| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-05-05 20:58:46 |
| Accession Number |
HMDB01413 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Citicoline |
| Description |
Citicoline is an essential intermediate in the biosynthetic pathway of structural phospholipids in cell membranes, particularly phosphatidylcholine. Once absorbed, citicoline is widely distributed throughout the body, crosses the blood-brain barrier and reaches the central nervous system (CNS), where it is incorporated into the membrane and microsomal phospholipid fraction. Citicoline activates biosynthesis of structural phospholipids of neuronal membranes, increases brain metabolism, and acts upon the levels of different neurotransmitters. Thus, citicoline has been experimentally shown to increase norepinephrine and dopamine levels in the CNS. Owing to these pharmacological mechanisms, citicoline has a neuroprotective effect in hypoxic and ischemic conditions, decreasing the volume of ischemic lesion, and also improves learning and memory performance in animal models of brain aging. In addition, citicoline has been shown to restore the activity of mitochondrial ATPase and membrane Na+/K+ATPase, to inhibit activation of certain phospholipases, and to accelerate reabsorption of cerebral edema in various experimental models. Citicoline has also been shown to be able to inhibit mechanisms of apoptosis associated to cerebral ischemia and in certain neurodegeneration models, and to potentiate neuroplasticity mechanisms. Citicoline is a safe drug, as shown by the toxicological tests conducted, that has no significant systemic cholinergic effects and is a well tolerated product. (PMID: 17171187) |
| Synonyms |
- Audes
- CDP-choline
- Cereb
- Choline 5'-cytidine diphosphate
- Choline cytidine diphosphate
- Citicholine
- Citicoline
- Citidoline
- Citifar
- Colite
- Corenalin
- Cyscholin
- Cytidine 5'-(choline diphosphate)
- Cytidine 5'-(cholinyl pyrophosphate)
- Cytidine 5'-diphosphate choline
- Cytidine 5'-diphosphocholine
- Cytidine 5-diphosphate-trihydrogen
- Cytidine choline diphosphate
- Cytidine diphosphate choline
- Cytidine diphosphate choline ester
- Cytidine diphosphocholine
- Cytidine diphosphorylcholine
- cytidine-5' diphosphocholine
- cytidine-5'-pyrophosphate-hydroxycholine
- Cytidoline
- Difosfocin
- Emicholine F
- Ensign
- Haocolin
- Hornbest
- Neucolis
- Nicholin
- Nicolin
- Niticolin
- P-hydroxide[2-(trimethylammonio)ethyl] ester
- Reagin
- Recofnan
- Recognan
- Rexort
- Sintoclar
- Somazina
- Somazine
- Suncholin
|
| Chemical IUPAC Name |
2-[[[5-(4-amino-2-oxo-pyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxyethyl-trimethyl-azanium |
| Chemical Formula |
C14H26N4O11P2 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Nucleosides and Nucleoside conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- cation
- anion
- secondary alcohol
- 1,2-diol
- primary amine
- primary aromatic amine
- quaternary ammonium salt
- oxo(het)arene
- phosphoric acid ester
- aromatic compound
- heterocyclic compound
|
| Biofunction |
- Component of Aminophosphonate metabolism
- Component of Glycerophospholipid metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
488.324 |
| Monoisotopic Molecular Weight |
488.107330 |
| Isomeric SMILES |
C[N+](C)(C)CCOP([O-])(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=CC(N)=NC1=O |
| Canonical SMILES |
C[N+](C)(C)CCOP([O-])(=O)OP(O)(=O)OCC1OC(C(O)C1O)N1C=CC(N)=NC1=O |
| KEGG Compound ID |
C00307  |
| BioCyc ID |
CDP-CHOLINE  |
| BiGG ID |
1485298  |
| Wikipedia Link |
Citicoline  |
| NuGOwiki Link |
HMDB01413  |
| Metagene Link |
HMDB01413  |
| METLIN ID |
6229  |
| PubChem Compound |
291  |
| PubChem Substance |
6048955  |
| ChEBI ID |
16436  |
| CAS Registry Number |
987-78-0 |
| InChI Identifier |
