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P35659

- DEK_HUMAN

UniProt

P35659 - DEK_HUMAN

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Protein
Protein DEK
Gene
DEK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in chromatin organization.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi337 – 351152 Publications
Add
BLAST
DNA bindingi367 – 37152 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. histone binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. regulation of double-strand break repair Source: MGI
  3. regulation of double-strand break repair via nonhomologous end joining Source: Ensembl
  4. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  5. signal transduction Source: ProtInc
  6. transcription from RNA polymerase II promoter Source: ProtInc
  7. viral genome replication Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DEK
Gene namesi
Name:DEK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2768. DEK.

Subcellular locationi

Nucleus
Note: Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei.2 Publications

GO - Cellular componenti

  1. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving DEK is found in a subset of acute myeloid leukemia (AML); also known as acute non-lymphocytic leukemia. Translocation t(6;9)(p23;q34) with NUP214/CAN. It results in the formation of a DEK-CAN fusion gene.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti98277. Acute myeloid leukemia with recurrent genetic anomaly.
PharmGKBiPA27251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 375374Protein DEK
PRO_0000079858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine5 Publications
Modified residuei13 – 131Phosphothreonine2 Publications
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei32 – 321Phosphoserine; by CK25 Publications
Modified residuei51 – 511Phosphoserine3 Publications
Modified residuei159 – 1591Phosphoserine; by CK21 Publication
Modified residuei199 – 1991Phosphothreonine; by CK21 Publication
Modified residuei201 – 2011Phosphoserine; by CK21 Publication
Modified residuei204 – 2041Phosphoserine; by CK21 Publication
Modified residuei210 – 2101Phosphoserine1 Publication
Modified residuei227 – 2271Phosphoserine1 Publication
Modified residuei230 – 2301Phosphoserine2 Publications
Modified residuei231 – 2311Phosphoserine2 Publications
Modified residuei232 – 2321Phosphoserine2 Publications
Modified residuei243 – 2431Phosphoserine; by CK21 Publication
Modified residuei244 – 2441Phosphoserine; by CK21 Publication
Modified residuei251 – 2511Phosphoserine; by CK21 Publication
Modified residuei287 – 2871Phosphoserine; by CK21 Publication
Modified residuei288 – 2881Phosphoserine; by CK21 Publication
Modified residuei289 – 2891Phosphothreonine; by CK21 Publication
Modified residuei290 – 2901Phosphothreonine; by CK21 Publication
Modified residuei296 – 2961Phosphoserine; by CK21 Publication
Modified residuei301 – 3011Phosphoserine; by CK22 Publications
Modified residuei303 – 3031Phosphoserine; by CK22 Publications
Modified residuei306 – 3061Phosphoserine; by CK23 Publications
Modified residuei307 – 3071Phosphoserine; by CK24 Publications

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35659.
PaxDbiP35659.
PeptideAtlasiP35659.
PRIDEiP35659.

PTM databases

PhosphoSiteiP35659.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at relatively high levels.

Gene expression databases

ArrayExpressiP35659.
BgeeiP35659.
CleanExiHS_DEK.
GenevestigatoriP35659.

Organism-specific databases

HPAiCAB015226.

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.3 Publications

Protein-protein interaction databases

BioGridi113643. 45 interactions.
IntActiP35659. 10 interactions.
MINTiMINT-2802925.
STRINGi9606.ENSP00000380414.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni88 – 903
Helixi92 – 998
Helixi103 – 11210
Beta strandi114 – 1163
Helixi121 – 1288
Helixi140 – 16223
Turni163 – 1653
Helixi172 – 18110
Turni182 – 1843
Helixi322 – 33312
Helixi338 – 3403
Helixi343 – 35311
Beta strandi355 – 3573
Helixi361 – 37515

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q1VNMR-A309-375[»]
2JX3NMR-A78-208[»]
ProteinModelPortaliP35659.
SMRiP35659. Positions 78-187, 309-375.

