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Q64287 (IRF4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon regulatory factor 4

Short name=IRF-4
Alternative name(s):
Lymphocyte-specific interferon regulatory factor
Short name=LSIRF
NF-EM5
PU.1 interaction partner
Transcriptional activator PIP
Gene names
Name:Irf4
Synonyms:Spip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8+ dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes. Ref.5 Ref.6 Ref.7

Subunit structure

Interacts with SPIB and DEF6 By similarity. Interacts with the BATF-JUNB heterodimer. Interacts with BATF (via bZIP domain); the interaction is direct. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus.

Tissue specificity

Lymphoid cells.

Induction

Not induced by interferons.

Post-translational modification

Phosphorylation by ROCK2 regulates IL-17 and IL-21 production.

Sequence similarities

Belongs to the IRF family.

Contains 1 IRF tryptophan pentad repeat DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT-helper 17 cell lineage commitment

Inferred from mutant phenotype Ref.7. Source: UniProtKB

defense response to protozoan

Inferred from mutant phenotype Ref.5. Source: UniProtKB

histone H3 acetylation

Inferred from mutant phenotype PubMed 16428437. Source: MGI

histone H4 acetylation

Inferred from mutant phenotype PubMed 16428437. Source: MGI

myeloid dendritic cell differentiation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

negative regulation of toll-like receptor signaling pathway

Inferred from mutant phenotype PubMed 16236719. Source: MGI

peptidyl-lysine methylation

Inferred from direct assay PubMed 22948820. Source: GOC

positive regulation of DNA binding

Inferred from mutant phenotype PubMed 16428437. Source: MGI

positive regulation of interleukin-10 biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-13 biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-2 biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-4 biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 16428437. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein methylation

Inferred from direct assay PubMed 22948820. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nuclear nucleosome

Inferred from direct assay PubMed 16428437. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction Ref.7Ref.6Ref.5. Source: UniProtKB

protein-lysine N-methyltransferase activity

Inferred from direct assay PubMed 22948820. Source: UniProtKB

regulatory region DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from direct assay Ref.7Ref.6Ref.5. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.7Ref.6Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BatfO352847EBI-6398485,EBI-6398523

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q64287-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q64287-2)

The sequence of this isoform differs from the canonical sequence as follows:
     165-165: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Interferon regulatory factor 4
PRO_0000154557

Regions

DNA binding21 – 129109IRF tryptophan pentad repeat

Amino acid modifications

Modified residue4461Phosphoserine; by ROCK2 Ref.4
Modified residue4471Phosphoserine; by ROCK2 Ref.4

Natural variations

Alternative sequence1651Missing in isoform 2.
VSP_002756

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 5FD94CA6C453869C

FASTA45051,577
        10         20         30         40         50         60 
MNLETGSRGS EFGMSAVSCG NGKLRQWLID QIDSGKYPGL VWENEEKSVF RIPWKHAGKQ 

        70         80         90        100        110        120 
DYNREEDAAL FKAWALFKGK FREGIDKPDP PTWKTRLRCA LNKSNDFEEL VERSQLDISD 

       130        140        150        160        170        180 
PYKVYRIVPE GAKKGAKQLT LDDTQMAMGH PYPMTAPYGS LPAQQVHNYM MPPHDRSWRD 

       190        200        210        220        230        240 
YAPDQSHPEI PYQCPVTFGP RGHHWQGPSC ENGCQVTGTF YACAPPESQA PGIPIEPSIR 

       250        260        270        280        290        300 
SAEALALSDC RLHICLYYRD ILVKELTTTS PEGCRISHGH TYDVSNLDQV LFPYPDDNGQ 

       310        320        330        340        350        360 
RKNIEKLLSH LERGLVLWMA PDGLYAKRLC QSRIYWDGPL ALCSDRPNKL ERDQTCKLFD 

       370        380        390        400        410        420 
TQQFLSELQV FAHHGRPAPR FQVTLCFGEE FPDPQRQRKL ITAHVEPLLA RQLYYFAQQN 

       430        440        450 
TGHFLRGYEL PEHVTTPDYH RSLRHSSIQE 

« Hide

Isoform 2 [UniParc].

