DEK_HUMAN - dbPTM
DEK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEK_HUMAN
UniProt AC P35659
Protein Name Protein DEK
Gene Name DEK
Organism Homo sapiens (Human).
Sequence Length 375
Subcellular Localization Nucleus . Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei.
Protein Description Involved in chromatin organization..
Protein Sequence MSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSASAPAAE
------CCCCCCCCC		30.8220068231
2Phosphorylation------MSASAPAAE
------CCCCCCCCC		30.8225159151
4Phosphorylation----MSASAPAAEGE
----CCCCCCCCCCC		27.7225159151
13PhosphorylationPAAEGEGTPTQPASE
CCCCCCCCCCCCCCC		20.8929255136
15PhosphorylationAEGEGTPTQPASEKE
CCCCCCCCCCCCCCC		47.2029255136
19PhosphorylationGTPTQPASEKEPEMP
CCCCCCCCCCCCCCC		56.7529255136
21AcetylationPTQPASEKEPEMPGP
CCCCCCCCCCCCCCC		75.8723749302
32PhosphorylationMPGPREESEEEEDED
CCCCCCCCCCCCCCC		45.6222167270
32 (in isoform 2)Phosphorylation-45.6224719451
51PhosphorylationEEEEKEKSLIVEGKR
HHHHHHHHHHECCHH		25.1529255136
57AcetylationKSLIVEGKREKKKVE
HHHHECCHHHHHHHH		43.8325953088
57UbiquitinationKSLIVEGKREKKKVE
HHHHECCHHHHHHHH		43.83-
67PhosphorylationKKKVERLTMQVSSLQ
HHHHHHHHCHHHHHC		16.2725159151
71PhosphorylationERLTMQVSSLQREPF
HHHHCHHHHHCCCCE		14.4023401153
72PhosphorylationRLTMQVSSLQREPFT
HHHCHHHHHCCCCEE		29.6623401153
77UbiquitinationVSSLQREPFTIAQGK
HHHHCCCCEEEEECC		33.5921890473
79PhosphorylationSLQREPFTIAQGKGQ
HHCCCCEEEEECCCC		26.5626434776
84MethylationPFTIAQGKGQKLCEI
CEEEEECCCCEEEEE		46.19-
84UbiquitinationPFTIAQGKGQKLCEI
CEEEEECCCCEEEEE		46.19-
842-HydroxyisobutyrylationPFTIAQGKGQKLCEI
CEEEEECCCCEEEEE		46.19-
84MalonylationPFTIAQGKGQKLCEI
CEEEEECCCCEEEEE		46.1930639696
84AcetylationPFTIAQGKGQKLCEI
CEEEEECCCCEEEEE		46.1925953088
87AcetylationIAQGKGQKLCEIERI
EEECCCCEEEEEEEE		64.8725953088
91UbiquitinationKGQKLCEIERIHFFL
CCCEEEEEEEEEEHH		4.1521890473
93MethylationQKLCEIERIHFFLSK
CEEEEEEEEEEHHCC		33.09-
100UbiquitinationRIHFFLSKKKTDELR
EEEEHHCCCCHHHHH		61.51-
1002-HydroxyisobutyrylationRIHFFLSKKKTDELR
EEEEHHCCCCHHHHH		61.51-
100AcetylationRIHFFLSKKKTDELR
EEEEHHCCCCHHHHH		61.5125953088
103UbiquitinationFFLSKKKTDELRNLH
EHHCCCCHHHHHHHH		43.5221890473
107MethylationKKKTDELRNLHKLLY
CCCHHHHHHHHHHHH		41.43-
111UbiquitinationDELRNLHKLLYNRPG
HHHHHHHHHHHCCCC		43.2721890473
111UbiquitinationDELRNLHKLLYNRPG
HHHHHHHHHHHCCCC		43.2721890473
114PhosphorylationRNLHKLLYNRPGTVS
HHHHHHHHCCCCCHH		21.4028152594
119PhosphorylationLLYNRPGTVSSLKKN
HHHCCCCCHHHHHHC		21.6428152594
121PhosphorylationYNRPGTVSSLKKNVG
HCCCCCHHHHHHCCC		29.7728348404
122PhosphorylationNRPGTVSSLKKNVGQ
CCCCCHHHHHHCCCC		39.6128152594
124UbiquitinationPGTVSSLKKNVGQFS
