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P14316

- IRF2_HUMAN

UniProt

P14316 - IRF2_HUMAN

Protein

Interferon regulatory factor 2

Gene

IRF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (11 Feb 2002)
      Previous versions | rss
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    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.4 Publications

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell proliferation Source: ProtInc
    3. cytokine-mediated signaling pathway Source: Reactome
    4. interferon-gamma-mediated signaling pathway Source: Reactome
    5. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW
    8. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    SignaLinkiP14316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon regulatory factor 2
    Short name:
    IRF-2
    Gene namesi
    Name:IRF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6117. IRF2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi75 – 751K → R: Diminished acetylation by both CREBBP/p300 and PCAF. Greatly reduced enhancement of H4 promoter activity. 1 Publication
    Mutagenesisi78 – 781K → R: Greatly diminished acetylation by PCAF. Lesser loss of acetylation by CREBBP/p300. Loss of DNA binding and no enhancement of H4 promoter activity. 1 Publication
    Mutagenesisi137 – 1371K → R: Some loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Additional small loss of sumoylation; when associated with R-166. Great loss of sumoylation; when associated with R-296. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-166 and R-293. 1 Publication
    Mutagenesisi166 – 1661K → R: Little loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Greater loss of sumoylation; when associated with R-137. Further loss of sumoylation; when associated with R-293. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-137 and R-293. 1 Publication
    Mutagenesisi293 – 2931K → R: Some loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Further small loss of sumoylation; when associated with R-166. Great loss of sumoylation; when associated with R-137. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-166 and R-293. 1 Publication

    Organism-specific databases

    PharmGKBiPA29916.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 349349Interferon regulatory factor 2PRO_0000154549Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751N6-acetyllysine1 Publication
    Modified residuei78 – 781N6-acetyllysine1 Publication
    Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki166 – 166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 is required for stimulation of H4 promoter activity.1 Publication
    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.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP14316.
    PaxDbiP14316.
    PRIDEiP14316.

    PTM databases

    PhosphoSiteiP14316.

    Expressioni

    Tissue specificityi

    Expressed throughout the epithelium of the colon. Also expressed in lamina propria.1 Publication

    Inductioni

    By viruses and IFN.

    Gene expression databases

    ArrayExpressiP14316.
    BgeeiP14316.
    CleanExiHS_IRF2.
    GenevestigatoriP14316.

    Organism-specific databases

    HPAiCAB032306.
    HPA030813.

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATG7O953522EBI-2866589,EBI-987834
    FOXK1P850372EBI-2866589,EBI-2509974
    FOXK2Q011672EBI-2866589,EBI-2509991
    PPP3CBP162982EBI-2866589,EBI-1759540

    Protein-protein interaction databases

    BioGridi109868. 27 interactions.
    IntActiP14316. 14 interactions.
    STRINGi9606.ENSP00000377218.

    Structurei

    3D structure databases

    ProteinModelPortaliP14316.
    SMRiP14316. Positions 5-113.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    InParanoidiP14316.
    KOiK10153.
    OMAiSWPPFPD.
    OrthoDBiEOG72ZCFD.
    PhylomeDBiP14316.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P14316-1) [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

    MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK    50
    DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIK 100
    KGNNAFRVYR MLPLSERPSK KGKKPKTEKE DKVKHIKQEP VESSLGLSNG 150
    VSDLSPEYAV LTSTIKNEVD STVNIIVVGQ SHLDSNIENQ EIVTNPPDIC 200
    QVVEVTTESD EQPVSMSELY PLQISPVSSY AESETTDSVP SDEESAEGRP 250
    HWRKRNIEGK QYLSNMGTRG SYLLPGMASF VTSNKPDLQV TIKEESNPVP 300
    YNSSWPPFQD LPLSSSMTPA SSSSRPDRET RASVIKKTSD ITQARVKSC 349
    Length:349
    Mass (Da):39,354
    Last modified:February 11, 2002 - v2
    Checksum:i6298341652466560
    GO
    Isoform 2 (identifier: P14316-2) [UniParc]FASTAAdd to Basket

    Also known as: IRF-2s, IRF-2[S]

    The sequence of this isoform differs from the canonical sequence as follows:
         177-178: Missing.

    Note: Unable to bind to IRF2BP1 and IRF2BP2 corepressors and cannot mediate repression.

    Show »
    Length:347
    Mass (Da):39,156
    Checksum:iEE67F41029BFD6BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581W → R in CAA34073. (PubMed:2813069)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei177 – 1782Missing in isoform 2. CuratedVSP_043965

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15949 mRNA. Translation: CAA34073.1.
    BT007264 mRNA. Translation: AAP35928.1.
    AK312953 mRNA. Translation: BAG35793.1.
    CR457077 mRNA. Translation: CAG33358.1.
    AC099343 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04677.1.
    CH471056 Genomic DNA. Translation: EAX04678.1.
    CH471056 Genomic DNA. Translation: EAX04680.1.
    BC015803 mRNA. Translation: AAH15803.1.
    CCDSiCCDS3835.1. [P14316-1]
    PIRiA53340.
    RefSeqiNP_002190.2. NM_002199.3. [P14316-1]
    XP_005263041.1. XM_005262984.1. [P14316-2]
    UniGeneiHs.654566.