InChI=1/C14H26N4O11P2/c1-18(2,3)6-7-26-30(22,23)29-31(24,25)27-8-9-11(19)12(20)13(28-9)17-5-4-10(15)16-14(17)21/h4-5,9,11-13,19-20H,6-8H2,1-3H3,(H3-,15,16,21,22,23,24,25)/t9-,11-,12-,13-/m1/s1 |
| Synthesis Reference |
Fujio, Tatsuro. New production method of useful substances using ATP regeneration system. Kiraru Tekunoroji no Shintenkai (2001), 187-198. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 7.99 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-6.94 [MEYLAN,WM & HOWARD,PH (1995)]; -1.38 [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
|
| Biofluid Location |
Not Available |
| Tissue Location |
| Tissue |
References |
| Brain |
— |
| Erythrocyte |
— |
| Intestine |
— |
|
| Concentrations (Normal) |
Not Available |
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Porciatti V, Schiavi C, Benedetti P, Baldi A, Campos EC: Cytidine-5'-diphosphocholine improves visual acuity, contrast sensitivity and visually-evoked potentials of amblyopic subjects. Curr Eye Res. 1998 Feb;17(2):141-8. [PubMed
]
- Babb SM, Wald LL, Cohen BM, Villafuerte RA, Gruber SA, Yurgelun-Todd DA, Renshaw PF: Chronic citicoline increases phosphodiesters in the brains of healthy older subjects: an in vivo phosphorus magnetic resonance spectroscopy study. Psychopharmacology (Berl). 2002 May;161(3):248-54. Epub 2002 Mar 22. [PubMed
]
- Alvarez XA, Mouzo R, Pichel V, Perez P, Laredo M, Fernandez-Novoa L, Corzo L, Zas R, Alcaraz M, Secades JJ, Lozano R, Cacabelos R: Double-blind placebo-controlled study with citicoline in APOE genotyped Alzheimer's disease patients. Effects on cognitive performance, brain bioelectrical activity and cerebral perfusion. Methods Find Exp Clin Pharmacol. 1999 Nov;21(9):633-44. [PubMed
]
- Laurence AD, Layton M, Duley JA, Simmonds HA: Elevated erythrocyte CDP-choline levels associated with beta-thalassaemia in patients with transfusion independent anaemia. Nucleosides Nucleotides Nucleic Acids. 2004 Oct;23(8-9):1265-7. [PubMed
]
- Friedman D, Cycowicz YM, Bersick M: The late negative episodic memory effect: the effect of recapitulating study details at test. Brain Res Cogn Brain Res. 2005 May;23(2-3):185-98. Epub 2004 Nov 21. [PubMed
]
- Alvarez XA, Laredo M, Corzo D, Fernandez-Novoa L, Mouzo R, Perea JE, Daniele D, Cacabelos R: Citicoline improves memory performance in elderly subjects. Methods Find Exp Clin Pharmacol. 1997 Apr;19(3):201-10. [PubMed
]
- Paglia DE, Valentine WN, Nakatani M, Rauth BJ: Selective accumulation of cytosol CDP-choline as an isolated erythrocyte defect in chronic hemolysis. Proc Natl Acad Sci U S A. 1983 May;80(10):3081-5. [PubMed
]
- Hayashida K: [Usefulness of SPECT images in helping radiologists understand brain diseases] Nippon Igaku Hoshasen Gakkai Zasshi. 2001 Apr;61(5):208-14. [PubMed
]
- Renshaw PF, Daniels S, Lundahl LH, Rogers V, Lukas SE: Short-term treatment with citicoline (CDP-choline) attenuates some measures of craving in cocaine-dependent subjects: a preliminary report. Psychopharmacology (Berl). 1999 Feb;142(2):132-8. [PubMed
]
- Weiss GB: Metabolism and actions of CDP-choline as an endogenous compound and administered exogenously as citicoline. Life Sci. 1995;56(9):637-60. [PubMed
]
- Petersen A, Borregaard N: A family with chronic haemolysis and selective accumulation of erythrocyte CDP-choline. Leukemia. 1997 Aug;11(8):1373-6. [PubMed
]
- de la Morena E: Efficacy of CDP-choline in the treatment of senile alterations in memory. Ann N Y Acad Sci. 1991;640:233-6. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Choline-phosphate cytidylyltransferase B
- Choline-phosphate cytidylyltransferase A
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Choline phosphotransferase 1
- cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c)
- cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6007 |
| Enzyme 1 Name |
