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Identification
HMDB Protein ID HMDBP02855
Secondary Accession Numbers
  • 8362
  • HMDBP03348
Name Cholinephosphotransferase 1
Synonyms
  1. AAPT1-like protein
  2. Diacylglycerol cholinephosphotransferase 1
  3. hCPT1
Gene Name CHPT1
Protein Type Unknown
Biological Properties
General Function Involved in phosphotransferase activity, for other substituted phosphate groups
Specific Function Catalyzes phosphatidylcholine biosynthesis from CDP-choline. It thereby plays a central role in the formation and maintenance of vesicular membranes.
Pathways
  • Ether lipid metabolism
  • Glycerophospholipid metabolism
  • Lamivudine Metabolism Pathway
  • phosphatidylcholine biosynthesis
  • Phospholipid Biosynthesis
Reactions
Citicoline + 1,2-diacylglycerol → Cytidine monophosphate + a phosphatidylcholine details
Citicoline + 1,2-Diacyl-sn-glycerol → Cytidine monophosphate + Phosphatidylcholine details
Citicoline + 1-Alkyl-2-acetyl-sn-glycerol → Cytidine monophosphate + 2-Acetyl-1-alkyl-sn-glycero-3-phosphocholine details
CMP-N-trimethyl-2-aminoethylphosphonate + Diacylglycerol → Cytidine monophosphate + Diacylglyceryl-N-trimethyl-2-aminoethylphosphonate details
1-Alkyl-2-acylglycerol + Citicoline → 1-Radyl-2-acyl-sn-glycero-3-phosphocholine + Cytidine monophosphate details
GO Classification
Biological Process
regulation of cell growth
platelet activating factor biosynthetic process
Cellular Component
integral to membrane
Golgi membrane
Component
membrane
cell part
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
phosphotransferase activity, for other substituted phosphate groups
Molecular Function
diacylglycerol binding
metal ion binding
diacylglycerol cholinephosphotransferase activity
Process
metabolic process
phospholipid biosynthetic process
organophosphate metabolic process
phospholipid metabolic process
Cellular Location
  1. Golgi apparatus membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location 12
Locus 12q
SNPs CHPT1
Gene Sequence
>1221 bp
ATGGCGGCAGGCGCCGGGGCCGGGTCCGCGCCGCGCTGGCTGAGGGCGCTGAGCGAGCCG
CTGAGCGCGGCGCAGCTGCGGCGACTGGAGGAGCACCGCTACAGCGCGGCGGGCGTCTCG
CTGCTCGAGCCGCCGCTGCAGCTCTACTGGACCTGGCTGCTCCAGTGGATCCCGCTCTGG
ATGGCCCCCAACTCCATCACCCTGCTGGGGCTCGCCGTCAACGTGGTCACCACGCTCGTG
CTCATCTCCTACTGTCCCACGGCCACCGAAGAGGCACCATACTGGACATACCTTTTATGT
GCACTGGGACTTTTTATTTACCAGTCACTGGATGCTATTGATGGGAAACAAGCCAGAAGA
ACAAACTCTTGTTCCCCTTTAGGGGAGCTCTTTGACCATGGCTGTGACTCTCTTTCCACA
GTATTTATGGCAGTGGGAGCTTCAATTGCCGCTCGCTTAGGAACTTATCCTGACTGGTTT
TTTTTCTGCTCTTTTATTGGGATGTTTGTGTTTTATTGCGCTCATTGGCAGACTTATGTT
TCAGGCATGTTGAGATTTGGAAAAGTGGATGTAACTGAAATTCAGATAGCTTTAGTGATT
GTCTTTGTGTTGTCTGCATTTGGAGGAGCAACAATGTGGGACTATACGATTCCTATTCTA
GAAATAAAATTGAAGATCCTTCCAGTTCTTGGATTTCTAGGTGGAGTAATATTTTCCTGT
TCAAATTATTTCCATGTTATCCTCCATGGTGGTGTTGGCAAGAATGGATCCACTATAGCA
GGCACCAGTGTCTTGTCACCTGGACTCCACATAGGACTAATTATTATACTGGCAATAATG
ATCTATAAAAAGTCAGCAACTGATGTGTTTGAAAAGCATCCTTGTCTTTATATCCTAATG
TTTGGATGTGTCTTTGCTAAAGTCTCACAAAAATTAGTGGTAGCTCACATGACCAAAAGT
GAACTATATCTTCAAGACACTGTCTTTTTGGGGCCAGGTCTTTTGTTTTTAGACCAGTAC
TTTAATAACTTTATAGACGAATATGTTGTTCTATGGATGGCAATGGTGATTTCTTCATTT
GATATGGTGATATACTTTAGTGCTTTGTGCCTGCAAATTTCAAGACACCTTCATCTAAAT
ATATTCAAGACTGCATGTCATCAAGCACCTGAACAGGTTCAAGTTCTTTCTTCAAAGAGT
CATCAGAATAACATGGATTGA
Protein Properties
Number of Residues 406
Molecular Weight 45096.535
Theoretical pI 6.92
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Cholinephosphotransferase 1
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
GenBank ID Protein 50726996
UniProtKB/Swiss-Prot ID Q8WUD6
UniProtKB/Swiss-Prot Entry Name CHPT1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_020244.2
GeneCard ID CHPT1
GenAtlas ID CHPT1
HGNC ID HGNC:17852
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  3. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed:16303743 ]
  4. Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [PubMed:10893425 ]
  5. Sinha Roy S, Mukherjee S, Kabir S, Rajaratnam V, Smith M, Das SK: Inhibition of cholinephosphotransferase activity in lung injury induced by 2-chloroethyl ethyl sulfide, a mustard analog. J Biochem Mol Toxicol. 2005;19(5):289-97. [PubMed:16292752 ]
  6. Ghosh A, Akech J, Mukherjee S, Das SK: Differential expression of cholinephosphotransferase in normal and cancerous human mammary epithelial cells. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1043-8. [PubMed:12359261 ]
  7. Henneberry AL, Wright MM, McMaster CR: The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity. Mol Biol Cell. 2002 Sep;13(9):3148-61. [PubMed:12221122 ]