Miscellaneous databases

EvolutionaryTraceiP35659.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi205 – 22117Nuclear localization signal Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 4920Asp/Glu-rich (highly acidic)
Add
BLAST
Compositional biasi228 – 2369Asp/Glu-rich (acidic)
Compositional biasi241 – 25414Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi300 – 31011Asp/Glu-rich (acidic)
Add
BLAST

Sequence similaritiesi

Contains 1 SAP domain.

Phylogenomic databases

eggNOGiNOG328552.
HOGENOMiHOG000059552.
HOVERGENiHBG004944.
InParanoidiP35659.
KOiK17046.
OMAiAKRTKYP.
OrthoDBiEOG7TF7C2.
PhylomeDBiP35659.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35659-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSASAPAAEG EGTPTQPASE KEPEMPGPRE ESEEEEDEDD EEEEEEEKEK    50
SLIVEGKREK KKVERLTMQV SSLQREPFTI AQGKGQKLCE IERIHFFLSK 100
KKTDELRNLH KLLYNRPGTV SSLKKNVGQF SGFPFEKGSV QYKKKEEMLK 150
KFRNAMLKSI CEVLDLERSG VNSELVKRIL NFLMHPKPSG KPLPKSKKTC 200
SKGSKKERNS SGMARKAKRT KCPEILSDES SSDEDEKKNK EESSDDEDKE 250
SEEEPPKKTA KREKPKQKAT SKSKKSVKSA NVKKADSSTT KKNQNSSKKE 300
SESEDSSDDE PLIKKLKKPP TDEELKETIK KLLASANLEE VTMKQICKKV 350
YENYPTYDLT ERKDFIKTTV KELIS 375
Length:375
Mass (Da):42,674
Last modified:June 1, 1994 - v1
Checksum:iC07D22B37B719A23
GO
Isoform 2 (identifier: P35659-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-82: Missing.

Note: No experimental confirmation available.

Show »
Length:341
Mass (Da):38,705
Checksum:i7BA02406C674EDD4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401V → A.
Corresponds to variant rs17336208 [ dbSNP | Ensembl ].
VAR_050949

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 8234Missing in isoform 2.
VSP_042951Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64229 mRNA. Translation: CAA45536.1.
AK297749 mRNA. Translation: BAG60099.1.
AK312616 mRNA. Translation: BAG35503.1.
AL031774 Genomic DNA. Translation: CAI20082.2.
CH471087 Genomic DNA. Translation: EAW55402.1.
BC035259 mRNA. Translation: AAH35259.1.
CCDSiCCDS34344.1. [P35659-1]
CCDS47382.1. [P35659-2]
PIRiS26059.
RefSeqiNP_001128181.1. NM_001134709.1. [P35659-2]
NP_003463.1. NM_003472.3. [P35659-1]
UniGeneiHs.484813.

Genome annotation databases

EnsembliENST00000244776; ENSP00000244776; ENSG00000124795. [P35659-2]
ENST00000397239; ENSP00000380414; ENSG00000124795. [P35659-1]
GeneIDi7913.
KEGGihsa:7913.
UCSCiuc003ncr.1. human. [P35659-1]
uc011djf.1. human. [P35659-2]

Polymorphism databases

DMDMi544150.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64229 mRNA. Translation: CAA45536.1 .
AK297749 mRNA. Translation: BAG60099.1 .
AK312616 mRNA. Translation: BAG35503.1 .
AL031774 Genomic DNA. Translation: CAI20082.2 .
CH471087 Genomic DNA. Translation: EAW55402.1 .
BC035259 mRNA. Translation: AAH35259.1 .
CCDSi CCDS34344.1. [P35659-1 ]
CCDS47382.1. [P35659-2 ]
PIRi S26059.
RefSeqi NP_001128181.1. NM_001134709.1. [P35659-2 ]
NP_003463.1. NM_003472.3. [P35659-1 ]
UniGenei Hs.484813.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q1V NMR - A 309-375 [» ]
2JX3 NMR - A 78-208 [» ]
ProteinModelPortali P35659.
SMRi P35659. Positions 78-187, 309-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113643. 45 interactions.
IntActi P35659. 10 interactions.
MINTi MINT-2802925.
STRINGi 9606.ENSP00000380414.

PTM databases

PhosphoSitei P35659.

Polymorphism databases

DMDMi 544150.

Proteomic databases

MaxQBi P35659.
PaxDbi P35659.
PeptideAtlasi P35659.
PRIDEi P35659.

Protocols and materials databases

DNASUi 7913.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244776 ; ENSP00000244776 ; ENSG00000124795 . [P35659-2 ]
ENST00000397239 ; ENSP00000380414 ; ENSG00000124795 . [P35659-1 ]
GeneIDi 7913.
KEGGi hsa:7913.
UCSCi uc003ncr.1. human. [P35659-1 ]
uc011djf.1. human. [P35659-2 ]

Organism-specific databases

CTDi 7913.
GeneCardsi GC06M018224.
HGNCi HGNC:2768. DEK.
HPAi CAB015226.
MIMi 125264. gene.
neXtProti NX_P35659.
Orphaneti 98277. Acute myeloid leukemia with recurrent genetic anomaly.
PharmGKBi PA27251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG328552.
HOGENOMi HOG000059552.
HOVERGENi HBG004944.
InParanoidi P35659.
KOi K17046.
OMAi AKRTKYP.
OrthoDBi EOG7TF7C2.
PhylomeDBi P35659.
TreeFami TF324696.

Miscellaneous databases

ChiTaRSi DEK. human.
EvolutionaryTracei P35659.
GeneWikii DEK_(gene).
GenomeRNAii 7913.
NextBioi 30376.
PROi P35659.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35659.
Bgeei P35659.
CleanExi HS_DEK.
Genevestigatori P35659.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
InterProi IPR014876. DEK_C.
IPR009057. Homeodomain-like.
IPR003034. SAP_dom.
[Graphical view ]
Pfami PF08766. DEK_C. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view ]
SMARTi SM00513. SAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA."
    Von Lindern M., Fornerod M., Van Baal S., Jaegle M., De Wit T., Buijs A., Grosveld G.
    Mol. Cell. Biol. 12:1687-1697(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Cervix.
  6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-21; 66-84; 94-100; 112-124; 126-137; 169-177; 179-187; 331-344 AND 349-362, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
    Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
    EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RBM8A; RNPS1; SRRM1 AND ALYREF/THOC4.
  8. "Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
    Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
    J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX.
  9. "Phosphorylation by protein kinase CK2 changes the DNA binding properties of the human chromatin protein DEK."
    Kappes F., Damoc C., Knippers R., Przybylski M., Pinna L.A., Gruss C.
    Mol. Cell. Biol. 24:6011-6020(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-32; SER-159; THR-199; SER-201; SER-204; SER-243; SER-244; SER-251; SER-287; SER-288; THR-289; THR-290; SER-296; SER-301; SER-303; SER-306 AND SER-307.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-51; SER-227; SER-230; SER-231 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
    Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
    J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
  12. "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.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: SUBCELLULAR LOCATION.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-19; SER-32; SER-51; SER-210; SER-230; SER-231; SER-232; SER-306 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-32; SER-51; SER-301; SER-303; SER-306 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Solution NMR structure of the C-terminal domain of the human protein DEK."
    Devany M., Kotharu N.P., Matsuo H.
    Protein Sci. 13:2252-2259(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 309-375, DNA-BINDING.
  22. "Solution NMR structure of the N-terminal domain of the human DEK protein."
    Devany M., Kappes F., Chen K.M., Markovitz D.M., Matsuo H.
    Protein Sci. 17:205-215(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 78-208, DNA-BINDING.

Entry informationi

Entry nameiDEK_HUMAN
AccessioniPrimary (citable) accession number: P35659
Secondary accession number(s): B2R6K6
, B4DN37, Q5TGV4, Q5TGV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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