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{{Infobox_gene}}
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'''Diacylglycerol kinase alpha''' is an [[enzyme]] that in humans is encoded by the ''DGKA'' [[gene]].<ref name="pmid8180475">{{cite journal | vauthors = Hart TC, Champagne C, Zhou J, Van Dyke TE | title = Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12 | journal = Mamm Genome | volume = 5 | issue = 2 | pages = 123–4 |date=Jun 1994 | pmid = 8180475 | pmc =  | doi =10.1007/BF00292343 }}</ref><ref name="pmid7959783">{{cite journal | vauthors = Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ | title = Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis | journal = Genomics | volume = 22 | issue = 1 | pages = 246–7 |date=Dec 1994 | pmid = 7959783 | pmc =  | doi = 10.1006/geno.1994.1376 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DGKA diacylglycerol kinase, alpha 80kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1606| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DGKA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1tuz.
| PDB = {{PDB2|1tuz}}
| Name = Diacylglycerol kinase, alpha 80kDa
| HGNCid = 2849
| Symbol = DGKA
| AltSymbols =; DAGK; DAGK1; DGK-alpha; MGC12821; MGC42356
| OMIM = 125855
| ECnumber =
| Homologene = 1028
| MGIid = 102952
| GeneAtlas_image1 = PBB_GE_DGKA_203385_at_tn.png
  | GeneAtlas_image2 = PBB_GE_DGKA_211272_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0004143 |text = diacylglycerol kinase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005543 |text = phospholipid binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1606
    | Hs_Ensembl = ENSG00000065357
    | Hs_RefseqProtein = NP_001336
    | Hs_RefseqmRNA = NM_001345
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 54611213
    | Hs_GenLoc_end = 54634072
    | Hs_Uniprot = P23743
    | Mm_EntrezGene = 13139
    | Mm_Ensembl = ENSMUSG00000025357
    | Mm_RefseqmRNA = NM_016811
    | Mm_RefseqProtein = NP_058091
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 128123083
    | Mm_GenLoc_end = 128147005
    | Mm_Uniprot = O88673
  }}
}}
'''Diacylglycerol kinase, alpha 80kDa''', also known as '''DGKA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DGKA diacylglycerol kinase, alpha 80kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1606| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: DGKA diacylglycerol kinase, alpha 80kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1606| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Topham MK, Prescott SM |title=Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions. |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11447-50 |year= 1999 |pmid= 10206945 |doi=  }}
*{{cite journal  | vauthors=Topham MK, Prescott SM |title=Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11447–50 |year= 1999 |pmid= 10206945 |doi=10.1074/jbc.274.17.11447 }}
*{{cite journal  | author=Schaap D, de Widt J, van der Wal J, ''et al.'' |title=Purification, cDNA-cloning and expression of human diacylglycerol kinase. |journal=FEBS Lett. |volume=275 |issue= 1-2 |pages= 151-8 |year= 1991 |pmid= 2175712 |doi=  }}
*{{cite journal  | author=Schaap D |title=Purification, cDNA-cloning and expression of human diacylglycerol kinase |journal=FEBS Lett. |volume=275 |issue= 1–2 |pages= 151–8 |year= 1991 |pmid= 2175712 |doi=10.1016/0014-5793(90)81461-V |name-list-format=vanc| author2=de Widt J | author3=van der Wal J  | display-authors=3  | last4=Vandekerckhove  | first4=Joel  | last5=Van Damme  | first5=Jose  | last6=Gussow  | first6=Detlef  | last7=Ploegh  | first7=Hidde L. | last8=Van Blitterswijk  | first8=Whim J.  | last9=Van Der Bend  | first9=Rob L. }}
*{{cite journal  | author=Hart TC, Zhou J, Champagne C, ''et al.'' |title=Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. |journal=Genomics |volume=22 |issue= 1 |pages= 246-7 |year= 1994 |pmid= 7959783 |doi= 10.1006/geno.1994.1376 }}
*{{cite journal  | author=Flores I |title=Phosphatidic acid generation through interleukin 2 (IL-2)-induced alpha-diacylglycerol kinase activation is an essential step in IL-2-mediated lymphocyte proliferation |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10334–40 |year= 1996 |pmid= 8626603 |doi=10.1074/jbc.271.17.10334 |name-list-format=vanc| author2=Casaseca T | author3=Martinez-A C | display-authors=3  | last4=Kanoh  | first4=H  | last5=Merida  | first5=I  }}
*{{cite journal  | author=Hart TC, Champagne C, Zhou J, Van Dyke TE |title=Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. |journal=Mamm. Genome |volume=5 |issue= 2 |pages= 123-4 |year= 1994 |pmid= 8180475 |doi=  }}
