DEK_MOUSE
ID DEK_MOUSE Reviewed; 380 AA.
AC Q7TNV0; Q80VC5; Q8BZV6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein DEK;
GN Name=Dek;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17524367}.
CC Note=Enriched in regions where chromatin is decondensed or sparse in
CC the interphase nuclei. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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DR EMBL; AK033451; BAC28296.1; -; mRNA.
DR EMBL; BC048844; AAH48844.1; -; mRNA.
DR EMBL; BC055451; AAH55451.1; -; mRNA.
DR CCDS; CCDS26490.1; -.
DR RefSeq; NP_080176.2; NM_025900.2.
DR AlphaFoldDB; Q7TNV0; -.
DR SMR; Q7TNV0; -.
DR BioGRID; 225256; 11.
DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
DR IntAct; Q7TNV0; 3.
DR MINT; Q7TNV0; -.
DR STRING; 10090.ENSMUSP00000021807; -.
DR iPTMnet; Q7TNV0; -.
DR PhosphoSitePlus; Q7TNV0; -.
DR CPTAC; non-CPTAC-3786; -.
DR EPD; Q7TNV0; -.
DR jPOST; Q7TNV0; -.
DR MaxQB; Q7TNV0; -.
DR PaxDb; Q7TNV0; -.
DR PeptideAtlas; Q7TNV0; -.
DR PRIDE; Q7TNV0; -.
DR ProteomicsDB; 279338; -.
DR Antibodypedia; 4456; 279 antibodies from 36 providers.
DR DNASU; 110052; -.
DR Ensembl; ENSMUST00000021807; ENSMUSP00000021807; ENSMUSG00000021377.
DR GeneID; 110052; -.
DR KEGG; mmu:110052; -.
DR UCSC; uc007qhw.2; mouse.
DR CTD; 7913; -.
DR MGI; MGI:1926209; Dek.
DR VEuPathDB; HostDB:ENSMUSG00000021377; -.
DR eggNOG; KOG2266; Eukaryota.
DR GeneTree; ENSGT00390000017282; -.
DR HOGENOM; CLU_041060_0_1_1; -.
DR InParanoid; Q7TNV0; -.
DR OMA; IAPGKGQ; -.
DR OrthoDB; 1505933at2759; -.
DR PhylomeDB; Q7TNV0; -.
DR TreeFam; TF324696; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
DR BioGRID-ORCS; 110052; 6 hits in 111 CRISPR screens.
DR ChiTaRS; Dek; mouse.
DR PRO; PR:Q7TNV0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q7TNV0; protein.
DR Bgee; ENSMUSG00000021377; Expressed in embryonic post-anal tail and 71 other tissues.
DR ExpressionAtlas; Q7TNV0; baseline and differential.
DR Genevisible; Q7TNV0; MM.
DR GO; GO:0110016; C:B-WICH complex; ISO:MGI.
DR GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; ISO:MGI.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IMP:MGI.
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 ADP-ribosylation; Chromatin regulator; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..380
FT /note="Protein DEK"
FT /id="PRO_0000079859"
FT DOMAIN 153..187
FT /note="SAP"
FT DOMAIN 324..380
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DNA_BIND 342..356
FT /evidence="ECO:0000250"
FT DNA_BIND 372..376
FT /evidence="ECO:0000250"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 209..225
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 30..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 284
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 294
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT CONFLICT 97
FT /note="R -> S (in Ref. 2; AAH48844)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="Y -> C (in Ref. 1; BAC28296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43159 MW; CE1F01CA16CE5AC1 CRC64;
MSAAAAPAAE GEDAPVPPSS EKEPEMPGPR EESEEEEEDD EDDDEEDEEE EKEKSLIVEG
KREKKKVERL TMQVSSLQRE PFTVTQGKGQ KLCEIERIHF FLSKKKPDEL RNLHKLLYNR
PGTVSSLKKN VGQFSGFPFE KGSTQYKKKE EMLKKFRNAM LKSICEVLDL ERSGVNSELV
KRILNFLMHP KPSGKPLPKS KKSSSKGSKK ERNSSGTTRK SKQTKCPEIL SDESSSDEDE
KKNKEESSED EEKESEEEQP PKKTSKKEKA KQKATAKSKK SVKSANVKKA DSSTTKKNQK
SSKKESESED SSDDEPLIKK LKKPPTDEEL KETVKKLLAD ANLEEVTMKQ ICKEVYENYP
AYDLTERKDF IKTTVKELIS
