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Q15306

- IRF4_HUMAN

UniProt

Q15306 - IRF4_HUMAN

Protein

Interferon regulatory factor 4

Gene

IRF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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 binding Source: IntAct
    2. protein-lysine N-methyltransferase activity Source: Ensembl
    3. regulatory region DNA binding Source: InterPro
    4. sequence-specific DNA binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    6. 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

    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

    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

    ArrayExpressiQ15306.
    BgeeiQ15306.
    CleanExiHS_IRF4.
    HS_MUM1.
    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.
    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

    MNLEGGGRGG EFGMSAVSCG NGKLRQWLID QIDSGKYPGL VWENEEKSIF    50
    RIPWKHAGKQ DYNREEDAAL FKAWALFKGK FREGIDKPDP PTWKTRLRCA 100
    LNKSNDFEEL VERSQLDISD PYKVYRIVPE GAKKGAKQLT LEDPQMSMSH 150
    PYTMTTPYPS LPAQQVHNYM MPPLDRSWRD YVPDQPHPEI PYQCPMTFGP 200
    RGHHWQGPAC ENGCQVTGTF YACAPPESQA PGVPTEPSIR SAEALAFSDC 250
    RLHICLYYRE ILVKELTTSS PEGCRISHGH TYDASNLDQV LFPYPEDNGQ 300
    RKNIEKLLSH LERGVVLWMA PDGLYAKRLC QSRIYWDGPL ALCNDRPNKL 350
    ERDQTCKLFD TQQFLSELQA FAHHGRSLPR FQVTLCFGEE FPDPQRQRKL 400
    ITAHVEPLLA RQLYYFAQQN SGHFLRGYDL PEHISNPEDY HRSIRHSSIQ 450
    E 451
    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.
    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

    ArrayExpressi Q15306.
    Bgeei Q15306.
    CleanExi HS_IRF4.
    HS_MUM1.
    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

    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 1, 2014
    This is version 152 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