DEK_RAT
ID DEK_RAT Reviewed; 378 AA.
AC Q6AXS3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein DEK;
GN Name=Dek;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16; SER-20; SER-33; SER-245;
RP SER-246; SER-253 AND SER-310, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in chromatin organization. {ECO:0000250}.
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. Note=Enriched in regions where chromatin
CC is decondensed or sparse in 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; BC079344; AAH79344.1; -; mRNA.
DR RefSeq; NP_001004255.1; NM_001004255.1.
DR AlphaFoldDB; Q6AXS3; -.
DR BMRB; Q6AXS3; -.
DR SMR; Q6AXS3; -.
DR BioGRID; 258556; 1.
DR IntAct; Q6AXS3; 5.
DR STRING; 10116.ENSRNOP00000021751; -.
DR iPTMnet; Q6AXS3; -.
DR PhosphoSitePlus; Q6AXS3; -.
DR jPOST; Q6AXS3; -.
DR PaxDb; Q6AXS3; -.
DR PRIDE; Q6AXS3; -.
DR Ensembl; ENSRNOT00000021751; ENSRNOP00000021751; ENSRNOG00000016152.
DR GeneID; 306817; -.
DR KEGG; rno:306817; -.
DR CTD; 7913; -.
DR RGD; 1303246; Dek.
DR eggNOG; KOG2266; Eukaryota.
DR GeneTree; ENSGT00390000017282; -.
DR HOGENOM; CLU_041060_0_1_1; -.
DR InParanoid; Q6AXS3; -.
DR OMA; IAPGKGQ; -.
DR OrthoDB; 1505933at2759; -.
DR PhylomeDB; Q6AXS3; -.
DR TreeFam; TF324696; -.
DR Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-RNO-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
DR PRO; PR:Q6AXS3; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016152; Expressed in thymus and 20 other tissues.
DR Genevisible; Q6AXS3; RN.
DR GO; GO:0110016; C:B-WICH complex; ISO:RGD.
DR GO; GO:0043292; C:contractile fiber; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:RGD.
DR GO; GO:2000779; P:regulation of double-strand break repair; ISO:RGD.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; ISO:RGD.
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..378
FT /note="Protein DEK"
FT /id="PRO_0000079860"
FT DOMAIN 149..183
FT /note="SAP"
FT DOMAIN 322..378
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DNA_BIND 340..354
FT /evidence="ECO:0000250"
FT DNA_BIND 370..374
FT /evidence="ECO:0000250"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..223
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 30..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 233
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 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 282
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 304
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 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 378 AA; 42892 MW; E3FE3DA24D0D2B05 CRC64;
MSAAAAPAAE GEDTPTPPAS EKEPEMPGPR EESEEEEEED DDDEDEEEEK EKSLIVEGKR
EKRKVERLTM QVSSLQREPF TIAQGKGQKL CEIERIHFFL SKKKTDELRN LHKLLYNRPG
TVSSLKKNVG QFSGFPFEKG STQYKKKEEM LKKYRNAMLK SICEVLDLER SGVNSELVKR
ILNFLMHPKP SGKPLPKSKK SSSKGSKKER NSSGTTRKSK QTKCPEILSD ESSSDEDEKK
NKDESSEDEE KESEEEQPPK KTSKKEKAKQ KATTKSKKSV KSANVKKADS STTKKNQNSS
KKESGSEDSS DDEPLIKKLK KPPTDEELKE TVKKLLADAN LEEVTMKQIC KEVYENYPAY
DLTERKDFIK TTVKELIS