Choline-phosphate cytidylyltransferase B |
| Enzyme 1 Synonyms |
- Phosphorylcholine transferase B
- CTP:phosphocholine cytidylyltransferase B
- CT B
- CCT B
- CCT-beta
|
| Enzyme 1 Gene Name |
PCYT1B |
| Enzyme 1 Protein Sequence |
>Choline-phosphate cytidylyltransferase B
MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHE
KLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHK
FKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRY
RFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWK
QMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISS
MSEGDEDEK
|
| Enzyme 1 Number of Residues |
369 |
| Enzyme 1 Molecular Weight |
41940 |
| Enzyme 1 Theoretical pI |
6.36 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 1 Specific Function |
Controls phosphatidylcholine synthesis |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- CTP + choline phosphate = diphosphate + CDP-choline
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
3153239  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9Y5K3  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PCY1B_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>993 bp
ATGCCAGTAGTTACCACTGATGCTGAGTCAGAAACAGGTATCCCAAAATCCCTTTCCAAT
GAGCCTCCCTCAGAAACCATGGAGGAAATAGAGCACACATGCCCACAGCCTCGACTGACC
CTGACTGCACCTGCCCCATTTGCTGATGAAACCAACTGCCAGTGTCAAGCACCCCATGAA
AAACTGACCATTGCTCAGGCCCGCTTAGGAACACCAGCTGACAGGCCTGTCAGAGTATAC
GCCGATGGAATATTTGACCTCTTCCACTCAGGTCATGCAAGAGCCCTTATGCAAGCAAAA
ACACTGTTTCCCAACAGCTACTTGTTGGTAGGAGTTTGCAGTGATGATCTCACCCACAAA
TTCAAAGGTTTCACCGTGATGAATGAAGCCGAGAGATACGAAGCTCTCAGACACTGTCGC
TACGTAGACGAAGTTATCAGAGATGCTCCCTGGACACTCACGCCAGAGTTTCTGGAAAAA
CACAAGATTGACTTTGTGGCTCATGATGACATTCCGTATTCCTCTGCTGGCTCTGATGAT
GTTTACAAGCACATAAAGGAAGCAGGGATGTTCGTTCCAACGCAGAGAACAGAAGGCATC
TCAACATCGGACATCATTACCAGAATTGTTCGTGACTATGATGTTTATGCCCGACGTAAC
CTCCAGAGAGGGTATACAGCCAAGGAACTGAATGTCAGCTTTATAAATGAGAAGAGGTAC
CGTTTCCAGAACCAAGTGGACAAAATGAAGGAAAAAGTCAAGAATGTGGAGGAAAGATCA
AAGGAATTTGTGAACAGAGTGGAAGAAAAGAGCCATGATCTAATTCAAAAGTGGGAAGAG
AAGTCAAGGGAATTCATTGGCAACTTCCTAGAACTGTTTGGACCTGATGGAGCATGGAAG
CAGATGTTCCAGGAGAGGAGCAGCCGGATGCTGCAGGCCTTATCCCCGAAGCAGAGCCCT
CTGAAGAGTTGGGCGAGGTGCAGAGACTTCTAG
|
| Enzyme 1 GenBank Gene ID |
AF052510  |
| Enzyme 1 GeneCard ID |
PCYT1B  |
| Enzyme 1 GenAtlas ID |
PCYT1B  |
| Enzyme 1 HGNC ID |
HGNC:8755  |
| Enzyme 1 Chromosome Location |
X |
| Enzyme 1 Locus |
Xp22.11 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Lykidis A, Murti KG, Jackowski S: Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. J Biol Chem. 1998 May 29;273(22):14022-9. [PubMed
]
- Lykidis A, Baburina I, Jackowski S: Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant. J Biol Chem. 1999 Sep 17;274(38):26992-7001. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6030 |
| Enzyme 2 Name |
Choline-phosphate cytidylyltransferase A |
| Enzyme 2 Synonyms |
- Phosphorylcholine transferase A
- CTP:phosphocholine cytidylyltransferase A
- CT A
- CCT A
- CCT-alpha
|
| Enzyme 2 Gene Name |
PCYT1A |
| Enzyme 2 Protein Sequence |
>Choline-phosphate cytidylyltransferase A
MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYV
RVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHN
FKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKY
HLQERVDKVKEKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALK
HMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYD
ISEDEED
|
| Enzyme 2 Number of Residues |
367 |
| Enzyme 2 Molecular Weight |
41732 |
| Enzyme 2 Theoretical pI |
6.85 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 2 Specific Function |
Controls phosphatidylcholine synthesis |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- CTP + choline phosphate = diphosphate + CDP-choline
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
