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P35659

- DEK_HUMAN

UniProt

P35659 - DEK_HUMAN

Protein

Protein DEK

Gene

DEK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Involved in chromatin organization.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi337 – 35115Add
    BLAST
    DNA bindingi367 – 3715

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. regulation of double-strand break repair Source: MGI
    3. regulation of double-strand break repair via nonhomologous end joining Source: Ensembl
    4. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    5. signal transduction Source: ProtInc
    6. transcription from RNA polymerase II promoter Source: ProtInc
    7. viral genome replication Source: ProtInc

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein DEK
    Gene namesi
    Name:DEK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2768. DEK.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei.

    GO - Cellular componenti

    1. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving DEK is found in a subset of acute myeloid leukemia (AML); also known as acute non-lymphocytic leukemia. Translocation t(6;9)(p23;q34) with NUP214/CAN. It results in the formation of a DEK-CAN fusion gene.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti98277. Acute myeloid leukemia with recurrent genetic anomaly.
    PharmGKBiPA27251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 375374Protein DEKPRO_0000079858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine5 Publications
    Modified residuei13 – 131Phosphothreonine2 Publications
    Modified residuei19 – 191Phosphoserine1 Publication
    Modified residuei32 – 321Phosphoserine; by CK25 Publications
    Modified residuei51 – 511Phosphoserine3 Publications
    Modified residuei159 – 1591Phosphoserine; by CK21 Publication
    Modified residuei199 – 1991Phosphothreonine; by CK21 Publication
    Modified residuei201 – 2011Phosphoserine; by CK21 Publication
    Modified residuei204 – 2041Phosphoserine; by CK21 Publication
    Modified residuei210 – 2101Phosphoserine1 Publication
    Modified residuei227 – 2271Phosphoserine1 Publication
    Modified residuei230 – 2301Phosphoserine2 Publications
    Modified residuei231 – 2311Phosphoserine2 Publications
    Modified residuei232 – 2321Phosphoserine2 Publications
    Modified residuei243 – 2431Phosphoserine; by CK21 Publication
    Modified residuei244 – 2441Phosphoserine; by CK21 Publication
    Modified residuei251 – 2511Phosphoserine; by CK21 Publication
    Modified residuei287 – 2871Phosphoserine; by CK21 Publication
    Modified residuei288 – 2881Phosphoserine; by CK21 Publication
    Modified residuei289 – 2891Phosphothreonine; by CK21 Publication
    Modified residuei290 – 2901Phosphothreonine; by CK21 Publication
    Modified residuei296 – 2961Phosphoserine; by CK21 Publication
    Modified residuei301 – 3011Phosphoserine; by CK22 Publications
    Modified residuei303 – 3031Phosphoserine; by CK22 Publications
    Modified residuei306 – 3061Phosphoserine; by CK23 Publications
    Modified residuei307 – 3071Phosphoserine; by CK24 Publications

    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.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP35659.
    PaxDbiP35659.
    PeptideAtlasiP35659.
    PRIDEiP35659.

    PTM databases

    PhosphoSiteiP35659.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expressed at relatively high levels.

    Gene expression databases

    ArrayExpressiP35659.
    BgeeiP35659.
    CleanExiHS_DEK.
    GenevestigatoriP35659.

    Organism-specific databases

    HPAiCAB015226.

    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.3 Publications

    Protein-protein interaction databases

    BioGridi113643. 45 interactions.
    IntActiP35659. 10 interactions.
    MINTiMINT-2802925.
    STRINGi9606.ENSP00000380414.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni88 – 903
    Helixi92 – 998
    Helixi103 – 11210
    Beta strandi114 – 1163
    Helixi121 – 1288
    Helixi140 – 16223
    Turni163 – 1653
    Helixi172 – 18110
    Turni182 – 1843
    Helixi322 – 33312
    Helixi338 – 3403
    Helixi343 – 35311
    Beta strandi355 – 3573
    Helixi361 – 37515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q1VNMR-A309-375[»]
    2JX3NMR-A78-208[»]
    ProteinModelPortaliP35659.
    SMRiP35659. Positions 78-187, 309-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35659.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini149 – 18335SAPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi205 – 22117Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi30 – 4920Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi228 – 2369Asp/Glu-rich (acidic)
    Compositional biasi241 – 25414Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi300 – 31011Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Contains 1 SAP domain.Curated

