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Q15306

- IRF4_HUMAN

UniProt

Q15306 - IRF4_HUMAN

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Protein

Interferon regulatory factor 4

Gene

IRF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi21 – 129109IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. protein-lysine N-methyltransferase activity Source: Ensembl
  2. regulatory region DNA binding Source: InterPro
  3. sequence-specific DNA binding Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Reactome
  2. defense response to protozoan Source: UniProtKB
  3. histone H3 acetylation Source: Ensembl
  4. histone H4 acetylation Source: Ensembl
  5. interferon-gamma-mediated signaling pathway Source: Reactome
  6. myeloid dendritic cell differentiation Source: Ensembl
  7. negative regulation of toll-like receptor signaling pathway Source: Ensembl
  8. positive regulation of DNA binding Source: Ensembl
  9. positive regulation of interleukin-10 biosynthetic process Source: UniProtKB
  10. positive regulation of interleukin-13 biosynthetic process Source: UniProtKB
  11. positive regulation of interleukin-2 biosynthetic process Source: UniProtKB
  12. positive regulation of interleukin-4 biosynthetic process Source: UniProtKB
  13. positive regulation of transcription, DNA-templated Source: UniProtKB
  14. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  15. regulation of T-helper cell differentiation Source: UniProtKB
  16. T cell activation Source: UniProtKB
  17. T-helper 17 cell lineage commitment Source: UniProtKB
  18. transcription, DNA-templated Source: UniProtKB-KW
  19. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon regulatory factor 4
Short name:
IRF-4
Alternative name(s):
Lymphocyte-specific interferon regulatory factor
Short name:
LSIRF
Multiple myeloma oncogene 1
NF-EM5
Gene namesi
Name:IRF4
Synonyms:MUM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6119. IRF4.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
  3. nuclear nucleosome Source: Ensembl
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia.1 Publication
Note: The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving IRF4 has been found in multiple myeloma. Translocation t(6;14)(p25;q32) with the IgH locus.

Organism-specific databases

MIMi254500. phenotype.
PharmGKBiPA29918.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Interferon regulatory factor 4PRO_0000154556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei447 – 4471Phosphoserine; by ROCK2By similarity
Modified residuei448 – 4481Phosphoserine; by ROCK2By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15306.
PaxDbiQ15306.
PRIDEiQ15306.

PTM databases

PhosphoSiteiQ15306.

Expressioni

Tissue specificityi

Lymphoid cells.

Inductioni

Not induced by interferons.

Gene expression databases

BgeeiQ15306.
CleanExiHS_IRF4.
HS_MUM1.
ExpressionAtlasiQ15306. baseline and differential.
GenevestigatoriQ15306.

Organism-specific databases

HPAiCAB013508.
HPA002038.
HPA002698.

Interactioni

Subunit structurei

Interacts with the BATF-JUNB heterodimer. Interacts with BATF (via bZIP domain); the interaction is direct (By similarity). Interacts with SPIB and DEF6.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKAPO951632EBI-751345,EBI-347559
IRAK1P516172EBI-751345,EBI-358664
TLK2Q86UE82EBI-751345,EBI-1047967
YTHDC2Q9H6S02EBI-751345,EBI-1057466

Protein-protein interaction databases

BioGridi109870. 22 interactions.
IntActiQ15306. 10 interactions.
STRINGi9606.ENSP00000370343.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3411
Beta strandi37 – 393
Beta strandi41 – 477
Beta strandi49 – 535
Beta strandi60 – 623
Helixi64 – 674
Helixi69 – 7810
Helixi90 – 10314
Beta strandi107 – 1093
Turni111 – 1133
Beta strandi115 – 1206
Beta strandi122 – 1276

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DLLNMR-A23-130[»]
ProteinModelPortaliQ15306.
SMRiQ15306. Positions 18-130, 252-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15306.

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

eggNOGiNOG39558.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000010107.
HOVERGENiHBG003072.
InParanoidiQ15306.
KOiK09445.
OMAiDNGQRKN.
OrthoDBiEOG7CCBR1.
PhylomeDBiQ15306.
TreeFamiTF328512.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProiIPR019817. 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]
PfamiPF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15306-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNLEGGGRGG EFGMSAVSCG NGKLRQWLID QIDSGKYPGL VWENEEKSIF
60 70 80 90 100
RIPWKHAGKQ DYNREEDAAL FKAWALFKGK FREGIDKPDP PTWKTRLRCA
110 120 130 140 150
LNKSNDFEEL VERSQLDISD PYKVYRIVPE GAKKGAKQLT LEDPQMSMSH
160 170 180 190 200
PYTMTTPYPS LPAQQVHNYM MPPLDRSWRD YVPDQPHPEI PYQCPMTFGP
210 220 230 240 250
RGHHWQGPAC ENGCQVTGTF YACAPPESQA PGVPTEPSIR SAEALAFSDC
260 270 280 290 300
RLHICLYYRE ILVKELTTSS PEGCRISHGH TYDASNLDQV LFPYPEDNGQ
310 320 330 340 350
RKNIEKLLSH LERGVVLWMA PDGLYAKRLC QSRIYWDGPL ALCNDRPNKL
360 370 380 390 400
ERDQTCKLFD TQQFLSELQA FAHHGRSLPR FQVTLCFGEE FPDPQRQRKL
410 420 430 440 450
ITAHVEPLLA RQLYYFAQQN SGHFLRGYDL PEHISNPEDY HRSIRHSSIQ

