- CDS2
CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2, also known as CDS2, is a human
gene .cite web | title = Entrez Gene: CDS2 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8760| accessdate = ]PBB_Summary
section_title =
summary_text = Breakdown products of phosphoinositides are ubiquitous second messengers that function downstream of many G protein-coupled receptors and tyrosine kinases regulating cell growth, calcium metabolism, and protein kinase C activity. This gene encodes an enzyme which regulates the amount of phosphatidylinositol available for signaling by catalyzing the conversion of phosphatidic acid to CDP-diacylglycerol. This enzyme is an integral membrane protein localized to two subcellular domains, the matrix side of the inner mitochondrial membrane where it is thought to be involved in the synthesis of phosphatidylglycerol and cardiolipin and the cytoplasmic side of the endoplasmic reticulum where it functions in phosphatidylinositol biosynthesis. Two genes encoding this enzyme have been identified in humans, one mapping to human chromosome 4q21 and a second to 20p13.cite web | title = Entrez Gene: CDS2 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8760| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Lykidis A, Jackson PD, Rock CO, Jackowski S |title=The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33402–9 |year= 1998 |pmid= 9407135 |doi=
*cite journal | author=Halford S, Dulai KS, Daw SC, "et al." |title=Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes. |journal=Genomics |volume=54 |issue= 1 |pages= 140–4 |year= 1999 |pmid= 9806839 |doi= 10.1006/geno.1998.5547
*cite journal | author=Volta M, Bulfone A, Gattuso C, "et al." |title=Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene. |journal=Genomics |volume=55 |issue= 1 |pages= 68–77 |year= 1999 |pmid= 9889000 |doi= 10.1006/geno.1998.5610
*cite journal | author=Deloukas P, Matthews LH, Ashurst J, "et al." |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a
*cite journal | author=Halford S, Inglis S, Gwilliam R, "et al." |title=Genomic organization of human CDS2 and evaluation as a candidate gene for corneal hereditary endothelial dystrophy 2 on chromosome 20p13. |journal=Exp. Eye Res. |volume=75 |issue= 5 |pages= 619–23 |year= 2002 |pmid= 12457874 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Olsen JV, Blagoev B, Gnad F, "et al." |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026PBB_Controls
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