*{{cite journal  | author=Jones DR |title=Interleukin-2 causes an increase in saturated/monounsaturated phosphatidic acid derived from 1,2-diacylglycerol and 1-O-alkyl-2-acylglycerol |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16846–52 |year= 1999 |pmid= 10358029 |doi=10.1074/jbc.274.24.16846 |name-list-format=vanc| author2=Pettitt TR | author3=Sanjuán MA | display-authors=3  | last4=Mérida  | first4=I  | last5=Wakelam  | first5=MJ  }}
*{{cite journal  | author=Flores I, Casaseca T, Martinez-A C, ''et al.'' |title=Phosphatidic acid generation through interleukin 2 (IL-2)-induced alpha-diacylglycerol kinase activation is an essential step in IL-2-mediated lymphocyte proliferation. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10334-40 |year= 1996 |pmid= 8626603 |doi= }}
*{{cite journal  | vauthors=Sanjuán MA, Jones DR, Izquierdo M, Mérida I |title=Role of Diacylglycerol Kinase α in the Attenuation of Receptor Signaling |journal=J. Cell Biol. |volume=153 |issue= 1 |pages= 207–20 |year= 2001 |pmid= 11285286 |doi=10.1083/jcb.153.1.207  | pmc=2185527  }}
*{{cite journal | author=Jones DR, Pettitt TR, Sanjuán MA, ''et al.'' |title=Interleukin-2 causes an increase in saturated/monounsaturated phosphatidic acid derived from 1,2-diacylglycerol and 1-O-alkyl-2-acylglycerol. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16846-52 |year= 1999 |pmid= 10358029 |doi= }}
*{{cite journal  | author=Strausberg RL |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 | pmc=139241 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Sanjuán MA, Jones DR, Izquierdo M, Mérida I |title=Role of diacylglycerol kinase alpha in the attenuation of receptor signaling. |journal=J. Cell Biol. |volume=153 |issue= 1 |pages= 207-20 |year= 2001 |pmid= 11285286 |doi=  }}
*{{cite journal  | author=Sanjuán MA |title=T cell activation in vivo targets diacylglycerol kinase alpha to the membrane: a novel mechanism for Ras attenuation |journal=J. Immunol. |volume=170 |issue= 6 |pages= 2877–83 |year= 2003 |pmid= 12626538 |doi=  10.4049/jimmunol.170.6.2877|name-list-format=vanc| author2=Pradet-Balade B | author3=Jones DR  | display-authors=3  | last4=Martínez-a  | first4=C  | last5=Stone  | first5=JC  | last6=Garcia-Sanz  | first6=JA  | last7=Mérida  | first7=I }}
*{{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=Li J |title=Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7437–47 |year= 2003 |pmid= 14559993 |doi=10.1128/MCB.23.21.7437-7447.2003 | pmc=207616  |name-list-format=vanc| author2=Hawkins IC  | author3=Harvey CD  | display-authors=3 | last4=Jennings  | first4=J. L.  | last5=Link  | first5=A. J.  | last6=Patton  | first6=J. G. }}
*{{cite journal  | author=Sanjuán MA, Pradet-Balade B, Jones DR, ''et al.'' |title=T cell activation in vivo targets diacylglycerol kinase alpha to the membrane: a novel mechanism for Ras attenuation. |journal=J. Immunol. |volume=170 |issue= 6 |pages= 2877-83 |year= 2003 |pmid= 12626538 |doi=  }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285  |name-list-format=vanc| author2=Suzuki Y | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal | author=Li J, Hawkins IC, Harvey CD, ''et al.'' |title=Regulation of alternative splicing by SRrp86 and its interacting proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7437-47 |year= 2003 |pmid= 14559993 |doi=  }}
*{{cite journal  | author=Gronert K |title=A molecular defect in intracellular lipid signaling in human neutrophils in localized aggressive periodontal tissue damage |journal=J. Immunol. |volume=172 |issue= 3 |pages= 1856–61 |year= 2004 |pmid= 14734770 |doi= 10.4049/jimmunol.172.3.1856|name-list-format=vanc| author2=Kantarci A  | author3=Levy BD  | display-authors=3  | last4=Clish  | first4=CB  | last5=Odparlik  | first5=S  | last6=Hasturk  | first6=H  | last7=Badwey  | first7=JA  | last8=Colgan  | first8=SP  | last9=Van Dyke  | first9=TE  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Verrier E |title=PPARgamma agonists ameliorate endothelial cell activation via inhibition of diacylglycerol-protein kinase C signaling pathway: role of diacylglycerol kinase |journal=Circ. Res. |volume=94 |issue= 11 |pages= 1515–22 |year= 2004 |pmid= 15117825 |doi= 10.1161/01.RES.0000130527.92537.06  |name-list-format=vanc| author2=Wang L  | author3=Wadham C  | display-authors=3  | last4=Albanese  | first4=N  | last5=Hahn  | first5=C  | last6=Gamble  | first6=JR  | last7=Chatterjee  | first7=VK  | last8=Vadas  | first8=MA  | last9=Xia  | first9=P }}
