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Interferon regulatory factor 4 (IRF-4) (Lymphocyte-specific interferon regulatory factor) (LSIRF) (Multiple myeloma oncogene 1) (NF-EM5)

 IRF4_HUMAN              Reviewed;         451 AA.
Q15306; Q5VUI7; Q99660;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 180.
RecName: Full=Interferon regulatory factor 4;
Short=IRF-4;
AltName: Full=Lymphocyte-specific interferon regulatory factor;
Short=LSIRF;
AltName: Full=Multiple myeloma oncogene 1;
AltName: Full=NF-EM5;
Name=IRF4; Synonyms=MUM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Spleen;
PubMed=8921401; DOI=10.1006/geno.1996.0547;
Grossman A., Mittrucker H.W., Nicholl J., Suzuki A., Chung S.,
Antonio L., Sugga S., Sutherland G.R., Siderovski D.P., Mak T.W.;
"Cloning of human lymphocyte-specific interferon regulatory factor
(hLSIRF/hIRF4) and mapping of the gene to 6p23-p25.";
Genomics 37:229-233(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN MULTIPLE
MYELOMA.
TISSUE=Spleen;
PubMed=9326949; DOI=10.1038/ng1097-226;
Iida S., Rao P.H., Butler M., Corradini P., Boccadoro M., Klein B.,
Chaganti R.S.K., Dalla-Favera R.;
"Deregulation of MUM1/IRF4 by chromosomal translocation in multiple
myeloma.";
Nat. Genet. 17:226-230(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH SPIB.
PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
Rao S., Matsumura A., Yoon J., Simon M.C.;
"SPI-B activates transcription via a unique proline, serine, and
threonine domain and exhibits DNA binding affinity differences from
PU.1.";
J. Biol. Chem. 274:11115-11124(1999).
[6]
INTERACTION WITH DEF6.
TISSUE=Lymph node;
PubMed=12651066; DOI=10.1016/S0198-8859(03)00024-7;
Gupta S., Lee A.E., Hu C., Fanzo J.C., Goldberg I., Cattoretti G.,
Pernis A.B.;
"Molecular cloning of IBP, a SWAP-70 homologous GEF, which is highly
expressed in the immune system.";
Hum. Immunol. 64:389-401(2003).
[7]
POLYMORPHISM.
PubMed=18483556; DOI=10.1371/journal.pgen.1000074;
Han J., Kraft P., Nan H., Guo Q., Chen C., Qureshi A., Hankinson S.E.,
Hu F.B., Duffy D.L., Zhao Z.Z., Martin N.G., Montgomery G.W.,
Hayward N.K., Thomas G., Hoover R.N., Chanock S., Hunter D.J.;
"A genome-wide association study identifies novel alleles associated
with hair color and skin pigmentation.";
PLoS Genet. 4:E1000074-E1000074(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
POLYMORPHISM.
PubMed=24267888; DOI=10.1016/j.cell.2013.10.022;
Praetorius C., Grill C., Stacey S.N., Metcalf A.M., Gorkin D.U.,
Robinson K.C., Van Otterloo E., Kim R.S., Bergsteinsdottir K.,
Ogmundsdottir M.H., Magnusdottir E., Mishra P.J., Davis S.R., Guo T.,
Zaidi M.R., Helgason A.S., Sigurdsson M.I., Meltzer P.S., Merlino G.,
Petit V., Larue L., Loftus S.K., Adams D.R., Sobhiafshar U.,
Emre N.C., Pavan W.J., Cornell R., Smith A.G., McCallion A.S.,
Fisher D.E., Stefansson K., Sturm R.A., Steingrimsson E.;
"A polymorphism in IRF4 affects human pigmentation through a
tyrosinase-dependent MITF/TFAP2A pathway.";
Cell 155:1022-1033(2013).
[10]
STRUCTURE BY NMR OF 22-130.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the IRF domain of human interferon regulator
factor 4.";
Submitted (OCT-2006) to the PDB data bank.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:Q64287}.
-!- SUBUNIT: Interacts with the BATF-JUNB heterodimer. Interacts with
BATF (via bZIP domain); the interaction is direct (By similarity).
Interacts with SPIB and DEF6. Directly interacts with NLRP3 in the
nucleus of Th2 cells; this interaction enhances IRF4 ability to
bind to the IL4 promoter and is required for optimal IRF4-
dependent IL4 transcription (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q64287, ECO:0000269|PubMed:10196196,
ECO:0000269|PubMed:12651066}.