575486  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P49585  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PCY1A_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1104 bp
ATGGATGCACAGTGTTCAGCCAAGGTCAATGCAAGGAAGAGGAGAAAAGAGGCGCCCGGA
CCCAACGGGGCAACAGAAGAAGATGGGGTTCCTTCCAAAGTGCAGCGCTGTGCAGTGGGC
TTACGGCAACCAGCTCCTTTTTCTGATGAAATTGAAGTTGACTTTAGTAAGCCCTATGTC
AGGGTAACTATGGAAGAAGCCAGCAGAGGAACTCCTTGTGAGCGACCTGTGAGAGTTTAT
GCCGATGGAATATTTGACTTATTTCACTCTGGTCACGCCCGAGCTCTGATGCAAGCGAAG
AACCTTTTCCCTAATACGTACCTCATTGTGGGAGTTTGCAGTGATGAGCTCACACACAAC
TTCAAAGGCTTCACGGTGATGAACGAGAATGAGCGCTATGACGCAGTCCAGCACTGCCGC
TACGTGGATGAGGTGGTGAGGAATGCGCCCTGGACGCTGACACCCGAGTTCCTGGCCGAA
CACCGGATTGATTTTGTAGCCCATGATGATATTCCTTATTCATCTGCTGGCAGTGATGAT
GTTTATAAGCACATCAAGGAGGCAGGCATGTTTGCTCCAACACAGAGGACAGAAGGTATC
TCCACATCAGACATCATCACCCGAATTGTGCGGGATTATGATGTGTATGCGAGGCGGAAC
CTGCAGAGGGGCTACACAGCAAAGGAGCTCAATGTCAGCTTTATCAACGAGAAGAAATAC
CACTTGCAGGAGAGGGTTGACAAAGTAAAGGAGAAAGTGAAAGATGTGGAGGAAAAGTCA
AAAGAATTTGTTCAGAAGGTGGAGGAAAAAAGCATTGACCTCATTCAGAAGTGGGAGGAG
AAGTCCCGAGAATTCATTGGAAGTTTTCTGGAAATGTTTGGTCCGGAAGGAGCACTGAAA
CATATGCTGAAAGAGGGGAAGGGCCGGATGCTGCAGGCCATCAGCCCGAAGCAGAGCCCC
AGCAGCAGCCCTACTCGCGAGCGCTCCCCCTCCCCCTCTTTCCGATGGCCCTTCTCCGGC
AAGACTTCCCCACCTTGCTCCCCAGCAAATCTCTCCAGGCACAAGGCTGCAGCCTATGAT
ATCAGTGAGGATGAAGAAGACTAA
|
| Enzyme 2 GenBank Gene ID |
L28957  |
| Enzyme 2 GeneCard ID |
PCYT1A  |
| Enzyme 2 GenAtlas ID |
PCYT1A  |
| Enzyme 2 HGNC ID |
HGNC:8754  |
| Enzyme 2 Chromosome Location |
3 |
| Enzyme 2 Locus |
3q29 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Kalmar GB, Kay RJ, LaChance AC, Cornell RB: Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase. Biochim Biophys Acta. 1994 Oct 18;1219(2):328-34. [PubMed
]
- Dunne SJ, Cornell RB, Johnson JE, Glover NR, Tracey AS: Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry. 1996 Sep 17;35(37):11975-84. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6054 |
| Enzyme 3 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 1 |
| Enzyme 3 Synonyms |
- Transmembrane protein 23
- Sphingomyelin synthase 1
- Protein Mob
|
| Enzyme 3 Gene Name |
TMEM23 |
| Enzyme 3 Protein Sequence |
>Phosphatidylcholine:ceramide cholinephosphotransferase 1
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSS
DNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKE
MIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFF
DHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTT
LPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYL
FIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQ
VLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT
|
| Enzyme 3 Number of Residues |
419 |
| Enzyme 3 Molecular Weight |
49208 |
| Enzyme 3 Theoretical pI |
8.51 |
| Enzyme 3 GO Classification |
Not Available |
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Bidirectional lipid cholinephosphotransferases capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
- 142-162
190-210
221-241
282-302
310-330
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
30908857  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q86VZ5  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SMS1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1242 bp
ATGAAGGAAGTGGTTTATTGGTCACCCAAGAAGGTGGCAGACTGGCTGCTGGAGAATGCT
ATGCCAGAATACTGTGAGCCTCTGGAGCATTTCACAGGCCAGGACTTGATCAACCTAACC
CAAGAGGATTTCAAAAAACCCCCCTTGTGCCGAGTCTCCTCTGACAACGGGCAGCGGCTC
CTGGACATGATAGAAACCCTGAAAATGGAGCACCATTTGGAAGCACACAAGAACGGCCAT
GCCAATGGGCACCTCAACATTGGCGTAGACATCCCCACCCCCGACGGCAGCTTCAGCATC
AAGATTAAACCCAACGGGATGCCAAATGGGTATAGGAAAGAGATGATAAAGATCCCCATG
CCAGAACTGGAGCGCTCTCAGTACCCCATGGAGTGGGGCAAGACTTTTCTGGCCTTTCTT
TATGCACTTTCCTGTTTCGTTCTCACCACAGTGATGATCTCGGTCGTCCACGAACGAGTA
CCTCCTAAGGAGGTGCAGCCTCCACTACCGGACACATTTTTTGACCATTTTAACCGGGTG
CAGTGGGCCTTTTCTATTTGTGAAATTAATGGCATGATCCTTGTAGGACTCTGGTTAATT
CAGTGGCTGCTCTTAAAATACAAGTCTATTATTAGCAGAAGATTTTTCTGCATAGTTGGC
