DGKA

Diacylglycerol kinase alpha is an enzyme that in humans is encoded by the DGKA gene.[5][6][7]

DGKA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1TUZ
Identifiers
Aliases	DGKA, DAGK, DAGK1, DGK-alpha, diacylglycerol kinase alpha
External IDs	OMIM: 125855 MGI: 102952 HomoloGene: 1028 GeneCards: DGKA
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.2 Start 55,927,319 bp[1] End 55,954,027 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 D3|10 77.14 cM Start 128,720,134 bp[2] End 128,744,855 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • calcium ion binding • phospholipid binding • ATP binding • metal ion binding • kinase activity • diacylglycerol kinase activity • NAD+ kinase activity Cellular component • cytosol • cell membrane • membrane • intracellular Biological process • platelet activation • protein kinase C-activating G-protein coupled receptor signaling pathway • GO:0007243 intracellular signal transduction • phosphorylation • glycerolipid metabolic process • phosphatidic acid biosynthetic process • diacylglycerol metabolic process • lipid phosphorylation • metabolism • signal transduction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1606	13139
Ensembl	ENSG00000065357	ENSMUSG00000025357
UniProt	P23743	O88673
RefSeq (mRNA)	NM_001345 NM_201444 NM_201445 NM_201554 NM_001351033 NM_001351034 NM_001351035 NM_001351036 NM_001351037 NM_001351038 NM_001351039 NM_001351040	NM_016811 NM_001358745 NM_001358746 NM_001372366 NM_001374028
RefSeq (protein)	NP_001336 NP_958852 NP_958853 NP_963848 NP_001337962 NP_001337963 NP_001337964 NP_001337965 NP_001337966 NP_001337967 NP_001337968 NP_001337969	NP_058091 NP_001345674 NP_001345675 NP_001359295 NP_001360957
Location (UCSC)	Chr 12: 55.93 – 55.95 Mb	Chr 10: 128.72 – 128.74 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene belongs to the eukaryotic diacylglycerol kinase family. It acts as a modulator that competes with protein kinase C for the second messenger diacylglycerol in intracellular signaling pathways. It also plays an important role in the resynthesis of phosphatidylinositols and phosphorylating diacylglycerol to phosphatidic acid. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000065357 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025357 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Hart TC, Champagne C, Zhou J, Van Dyke TE (Jun 1994). "Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12". Mamm Genome. 5 (2): 123–4. doi:10.1007/BF00292343. PMID 8180475. S2CID 305119.
6. Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ (Dec 1994). "Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis". Genomics. 22 (1): 246–7. doi:10.1006/geno.1994.1376. PMID 7959783.
7. "Entrez Gene: DGKA diacylglycerol kinase, alpha 80kDa".

Further reading

• Topham MK, Prescott SM (1999). "Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions". J. Biol. Chem. 274 (17): 11447–50. doi:10.1074/jbc.274.17.11447. PMID 10206945.
• Schaap D, de Widt J, van der Wal J, et al. (1991). "Purification, cDNA-cloning and expression of human diacylglycerol kinase". FEBS Lett. 275 (1–2): 151–8. doi:10.1016/0014-5793(90)81461-V. PMID 2175712. S2CID 45452518.
• Flores I, Casaseca T, Martinez-A C, et al. (1996). "Phosphatidic acid generation through interleukin 2 (IL-2)-induced alpha-diacylglycerol kinase activation is an essential step in IL-2-mediated lymphocyte proliferation". J. Biol. Chem. 271 (17): 10334–40. doi:10.1074/jbc.271.17.10334. PMID 8626603.
• Jones DR, Pettitt TR, Sanjuán MA, et al. (1999). "Interleukin-2 causes an increase in saturated/monounsaturated phosphatidic acid derived from 1,2-diacylglycerol and 1-O-alkyl-2-acylglycerol". J. Biol. Chem. 274 (24): 16846–52. doi:10.1074/jbc.274.24.16846. PMID 10358029.
• Sanjuán MA, Jones DR, Izquierdo M, Mérida I (2001). "Role of Diacylglycerol Kinase α in the Attenuation of Receptor Signaling". J. Cell Biol. 153 (1): 207–20. doi:10.1083/jcb.153.1.207. PMC 2185527. PMID 11285286.
• 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. PMC 139241. PMID 12477932.
• Sanjuán MA, Pradet-Balade B, Jones DR, et al. (2003). "T cell activation in vivo targets diacylglycerol kinase alpha to the membrane: a novel mechanism for Ras attenuation". J. Immunol. 170 (6): 2877–83. doi:10.4049/jimmunol.170.6.2877. PMID 12626538.
• Li J, Hawkins IC, Harvey CD, et al. (2003). "Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins". Mol. Cell. Biol. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616. PMID 14559993.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gronert K, Kantarci A, Levy BD, et al. (2004). "A molecular defect in intracellular lipid signaling in human neutrophils in localized aggressive periodontal tissue damage". J. Immunol. 172 (3): 1856–61. doi:10.4049/jimmunol.172.3.1856. PMC 4318492. PMID 14734770.
• Verrier E, Wang L, Wadham C, et al. (2004). "PPARgamma agonists ameliorate endothelial cell activation via inhibition of diacylglycerol-protein kinase C signaling pathway: role of diacylglycerol kinase". Circ. Res. 94 (11): 1515–22. doi:10.1161/01.RES.0000130527.92537.06. PMID 15117825.
• Baldanzi G, Mitola S, Cutrupi S, et al. (2004). "Activation of diacylglycerol kinase alpha is required for VEGF-induced angiogenic signaling in vitro". Oncogene. 23 (28): 4828–38. doi:10.1038/sj.onc.1207633. PMID 15122338.
• 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. PMC 528928. PMID 15489334.
• Alonso R, Rodríguez MC, Pindado J, et al. (2005). "Diacylglycerol kinase alpha regulates the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes". J. Biol. Chem. 280 (31): 28439–50. doi:10.1074/jbc.M501112200. PMID 15870081.
• Bacchiocchi R, Baldanzi G, Carbonari D, et al. (2005). "Activation of alpha-diacylglycerol kinase is critical for the mitogenic properties of anaplastic lymphoma kinase". Blood. 106 (6): 2175–82. doi:10.1182/blood-2005-01-0316. PMID 15928040.
• Yanagisawa K, Yasuda S, Kai M, et al. (2007). "Diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation". Biochim. Biophys. Acta. 1771 (4): 462–74. doi:10.1016/j.bbalip.2006.12.008. PMID 17276726.

External links

• DAG-kinase catalytic (DAGKc) domain in PROSITE