CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006523
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein DEK 
Protein Synonyms/Alias
  
Gene Name
 DEK 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
57KSLIVEGKREKKKVEubiquitination[1]
84PFTIAQGKGQKLCEIubiquitination[1]
111DELRNLHKLLYNRPGubiquitination[2, 3, 4]
125GTVSSLKKNVGQFSGubiquitination[2, 4]
137FSGFPFEKGSVQYKKubiquitination[2, 4]
177GVNSELVKRILNFLMubiquitination[1, 5]
326PPTDEELKETIKKLLacetylation[6]
331ELKETIKKLLASANLubiquitination[2, 4]
349TMKQICKKVYENYPTubiquitination[2, 3, 4]
371DFIKTTVKELIS***ubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Involved in chromatin organization. 
Sequence Annotation
 DOMAIN 149 183 SAP.
 DNA_BIND 337 351
 DNA_BIND 367 371
 MOTIF 205 221 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 13 13 Phosphothreonine.
 MOD_RES 19 19 Phosphoserine.
 MOD_RES 32 32 Phosphoserine; by CK2.
 MOD_RES 51 51 Phosphoserine.
 MOD_RES 159 159 Phosphoserine; by CK2.
 MOD_RES 199 199 Phosphothreonine; by CK2.
 MOD_RES 201 201 Phosphoserine; by CK2.
 MOD_RES 204 204 Phosphoserine; by CK2.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 230 230 Phosphoserine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 232 232 Phosphoserine.
 MOD_RES 243 243 Phosphoserine; by CK2.
 MOD_RES 244 244 Phosphoserine; by CK2.
 MOD_RES 251 251 Phosphoserine; by CK2.
 MOD_RES 287 287 Phosphoserine; by CK2.
 MOD_RES 288 288 Phosphoserine; by CK2.
 MOD_RES 289 289 Phosphothreonine; by CK2.
 MOD_RES 290 290 Phosphothreonine; by CK2.
 MOD_RES 296 296 Phosphoserine; by CK2.
 MOD_RES 301 301 Phosphoserine; by CK2.
 MOD_RES 303 303 Phosphoserine; by CK2.
 MOD_RES 306 306 Phosphoserine; by CK2.
 MOD_RES 307 307 Phosphoserine; by CK2.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Chromosomal rearrangement; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 375 AA 
Protein Sequence
MSASAPAAEG EGTPTQPASE KEPEMPGPRE ESEEEEDEDD EEEEEEEKEK SLIVEGKREK 60
KKVERLTMQV SSLQREPFTI AQGKGQKLCE IERIHFFLSK KKTDELRNLH KLLYNRPGTV 120
SSLKKNVGQF SGFPFEKGSV QYKKKEEMLK KFRNAMLKSI CEVLDLERSG VNSELVKRIL 180
NFLMHPKPSG KPLPKSKKTC SKGSKKERNS SGMARKAKRT KCPEILSDES SSDEDEKKNK 240
EESSDDEDKE SEEEPPKKTA KREKPKQKAT SKSKKSVKSA NVKKADSSTT KKNQNSSKKE 300
SESEDSSDDE PLIKKLKKPP TDEELKETIK KLLASANLEE VTMKQICKKV YENYPTYDLT 360
ERKDFIKTTV KELIS 375 
Gene Ontology
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:2000779; P:regulation of double-strand break repair; IMP:MGI.
 GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IEA:Compara.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0019079; P:viral genome replication; TAS:ProtInc. 
Interpro
 IPR014876; DEK_C.
 IPR009057; Homeodomain-like.
 IPR003034; SAP_dom. 
Pfam
 PF08766; DEK_C
 PF02037; SAP 
SMART
 SM00513; SAP 
PROSITE
 PS50800; SAP 
PRINTS