Reviewed, UniProtKB/Swiss-Prot P35659 (DEK_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein DEK

Gene names

Name:

DEK

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May have a function in the nucleus.
Subunit structure	Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, RBM8A, RNPS1, SRRM1 and THOC4. Interacts with histones H2A, H2B, H3, H4, acetylated histone H4, non-phosporylated 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. Ref.8
Subcellular location	Nucleus Potential.
Tissue specificity	Ubiquitous. Expressed at relatively high levels.
Involvement in disease	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.
Sequence similarities	Contains 1 SAP domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc signal transduction Traceable author statement. Source: ProtInc viral genome replication Traceable author statement. Source: ProtInc
Cellular component	nucleus Traceable author statement. Source: ProtInc
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone binding Ref.8 Inferred from direct assay. Source: UniProtKB specific RNA polymerase II transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 375

374

Protein DEK

PRO_0000079858

Regions

Domain

149 – 183

35

SAP

DNA binding

337 – 351

15

Ref.19

DNA binding

367 – 371

5

Ref.19

Motif

205 – 221

17

Nuclear localization signal Potential

Compositional bias

30 – 49

20

Asp/Glu-rich (highly acidic)

Compositional bias

228 – 236

9

Asp/Glu-rich (acidic)

Compositional bias

241 – 254

14

Asp/Glu-rich (acidic)

Compositional bias

300 – 310

11

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.5

Modified residue

13

1

Phosphothreonine Ref.17

Modified residue

15

1

Phosphothreonine Ref.17

Modified residue

32

1

Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14 Ref.15

Modified residue

51

1

Phosphoserine Ref.9 Ref.13

Modified residue

227

1

Phosphoserine Ref.9

Modified residue

230

1

Phosphoserine Ref.9

Modified residue

231

1

Phosphoserine Ref.9

Modified residue

232

1

Phosphoserine Ref.9

Modified residue

243

1

Phosphoserine Ref.12

Modified residue

244

1

Phosphoserine Ref.9 Ref.12

Modified residue

251

1

Phosphoserine Ref.9 Ref.12

Modified residue

276

1

Phosphoserine Ref.11

Modified residue

301

1

Phosphoserine Ref.9 Ref.14

Modified residue

303

1

Phosphoserine Ref.9 Ref.14

Modified residue

306

1

Phosphoserine Ref.9 Ref.14 Ref.15

Modified residue

307

1

Phosphoserine Ref.9 Ref.14 Ref.15

Modified residue

326

1

N6-acetyllysine Ref.18

Natural variations

Natural variant

140

1

V → A: dbSNP rs17336208.

VAR_050949

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

375

Helix Strand Turn

Details...

Turn

88 – 90

3

Helix

92 – 99

8

Helix

103 – 112

10

Beta strand

114 – 116

3

Helix

121 – 128

8

Helix

140 – 162

23

Turn

163 – 165

3

Helix

172 – 181

10

Turn

182 – 184

3

Helix

322 – 333

12

Helix

338 – 340

3

Helix

343 – 353

11

Beta strand

355 – 357

3

Helix

361 – 375

15

Sequences

	Sequence		Length	Mass (Da)
	P35659-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: C07D22B37B719A23	FASTA	375	42,674
	10 20 30 40 50 60 MSASAPAAEG EGTPTQPASE KEPEMPGPRE ESEEEEDEDD EEEEEEEKEK SLIVEGKREK 70 80 90 100 110 120 KKVERLTMQV SSLQREPFTI AQGKGQKLCE IERIHFFLSK KKTDELRNLH KLLYNRPGTV 130 140 150 160 170 180 SSLKKNVGQF SGFPFEKGSV QYKKKEEMLK KFRNAMLKSI CEVLDLERSG VNSELVKRIL 190 200 210 220 230 240 NFLMHPKPSG KPLPKSKKTC SKGSKKERNS SGMARKAKRT KCPEILSDES SSDEDEKKNK 250 260 270 280 290 300 EESSDDEDKE SEEEPPKKTA KREKPKQKAT SKSKKSVKSA NVKKADSSTT KKNQNSSKKE 310 320 330 340 350 360 SESEDSSDDE PLIKKLKKPP TDEELKETIK KLLASANLEE VTMKQICKKV YENYPTYDLT 370 ERKDFIKTTV KELIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1549122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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, 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: 11118221] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RBM8A; RNPS1; SRRM1 AND 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: 12140263] [Abstract] Cited for: INTERACTION WITH DAXX.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-51; SER-227; SER-230; SER-231; SER-232; SER-244; SER-251; SER-301; SER-303; SER-306 AND SER-307, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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: 16603771] [Abstract] Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
[11]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-243; SER-244 AND SER-251, MASS SPECTROMETRY.
[13]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-51, MASS SPECTROMETRY.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-301; SER-303; SER-306 AND SER-307, MASS SPECTROMETRY.
[15]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-306 AND SER-307, MASS SPECTROMETRY. Tissue: Liver.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13 AND THR-15, MASS SPECTROMETRY.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, MASS SPECTROMETRY.
[19]	"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: 15238633] [Abstract] Cited for: STRUCTURE BY NMR OF 309-375, DNA-BINDING.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X64229 mRNA. Translation: CAA45536.1.
AK312616 mRNA. Translation: BAG35503.1.
AL031774 Genomic DNA. Translation: CAI20082.2.
CH471087 Genomic DNA. Translation: EAW55402.1.
BC035259 mRNA. Translation: AAH35259.1.

IPI

IPI00020021.

PIR

S26059.

RefSeq

NP_001128181.1.
NP_003463.1.

UniGene

Hs.484813

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q1V	NMR	-	A	309-375	[»]
2JX3	NMR	-	A	78-208	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P35659.

PTM databases

PhosphoSite

P35659.

Proteomic databases

PeptideAtlas

P35659.

PRIDE

P35659.

Genome annotation databases

Ensembl

ENST00000397239; ENSP00000380414; ENSG00000124795; Homo sapiens. [Genome view]

GeneID

7913.

KEGG

hsa:7913.

UCSC

uc003ncr.1. human.

Organism-specific databases

CTD

7913.

GeneCards

GC06M018332.

H-InvDB

HIX0025066.

HGNC

HGNC:2768. DEK.

HPA

CAB015226.

MIM

125264. gene.

Orphanet

52688. Myelodysplastic syndromes.
86839. Refractory anemia with excess blasts.

PharmGKB

PA27251.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17553.

HOGENOM

HBG279515.

HOVERGEN

P35659.

InParanoid

P35659.

OMA

EFIKTTV.

Gene expression databases

ArrayExpress

P35659.

Bgee

P35659.

CleanEx

HS_DEK.

Genevestigator

P35659.

GermOnline

ENSG00000124795. Homo sapiens.

Family and domain databases

InterPro

IPR014876. DEK_C.
IPR003034. SAP_DNA_bd.
[Graphical view]

Pfam

PF08766. DEK_C. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]

SMART

SM00513. SAP. 1 hit.
[Graphical view]

PROSITE

PS50800. SAP. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

30376.

SOURCE

Search...

Entry information

Entry name

DEK_HUMAN

Accession

Primary (citable) accession number: P35659
Secondary accession number(s): B2R6K6, Q5TGV4, Q5TGV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	January 19, 2010
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.