DGKA

Protein-coding gene in humans
DGKA
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1TUZ

Identifiers
AliasesDGKA, DAGK, DAGK1, DGK-alpha, diacylglycerol kinase alpha
External IDsOMIM: 125855 MGI: 102952 HomoloGene: 1028 GeneCards: DGKA
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for DGKA
Genomic location for DGKA
Band12q13.2Start55,927,319 bp[1]
End55,954,027 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for DGKA
Genomic location for DGKA
Band10 D3|10 77.14 cMStart128,556,003 bp[2]
End128,580,724 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • skin of abdomen

  • spleen

  • lymph node

  • minor salivary glands

  • thymus

  • rectum

  • appendix

  • jejunal mucosa

  • thymus

  • ascending aorta
Top expressed in
  • thymus

  • lymph node

  • corneal stroma

  • blood

  • spleen

  • spermatid

  • colon

  • left colon

  • seminiferous tubule

  • submandibular gland
More reference expression data
BioGPS


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
  • plasma membrane
  • membrane
  • intracellular anatomical structure
Biological process
  • platelet activation
  • protein kinase C-activating G protein-coupled receptor signaling pathway
  • intracellular signal transduction
  • phosphorylation
  • glycerolipid metabolic process
  • phosphatidic acid biosynthetic process
  • diacylglycerol metabolic process
  • lipid phosphorylation
  • metabolism
  • signal transduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
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 MbChr 10: 128.56 – 128.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000065357 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: DGKA diacylglycerol kinase, alpha 80kDa".

Further reading

[1]*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, Vandekerckhove J, Van Damme J, Gussow D, Ploegh HL, Van Blitterswijk WJ, Van Der Bend RL (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, Kanoh H, Merida I (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, Mérida I, Wakelam MJ (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, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Sanjuán MA, Pradet-Balade B, Jones DR, Martínez-a C, Stone JC, Garcia-Sanz JA, Mérida I (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, Jennings JL, Link AJ, Patton JG (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, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H (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, Clish CB, Odparlik S, Hasturk H, Badwey JA, Colgan SP, Van Dyke TE (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, Albanese N, Hahn C, Gamble JR, Chatterjee VK, Vadas MA, Xia P (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. S2CID 25057646.
  • Baldanzi G, Mitola S, Cutrupi S, Filigheddu N, Van Blitterswijk WJ, Sinigaglia F, Bussolino F, Graziani A (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. hdl:11379/21460. PMID 15122338.
  • Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (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, Merino E, Mérida I, Izquierdo M (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, Capomagi C, Colombo E, Van Blitterswijk WJ, Graziani A, Fazioli F (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, Imai S, Yamada K, Yamashita T, Jimbow K, Kanoh H, Sakane F (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
  • v
  • t
  • e
  • 1tuz: NMR Structure of the Diacylglycerol kinase alpha, NESGC target HR532
    1tuz: NMR Structure of the Diacylglycerol kinase alpha, NESGC target HR532


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  1. ^ Kovalenko A, Sanin A, Kosmas K, Zhang L, Wang J, Giannikou K, Probst CK, Hougard TR, Rue RW, Krymskaya VP, Asara JM, Lam HC, Kwiatkowski DJ, Henske EP, Filippakis H (2021). "Therapeutic Targeting of DGKA-Mediated Macropinocytosis Leads to Phospholipid Reprogramming in Tuberous Sclerosis Complex". Cancer Research. 81 (8): 2086–2100. doi:10.1158/0008-5472.CAN-20-2218. PMC 8137542. PMID 33593821.