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P35659 (DEK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein DEK
Gene names
Name:DEK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.16

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 375374Protein DEK
PRO_0000079858

Regions

Domain149 – 18335SAP
DNA binding337 – 35115 Ref.21 Ref.22
DNA binding367 – 3715 Ref.21 Ref.22
Motif205 – 22117Nuclear localization signal Potential
Compositional bias30 – 4920Asp/Glu-rich (highly acidic)
Compositional bias228 – 2369Asp/Glu-rich (acidic)
Compositional bias241 – 25414Asp/Glu-rich (acidic)
Compositional bias300 – 31011Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.15 Ref.17 Ref.19 Ref.20
Modified residue131Phosphothreonine Ref.17 Ref.19
Modified residue191Phosphoserine Ref.17
Modified residue321Phosphoserine; by CK2 Ref.9 Ref.10 Ref.14 Ref.17 Ref.19
Modified residue511Phosphoserine Ref.10 Ref.17 Ref.19
Modified residue1591Phosphoserine; by CK2 Ref.9
Modified residue1991Phosphothreonine; by CK2 Ref.9
Modified residue2011Phosphoserine; by CK2 Ref.9
Modified residue2041Phosphoserine; by CK2 Ref.9
Modified residue2101Phosphoserine Ref.17
Modified residue2271Phosphoserine Ref.10
Modified residue2301Phosphoserine Ref.10 Ref.17
Modified residue2311Phosphoserine Ref.10 Ref.17
Modified residue2321Phosphoserine Ref.10 Ref.17
Modified residue2431Phosphoserine; by CK2 Ref.9
Modified residue2441Phosphoserine; by CK2 Ref.9
Modified residue2511Phosphoserine; by CK2 Ref.9
Modified residue2871Phosphoserine; by CK2 Ref.9
Modified residue2881Phosphoserine; by CK2 Ref.9
Modified residue2891Phosphothreonine; by CK2 Ref.9
Modified residue2901Phosphothreonine; by CK2 Ref.9
Modified residue2961Phosphoserine; by CK2 Ref.9
Modified residue3011Phosphoserine; by CK2 Ref.9 Ref.19
Modified residue3031Phosphoserine; by CK2 Ref.9 Ref.19
Modified residue3061Phosphoserine; by CK2 Ref.9 Ref.17 Ref.19
Modified residue3071Phosphoserine; by CK2 Ref.9 Ref.13 Ref.17 Ref.19

Natural variations

Alternative sequence49 – 8234Missing in isoform 2.
VSP_042951
Natural variant1401V → A.
Corresponds to variant rs17336208 [ dbSNP | Ensembl ].
VAR_050949

Secondary structure

.......................... 375
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: C07D22B37B719A23

FASTA37542,674
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7BA02406C674EDD4
Show »

FASTA34138,705

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, 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]"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, 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]"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.
[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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

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.
PIRS26059.
RefSeqNP_001128181.1. NM_001134709.1.
NP_003463.1. NM_003472.3.
UniGeneHs.484813.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q1VNMR-A309-375[»]
2JX3NMR-A78-208[»]
ProteinModelPortalP35659.
SMRP35659. Positions 78-187, 309-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113643. 44 interactions.
IntActP35659. 10 interactions.
MINTMINT-2802925.
STRING9606.ENSP00000380414.

PTM databases

PhosphoSiteP35659.

Polymorphism databases

DMDM544150.

Proteomic databases

PaxDbP35659.
PeptideAtlasP35659.
PRIDEP35659.

Protocols and materials databases

DNASU7913.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244776; ENSP00000244776; ENSG00000124795. [P35659-2]
ENST00000397239; ENSP00000380414; ENSG00000124795. [P35659-1]
GeneID7913.
KEGGhsa:7913.
UCSCuc003ncr.1. human. [P35659-1]
uc011djf.1. human. [P35659-2]

Organism-specific databases

CTD7913.
GeneCardsGC06M018224.
HGNCHGNC:2768. DEK.
HPACAB015226.
MIM125264. gene.
neXtProtNX_P35659.
Orphanet98277. Acute myeloid leukemia with recurrent genetic anomaly.
PharmGKBPA27251.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328552.
HOGENOMHOG000059552.
HOVERGENHBG004944.
InParanoidP35659.
KOK17046.
OMADAINEMS.
OrthoDBEOG7TF7C2.
PhylomeDBP35659.
TreeFamTF324696.

Gene expression databases

ArrayExpressP35659.
BgeeP35659.
CleanExHS_DEK.
GenevestigatorP35659.

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]
ProtoNetSearch...

Other

ChiTaRSDEK. human.
EvolutionaryTraceP35659.
GeneWikiDEK_(gene).
GenomeRNAi7913.
NextBio30376.
PROP35659.
SOURCESearch...

Entry information

Entry nameDEK_HUMAN
AccessionPrimary (citable) accession number: P35659
Secondary accession number(s): B2R6K6 expand/collapse secondary AC list , B4DN37, Q5TGV4, Q5TGV5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM