DEK_HUMAN
ID DEK_HUMAN Reviewed; 375 AA.
AC P35659; B2R6K6; B4DN37; Q5TGV4; Q5TGV5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Protein DEK;
GN Name=DEK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH
RP NUP214, AND INVOLVEMENT IN ACUTE MYELOID LEUKEMIA.
RC TISSUE=Testis;
RX PubMed=1549122; DOI=10.1128/mcb.12.4.1687-1697.1992;
RA Von Lindern M., Fornerod M., Van Baal S., Jaegle M., De Wit T., Buijs A.,
RA Grosveld G.;
RT "The translocation (6;9), associated with a specific subtype of acute
RT myeloid leukemia, results in the fusion of two genes, dek and can, and the
RT expression of a chimeric, leukemia-specific dek-can mRNA.";
RL Mol. Cell. Biol. 12:1687-1697(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-21; 66-84; 94-100; 112-124; 126-137; 169-177;
RP 179-187; 331-344 AND 349-362, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC)
RP WITH RBM8A; RNPS1; SRRM1 AND ALYREF/THOC4.
RX PubMed=11118221; DOI=10.1093/emboj/19.24.6860;
RA Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.;
RT "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of
RT mRNA exon-exon junctions.";
RL EMBO J. 19:6860-6869(2000).
RN [8]
RP INTERACTION WITH DAXX.
RX PubMed=12140263; DOI=10.1242/jcs.115.16.3319;
RA Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.;
RT "Daxx and histone deacetylase II associate with chromatin through an
RT interaction with core histones and the chromatin-associated protein Dek.";
RL J. Cell Sci. 115:3319-3330(2002).
RN [9]
RP PHOSPHORYLATION AT SER-32; SER-159; THR-199; SER-201; SER-204; SER-243;
RP SER-244; SER-251; SER-287; SER-288; THR-289; THR-290; SER-296; SER-301;
RP SER-303; SER-306 AND SER-307.
RX PubMed=15199154; DOI=10.1128/mcb.24.13.6011-6020.2004;
RA Kappes F., Damoc C., Knippers R., Przybylski M., Pinna L.A., Gruss C.;
RT "Phosphorylation by protein kinase CK2 changes the DNA binding properties
RT of the human chromatin protein DEK.";
RL Mol. Cell. Biol. 24:6011-6020(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-51; SER-227; SER-230;
RP SER-231 AND SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION IN THE B-WICH COMPLEX.
RX PubMed=16603771; DOI=10.1074/jbc.m600233200;
RA Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.;
RT "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear
RT proteins in transcription.";
RL J. Biol. Chem. 281:16264-16271(2006).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17524367; DOI=10.1016/j.bbrc.2007.05.019;
RA Hu H.G., Scholten I., Gruss C., Knippers R.;
RT "The distribution of the DEK protein in mammalian chromatin.";
RL Biochem. Biophys. Res. Commun. 358:1008-1014(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=19695025; DOI=10.1111/j.1365-2443.2009.01324.x;
RA Takata H., Nishijima H., Ogura S., Sakaguchi T., Bubulya P.A.,
RA Mochizuki T., Shibahara K.;
RT "Proteome analysis of human nuclear insoluble fractions.";
RL Genes Cells 14:975-990(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-13; SER-19; SER-32; SER-51; SER-210; SER-230; SER-231;
RP SER-232; SER-306 AND SER-307, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-13; SER-32; SER-51; SER-301; SER-303; SER-306 AND SER-307,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-32; SER-51; SER-72;
RP SER-121; SER-122; SER-301; SER-306 AND SER-307, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-231; SER-232;
RP SER-301; SER-303; SER-306 AND SER-307, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP ADP-RIBOSYLATION AT SER-279.
RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT "Serine ADP-ribosylation depends on HPF1.";
RL Mol. Cell 0:0-0(2017).
RN [25]
RP STRUCTURE BY NMR OF 309-375, AND DNA-BINDING.
RX PubMed=15238633; DOI=10.1110/ps.04797104;
RA Devany M., Kotharu N.P., Matsuo H.;
RT "Solution NMR structure of the C-terminal domain of the human protein
RT DEK.";
RL Protein Sci. 13:2252-2259(2004).
RN [26]
RP STRUCTURE BY NMR OF 78-208, AND DNA-BINDING.
RX PubMed=18227428; DOI=10.1110/ps.073244108;
RA Devany M., Kappes F., Chen K.M., Markovitz D.M., Matsuo H.;
RT "Solution NMR structure of the N-terminal domain of the human DEK
RT protein.";
RL Protein Sci. 17:205-215(2008).
CC -!- FUNCTION: Involved in chromatin organization.
CC {ECO:0000269|PubMed:17524367}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex (EJC)
CC with DEK, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with histones
CC H2A, H2B, H3, H4, acetylated histone H4, non-phosphorylated DAXX and
CC HDAC2. Component of the B-WICH complex, at least composed of
CC SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21.
CC Binds DNA. {ECO:0000269|PubMed:11118221, ECO:0000269|PubMed:12140263,
CC ECO:0000269|PubMed:16603771}.
CC -!- INTERACTION:
CC P35659; P68400: CSNK2A1; NbExp=2; IntAct=EBI-301977, EBI-347804;
CC P35659; Q8N954-2: GPATCH11; NbExp=3; IntAct=EBI-301977, EBI-12178961;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17524367,
CC ECO:0000269|PubMed:19695025}. Note=Enriched in regions where chromatin
CC is decondensed or sparse in the interphase nuclei.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35659-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35659-2; Sequence=VSP_042951;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at relatively high levels.
CC -!- PTM: Phosphorylated by CK2. Phosphorylation fluctuates during the cell
CC cycle with a moderate peak during G(1) phase, and weakens the binding
CC of DEK to DNA. {ECO:0000269|PubMed:15199154}.
CC -!- DISEASE: Note=A chromosomal aberration involving DEK is found in a
CC subset of acute myeloid leukemia (AML); also known as acute non-
CC lymphocytic leukemia (PubMed:1549122). Translocation t(6;9)(p23;q34)
CC with NUP214/CAN (PubMed:1549122). It results in the formation of a DEK-
CC NUP214 fusion gene (PubMed:1549122). {ECO:0000269|PubMed:1549122}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DEKID23.html";
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DR EMBL; X64229; CAA45536.1; -; mRNA.
DR EMBL; AK297749; BAG60099.1; -; mRNA.
DR EMBL; AK312616; BAG35503.1; -; mRNA.
DR EMBL; AL031774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55402.1; -; Genomic_DNA.
DR EMBL; BC035259; AAH35259.1; -; mRNA.
DR CCDS; CCDS34344.1; -. [P35659-1]
DR CCDS; CCDS47382.1; -. [P35659-2]
DR PIR; S26059; S26059.
DR RefSeq; NP_001128181.1; NM_001134709.1. [P35659-2]
DR RefSeq; NP_003463.1; NM_003472.3. [P35659-1]
DR PDB; 1Q1V; NMR; -; A=309-375.
DR PDB; 2JX3; NMR; -; A=78-208.
DR PDBsum; 1Q1V; -.
DR PDBsum; 2JX3; -.
DR AlphaFoldDB; P35659; -.
DR BMRB; P35659; -.
DR SMR; P35659; -.
DR BioGRID; 113643; 133.
DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex.
DR CORUM; P35659; -.
DR IntAct; P35659; 48.
DR MINT; P35659; -.
DR STRING; 9606.ENSP00000380414; -.
DR GlyGen; P35659; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35659; -.
DR MetOSite; P35659; -.
DR PhosphoSitePlus; P35659; -.
DR SwissPalm; P35659; -.
DR BioMuta; DEK; -.
DR DMDM; 544150; -.
DR EPD; P35659; -.
DR jPOST; P35659; -.
DR MassIVE; P35659; -.
DR MaxQB; P35659; -.
DR PaxDb; P35659; -.
DR PeptideAtlas; P35659; -.
DR PRIDE; P35659; -.
DR ProteomicsDB; 55127; -. [P35659-1]
DR ProteomicsDB; 55128; -. [P35659-2]
DR Antibodypedia; 4456; 279 antibodies from 36 providers.
DR DNASU; 7913; -.
DR Ensembl; ENST00000244776.11; ENSP00000244776.7; ENSG00000124795.17. [P35659-2]
DR Ensembl; ENST00000652576.1; ENSP00000498335.1; ENSG00000124795.17. [P35659-1]
DR Ensembl; ENST00000652689.1; ENSP00000498653.1; ENSG00000124795.17. [P35659-1]
DR GeneID; 7913; -.
