CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021283
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA replication factor Cdt1 
Protein Synonyms/Alias
 Double parked homolog; DUP 
Gene Name
 CDT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
24PPRIAPPKLACRTPSacetylation[1]
24PPRIAPPKLACRTPSubiquitination[2, 3]
49SATSGSRKRARPPAAacetylation[1]
141GARVRALKASAQDAGubiquitination[2, 4, 5]
166PEEPCGEKAPAYQRFubiquitination[2, 4]
189PGLVLPYKYQVLAEMubiquitination[6]
218SETPTFAKVQRGVQDubiquitination[2]
240ECNVGQIKTVYPASYubiquitination[7, 8]
259ERSVPTFKDGTRRSDubiquitination[2]
301RRQIFSQKLVEHVKEubiquitination[2]
307QKLVEHVKEHHKAFLubiquitination[8]
356PQPPATEKLTTAQEVubiquitination[2, 6, 8]
377LISPRMEKALSQLALubiquitination[2, 8]
416AASPSALKGVSQDLLubiquitination[2, 8]
433IRAKEAQKQLAQMTRubiquitination[2, 8]
470SVFVSERKPALSMEVubiquitination[2]
522IRTDTYVKLDKAADLubiquitination[2, 8]
525DTYVKLDKAADLAHIubiquitination[2]
Reference
 [1] Acetylation/deacetylation modulates the stability of DNA replication licensing factor Cdt1.
 Glozak MA, Seto E.
 J Biol Chem. 2009 Apr 24;284(17):11446-53. [PMID: 19276081]
 [2] 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]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] 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]
 [8] 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
Functional Description
 Cooperates with CDC6 to promote the loading of the mini- chromosome maintenance complex onto chromatin to form the pre- replication complex necessary to initiate DNA replication. Binds DNA in a sequence-, strand-, and conformation-independent manner. Potential oncogene. 
Sequence Annotation
 REGION 150 190 Interaction with GMNN.
 MOTIF 1 23 PIP-box K+4 motif.
 MOTIF 68 70 Cyclin-binding motif.
 MOD_RES 29 29 Phosphothreonine; by MAPK8.
 MOD_RES 318 318 Phosphoserine.
 MOD_RES 394 394 Phosphoserine.  
Keyword
 3D-structure; Cell cycle; Complete proteome; Disease mutation; DNA replication; DNA-binding; Dwarfism; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 546 AA 
Protein Sequence
MEQRRVTDFF ARRRPGPPRI APPKLACRTP SPARPALRAP ASATSGSRKR ARPPAAPGRD 60
QARPPARRRL RLSVDEVSSP STPEAPDIPA CPSPGQKIKK STPAAGQPPH LTSAQDQDTI 120
SELASCLQRA RELGARVRAL KASAQDAGES CTPEAEGRPE EPCGEKAPAY QRFHALAQPG 180
LPGLVLPYKY QVLAEMFRSM DTIVGMLHNR SETPTFAKVQ RGVQDMMRRR FEECNVGQIK 240
TVYPASYRFR QERSVPTFKD GTRRSDYQLT IEPLLEQEAD GAAPQLTASR LLQRRQIFSQ 300
KLVEHVKEHH KAFLASLSPA MVVPEDQLTR WHPRFNVDEV PDIEPAALPQ PPATEKLTTA 360
QEVLARARNL ISPRMEKALS QLALRSAAPS SPGSPRPALP ATPPATPPAA SPSALKGVSQ 420
DLLERIRAKE AQKQLAQMTR CPEQEQRLQR LERLPELARV LRSVFVSERK PALSMEVACA 480
RMVGSCCTIM SPGEMEKHLL LLSELLPDWL SLHRIRTDTY VKLDKAADLA HITARLAHQT 540
RAEEGL 546 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; ISS:UniProtKB.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0000076; P:DNA replication checkpoint; IDA:UniProtKB.
 GO:0030174; P:regulation of DNA-dependent DNA replication initiation; IDA:UniProtKB.
 GO:0000083; P:regulation of transcription involved in G1/S phase of mitotic cell cycle; TAS:Reactome. 
Interpro
 IPR014939; CDT1_Gemini-bd-like. 
Pfam
 PF08839; CDT1 
SMART
 SM01075; CDT1 
PROSITE
  
PRINTS