CCCHHHHHHCCCCCC		44.22-
124AcetylationPGTVSSLKKNVGQFS
CCCHHHHHHCCCCCC		44.2225953088
125UbiquitinationGTVSSLKKNVGQFSG
CCHHHHHHCCCCCCC		63.2621890473
125UbiquitinationGTVSSLKKNVGQFSG
CCHHHHHHCCCCCCC		63.2621890473
131PhosphorylationKKNVGQFSGFPFEKG
HHCCCCCCCCCCCCC		31.4729514088
137UbiquitinationFSGFPFEKGSVQYKK
CCCCCCCCCCCCHHH		57.7921890473
137MalonylationFSGFPFEKGSVQYKK
CCCCCCCCCCCCHHH		57.7930639696
137UbiquitinationFSGFPFEKGSVQYKK
CCCCCCCCCCCCHHH		57.7921890473
137AcetylationFSGFPFEKGSVQYKK
CCCCCCCCCCCCHHH		57.7926051181
143AcetylationEKGSVQYKKKEEMLK
CCCCCCHHHHHHHHH		40.0325953088
158AcetylationKFRNAMLKSICEVLD
HHHHHHHHHHHHHHC		25.3726051181
158UbiquitinationKFRNAMLKSICEVLD
HHHHHHHHHHHHHHC		25.37-
159PhosphorylationFRNAMLKSICEVLDL
HHHHHHHHHHHHHCH		28.6315199154
161GlutathionylationNAMLKSICEVLDLER
HHHHHHHHHHHCHHH		3.6922555962
177UbiquitinationGVNSELVKRILNFLM
CCCHHHHHHHHHHHH		46.4721890473
1772-HydroxyisobutyrylationGVNSELVKRILNFLM
CCCHHHHHHHHHHHH		46.47-
177AcetylationGVNSELVKRILNFLM
CCCHHHHHHHHHHHH		46.4725953088
191UbiquitinationMHPKPSGKPLPKSKK
HCCCCCCCCCCCCCC		47.95-
199PhosphorylationPLPKSKKTCSKGSKK
CCCCCCCCCCCCCCC		26.2515199154
201PhosphorylationPKSKKTCSKGSKKER
CCCCCCCCCCCCCCC		45.3315199154
204PhosphorylationKKTCSKGSKKERNSS
CCCCCCCCCCCCCCH		44.2715199154
210PhosphorylationGSKKERNSSGMARKA
CCCCCCCCHHHHHHH		34.1925849741
211PhosphorylationSKKERNSSGMARKAK
CCCCCCCHHHHHHHH		35.8220068231
220PhosphorylationMARKAKRTKCPEILS
HHHHHHHCCCCHHHC		35.9724144214
227PhosphorylationTKCPEILSDESSSDE
CCCCHHHCCCCCCHH		45.0223927012
230PhosphorylationPEILSDESSSDEDEK
CHHHCCCCCCHHHHH		39.8823927012
231PhosphorylationEILSDESSSDEDEKK
HHHCCCCCCHHHHHH		39.5023927012
232PhosphorylationILSDESSSDEDEKKN
HHCCCCCCHHHHHHH		55.0623927012
243PhosphorylationEKKNKEESSDDEDKE
HHHHHHCCCCCCCHH		39.9120164059
244PhosphorylationKKNKEESSDDEDKES
HHHHHCCCCCCCHHC		52.9720164059
251PhosphorylationSDDEDKESEEEPPKK
CCCCCHHCCCCCCHH		56.9228355574
259O-linked_GlycosylationEEEPPKKTAKREKPK
CCCCCHHHCCCCCCC		43.4623301498
276PhosphorylationATSKSKKSVKSANVK
CCHHHHHHHHHHCCC		38.2117924679
279PhosphorylationKSKKSVKSANVKKAD
HHHHHHHHHCCCCCC		23.95-
279ADP-ribosylationKSKKSVKSANVKKAD
HHHHHHHHHCCCCCC		23.9528190768
283AcetylationSVKSANVKKADSSTT
HHHHHCCCCCCCCCC		41.897491859
284AcetylationVKSANVKKADSSTTK
HHHHCCCCCCCCCCC		53.827491869
287PhosphorylationANVKKADSSTTKKNQ
HCCCCCCCCCCCCCC		34.1515199154
288PhosphorylationNVKKADSSTTKKNQN
CCCCCCCCCCCCCCC		40.4115199154
289PhosphorylationVKKADSSTTKKNQNS
CCCCCCCCCCCCCCC		46.7315199154
290PhosphorylationKKADSSTTKKNQNSS
CCCCCCCCCCCCCCC		41.8015199154
292AcetylationADSSTTKKNQNSSKK
CCCCCCCCCCCCCCC		62.7719608861
