Phosphatidic acid phosphatase type 2B, also known as PPAP2B, is a human gene.cite web | title = Entrez Gene: PPAP2B phosphatidic acid phosphatase type 2B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8613| accessdate = ]

section_title =
summary_text = The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is a membrane glycoprotein localized at the cell plasma membrane. It has been shown to actively hydrolyze extracellular lysophosphatidic acid and short-chain phosphatidic acid. The expression of this gene is found to be enhanced by epidermal growth factor in Hela cells. Alternatively spliced transcript variants encoding the same protein have been described.cite web | title = Entrez Gene: PPAP2B phosphatidic acid phosphatase type 2B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8613| accessdate = ]


Further reading

citations =
*cite journal | author=Nanjundan M, Possmayer F |title=Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase. |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=284 |issue= 1 |pages= L1–23 |year= 2003 |pmid= 12471011 |doi= 10.1152/ajplung.00029.2002
*cite journal | author=Andersson B, Wentland MA, Ricafrente JY, "et al." |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Yu W, Andersson B, Worley KC, "et al." |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=
*cite journal | author=Kai M, Wada I, Imai S, "et al." |title=Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24572–8 |year= 1997 |pmid= 9305923 |doi=
*cite journal | author=Roberts R, Sciorra VA, Morris AJ |title=Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 22059–67 |year= 1998 |pmid= 9705349 |doi=
*cite journal | author=Sciorra VA, Morris AJ |title=Sequential actions of phospholipase D and phosphatidic acid phosphohydrolase 2b generate diglyceride in mammalian cells. |journal=Mol. Biol. Cell |volume=10 |issue= 11 |pages= 3863–76 |year= 1999 |pmid= 10564277 |doi=
*cite journal | author=Ishikawa T, Kai M, Wada I, Kanoh H |title=Cell surface activities of the human type 2b phosphatidic acid phosphatase. |journal=J. Biochem. |volume=127 |issue= 4 |pages= 645–51 |year= 2000 |pmid= 10739957 |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=Humtsoe JO, Feng S, Thakker GD, "et al." |title=Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP. |journal=EMBO J. |volume=22 |issue= 7 |pages= 1539–54 |year= 2003 |pmid= 12660161 |doi= 10.1093/emboj/cdg165
*cite journal | author=Burnett C, Howard K |title=Fly and mammalian lipid phosphate phosphatase isoforms differ in activity both in vitro and in vivo. |journal=EMBO Rep. |volume=4 |issue= 8 |pages= 793–9 |year= 2004 |pmid= 12856002 |doi= 10.1038/sj.embor.embor900
*cite journal | author=Burnett C, Makridou P, Hewlett L, Howard K |title=Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity. |journal=BMC Biochem. |volume=5 |issue= |pages= 2 |year= 2004 |pmid= 14725715 |doi= 10.1186/1471-2091-5-2
*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=Kai M, Sakane F, Jia YJ, "et al." |title=Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts. |journal=J. Biochem. |volume=140 |issue= 5 |pages= 677–86 |year= 2007 |pmid= 17005594 |doi= 10.1093/jb/mvj195
*cite journal | author=Mechtcheriakova D, Wlachos A, Sobanov J, "et al." |title=FTY720-phosphate is dephosphorylated by lipid phosphate phosphatase 3. |journal=FEBS Lett. |volume=581 |issue= 16 |pages= 3063–8 |year= 2007 |pmid= 17555747 |doi= 10.1016/j.febslet.2007.05.069

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