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Q7TNV0 (DEK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein DEK
Gene names
Name:Dek
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in chromatin organization. Ref.3

Subunit structure

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.

Subcellular location

Nucleus. Note: Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei By similarity. Ref.3

Post-translational modification

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.

Sequence similarities

Contains 1 SAP domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionChromatin regulator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype PubMed 21653549. Source: MGI

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Protein DEK
PRO_0000079859

Regions

Domain153 – 18735SAP
DNA binding342 – 35615 By similarity
DNA binding372 – 3765 By similarity
Motif209 – 22517Nuclear localization signal Potential
Compositional bias31 – 5323Asp/Glu-rich (highly acidic)
Compositional bias232 – 2409Asp/Glu-rich (acidic)
Compositional bias245 – 25814Asp/Glu-rich (acidic)
Compositional bias305 – 31511Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue201Phosphoserine By similarity
Modified residue331Phosphoserine By similarity
Modified residue551Phosphoserine By similarity
Modified residue1631Phosphoserine By similarity
Modified residue2051Phosphoserine By similarity
Modified residue2081Phosphoserine By similarity
Modified residue2141Phosphoserine By similarity
Modified residue2311Phosphoserine Ref.5
Modified residue2341Phosphoserine Ref.5
Modified residue2351Phosphoserine Ref.5
Modified residue2361Phosphoserine Ref.5
Modified residue2471Phosphoserine Ref.4 Ref.5
Modified residue2481Phosphoserine Ref.4 Ref.5
Modified residue2551Phosphoserine Ref.4
Modified residue2921Phosphoserine By similarity
Modified residue2931Phosphoserine By similarity
Modified residue2941Phosphothreonine By similarity
Modified residue2951Phosphothreonine By similarity
Modified residue3011Phosphoserine By similarity
Modified residue3061Phosphoserine Ref.4 Ref.5
Modified residue3081Phosphoserine Ref.4 Ref.5
Modified residue3111Phosphoserine Ref.4 Ref.5
Modified residue3121Phosphoserine Ref.4 Ref.5

Experimental info

Sequence conflict971R → S in AAH48844. Ref.2
Sequence conflict3621Y → C in BAC28296. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7TNV0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: CE1F01CA16CE5AC1

FASTA38043,159
        10         20         30         40         50         60 
MSAAAAPAAE GEDAPVPPSS EKEPEMPGPR EESEEEEEDD EDDDEEDEEE EKEKSLIVEG 

        70         80         90        100        110        120 
KREKKKVERL TMQVSSLQRE PFTVTQGKGQ KLCEIERIHF FLSKKKPDEL RNLHKLLYNR 

       130        140        150        160        170        180 
PGTVSSLKKN VGQFSGFPFE KGSTQYKKKE EMLKKFRNAM LKSICEVLDL ERSGVNSELV 

       190        200        210        220        230        240 
KRILNFLMHP KPSGKPLPKS KKSSSKGSKK ERNSSGTTRK SKQTKCPEIL SDESSSDEDE 

       250        260        270        280        290        300 
KKNKEESSED EEKESEEEQP PKKTSKKEKA KQKATAKSKK SVKSANVKKA DSSTTKKNQK 

       310        320        330        340        350        360 
SSKKESESED SSDDEPLIKK LKKPPTDEEL KETVKKLLAD ANLEEVTMKQ ICKEVYENYP 

       370        380 
AYDLTERKDF IKTTVKELIS

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-248; SER-255; SER-306; SER-308; SER-311 AND SER-312, MASS SPECTROMETRY.
Tissue: Teratocarcinoma.
[5]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-234; SER-235; SER-236; SER-247; SER-248; SER-306; SER-308; SER-311 AND SER-312, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK033451 mRNA. Translation: BAC28296.1.
BC048844 mRNA. Translation: AAH48844.1.
BC055451 mRNA. Translation: AAH55451.1.
IPIIPI00227720.
RefSeqNP_080176.2. NM_025900.2.
UniGeneMm.131150.

3D structure databases

ProteinModelPortalQ7TNV0.
SMRQ7TNV0. Positions 82-191, 314-380.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1868135.
STRING10090.ENSMUSP00000021807.

PTM databases

PhosphoSiteQ7TNV0.

Proteomic databases

PaxDbQ7TNV0.
PRIDEQ7TNV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021807; ENSMUSP00000021807; ENSMUSG00000021377.
GeneID110052.
KEGGmmu:110052.
UCSCuc007qhw.2. mouse.

Organism-specific databases

CTD7913.
MGIMGI:1926209. Dek.

Phylogenomic databases

eggNOGNOG328552.
GeneTreeENSGT00390000017282.
HOGENOMHOG000059552.
HOVERGENHBG004944.
InParanoidQ7TNV0.
OMANDPHEED.
OrthoDBEOG4HHP3C.

Gene expression databases

ArrayExpressQ7TNV0.
BgeeQ7TNV0.
CleanExMM_DEK.
GenevestigatorQ7TNV0.
GermOnlineENSMUSG00000021377. Mus musculus.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR014876. DEK_C.
IPR009057. Homeodomain-like.
IPR003034. SAP_dom.
[Graphical view]
PfamPF08766. DEK_C. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. False negative.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDEK. mouse.
NextBio363227.
SOURCESearch...

Entry information

Entry nameDEK_MOUSE
AccessionPrimary (citable) accession number: Q7TNV0
Secondary accession number(s): Q80VC5, Q8BZV6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2003
Last modified: May 29, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents