DGKG

Diacylglycerol kinase, gamma 90kDa
Identifiers
Symbols	DGKG ; DAGK3; DGK-GAMMA; MGC104993; MGC133330
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1029
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
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

Diacylglycerol kinase, gamma 90kDa, also known as DGKG, is a human gene.

This gene encodes an enzyme that is a member of the type I subfamily of diacylglycerol kinases, which are involved in lipid metabolism. These enzymes generate phosphatidic acid by catalyzing the phosphorylation of diacylglycerol, a fundamental lipid second messenger that activates numerous proteins, including protein kinase C isoforms, Ras guanyl nucleotide-releasing proteins and some transient receptor potential channels. Diacylglycerol kinase gamma has been implicated in cell cycle regulation and in the negative regulation of macrophage differentiation in leukemia cells. Multiple transcript variants encoding different isoforms have been found for this gene.

Further reading

• Brose N, Betz A, Wegmeyer H (2004). "Divergent and convergent signaling by the diacylglycerol second messenger pathway in mammals". Curr. Opin. Neurobiol. 14 (3): 328–40. doi:10.1016/j.conb.2004.05.006. PMID 15194113.CS1 maint: Multiple names: authors list (link)
• Luo B, Regier DS, Prescott SM, Topham MK (2005). "Diacylglycerol kinases". Cell. Signal. 16 (9): 983–9. doi:10.1016/j.cellsig.2004.03.016. PMID 15212759.CS1 maint: Multiple names: authors list (link)
• Topham MK (2006). "Signaling roles of diacylglycerol kinases". J. Cell. Biochem. 97 (3): 474–84. doi:10.1002/jcb.20704. PMID 16288460.
• Kai M, Sakane F, Imai S; et al. (1994). "Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells". J. Biol. Chem. 269 (28): 18492–8. PMID 8034597.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)
• Yamada K, Sakane F, Matsushima N, Kanoh H (1997). "EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes". Biochem. J. 321 ( Pt 1): 59–64. PMID 9003401.CS1 maint: Multiple names: authors list (link)
• Stöhr H, Klein J, Gehrig A; et al. (1999). "Mapping and genomic characterization of the gene encoding diacylglycerol kinase gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1)". Hum. Genet. 104 (1): 99–105. PMID 10071200.CS1 maint: Explicit use of et al. (link) 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)
• Yamada K, Sakane F, Imai S; et al. (2003). "Regulatory role of diacylglycerol kinase gamma in macrophage differentiation of leukemia cells". Biochem. Biophys. Res. Commun. 305 (1): 101–7. PMID 12732202.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Oyaizu K, Kantarci A, Maeda H; et al. (2003). "Identification of mRNAs for the various diacylglycerol kinase isoforms in neutrophils from patients with localized aggressive periodontitis". J. Periodont. Res. 38 (5): 488–95. PMID 12941073.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tsushima S, Kai M, Yamada K; et al. (2004). "Diacylglycerol kinase gamma serves as an upstream suppressor of Rac1 and lamellipodium formation". J. Biol. Chem. 279 (27): 28603–13. doi:10.1074/jbc.M314031200. PMID 15102830.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Filosto M, Mancuso M, Tomelleri G; et al. (2004). "Hepato-cerebral syndrome: genetic and pathological studies in an infant with a dGK mutation". Acta Neuropathol. 108 (2): 168–71. doi:10.1007/s00401-004-0872-9. PMID 15150663.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Batista EL, Warbington M, Badwey JA, Van Dyke TE (2005). "Differentiation of HL-60 cells to granulocytes involves regulation of select diacylglycerol kinases (DGKs)". J. Cell. Biochem. 94 (4): 774–93. doi:10.1002/jcb.20356. PMID 15578578.CS1 maint: Multiple names: authors list (link)
• Matsubara T, Shirai Y, Miyasaka K; et al. (2006). "Nuclear transportation of diacylglycerol kinase gamma and its possible function in the nucleus". J. Biol. Chem. 281 (10): 6152–64. doi:10.1074/jbc.M509873200. PMID 16407189.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yamaguchi Y, Shirai Y, Matsubara T; et al. (2006). "Phosphorylation and up-regulation of diacylglycerol kinase gamma via its interaction with protein kinase C gamma". J. Biol. Chem. 281 (42): 31627–37. doi:10.1074/jbc.M606992200. PMID 16905533.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)