Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein DEK

Gene

Dek

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in chromatin organization.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi340 – 35415By similarityAdd
BLAST
DNA bindingi370 – 3745By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-5250924. B-WICH complex positively regulates rRNA expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DEK
Gene namesi
Name:Dek
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1303246. Dek.

Subcellular locationi

  • Nucleus

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Protein DEKPRO_0000079860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei16 – 161PhosphothreonineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei33 – 331PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineBy similarity
Modified residuei161 – 1611PhosphoserineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei232 – 2321PhosphoserineBy similarity
Modified residuei233 – 2331PhosphoserineBy similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineCombined sources
Modified residuei246 – 2461PhosphoserineCombined sources
Modified residuei253 – 2531PhosphoserineCombined sources
Modified residuei290 – 2901PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei292 – 2921PhosphothreonineBy similarity
Modified residuei293 – 2931PhosphothreonineBy similarity
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei304 – 3041PhosphoserineBy similarity
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei309 – 3091PhosphoserineBy similarity
Modified residuei310 – 3101PhosphoserineCombined sources

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

PaxDbiQ6AXS3.
PRIDEiQ6AXS3.

PTM databases

iPTMnetiQ6AXS3.
PhosphoSiteiQ6AXS3.

Expressioni

Gene expression databases

GenevisibleiQ6AXS3. RN.

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

STRINGi10116.ENSRNOP00000021751.

Structurei

3D structure databases

ProteinModelPortaliQ6AXS3.
SMRiQ6AXS3. Positions 80-189, 312-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini149 – 18335SAPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 22317Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 5121Asp/Glu-rich (highly acidic)Add
BLAST
Compositional biasi230 – 2389Asp/Glu-rich (acidic)
Compositional biasi243 – 25614Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi303 – 31311Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Contains 1 SAP domain.Curated

Phylogenomic databases

eggNOGiKOG2266. Eukaryota.
ENOG410XTU9. LUCA.
GeneTreeiENSGT00390000017282.
HOGENOMiHOG000059552.
HOVERGENiHBG004944.
InParanoidiQ6AXS3.
KOiK17046.
OMAiXPLPKSK.
OrthoDBiEOG7TF7C2.
PhylomeDBiQ6AXS3.
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.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AXS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAAAPAAE GEDTPTPPAS EKEPEMPGPR EESEEEEEED DDDEDEEEEK
60 70 80 90 100
EKSLIVEGKR EKRKVERLTM QVSSLQREPF TIAQGKGQKL CEIERIHFFL
110 120 130 140 150
SKKKTDELRN LHKLLYNRPG TVSSLKKNVG QFSGFPFEKG STQYKKKEEM
160 170 180 190 200
LKKYRNAMLK SICEVLDLER SGVNSELVKR ILNFLMHPKP SGKPLPKSKK
210 220 230 240 250
SSSKGSKKER NSSGTTRKSK QTKCPEILSD ESSSDEDEKK NKDESSEDEE
260 270 280 290 300
KESEEEQPPK KTSKKEKAKQ KATTKSKKSV KSANVKKADS STTKKNQNSS
310 320 330 340 350
KKESGSEDSS DDEPLIKKLK KPPTDEELKE TVKKLLADAN LEEVTMKQIC
360 370
KEVYENYPAY DLTERKDFIK TTVKELIS
Length:378
Mass (Da):42,892
Last modified:September 13, 2004 - v1
Checksum:iE3FE3DA24D0D2B05
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079344 mRNA. Translation: AAH79344.1.
RefSeqiNP_001004255.1. NM_001004255.1.
UniGeneiRn.25099.

Genome annotation databases

EnsembliENSRNOT00000021751; ENSRNOP00000021751; ENSRNOG00000016152.
GeneIDi306817.
KEGGirno:306817.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079344 mRNA. Translation: AAH79344.1.
RefSeqiNP_001004255.1. NM_001004255.1.
UniGeneiRn.25099.

3D structure databases

ProteinModelPortaliQ6AXS3.
SMRiQ6AXS3. Positions 80-189, 312-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021751.

PTM databases

iPTMnetiQ6AXS3.
PhosphoSiteiQ6AXS3.

Proteomic databases

PaxDbiQ6AXS3.
PRIDEiQ6AXS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021751; ENSRNOP00000021751; ENSRNOG00000016152.
GeneIDi306817.
KEGGirno:306817.

Organism-specific databases

CTDi7913.
RGDi1303246. Dek.

Phylogenomic databases

eggNOGiKOG2266. Eukaryota.
ENOG410XTU9. LUCA.
GeneTreeiENSGT00390000017282.
HOGENOMiHOG000059552.
HOVERGENiHBG004944.
InParanoidiQ6AXS3.
KOiK17046.
OMAiXPLPKSK.
OrthoDBiEOG7TF7C2.
PhylomeDBiQ6AXS3.
TreeFamiTF324696.

Enzyme and pathway databases

ReactomeiR-RNO-5250924. B-WICH complex positively regulates rRNA expression.

Miscellaneous databases

NextBioi656567.
PROiQ6AXS3.

Gene expression databases

GenevisibleiQ6AXS3. RN.

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.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Tissue: Kidney.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16; SER-20; SER-33; SER-245; SER-246; SER-253 AND SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDEK_RAT
AccessioniPrimary (citable) accession number: Q6AXS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: September 13, 2004
Last modified: February 17, 2016
This is version 80 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.