P35659 (DEK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein DEK

Gene names

Name:

DEK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	Involved in chromatin organization. Ref.12
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. Ref.7 Ref.8 Ref.11
Subcellular location	Nucleus. Note: Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei. Ref.12 Ref.15
Tissue specificity	Ubiquitous. Expressed at relatively high levels.
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. Ref.9
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	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	DNA-binding
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of double-strand break repair Inferred from mutant phenotype PubMed 21653549. Source: MGI regulation of double-strand break repair via nonhomologous end joining Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 9050861. Source: ProtInc signal transduction Traceable author statement PubMed 9050861. Source: ProtInc transcription from RNA polymerase II promoter Traceable author statement PubMed 9050861. Source: ProtInc viral genome replication Traceable author statement PubMed 9050861. Source: ProtInc
Cellular_component	nucleus Inferred from direct assay PubMed 21653549. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone binding Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35659-1)

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.

Isoform 2 (identifier: P35659-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 375

374

Protein DEK

PRO_0000079858

Regions

Domain

149 – 183

35

SAP

DNA binding

337 – 351

15

Ref.19 Ref.20

DNA binding

367 – 371

5

Ref.19 Ref.20

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.6 Ref.16 Ref.18

Modified residue

13

1

Phosphothreonine Ref.16 Ref.18

Modified residue

19

1

Phosphoserine Ref.16

Modified residue

32

1

Phosphoserine; by CK2 Ref.9 Ref.10 Ref.14 Ref.16 Ref.18

Modified residue

51

1

Phosphoserine Ref.10 Ref.16 Ref.18

Modified residue

159

1

Phosphoserine; by CK2 Ref.9

Modified residue

199

1

Phosphothreonine; by CK2 Ref.9

Modified residue

201

1

Phosphoserine; by CK2 Ref.9

Modified residue

204

1

Phosphoserine; by CK2 Ref.9

Modified residue

210

1

Phosphoserine Ref.16

Modified residue

227

1

Phosphoserine Ref.10

Modified residue

230

1

Phosphoserine Ref.10 Ref.16

Modified residue

231

1

Phosphoserine Ref.10 Ref.16

Modified residue

232

1

Phosphoserine Ref.10 Ref.16

Modified residue

243

1

Phosphoserine; by CK2 Ref.9

Modified residue

244

1

Phosphoserine; by CK2 Ref.9

Modified residue

251

1

Phosphoserine; by CK2 Ref.9

Modified residue

287

1

Phosphoserine; by CK2 Ref.9

Modified residue

288

1

Phosphoserine; by CK2 Ref.9

Modified residue

289

1

Phosphothreonine; by CK2 Ref.9

Modified residue

290

1

Phosphothreonine; by CK2 Ref.9

Modified residue

296

1

Phosphoserine; by CK2 Ref.9

Modified residue

301

1

Phosphoserine; by CK2 Ref.9 Ref.18

Modified residue

303

1

Phosphoserine; by CK2 Ref.9 Ref.18

Modified residue

306

1

Phosphoserine; by CK2 Ref.9 Ref.16 Ref.18

Modified residue

307

1

Phosphoserine; by CK2 Ref.9 Ref.13 Ref.16 Ref.18

Natural variations

Alternative sequence

49 – 82

34

Missing in isoform 2.

VSP_042951

Natural variant

140

1

V → A.
Corresponds to variant rs17336208 [ dbSNP | Ensembl ].

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)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 7BA02406C674EDD4	FASTA	341	38,705
	10 20 30 40 50 60 MSASAPAAEG EGTPTQPASE KEPEMPGPRE ESEEEEDEDD EEEEEEEKGK GQKLCEIERI 70 80 90 100 110 120 HFFLSKKKTD ELRNLHKLLY NRPGTVSSLK KNVGQFSGFP FEKGSVQYKK KEEMLKKFRN 130 140 150 160 170 180 AMLKSICEVL DLERSGVNSE LVKRILNFLM HPKPSGKPLP KSKKTCSKGS KKERNSSGMA 190 200 210 220 230 240 RKAKRTKCPE ILSDESSSDE DEKKNKEESS DDEDKESEEE PPKKTAKREK PKQKATSKSK 250 260 270 280 290 300 KSVKSANVKK ADSSTTKKNQ NSSKKESESE DSSDDEPLIK KLKKPPTDEE LKETIKKLLA 310 320 330 340 SANLEEVTMK QICKKVYENY PTYDLTERKD FIKTTVKELI S

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] [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]	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] [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, 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, MASS SPECTROMETRY. 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[15]	"Proteome analysis of human nuclear insoluble fractions." Takata H., Nishijima H., Ogura S., Sakaguchi T., Bubulya P.A., Mochizuki T., Shibahara K. Genes Cells 14:975-990(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"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, 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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 309-375, DNA-BINDING.
[20]	"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.
+	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.
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.

IPI

IPI00020021.
IPI00942944.

PIR

S26059.

RefSeq

NP_001128181.1. NM_001134709.1.
NP_003463.1. NM_003472.3.

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	[»]

ProteinModelPortal

P35659.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35659. 9 interactions.

MINT

MINT-2802925.

STRING

9606.ENSP00000380414.

PTM databases

PhosphoSite

P35659.

Polymorphism databases

DMDM

544150.

Proteomic databases

PaxDb

P35659.

PeptideAtlas

P35659.

PRIDE

P35659.

Protocols and materials databases

DNASU

7913.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244776; ENSP00000244776; ENSG00000124795.
ENST00000397239; ENSP00000380414; ENSG00000124795.

GeneID

7913.

KEGG

hsa:7913.

UCSC

uc003ncr.1. human.
uc011djf.1. human.

Organism-specific databases

CTD

7913.

GeneCards

GC06M018224.

HGNC

HGNC:2768. DEK.

HPA

CAB015226.

MIM

125264. gene.

neXtProt

NX_P35659.

Orphanet

98277. Acute myeloid leukemia with recurrent genetic anomaly.

PharmGKB

PA27251.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG328552.

HOGENOM

HOG000059552.

HOVERGEN

HBG004944.

InParanoid

P35659.

OMA

DAINEMS.

OrthoDB

EOG4HHP3C.

Gene expression databases

ArrayExpress

P35659.

Bgee

P35659.

CleanEx

HS_DEK.

Genevestigator

P35659.

GermOnline

ENSG00000124795. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.

InterPro

IPR014876. DEK_C.
IPR009057. Homeodomain-like.
IPR003034. SAP_dom.
[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

ChiTaRS

DEK. human.

EvolutionaryTrace

P35659.

GenomeRNAi

7913.

NextBio

30376.

SOURCE

Search...

Entry information

Entry name

DEK_HUMAN

Accession

Primary (citable) accession number: P35659
Secondary accession number(s): B2R6K6 , B4DN37, Q5TGV4, Q5TGV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.