CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004626
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cholinephosphotransferase 1 
Protein Synonyms/Alias
 Aminoalcohol phosphotransferase CPT1; Diacylglycerol cholinephosphotransferase 1; Sn-1,2-diacylglycerol cholinephosphotransferase; CHOPT 
Gene Name
 CPT1 
Gene Synonyms/Alias
 YNL130C; N1218; N1867 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
17LGNLKLYKYQSDDRSacetylation[1]
17LGNLKLYKYQSDDRSubiquitination[2]
250YYESQSTKSATPSKTubiquitination[2]
256TKSATPSKTAENISKubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Catalyzes the final step in the CDP-choline route leading to phosphatidylcholin (PC). Preferentially uses CDP- monomethylethanolamine as aminoalcohol substrate. Shows highest activity toward di- and mono-unsaturated diacylglycerol species as lipid substrates. The CDP-choline pathway only contributes to net PC synthesis if exogenous choline is present. In its absence, this pathway recycles choline from PC turnover and may contribute to maintaining the proper PC species composition. 
Sequence Annotation
  
Keyword
 Complete proteome; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane; Metal-binding; Microsome; Mitochondrion; Mitochondrion outer membrane; Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 393 AA 
Protein Sequence
MGFFIPQSSL GNLKLYKYQS DDRSFLSNHV LRPFWRKFAT IFPLWMAPNL VTLLGFCFII 60
FNVLTTLYYD PYFDQESPRW TYFSYAIGLF LYQTFDACDG MHARRTGQQG PLGELFDHCI 120
DSINTTLSMI PVCSMTGMGY TYMTIFSQFA ILCSFYLSTW EEYHTHKLYL AEFCGPVEGI 180
IVLCISFIAV GIYGPQTIWH TKVAQFSWQD FVFDVETVHL MYAFCTGALI FNIVTAHTNV 240
VRYYESQSTK SATPSKTAEN ISKAVNGLLP FFAYFSSIFT LVLIQPSFIS LALILSIGFS 300
VAFVVGRMII AHLTMQPFPM VNFPFLIPTI QLVLYAFMVY VLDYQKGSIV SALVWMGLGL 360
TLAIHGMFIN DIIYDITTFL DIYALSIKHP KEI 393 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:SGD.
 GO:0016021; C:integral to membrane; ISM:SGD.
 GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
 GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR000462; CDP-OH_P_trans.
 IPR014472; CHOPT. 
Pfam
 PF01066; CDP-OH_P_transf 
SMART
  
PROSITE
 PS00379; CDP_ALCOHOL_P_TRANSF 
PRINTS