    Genome annotation databases

    EnsembliENST00000393593; ENSP00000377218; ENSG00000168310. [P14316-1]
    GeneIDi3660.
    KEGGihsa:3660.
    UCSCiuc003iwf.4. human. [P14316-1]

    Polymorphism databases

    DMDMi20141499.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15949 mRNA. Translation: CAA34073.1 .
    BT007264 mRNA. Translation: AAP35928.1 .
    AK312953 mRNA. Translation: BAG35793.1 .
    CR457077 mRNA. Translation: CAG33358.1 .
    AC099343 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04677.1 .
    CH471056 Genomic DNA. Translation: EAX04678.1 .
    CH471056 Genomic DNA. Translation: EAX04680.1 .
    BC015803 mRNA. Translation: AAH15803.1 .
    CCDSi CCDS3835.1. [P14316-1 ]
    PIRi A53340.
    RefSeqi NP_002190.2. NM_002199.3. [P14316-1 ]
    XP_005263041.1. XM_005262984.1. [P14316-2 ]
    UniGenei Hs.654566.

    3D structure databases

    ProteinModelPortali P14316.
    SMRi P14316. Positions 5-113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109868. 27 interactions.
    IntActi P14316. 14 interactions.
    STRINGi 9606.ENSP00000377218.

    PTM databases

    PhosphoSitei P14316.

    Polymorphism databases

    DMDMi 20141499.

    Proteomic databases

    MaxQBi P14316.
    PaxDbi P14316.
    PRIDEi P14316.

    Protocols and materials databases

    DNASUi 3660.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393593 ; ENSP00000377218 ; ENSG00000168310 . [P14316-1 ]
    GeneIDi 3660.
    KEGGi hsa:3660.
    UCSCi uc003iwf.4. human. [P14316-1 ]

    Organism-specific databases

    CTDi 3660.
    GeneCardsi GC04M185308.
    H-InvDB HIX0004671.
    HGNCi HGNC:6117. IRF2.
    HPAi CAB032306.
    HPA030813.
    MIMi 147576. gene.
    neXtProti NX_P14316.
    PharmGKBi PA29916.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41436.
    HOGENOMi HOG000037937.
    HOVERGENi HBG003455.
    InParanoidi P14316.
    KOi K10153.
    OMAi SWPPFPD.
    OrthoDBi EOG72ZCFD.
    PhylomeDBi P14316.
    TreeFami TF328512.

    Enzyme and pathway databases

    Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    SignaLinki P14316.

    Miscellaneous databases

    GeneWikii IRF2.
    GenomeRNAii 3660.
    NextBioi 14315.
    PROi P14316.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14316.
    Bgeei P14316.
    CleanExi HS_IRF2.
    Genevestigatori P14316.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR017431. Interferon_reg_fac-1/2.
    IPR019817. Interferon_reg_fac_CS.
    IPR001346. Interferon_reg_fact_DNA-bd_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00605. IRF. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038196. IFN_RF1/2. 1 hit.
    PRINTSi PR00267. INTFRNREGFCT.
    SMARTi SM00348. IRF. 1 hit.
    [Graphical view ]
    PROSITEi PS00601. IRF_1. 1 hit.
    PS51507. IRF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: T-cell.
    2. "Human interferon regulatory factor 2 gene. Intron-exon organization and functional analysis of 5'-flanking region."
      Cha Y., Deisseroth A.B.
      J. Biol. Chem. 269:5279-5287(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Trachea.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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.
    9. "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 gene: mechanistic differences between distinct H4 genes."
      Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., Soprano K.J., Stein J.L., Stein G.S.
      Mol. Biol. Rep. 25:1-12(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, FUNCTION AS AN ACTIVATOR.
    10. "Molecular characterization of celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2."
      Staal A., Enserink J.M., Stein J.L., Stein G.S., van Wijnen A.J.
      J. Cell. Physiol. 185:269-279(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRD7.
    11. "Cloning of an interferon regulatory factor 2 isoform with different regulatory ability."
      Koenig Merediz S.A., Schmidt M., Hoppe G.J., Alfken J., Meraro D., Levi B.Z., Neubauer A., Wittig B.
      Nucleic Acids Res. 28:4219-4224(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    12. "Interferon regulatory factor-2 regulates cell growth through its acetylation."
      Masumi A., Yamakawa Y., Fukazawa H., Ozato K., Komuro K.
      J. Biol. Chem. 278:25401-25407(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-75 AND LYS-78, INTERACTION WITH CREBBP, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-75 AND LYS-78.
    13. "Identification of novel co-repressor molecules for interferon regulatory factor-2."
      Childs K.S., Goodbourn S.
      Nucleic Acids Res. 31:3016-3026(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, INTERACTION WITH IRF2BP1 AND IRF2BP2.
    14. "Interferon regulatory factor 1 (IRF-1) and IRF-2 distinctively up-regulate gene expression and production of interleukin-7 in human intestinal epithelial cells."
      Oshima S., Nakamura T., Namiki S., Okada E., Tsuchiya K., Okamoto R., Yamazaki M., Yokota T., Aida M., Yamaguchi Y., Kanai T., Handa H., Watanabe M.
      Mol. Cell. Biol. 24:6298-6310(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    15. "Regulation of IRF2 transcriptional activity by its sumoylation."
      Han K.-J., Jiang L., Shu H.-B.
      Biochem. Biophys. Res. Commun. 372:772-778(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-137; LYS-166 AND LYS-293, FUNCTION, MUTAGENESIS OF LYS-137; LYS-166 AND LYS-293.

    Entry informationi

    Entry nameiIRF2_HUMAN
    AccessioniPrimary (citable) accession number: P14316
    Secondary accession number(s): D6RCK5
    , H0Y8S3, Q6IAS7, Q96B99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: February 11, 2002
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3