E
Length:451
Mass (Da):51,772
Last modified:November 1, 1997 - v1
Checksum:i17CD1327C6F5BFFA
GO
Isoform 2 (identifier: Q15306-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:450
Mass (Da):51,644
Checksum:i85056FCEB84B0EBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001Q → H in AAB37258. (PubMed:9326949)Curated
Sequence conflicti306 – 3061K → N in AAB37258. (PubMed:9326949)Curated
Sequence conflicti333 – 3331R → T in AAB37258. (PubMed:9326949)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei165 – 1651Missing in isoform 2. 1 PublicationVSP_002755

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52682 mRNA. Translation: AAC50779.1.
U63738 mRNA. Translation: AAB37258.1.
AL589962, AL365272 Genomic DNA. Translation: CAH71554.1.
AL365272, AL589962 Genomic DNA. Translation: CAH72537.1.
BC015752 mRNA. Translation: AAH15752.1.
CCDSiCCDS4469.1. [Q15306-1]
RefSeqiNP_001182215.1. NM_001195286.1. [Q15306-2]
NP_002451.2. NM_002460.3. [Q15306-1]
UniGeneiHs.401013.

Genome annotation databases

EnsembliENST00000380956; ENSP00000370343; ENSG00000137265. [Q15306-1]
GeneIDi3662.
KEGGihsa:3662.
UCSCiuc003msz.4. human. [Q15306-1]
uc003mtb.4. human. [Q15306-2]

Polymorphism databases

DMDMi2497445.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52682 mRNA. Translation: AAC50779.1 .
U63738 mRNA. Translation: AAB37258.1 .
AL589962 , AL365272 Genomic DNA. Translation: CAH71554.1 .
AL365272 , AL589962 Genomic DNA. Translation: CAH72537.1 .
BC015752 mRNA. Translation: AAH15752.1 .
CCDSi CCDS4469.1. [Q15306-1 ]
RefSeqi NP_001182215.1. NM_001195286.1. [Q15306-2 ]
NP_002451.2. NM_002460.3. [Q15306-1 ]
UniGenei Hs.401013.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DLL NMR - A 23-130 [» ]
ProteinModelPortali Q15306.
SMRi Q15306. Positions 18-130, 252-446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109870. 22 interactions.
IntActi Q15306. 10 interactions.
STRINGi 9606.ENSP00000370343.

PTM databases

PhosphoSitei Q15306.

Polymorphism databases

DMDMi 2497445.

Proteomic databases

MaxQBi Q15306.
PaxDbi Q15306.
PRIDEi Q15306.

Protocols and materials databases

DNASUi 3662.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380956 ; ENSP00000370343 ; ENSG00000137265 . [Q15306-1 ]
GeneIDi 3662.
KEGGi hsa:3662.
UCSCi uc003msz.4. human. [Q15306-1 ]
uc003mtb.4. human. [Q15306-2 ]

Organism-specific databases

CTDi 3662.
GeneCardsi GC06P000391.
HGNCi HGNC:6119. IRF4.
HPAi CAB013508.
HPA002038.
HPA002698.
MIMi 254500. phenotype.
601900. gene.
neXtProti NX_Q15306.
PharmGKBi PA29918.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39558.
GeneTreei ENSGT00760000119093.
HOGENOMi HOG000010107.
HOVERGENi HBG003072.
InParanoidi Q15306.
KOi K09445.
OMAi DNGQRKN.
OrthoDBi EOG7CCBR1.
PhylomeDBi Q15306.
TreeFami TF328512.

Enzyme and pathway databases

Reactomei REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Miscellaneous databases

EvolutionaryTracei Q15306.
GeneWikii IRF4.
GenomeRNAii 3662.
NextBioi 14323.
PROi Q15306.
SOURCEi Search...

Gene expression databases

Bgeei Q15306.
CleanExi HS_IRF4.
HS_MUM1.
ExpressionAtlasi Q15306. baseline and differential.
Genevestigatori Q15306.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProi IPR019817. 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 ]
Pfami PF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view ]
PRINTSi PR00267. INTFRNREGFCT.
SMARTi SM00348. IRF. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
PROSITEi PS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human lymphocyte-specific interferon regulatory factor (hLSIRF/hIRF4) and mapping of the gene to 6p23-p25."
    Grossman A., Mittrucker H.W., Nicholl J., Suzuki A., Chung S., Antonio L., Sugga S., Sutherland G.R., Siderovski D.P., Mak T.W.
    Genomics 37:229-233(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Spleen.
  2. "Deregulation of MUM1/IRF4 by chromosomal translocation in multiple myeloma."
    Iida S., Rao P.H., Butler M., Corradini P., Boccadoro M., Klein B., Chaganti R.S.K., Dalla-Favera R.
    Nat. Genet. 17:226-230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MULTIPLE MYELOMA.
    Tissue: Spleen.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  5. "SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1."
    Rao S., Matsumura A., Yoon J., Simon M.C.
    J. Biol. Chem. 274:11115-11124(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPIB.
  6. "Molecular cloning of IBP, a SWAP-70 homologous GEF, which is highly expressed in the immune system."
    Gupta S., Lee A.E., Hu C., Fanzo J.C., Goldberg I., Cattoretti G., Pernis A.B.
    Hum. Immunol. 64:389-401(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DEF6.
    Tissue: Lymph node.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Solution structure of the IRF domain of human interferon regulator factor 4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 22-130.

Entry informationi

Entry nameiIRF4_HUMAN
AccessioniPrimary (citable) accession number: Q15306
Secondary accession number(s): Q5VUI7, Q99660
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3