296PhosphorylationTTKKNQNSSKKESES
CCCCCCCCCCCCCCC		33.5018669648
297PhosphorylationTKKNQNSSKKESESE
CCCCCCCCCCCCCCC		56.1226552605
297UbiquitinationTKKNQNSSKKESESE
CCCCCCCCCCCCCCC		56.1221890473
301PhosphorylationQNSSKKESESEDSSD
CCCCCCCCCCCCCCC		56.1329255136
303PhosphorylationSSKKESESEDSSDDE
CCCCCCCCCCCCCCH		56.8529255136
306PhosphorylationKESESEDSSDDEPLI
CCCCCCCCCCCHHHH		31.4529255136
307PhosphorylationESESEDSSDDEPLIK
CCCCCCCCCCHHHHH		62.4929255136
315UbiquitinationDDEPLIKKLKKPPTD
CCHHHHHHHCCCCCH		59.5521890473
317UbiquitinationEPLIKKLKKPPTDEE
HHHHHHHCCCCCHHH		72.60-
321PhosphorylationKKLKKPPTDEELKET
HHHCCCCCHHHHHHH		65.6520068231
326AcetylationPPTDEELKETIKKLL
CCCHHHHHHHHHHHH		56.9719608861
326UbiquitinationPPTDEELKETIKKLL
CCCHHHHHHHHHHHH		56.9719608861
328PhosphorylationTDEELKETIKKLLAS
CHHHHHHHHHHHHHH		36.1920068231
331UbiquitinationELKETIKKLLASANL
HHHHHHHHHHHHCCC		44.9021890473
3312-HydroxyisobutyrylationELKETIKKLLASANL
HHHHHHHHHHHHCCC		44.90-
331UbiquitinationELKETIKKLLASANL
HHHHHHHHHHHHCCC		44.9021890473
335PhosphorylationTIKKLLASANLEEVT
HHHHHHHHCCCCHHC		20.0521815630
342PhosphorylationSANLEEVTMKQICKK
HCCCCHHCHHHHHHH		23.1822496350
343SulfoxidationANLEEVTMKQICKKV
CCCCHHCHHHHHHHH		3.4821406390
344AcetylationNLEEVTMKQICKKVY
CCCHHCHHHHHHHHH		27.4425953088
348AcetylationVTMKQICKKVYENYP
HCHHHHHHHHHHHCC		47.077712277
349UbiquitinationTMKQICKKVYENYPT
CHHHHHHHHHHHCCC		45.7121890473
349MalonylationTMKQICKKVYENYPT
CHHHHHHHHHHHCCC		45.7126320211
349UbiquitinationTMKQICKKVYENYPT
CHHHHHHHHHHHCCC		45.7121890473
349AcetylationTMKQICKKVYENYPT
CHHHHHHHHHHHCCC		45.7126051181
351PhosphorylationKQICKKVYENYPTYD
HHHHHHHHHHCCCCC		13.82-
367AcetylationTERKDFIKTTVKELI
HHCHHHHHHHHHHHH		37.8326051181
368PhosphorylationERKDFIKTTVKELIS
HCHHHHHHHHHHHHC		31.8220068231
369PhosphorylationRKDFIKTTVKELIS-
CHHHHHHHHHHHHC-		25.2820068231
371UbiquitinationDFIKTTVKELIS---
HHHHHHHHHHHC---		44.72-
375PhosphorylationTTVKELIS-------
HHHHHHHC-------		46.9520068231
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
32SPhosphorylationKinaseCK2-FAMILY-GPS
32SPhosphorylationKinaseCK2-Uniprot
32SPhosphorylationKinaseCSNK2A1P19139
GPS
67TPhosphorylationKinaseAURKBQ96GD4
GPS
159SPhosphorylationKinaseCK2-Uniprot
159SPhosphorylationKinaseCK2-FAMILY-GPS
199TPhosphorylationKinaseCK2-Uniprot
199TPhosphorylationKinaseCK2-FAMILY-GPS
201SPhosphorylationKinaseCK2-Uniprot
201SPhosphorylationKinaseCK2-FAMILY-GPS
204SPhosphorylationKinaseCK2-Uniprot
204SPhosphorylationKinaseCK2-FAMILY-GPS
243SPhosphorylationKinaseCSNK2A1P19139
GPS
243SPhosphorylationKinaseCK2-FAMILY-GPS
243SPhosphorylationKinaseCK2-Uniprot
244SPhosphorylationKinaseCK2-FAMILY-GPS
