PPAP2B

Phosphatidic acid phosphatase type 2B
Identifiers
Symbols	PPAP2B ; Dri42; LPP3; MGC15306; PAP-2b; PAP2-b; PAP2-beta; VCIP
External IDs	Template:OMIM5 Template:MGI HomoloGene: 15410
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PPAP2B 209355 s at tn.png
File:PBB GE PPAP2B 212226 s at tn.png
File:PBB GE PPAP2B 212230 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Phosphatidic acid phosphatase type 2B, also known as PPAP2B, is a human gene.

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.

Further reading

• Nanjundan M, Possmayer F (2003). "Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase". Am. J. Physiol. Lung Cell Mol. Physiol. 284 (1): L1–23. doi:10.1152/ajplung.00029.2002. PMID 12471011.
• Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.CS1 maint: Multiple names: authors list (link)
• Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kai M, Wada I, Imai S; et al. (1997). "Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase". J. Biol. Chem. 272 (39): 24572–8. PMID 9305923.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Roberts R, Sciorra VA, Morris AJ (1998). "Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform". J. Biol. Chem. 273 (34): 22059–67. PMID 9705349.CS1 maint: Multiple names: authors list (link)
• Sciorra VA, Morris AJ (1999). "Sequential actions of phospholipase D and phosphatidic acid phosphohydrolase 2b generate diglyceride in mammalian cells". Mol. Biol. Cell. 10 (11): 3863–76. PMID 10564277.
• Ishikawa T, Kai M, Wada I, Kanoh H (2000). "Cell surface activities of the human type 2b phosphatidic acid phosphatase". J. Biochem. 127 (4): 645–51. PMID 10739957.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Humtsoe JO, Feng S, Thakker GD; et al. (2003). "Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP". EMBO J. 22 (7): 1539–54. doi:10.1093/emboj/cdg165. PMID 12660161.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Burnett C, Howard K (2004). "Fly and mammalian lipid phosphate phosphatase isoforms differ in activity both in vitro and in vivo". EMBO Rep. 4 (8): 793–9. doi:10.1038/sj.embor.embor900. PMID 12856002.
• Burnett C, Makridou P, Hewlett L, Howard K (2004). "Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity". BMC Biochem. 5: 2. doi:10.1186/1471-2091-5-2. PMID 14725715.CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kai M, Sakane F, Jia YJ; et al. (2007). "Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts". J. Biochem. 140 (5): 677–86. doi:10.1093/jb/mvj195. PMID 17005594.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mechtcheriakova D, Wlachos A, Sobanov J; et al. (2007). "FTY720-phosphate is dephosphorylated by lipid phosphate phosphatase 3". FEBS Lett. 581 (16): 3063–8. doi:10.1016/j.febslet.2007.05.069. PMID 17555747.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)