DR KEGG; hsa:7913; -.
DR MANE-Select; ENST00000652689.1; ENSP00000498653.1; NM_003472.4; NP_003463.1.
DR UCSC; uc003ncr.2; human. [P35659-1]
DR CTD; 7913; -.
DR DisGeNET; 7913; -.
DR GeneCards; DEK; -.
DR HGNC; HGNC:2768; DEK.
DR HPA; ENSG00000124795; Low tissue specificity.
DR MalaCards; DEK; -.
DR MIM; 125264; gene.
DR neXtProt; NX_P35659; -.
DR OpenTargets; ENSG00000124795; -.
DR Orphanet; 402014; Acute myeloid leukemia with t(6;9)(p23;q34).
DR PharmGKB; PA27251; -.
DR VEuPathDB; HostDB:ENSG00000124795; -.
DR eggNOG; KOG2266; Eukaryota.
DR GeneTree; ENSGT00390000017282; -.
DR HOGENOM; CLU_041060_0_1_1; -.
DR InParanoid; P35659; -.
DR OMA; IAPGKGQ; -.
DR OrthoDB; 1505933at2759; -.
DR PhylomeDB; P35659; -.
DR TreeFam; TF324696; -.
DR PathwayCommons; P35659; -.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; P35659; -.
DR SIGNOR; P35659; -.
DR BioGRID-ORCS; 7913; 97 hits in 1094 CRISPR screens.
DR ChiTaRS; DEK; human.
DR EvolutionaryTrace; P35659; -.
DR GeneWiki; DEK_(gene); -.
DR GenomeRNAi; 7913; -.
DR Pharos; P35659; Tbio.
DR PRO; PR:P35659; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P35659; protein.
DR Bgee; ENSG00000124795; Expressed in calcaneal tendon and 205 other tissues.
DR ExpressionAtlas; P35659; baseline and differential.
DR Genevisible; P35659; HS.
DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal.
DR GO; GO:0043292; C:contractile fiber; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IMP:MGI.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0019079; P:viral genome replication; TAS:ProtInc.
DR InterPro; IPR044198; DEK.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR003034; SAP_dom.
DR PANTHER; PTHR13468; PTHR13468; 1.
DR Pfam; PF08766; DEK_C; 1.
DR SMART; SM00513; SAP; 1.
DR PROSITE; PS51998; DEK_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Chromatin regulator; Chromosomal rearrangement; Direct protein sequencing;
KW DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..375
FT /note="Protein DEK"
FT /id="PRO_0000079858"
FT DOMAIN 149..183
FT /note="SAP"
FT DOMAIN 319..375
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DNA_BIND 337..351
FT DNA_BIND 367..371
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 205..221
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 29..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXS3"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 32
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 199
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 201
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 204
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 243
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 244
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 251
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 279
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 287
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 288
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 289
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 290
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 296
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154"
FT MOD_RES 301
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 303
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 306
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 307
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15199154,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 49..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042951"
FT VARIANT 140
FT /note="V -> A (in dbSNP:rs17336208)"
FT /id="VAR_050949"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2JX3"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:2JX3"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:2JX3"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2JX3"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:2JX3"
FT HELIX 140..162
FT /evidence="ECO:0007829|PDB:2JX3"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2JX3"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:2JX3"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2JX3"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:1Q1V"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1Q1V"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:1Q1V"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1Q1V"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:1Q1V"
SQ SEQUENCE 375 AA; 42674 MW; C07D22B37B719A23 CRC64;
MSASAPAAEG EGTPTQPASE KEPEMPGPRE ESEEEEDEDD EEEEEEEKEK SLIVEGKREK
KKVERLTMQV SSLQREPFTI AQGKGQKLCE IERIHFFLSK KKTDELRNLH KLLYNRPGTV
SSLKKNVGQF SGFPFEKGSV QYKKKEEMLK KFRNAMLKSI CEVLDLERSG VNSELVKRIL
NFLMHPKPSG KPLPKSKKTC SKGSKKERNS SGMARKAKRT KCPEILSDES SSDEDEKKNK
EESSDDEDKE SEEEPPKKTA KREKPKQKAT SKSKKSVKSA NVKKADSSTT KKNQNSSKKE
SESEDSSDDE PLIKKLKKPP TDEELKETIK KLLASANLEE VTMKQICKKV YENYPTYDLT
ERKDFIKTTV KELIS
