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Protein

Protein DEK

Gene

Dek

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1926209. Dek.

Subcellular locationi

GO - Cellular componenti

  • contractile fiber Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

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

BgeeiQ7TNV0.
CleanExiMM_DEK.
ExpressionAtlasiQ7TNV0. baseline and differential.
GenevisibleiQ7TNV0. MM.

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. 2 interactions.
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.
OMAiKNQNSSR.
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

        10         20         30         40         50
MSAAAAPAAE GEDAPVPPSS EKEPEMPGPR EESEEEEEDD EDDDEEDEEE
60 70 80 90 100
EKEKSLIVEG KREKKKVERL TMQVSSLQRE PFTVTQGKGQ KLCEIERIHF
110 120 130 140 150
FLSKKKPDEL RNLHKLLYNR PGTVSSLKKN VGQFSGFPFE KGSTQYKKKE
160 170 180 190 200
EMLKKFRNAM LKSICEVLDL ERSGVNSELV KRILNFLMHP KPSGKPLPKS
210 220 230 240 250
KKSSSKGSKK ERNSSGTTRK SKQTKCPEIL SDESSSDEDE KKNKEESSED
260 270 280 290 300
EEKESEEEQP PKKTSKKEKA KQKATAKSKK SVKSANVKKA DSSTTKKNQK
310 320 330 340 350
SSKKESESED SSDDEPLIKK LKKPPTDEEL KETVKKLLAD ANLEEVTMKQ
360 370 380
ICKEVYENYP AYDLTERKDF IKTTVKELIS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi225256. 1 interaction.
IntActiQ7TNV0. 2 interactions.
MINTiMINT-1868135.
STRINGi10090.ENSMUSP00000021807.

PTM databases

PhosphoSiteiQ7TNV0.

Proteomic databases

MaxQBiQ7TNV0.
PaxDbiQ7TNV0.
PRIDEiQ7TNV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7913.
MGIiMGI:1926209. Dek.

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiDek. mouse.
NextBioi363227.
PROiQ7TNV0.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TNV0.
CleanExiMM_DEK.
ExpressionAtlasiQ7TNV0. baseline and differential.
GenevisibleiQ7TNV0. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.