    Phylogenomic databases

    eggNOGiNOG328552.
    HOGENOMiHOG000059552.
    HOVERGENiHBG004944.
    InParanoidiP35659.
    KOiK17046.
    OMAiAKRTKYP.
    OrthoDBiEOG7TF7C2.
    PhylomeDBiP35659.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35659-1) [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

    MSASAPAAEG EGTPTQPASE KEPEMPGPRE ESEEEEDEDD EEEEEEEKEK    50
    SLIVEGKREK KKVERLTMQV SSLQREPFTI AQGKGQKLCE IERIHFFLSK 100
    KKTDELRNLH KLLYNRPGTV SSLKKNVGQF SGFPFEKGSV QYKKKEEMLK 150
    KFRNAMLKSI CEVLDLERSG VNSELVKRIL NFLMHPKPSG KPLPKSKKTC 200
    SKGSKKERNS SGMARKAKRT KCPEILSDES SSDEDEKKNK EESSDDEDKE 250
    SEEEPPKKTA KREKPKQKAT SKSKKSVKSA NVKKADSSTT KKNQNSSKKE 300
    SESEDSSDDE PLIKKLKKPP TDEELKETIK KLLASANLEE VTMKQICKKV 350
    YENYPTYDLT ERKDFIKTTV KELIS 375
    Length:375
    Mass (Da):42,674
    Last modified:June 1, 1994 - v1
    Checksum:iC07D22B37B719A23
    GO
    Isoform 2 (identifier: P35659-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         49-82: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:341
    Mass (Da):38,705
    Checksum:i7BA02406C674EDD4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401V → A.
    Corresponds to variant rs17336208 [ dbSNP | Ensembl ].
    VAR_050949

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei49 – 8234Missing in isoform 2. 1 PublicationVSP_042951Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64229 mRNA. Translation: CAA45536.1.
    AK297749 mRNA. Translation: BAG60099.1.
    AK312616 mRNA. Translation: BAG35503.1.
    AL031774 Genomic DNA. Translation: CAI20082.2.
    CH471087 Genomic DNA. Translation: EAW55402.1.
    BC035259 mRNA. Translation: AAH35259.1.
    CCDSiCCDS34344.1. [P35659-1]
    CCDS47382.1. [P35659-2]
    PIRiS26059.
    RefSeqiNP_001128181.1. NM_001134709.1. [P35659-2]
    NP_003463.1. NM_003472.3. [P35659-1]
    UniGeneiHs.484813.

    Genome annotation databases

    EnsembliENST00000244776; ENSP00000244776; ENSG00000124795. [P35659-2]
    ENST00000397239; ENSP00000380414; ENSG00000124795. [P35659-1]
    GeneIDi7913.
    KEGGihsa:7913.
    UCSCiuc003ncr.1. human. [P35659-1]
    uc011djf.1. human. [P35659-2]

    Polymorphism databases

    DMDMi544150.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64229 mRNA. Translation: CAA45536.1 .
    AK297749 mRNA. Translation: BAG60099.1 .
    AK312616 mRNA. Translation: BAG35503.1 .
    AL031774 Genomic DNA. Translation: CAI20082.2 .
    CH471087 Genomic DNA. Translation: EAW55402.1 .
    BC035259 mRNA. Translation: AAH35259.1 .
    CCDSi CCDS34344.1. [P35659-1 ]
    CCDS47382.1. [P35659-2 ]
    PIRi S26059.
    RefSeqi NP_001128181.1. NM_001134709.1. [P35659-2 ]
    NP_003463.1. NM_003472.3. [P35659-1 ]
    UniGenei Hs.484813.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q1V NMR - A 309-375 [» ]
    2JX3 NMR - A 78-208 [» ]
    ProteinModelPortali P35659.
    SMRi P35659. Positions 78-187, 309-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113643. 45 interactions.
    IntActi P35659. 10 interactions.
    MINTi MINT-2802925.
    STRINGi 9606.ENSP00000380414.