*{{cite journal | author=Gronert K, Kantarci A, Levy BD, ''et al.'' |title=A molecular defect in intracellular lipid signaling in human neutrophils in localized aggressive periodontal tissue damage. |journal=J. Immunol. |volume=172 |issue= 3 |pages= 1856-61 |year= 2004 |pmid= 14734770 |doi=  }}
*{{cite journal  | author=Baldanzi G |title=Activation of diacylglycerol kinase alpha is required for VEGF-induced angiogenic signaling in vitro |journal=Oncogene |volume=23 |issue= 28 |pages= 4828–38 |year= 2004 |pmid= 15122338 |doi= 10.1038/sj.onc.1207633  |name-list-format=vanc| author2=Mitola S  | author3=Cutrupi S  | display-authors=3  | last4=Filigheddu  | first4=Nicoletta  | last5=Van Blitterswijk  | first5=Wim J  | last6=Sinigaglia  | first6=Fabiola  | last7=Bussolino  | first7=Federico  | last8=Graziani  | first8=Andrea }}
*{{cite journal  | author=Verrier E, Wang L, Wadham C, ''et al.'' |title=PPARgamma agonists ameliorate endothelial cell activation via inhibition of diacylglycerol-protein kinase C signaling pathway: role of diacylglycerol kinase. |journal=Circ. Res. |volume=94 |issue= 11 |pages= 1515-22 |year= 2004 |pmid= 15117825 |doi= 10.1161/01.RES.0000130527.92537.06 }}
*{{cite journal  | author=Gerhard DS |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  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal | author=Baldanzi G, Mitola S, Cutrupi S, ''et al.'' |title=Activation of diacylglycerol kinase alpha is required for VEGF-induced angiogenic signaling in vitro. |journal=Oncogene |volume=23 |issue= 28 |pages= 4828-38 |year= 2004 |pmid= 15122338 |doi= 10.1038/sj.onc.1207633 }}
*{{cite journal  | author=Alonso R |title=Diacylglycerol kinase alpha regulates the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes |journal=J. Biol. Chem. |volume=280 |issue= 31 |pages= 28439–50 |year= 2005 |pmid= 15870081 |doi= 10.1074/jbc.M501112200  |name-list-format=vanc| author2=Rodríguez MC  | author3=Pindado J  | display-authors=3  | last4=Merino  | first4=E  | last5=Mérida  | first5=I  | last6=Izquierdo  | first6=M }}
*{{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=Bacchiocchi R |title=Activation of alpha-diacylglycerol kinase is critical for the mitogenic properties of anaplastic lymphoma kinase |journal=Blood |volume=106 |issue= 6 |pages= 2175–82 |year= 2005 |pmid= 15928040 |doi= 10.1182/blood-2005-01-0316  |name-list-format=vanc| author2=Baldanzi G  | author3=Carbonari D  | display-authors=3  | last4=Capomagi  | first4=C  | last5=Colombo  | first5=E  | last6=Van Blitterswijk  | first6=WJ  | last7=Graziani  | first7=A  | last8=Fazioli  | first8=F }}
*{{cite journal  | author=Alonso R, Rodríguez MC, Pindado J, ''et al.'' |title=Diacylglycerol kinase alpha regulates the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes. |journal=J. Biol. Chem. |volume=280 |issue= 31 |pages= 28439-50 |year= 2005 |pmid= 15870081 |doi= 10.1074/jbc.M501112200 }}
*{{cite journal  | author=Yanagisawa K |title=Diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation |journal=Biochim. Biophys. Acta |volume=1771 |issue= 4 |pages= 462–74 |year= 2007 |pmid= 17276726 |doi= 10.1016/j.bbalip.2006.12.008  |name-list-format=vanc| author2=Yasuda S  | author3=Kai M  | display-authors=3  | last4=Imai  | first4=S  | last5=Yamada  | first5=K  | last6=Yamashita  | first6=T  | last7=Jimbow  | first7=K  | last8=Kanoh  | first8=H  | last9=Sakane  | first9=F }}
*{{cite journal  | author=Bacchiocchi R, Baldanzi G, Carbonari D, ''et al.'' |title=Activation of alpha-diacylglycerol kinase is critical for the mitogenic properties of anaplastic lymphoma kinase. |journal=Blood |volume=106 |issue= 6 |pages= 2175-82 |year= 2005 |pmid= 15928040 |doi= 10.1182/blood-2005-01-0316 }}
*{{cite journal  | author=Yanagisawa K, Yasuda S, Kai M, ''et al.'' |title=Diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation. |journal=Biochim. Biophys. Acta |volume=1771 |issue= 4 |pages= 462-74 |year= 2007 |pmid= 17276726 |doi= 10.1016/j.bbalip.2006.12.008 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* [http://www.expasy.org/prosite/PDOC50146 DAG-kinase catalytic (DAGKc) domain] in [[PROSITE]]
 
{{PDB Gallery|geneid=1606}}
 
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{{gene-12-stub}}
 
[[Category:EF-hand-containing proteins]]

Latest revision as of 18:24, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Diacylglycerol kinase alpha is an enzyme that in humans is encoded by the DGKA gene.[1][2][3]

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.[3]

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: DGKA diacylglycerol kinase, alpha 80kDa".

Further reading

External links



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