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Q7TNV0

- DEK_MOUSE

UniProt

Q7TNV0 - DEK_MOUSE

Protein

Protein DEK

Gene

Dek

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Involved in chromatin organization.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi342 – 35615By similarityAdd
    BLAST
    DNA bindingi372 – 3765By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. regulation of double-strand break repair via nonhomologous end joining Source: MGI

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein DEK
    Gene namesi
    Name:Dek
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1926209. Dek.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei.By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380Protein DEKPRO_0000079859Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201PhosphoserineBy similarity
    Modified residuei33 – 331Phosphoserine1 Publication
    Modified residuei55 – 551Phosphoserine1 Publication
    Modified residuei163 – 1631PhosphoserineBy similarity
    Modified residuei205 – 2051PhosphoserineBy similarity
    Modified residuei208 – 2081PhosphoserineBy similarity
    Modified residuei214 – 2141PhosphoserineBy similarity
    Modified residuei231 – 2311PhosphoserineBy similarity
    Modified residuei234 – 2341PhosphoserineBy similarity
    Modified residuei235 – 2351PhosphoserineBy similarity
    Modified residuei236 – 2361PhosphoserineBy similarity
    Modified residuei247 – 2471PhosphoserineBy similarity
    Modified residuei248 – 2481PhosphoserineBy similarity
    Modified residuei255 – 2551PhosphoserineBy similarity
    Modified residuei292 – 2921PhosphoserineBy similarity
    Modified residuei293 – 2931PhosphoserineBy similarity
    Modified residuei294 – 2941PhosphothreonineBy similarity
    Modified residuei295 – 2951PhosphothreonineBy similarity
    Modified residuei301 – 3011PhosphoserineBy similarity
    Modified residuei306 – 3061PhosphoserineBy similarity
    Modified residuei308 – 3081PhosphoserineBy similarity
    Modified residuei311 – 3111PhosphoserineBy similarity
    Modified residuei312 – 3121PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by CK2. Phosphorylation fluctuates during the cell cycle with a moderate peak during G1 phase, and weakens the binding of DEK to DNA By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7TNV0.
    PaxDbiQ7TNV0.
    PRIDEiQ7TNV0.

    PTM databases

    PhosphoSiteiQ7TNV0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7TNV0.
    BgeeiQ7TNV0.
    CleanExiMM_DEK.
    GenevestigatoriQ7TNV0.

    Interactioni

    Subunit structurei

    Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with histones H2A, H2B, H3, H4, acetylated histone H4, non-phosphorylated DAXX and HDAC2. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Binds DNA By similarity.By similarity

    Protein-protein interaction databases

    BioGridi225256. 1 interaction.
    IntActiQ7TNV0. 1 interaction.
    MINTiMINT-1868135.
    STRINGi10090.ENSMUSP00000021807.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TNV0.
    SMRiQ7TNV0. Positions 82-191, 314-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini153 – 18735SAPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi209 – 22517Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi31 – 5323Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi232 – 2409Asp/Glu-rich (acidic)
    Compositional biasi245 – 25814Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi305 – 31511Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Contains 1 SAP domain.Curated

