CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012278
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription factor Dp-1 
Protein Synonyms/Alias
 DRTF1-polypeptide 1; DRTF1; E2F dimerization partner 1 
Gene Name
 TFDP1 
Gene Synonyms/Alias
 DP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MAKDAGLIEAacetylation[1, 2]
3*****MAKDAGLIEAubiquitination[3]
26DQNLSPGKGVVSLVAubiquitination[3]
44STVNPLGKQLLPKTFubiquitination[2, 3, 4]
190SKEKKEIKWIGLPTNubiquitination[3]
217QRRLERIKQKQSQLQubiquitination[3]
219RLERIKQKQSQLQELubiquitination[3]
234ILQQIAFKNLVQRNRubiquitination[3]
320SCSAEDLKMARSLVPubiquitination[3, 5, 6]
Reference
 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] 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]
 [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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DP2/E2F complex functions in the control of cell-cycle progression from G1 to S phase. The E2F1/DP complex appears to mediate both cell proliferation and apoptosis. 
Sequence Annotation
 DNA_BIND 113 195 Potential.
 REGION 204 277 Dimerization (Potential).
 REGION 211 327 Enhances binding of RB protein to E2F.
 REGION 214 246 DCB1.
 REGION 259 315 DCB2.
 MOTIF 161 195 DEF box.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 3 3 N6-acetyllysine.
 MOD_RES 23 23 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Activator; Cell cycle; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 410 AA 
Protein Sequence
MAKDAGLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN PLGKQLLPKT FGQSNVNIAQ 60
QVVIGTPQRP AASNTLVVGS PHTPSTHFAS QNQPSDSSPW SAGKRNRKGE KNGKGLRHFS 120
MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD NHILPNESAY DQKNIRRRVY DALNVLMAMN 180
IISKEKKEIK WIGLPTNSAQ ECQNLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN 240
RHAEQQASRP PPPNSVIHLP FIIVNTSKKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL 300
KRMGMACGLE SGSCSAEDLK MARSLVPKAL EPYVTEMAQG TVGGVFITTA GSTSNGTRFS 360
ASDLTNGADG MLATSSNGSQ YSGSRVETPV SYVGEDDEED DDFNENDEDD 410 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005667; C:transcription factor complex; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome. 
Interpro
 IPR003316; E2F_TDP.
 IPR014889; Transc_factor_DP_C.
 IPR016556; Transcription_factor_DP_subgr.
 IPR015648; Transcrpt_fac_DP.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF08781; DP
 PF02319; E2F_TDP 
SMART
  
PROSITE
  
PRINTS