ACGCTGTACCTGTATCGGTGTATTACAATGTATGTAACTACACTCCCAGTACCTGGTATG
CATTTCAACTGTTCTCCGAAGCTTTTCGGAGACTGGGAAGCCCAACTGCGAAGAATAATG
AAGCTCATTGCTGGAGGTGGCTTGTCTATCACTGGCTCTCACAACATGTGTGGGGACTAT
CTGTACAGCGGCCACACGGTCATGCTAACACTTACCTACTTATTTATCAAAGAGTATTCC
CCTCGGCGACTCTGGTGGTATCACTGGATTTGCTGGCTTCTCAGCGTAGTTGGAATCTTC
TGTATTCTCTTAGCGCATGACCACTACACTGTGGACGTGGTGGTGGCATATTACATCACC
ACGAGACTCTTCTGGTGGTATCACACTATGGCCAATCAGCAAGTGCTAAAGGAAGCTTCC
CAGATGAACCTCCTGGCCAGGGTGTGGTGGTACAGGCCATTTCAGTACTTTGAAAAGAAT
GTCCAAGGAATTGTACCTCGATCTTACCATTGGCCTTTCCCCTGGCCAGTAGTCCACCTC
AGTAGGCAAGTTAAATACAGCCGGCTGGTGAATGACACATAA
|
| Enzyme 3 GenBank Gene ID |
AY280959  |
| Enzyme 3 GeneCard ID |
TMEM23  |
| Enzyme 3 GenAtlas ID |
TMEM23  |
| Enzyme 3 HGNC ID |
HGNC:29799  |
| Enzyme 3 Chromosome Location |
10 |
| Enzyme 3 Locus |
10q11.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
Not Available |
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
8362 |
| Enzyme 4 Name |
Choline phosphotransferase 1 |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
CHPT1 |
| Enzyme 4 Protein Sequence |
>Choline phosphotransferase 1
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
|
| Enzyme 4 Number of Residues |
406 |
| Enzyme 4 Molecular Weight |
45097 |
| Enzyme 4 Theoretical pI |
6.92 |
| Enzyme 4 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 4 General Function |
Lipid transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
- 60-82
- 92-110
- 159-181
- 191-213
- 226-248
- 263-282
- 295-317
- 349-371
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
18089162  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q8WUD6  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
Q8WUD6_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 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
|
| Enzyme 4 GenBank Gene ID |
BC020819  |
| Enzyme 4 GeneCard ID |
CHPT1  |
| Enzyme 4 GenAtlas ID |
CHPT1  |
| Enzyme 4 HGNC ID |
HGNC:17852  |
| Enzyme 4 Chromosome Location |
12 |
| Enzyme 4 Locus |
12q |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
16483 |
| Enzyme 5 Name |
cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c) |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
CHPT1 |
| Enzyme 5 Protein Sequence |
>cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c)
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
|
| Enzyme 5 Number of Residues |
406 |
| Enzyme 5 Molecular Weight |
45097 |
| Enzyme 5 Theoretical pI |
6.92 |
| Enzyme 5 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 5 General Function |
Lipid transport and metabolism |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
B3KQM2  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
B3KQM2_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AK075211  |
| Enzyme 5 GeneCard ID |
B3KQM2  |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
Not Available |
| Enzyme 5 Chromosome Location |
12 |
| Enzyme 5 Locus |
12q |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
16484 |
| Enzyme 6 Name |
cDNA, FLJ94713 (Putative uncharacterized protein MGC26963) |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
MGC26963 |
| Enzyme 6 Protein Sequence |
>cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
|
| Enzyme 6 Number of Residues |
365 |
| Enzyme 6 Molecular Weight |
42281 |
| Enzyme 6 Theoretical pI |
9.00 |
| Enzyme 6 GO Classification |
Not Available |
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
Not Available |
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
B2RA61  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
B2RA61_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
AK314049  |
| Enzyme 6 GeneCard ID |
B2RA61  |
| Enzyme 6 GenAtlas ID |
Not Available |
| Enzyme 6 HGNC ID |
Not Available |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |