_006509288.2.
XP_006509352.1. XM_006509289.2.
UniGeneiMm.1149.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRFNMR-A2-113[»]
1IRGNMR-A2-113[»]
2IRFX-ray2.20G/H/I/J/K/L1-113[»]
ProteinModelPortaliP23906.
SMRiP23906. Positions 5-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200785. 1 interaction.
IntActiP23906. 1 interaction.
MINTiMINT-4098768.
STRINGi10090.ENSMUSP00000034041.

PTM databases

PhosphoSiteiP23906.

Proteomic databases

PaxDbiP23906.
PRIDEiP23906.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034041; ENSMUSP00000034041; ENSMUSG00000031627.
GeneIDi16363.
KEGGimmu:16363.
UCSCiuc009lqo.2. mouse.

Organism-specific databases

CTDi3660.
MGIiMGI:96591. Irf2.

Phylogenomic databases

eggNOGiNOG41436.
HOGENOMiHOG000037937.
HOVERGENiHBG003455.
InParanoidiP23906.
KOiK10153.
OMAiSWPPFPD.
OrthoDBiEOG72ZCFD.
PhylomeDBiP23906.
TreeFamiTF328512.

Enzyme and pathway databases

ReactomeiREACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_311354. TRAF6 mediated IRF7 activation.
REACT_349056. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiIrf2. mouse.
EvolutionaryTraceiP23906.
NextBioi289470.
PROiP23906.
SOURCEiSearch...

Gene expression databases

BgeeiP23906.
CleanExiMM_IRF2.
ExpressionAtlasiP23906. baseline and differential.
GenevisibleiP23906. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR017431. Interferon_reg_fac-1/2.
IPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00605. IRF. 1 hit.
[Graphical view]
PIRSFiPIRSF038196. IFN_RF1/2. 1 hit.
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
[Graphical view]
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-113.

Entry informationi

Entry nameiIRF2_MOUSE
AccessioniPrimary (citable) accession number: P23906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 24, 2015
This is version 132 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, Direct protein sequencing, 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

External Data

Dasty 3

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 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.