Checksum: C4E4A0DC04AA8A52
Show »

FASTA44951,449

References

[1]"Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator."
Eisenbeis C.F., Singh H., Storb U.
Genes Dev. 9:1377-1387(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Molecular cloning of LSIRF, a lymphoid-specific member of the interferon regulatory factor family that binds the interferon-stimulated response element (ISRE)."
Matsuyama T., Grossman A., Mittruecker H.-W., Siderovski D.P., Kiefer F., Kawakami T., Richardson C.D., Taniguchi T., Yoshinaga S.K., Mak T.W.
Nucleic Acids Res. 23:2127-2136(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ and C57BL/6.
Tissue: Spleen.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 65-72, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"Phosphorylation of IRF4 by ROCK2 regulates IL-17 and IL-21 production and the development of autoimmunity in mice."
Biswas P.S., Gupta S., Chang E., Song L., Stirzaker R.A., Liao J.K., Bhagat G., Pernis A.B.
J. Clin. Invest. 120:3280-3295(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-446 AND SER-447.
[5]"Compensatory dendritic cell development mediated by BATF-IRF interactions."
Tussiwand R., Lee W.L., Murphy T.L., Mashayekhi M., Kc W., Albring J.C., Satpathy A.T., Rotondo J.A., Edelson B.T., Kretzer N.M., Wu X., Weiss L.A., Glasmacher E., Li P., Liao W., Behnke M., Lam S.S., Aurthur C.T. expand/collapse author list , Leonard W.J., Singh H., Stallings C.L., Sibley L.D., Schreiber R.D., Murphy K.M.
Nature 490:502-507(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BATF.
[6]"BATF-JUN is critical for IRF4-mediated transcription in T cells."
Li P., Spolski R., Liao W., Wang L., Murphy T.L., Murphy K.M., Leonard W.J.
Nature 490:543-546(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BATF.
[7]"A genomic regulatory element that directs assembly and function of immune-specific AP-1-IRF complexes."
Glasmacher E., Agrawal S., Chang A.B., Murphy T.L., Zeng W., Vander Lugt B., Khan A.A., Ciofani M., Spooner C., Rutz S., Hackney J., Nurieva R., Escalante C.R., Ouyang W., Littman D.R., Murphy K.M., Singh H.
Science 338:975-980(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BATF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U34307 mRNA. Translation: AAA75283.1.
U11692 mRNA. Translation: AAA75309.1.
U20949 Genomic DNA. Translation: AAA75316.1.
U20949 Genomic DNA. Translation: AAA75317.1.
CCDSCCDS26419.1. [Q64287-1]
PIRS57837.
RefSeqNP_038702.1. NM_013674.1. [Q64287-1]
XP_006516623.1. XM_006516560.1. [Q64287-2]
UniGeneMm.4677.

3D structure databases

ProteinModelPortalQ64287.
SMRQ64287. Positions 18-130, 252-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200786. 3 interactions.
DIPDIP-59740N.
IntActQ64287. 1 interaction.

PTM databases

PhosphoSiteQ64287.

Proteomic databases

PRIDEQ64287.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021784; ENSMUSP00000021784; ENSMUSG00000021356. [Q64287-1]
ENSMUST00000110307; ENSMUSP00000105936; ENSMUSG00000021356. [Q64287-2]
GeneID16364.
KEGGmmu:16364.
UCSCuc007pyz.1. mouse. [Q64287-1]

Organism-specific databases

CTD3662.
MGIMGI:1096873. Irf4.

Phylogenomic databases

eggNOGNOG39558.
GeneTreeENSGT00740000114956.
HOGENOMHOG000010107.
HOVERGENHBG003072.
InParanoidQ64287.
KOK09445.
OMADNGQRKN.
OrthoDBEOG7CCBR1.
PhylomeDBQ64287.
TreeFamTF328512.

Gene expression databases

ArrayExpressQ64287.
BgeeQ64287.
CleanExMM_IRF4.
GenevestigatorQ64287.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProIPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR019471. Interferon_reg_factor-3.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]
PRINTSPR00267. INTFRNREGFCT.
SMARTSM00348. IRF. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio289474.
PROQ64287.
SOURCESearch...

Entry information

Entry nameIRF4_MOUSE
AccessionPrimary (citable) accession number: Q64287
Secondary accession number(s): Q60802
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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