-!- INTERACTION:
O95163:IKBKAP; NbExp=2; IntAct=EBI-751345, EBI-347559;
P51617:IRAK1; NbExp=2; IntAct=EBI-751345, EBI-358664;
Q86UE8:TLK2; NbExp=2; IntAct=EBI-751345, EBI-1047967;
Q9H6S0:YTHDC2; NbExp=2; IntAct=EBI-751345, EBI-1057466;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15306-1; Sequence=Displayed;
Name=2;
IsoId=Q15306-2; Sequence=VSP_002755;
-!- TISSUE SPECIFICITY: Lymphoid cells.
-!- INDUCTION: Not induced by interferons.
-!- PTM: Phosphorylation by ROCK2 regulates IL-17 and IL-21
production. {ECO:0000250}.
-!- POLYMORPHISM: Genetic variants in IRF4 define the skin/hair/eye
pigmentation variation locus 8 (SHEP8) [MIM:611724]. Hair, eye and
skin pigmentation are among the most visible examples of human
phenotypic variation, with a broad normal range that is subject to
substantial geographic stratification. In the case of skin,
individuals tend to have lighter pigmentation with increasing
distance from the equator. By contrast, the majority of variation
in human eye and hair color is found among individuals of European
ancestry, with most other human populations fixed for brown eyes
and black hair. {ECO:0000269|PubMed:18483556,
ECO:0000269|PubMed:24267888}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:9326949}. 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.
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IRF4ID231ch6p25.html";
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EMBL; U52682; AAC50779.1; -; mRNA.
EMBL; U63738; AAB37258.1; -; mRNA.
EMBL; AL589962; CAH71554.1; -; Genomic_DNA.
EMBL; AL365272; CAH71554.1; JOINED; Genomic_DNA.
EMBL; AL365272; CAH72537.1; -; Genomic_DNA.
EMBL; AL589962; CAH72537.1; JOINED; Genomic_DNA.
EMBL; BC015752; AAH15752.1; -; mRNA.
CCDS; CCDS4469.1; -. [Q15306-1]
RefSeq; NP_001182215.1; NM_001195286.1. [Q15306-2]
RefSeq; NP_002451.2; NM_002460.3. [Q15306-1]
UniGene; Hs.401013; -.
PDB; 2DLL; NMR; -; A=23-130.
PDBsum; 2DLL; -.
ProteinModelPortal; Q15306; -.
SMR; Q15306; -.
BioGrid; 109870; 24.
IntAct; Q15306; 11.
STRING; 9606.ENSP00000370343; -.
iPTMnet; Q15306; -.
PhosphoSitePlus; Q15306; -.
BioMuta; IRF4; -.
DMDM; 2497445; -.
MaxQB; Q15306; -.
PaxDb; Q15306; -.
PeptideAtlas; Q15306; -.
PRIDE; Q15306; -.
DNASU; 3662; -.
Ensembl; ENST00000380956; ENSP00000370343; ENSG00000137265. [Q15306-1]
GeneID; 3662; -.
KEGG; hsa:3662; -.
UCSC; uc003msz.5; human. [Q15306-1]
CTD; 3662; -.
DisGeNET; 3662; -.
EuPathDB; HostDB:ENSG00000137265.14; -.
GeneCards; IRF4; -.
HGNC; HGNC:6119; IRF4.
HPA; CAB013508; -.
HPA; HPA002038; -.
HPA; HPA002698; -.
MIM; 254500; phenotype.
MIM; 601900; gene.
MIM; 611724; phenotype.
neXtProt; NX_Q15306; -.
OpenTargets; ENSG00000137265; -.
PharmGKB; PA29918; -.
eggNOG; ENOG410IES5; Eukaryota.
eggNOG; ENOG411023V; LUCA.
GeneTree; ENSGT00760000119093; -.
HOGENOM; HOG000010107; -.
HOVERGEN; HBG003072; -.
InParanoid; Q15306; -.
KO; K09445; -.
OMA; SDCRLHI; -.
OrthoDB; EOG091G067P; -.
PhylomeDB; Q15306; -.
TreeFam; TF328512; -.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
SIGNOR; Q15306; -.
ChiTaRS; IRF4; human.
EvolutionaryTrace; Q15306; -.
GeneWiki; IRF4; -.