244SPhosphorylationKinaseCK2-Uniprot
244SPhosphorylationKinaseCSNK2A1P19139
GPS
251SPhosphorylationKinaseCK2-Uniprot
251SPhosphorylationKinaseCK2-FAMILY-GPS
251SPhosphorylationKinaseCSNK2A1P19139
GPS
287SPhosphorylationKinaseCK2-FAMILY-GPS
287SPhosphorylationKinaseCK2-Uniprot
288SPhosphorylationKinaseCK2-FAMILY-GPS
288SPhosphorylationKinaseCK2-Uniprot
289TPhosphorylationKinaseCK2-FAMILY-GPS
289TPhosphorylationKinaseCK2-Uniprot
290TPhosphorylationKinaseCK2-FAMILY-GPS
290TPhosphorylationKinaseCK2-Uniprot
296SPhosphorylationKinaseCK2-FAMILY-GPS
296SPhosphorylationKinaseCK2-Uniprot
301SPhosphorylationKinaseCK2-Uniprot
301SPhosphorylationKinaseCK2-FAMILY-GPS
301SPhosphorylationKinaseCSNK2A1P19139
GPS
303SPhosphorylationKinaseCK2-FAMILY-GPS
303SPhosphorylationKinaseCSNK2A1P19139
GPS
303SPhosphorylationKinaseCK2-Uniprot
306SPhosphorylationKinaseCK2-FAMILY-GPS
306SPhosphorylationKinaseCSNK2A1P19139
GPS
306SPhosphorylationKinaseCK2-Uniprot
307SPhosphorylationKinaseCK2-FAMILY-GPS
307SPhosphorylationKinaseCK2-Uniprot
-KUbiquitinationE3 ubiquitin ligaseSPOPO43791
PMID:25278611
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEK_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DEK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRSF2_HUMANSRSF2physical
10908574
DAXX_HUMANDAXXphysical
12140263
HDAC2_HUMANHDAC2physical
12140263
PYM1_HUMANWIBGphysical
22939629
DHX15_HUMANDHX15physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
SPB1_HUMANFTSJ3physical
22939629
S10A9_HUMANS100A9physical
22939629
RL37A_HUMANRPL37Aphysical
22939629
TR150_HUMANTHRAP3physical
22939629
EXOS2_HUMANEXOSC2physical
22939629
VTNC_HUMANVTNphysical
22939629
TMED9_HUMANTMED9physical
22939629
I2BP2_HUMANIRF2BP2physical
22863883
PTN12_HUMANPTPN12physical
22863883
SPOP_HUMANSPOPphysical
25278611
BPTF_HUMANBPTFphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DEK_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-306 AND SER-307,AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-301; SER-303;SER-306 AND SER-307, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-51, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-243; SER-244 ANDSER-251, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
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-306AND SER-307, AND MASS SPECTROMETRY.
"Phosphorylation by protein kinase CK2 changes the DNA bindingproperties 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).
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.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13 AND THR-15, AND MASSSPECTROMETRY.

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