    Phylogenomic databases

    eggNOGiNOG328552.
    GeneTreeiENSGT00390000017282.
    HOGENOMiHOG000059552.
    HOVERGENiHBG004944.
    InParanoidiQ7TNV0.
    KOiK17046.
    OMAiNDPHEED.
    OrthoDBiEOG7TF7C2.
    PhylomeDBiQ7TNV0.
    TreeFamiTF324696.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR014876. DEK_C.
    IPR009057. Homeodomain-like.
    IPR003034. SAP_dom.
    [Graphical view]
    PfamiPF08766. DEK_C. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view]
    SMARTiSM00513. SAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7TNV0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAAAAPAAE GEDAPVPPSS EKEPEMPGPR EESEEEEEDD EDDDEEDEEE    50
    EKEKSLIVEG KREKKKVERL TMQVSSLQRE PFTVTQGKGQ KLCEIERIHF 100
    FLSKKKPDEL RNLHKLLYNR PGTVSSLKKN VGQFSGFPFE KGSTQYKKKE 150
    EMLKKFRNAM LKSICEVLDL ERSGVNSELV KRILNFLMHP KPSGKPLPKS 200
    KKSSSKGSKK ERNSSGTTRK SKQTKCPEIL SDESSSDEDE KKNKEESSED 250
    EEKESEEEQP PKKTSKKEKA KQKATAKSKK SVKSANVKKA DSSTTKKNQK 300
    SSKKESESED SSDDEPLIKK LKKPPTDEEL KETVKKLLAD ANLEEVTMKQ 350
    ICKEVYENYP AYDLTERKDF IKTTVKELIS 380
    Length:380
    Mass (Da):43,159
    Last modified:October 1, 2003 - v1
    Checksum:iCE1F01CA16CE5AC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971R → S in AAH48844. (PubMed:15489334)Curated
    Sequence conflicti362 – 3621Y → C in BAC28296. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033451 mRNA. Translation: BAC28296.1.
    BC048844 mRNA. Translation: AAH48844.1.
    BC055451 mRNA. Translation: AAH55451.1.
    CCDSiCCDS26490.1.
    RefSeqiNP_080176.2. NM_025900.2.
    UniGeneiMm.131150.

    Genome annotation databases

    EnsembliENSMUST00000021807; ENSMUSP00000021807; ENSMUSG00000021377.
    GeneIDi110052.
    KEGGimmu:110052.
    UCSCiuc007qhw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033451 mRNA. Translation: BAC28296.1 .
    BC048844 mRNA. Translation: AAH48844.1 .
    BC055451 mRNA. Translation: AAH55451.1 .
    CCDSi CCDS26490.1.
    RefSeqi NP_080176.2. NM_025900.2.
    UniGenei Mm.131150.

    3D structure databases

    ProteinModelPortali Q7TNV0.
    SMRi Q7TNV0. Positions 82-191, 314-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 225256. 1 interaction.
    IntActi Q7TNV0. 1 interaction.
    MINTi MINT-1868135.
    STRINGi 10090.ENSMUSP00000021807.

    PTM databases

    PhosphoSitei Q7TNV0.

    Proteomic databases

    MaxQBi Q7TNV0.
    PaxDbi Q7TNV0.
    PRIDEi Q7TNV0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021807 ; ENSMUSP00000021807 ; ENSMUSG00000021377 .
    GeneIDi 110052.
    KEGGi mmu:110052.
    UCSCi uc007qhw.2. mouse.

    Organism-specific databases

    CTDi 7913.
    MGIi MGI:1926209. Dek.

    Phylogenomic databases

    eggNOGi NOG328552.
    GeneTreei ENSGT00390000017282.
    HOGENOMi HOG000059552.
    HOVERGENi HBG004944.
    InParanoidi Q7TNV0.
    KOi K17046.
    OMAi NDPHEED.
    OrthoDBi EOG7TF7C2.
    PhylomeDBi Q7TNV0.
    TreeFami TF324696.

    Miscellaneous databases

    ChiTaRSi DEK. mouse.
    NextBioi 363227.
    PROi Q7TNV0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7TNV0.
    Bgeei Q7TNV0.
    CleanExi MM_DEK.
    Genevestigatori Q7TNV0.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR014876. DEK_C.
    IPR009057. Homeodomain-like.
    IPR003034. SAP_dom.
    [Graphical view ]
    Pfami PF08766. DEK_C. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view ]
    SMARTi SM00513. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Colon.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary gland and Salivary gland.
    3. "The distribution of the DEK protein in mammalian chromatin."
      Hu H.G., Scholten I., Gruss C., Knippers R.
      Biochem. Biophys. Res. Commun. 358:1008-1014(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiDEK_MOUSE
    AccessioniPrimary (citable) accession number: Q7TNV0
    Secondary accession number(s): Q80VC5, Q8BZV6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3