GenomeRNAi; 3662; -.
PRO; PR:Q15306; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000137265; -.
CleanEx; HS_IRF4; -.
CleanEx; HS_MUM1; -.
ExpressionAtlas; Q15306; baseline and differential.
Genevisible; Q15306; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0000788; C:nuclear nucleosome; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; NAS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IEA:Ensembl.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0045082; P:positive regulation of interleukin-10 biosynthetic process; IDA:UniProtKB.
GO; GO:0045368; P:positive regulation of interleukin-13 biosynthetic process; IDA:UniProtKB.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IDA:UniProtKB.
GO; GO:0045404; P:positive regulation of interleukin-4 biosynthetic process; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045622; P:regulation of T-helper cell differentiation; NAS:UniProtKB.
GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd00103; IRF; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.200.10; -; 1.
InterPro; IPR019817; Interferon_reg_fac_CS.
InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
InterPro; IPR019471; Interferon_reg_factor-3.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR11949; PTHR11949; 1.
Pfam; PF00605; IRF; 1.
Pfam; PF10401; IRF-3; 1.
PRINTS; PR00267; INTFRNREGFCT.
SMART; SM00348; IRF; 1.
SMART; SM01243; IRF-3; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS00601; IRF_1; 1.
PROSITE; PS51507; IRF_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing;
Chromosomal rearrangement; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 451 Interferon regulatory factor 4.
/FTId=PRO_0000154556.
DNA_BIND 21 129 IRF tryptophan pentad repeat.
{ECO:0000255|PROSITE-ProRule:PRU00840}.
MOD_RES 447 447 Phosphoserine; by ROCK2.
{ECO:0000250|UniProtKB:Q64287}.
MOD_RES 448 448 Phosphoserine; by ROCK2.
{ECO:0000250|UniProtKB:Q64287}.
VAR_SEQ 165 165 Missing (in isoform 2).
{ECO:0000303|PubMed:8921401}.
/FTId=VSP_002755.
CONFLICT 300 300 Q -> H (in Ref. 2; AAB37258).
{ECO:0000305}.
CONFLICT 306 306 K -> N (in Ref. 2; AAB37258).
{ECO:0000305}.
CONFLICT 333 333 R -> T (in Ref. 2; AAB37258).
{ECO:0000305}.
HELIX 24 34 {ECO:0000244|PDB:2DLL}.
STRAND 37 39 {ECO:0000244|PDB:2DLL}.
STRAND 41 47 {ECO:0000244|PDB:2DLL}.
STRAND 49 53 {ECO:0000244|PDB:2DLL}.
STRAND 60 62 {ECO:0000244|PDB:2DLL}.
HELIX 64 67 {ECO:0000244|PDB:2DLL}.
HELIX 69 78 {ECO:0000244|PDB:2DLL}.
HELIX 90 103 {ECO:0000244|PDB:2DLL}.
STRAND 107 109 {ECO:0000244|PDB:2DLL}.
TURN 111 113 {ECO:0000244|PDB:2DLL}.
STRAND 115 120 {ECO:0000244|PDB:2DLL}.
STRAND 122 127 {ECO:0000244|PDB:2DLL}.
SEQUENCE 451 AA; 51772 MW; 17CD1327C6F5BFFA CRC64;
MNLEGGGRGG EFGMSAVSCG NGKLRQWLID QIDSGKYPGL VWENEEKSIF RIPWKHAGKQ
DYNREEDAAL FKAWALFKGK FREGIDKPDP PTWKTRLRCA LNKSNDFEEL VERSQLDISD
PYKVYRIVPE GAKKGAKQLT LEDPQMSMSH PYTMTTPYPS LPAQQVHNYM MPPLDRSWRD
YVPDQPHPEI PYQCPMTFGP RGHHWQGPAC ENGCQVTGTF YACAPPESQA PGVPTEPSIR
SAEALAFSDC RLHICLYYRE ILVKELTTSS PEGCRISHGH TYDASNLDQV LFPYPEDNGQ
RKNIEKLLSH LERGVVLWMA PDGLYAKRLC QSRIYWDGPL ALCNDRPNKL ERDQTCKLFD
TQQFLSELQA FAHHGRSLPR FQVTLCFGEE FPDPQRQRKL ITAHVEPLLA RQLYYFAQQN
SGHFLRGYDL PEHISNPEDY HRSIRHSSIQ E


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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