    PTM databases

    PhosphoSitei P35659.

    Polymorphism databases

    DMDMi 544150.

    Proteomic databases

    MaxQBi P35659.
    PaxDbi P35659.
    PeptideAtlasi P35659.
    PRIDEi P35659.

    Protocols and materials databases

    DNASUi 7913.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244776 ; ENSP00000244776 ; ENSG00000124795 . [P35659-2 ]
    ENST00000397239 ; ENSP00000380414 ; ENSG00000124795 . [P35659-1 ]
    GeneIDi 7913.
    KEGGi hsa:7913.
    UCSCi uc003ncr.1. human. [P35659-1 ]
    uc011djf.1. human. [P35659-2 ]

    Organism-specific databases

    CTDi 7913.
    GeneCardsi GC06M018224.
    HGNCi HGNC:2768. DEK.
    HPAi CAB015226.
    MIMi 125264. gene.
    neXtProti NX_P35659.
    Orphaneti 98277. Acute myeloid leukemia with recurrent genetic anomaly.
    PharmGKBi PA27251.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG328552.
    HOGENOMi HOG000059552.
    HOVERGENi HBG004944.
    InParanoidi P35659.
    KOi K17046.
    OMAi AKRTKYP.
    OrthoDBi EOG7TF7C2.
    PhylomeDBi P35659.
    TreeFami TF324696.

    Miscellaneous databases

    ChiTaRSi DEK. human.
    EvolutionaryTracei P35659.
    GeneWikii DEK_(gene).
    GenomeRNAii 7913.
    NextBioi 30376.
    PROi P35659.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35659.
    Bgeei P35659.
    CleanExi HS_DEK.
    Genevestigatori P35659.

    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 translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA."
      Von Lindern M., Fornerod M., Van Baal S., Jaegle M., De Wit T., Buijs A., Grosveld G.
      Mol. Cell. Biol. 12:1687-1697(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Cervix.
    6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-21; 66-84; 94-100; 112-124; 126-137; 169-177; 179-187; 331-344 AND 349-362, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
      Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
      EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RBM8A; RNPS1; SRRM1 AND ALYREF/THOC4.
    8. "Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
      Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
      J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAXX.
    9. "Phosphorylation by protein kinase CK2 changes the DNA binding properties of the human chromatin protein DEK."
      Kappes F., Damoc C., Knippers R., Przybylski M., Pinna L.A., Gruss C.
      Mol. Cell. Biol. 24:6011-6020(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-32; SER-159; THR-199; SER-201; SER-204; SER-243; SER-244; SER-251; SER-287; SER-288; THR-289; THR-290; SER-296; SER-301; SER-303; SER-306 AND SER-307.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-51; SER-227; SER-230; SER-231 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
      Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
      J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
    12. "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.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: SUBCELLULAR LOCATION.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-19; SER-32; SER-51; SER-210; SER-230; SER-231; SER-232; SER-306 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-32; SER-51; SER-301; SER-303; SER-306 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Solution NMR structure of the C-terminal domain of the human protein DEK."
      Devany M., Kotharu N.P., Matsuo H.
      Protein Sci. 13:2252-2259(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 309-375, DNA-BINDING.
    22. "Solution NMR structure of the N-terminal domain of the human DEK protein."
      Devany M., Kappes F., Chen K.M., Markovitz D.M., Matsuo H.
      Protein Sci. 17:205-215(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 78-208, DNA-BINDING.

    Entry informationi

    Entry nameiDEK_HUMAN
    AccessioniPrimary (citable) accession number: P35659
    Secondary accession number(s): B2R6K6
    , B4DN37, Q5TGV4, Q5TGV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 143 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3