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DGKA (diacylglycerol kinase, alpha 80kDa)

Written2013-12Isabel Merida, Antonia Avila-Flores
Department of Immunology, Oncology, National Center for Biotechnology (CNB/CSIC). Darwin 3, Campus Autonoma/CSIC, Madrid 28049, Spain

(Note : for Links provided by Atlas : click)

Identity

Alias_namesDAGK
DAGK1
diacylglycerol kinase, alpha (80kD)
diacylglycerol kinase, alpha 80kDa
Alias_symbol (synonym)DGK-alpha
Other alias
HGNC (Hugo) DGKA
LocusID (NCBI) 1606
Atlas_Id 40299
Location 12q13.2  [Link to chromosome band 12q13]
Location_base_pair Starts at 55931162 and ends at 55954023 bp from pter ( according to hg19-Feb_2009)  [Mapping DGKA.png]
Local_order GSTP1-WIBG-DGKA-PMEL-CDK2.
Fusion genes
(updated 2016)
DGKA (12q13.2) / RGS22 (8q22.2)EML3 (11q12.3) / DGKA (12q13.2)NAV2 (11p15.1) / DGKA (12q13.2)
NDUFB5 (3q26.33) / DGKA (12q13.2)
Note Diacylglycerol kinase alpha (DGKA) is a lipid kinase that phosphorylates the lipid diacylglycerol (DAG), transforming it into phosphatidic acid (PA). DGKA is classified as a type I DGK, characterized by possessing EF-hand motifs, which allow calcium mediated regulation. DGKA has been characterized as a negative regulator of Ras-MAPK pathway in T lymphocytes. DGKA has a dual role in cancer; it exhibits properties similar to a tumor suppressor and has also a positive role in the maintenance of cancerous states. DGKA function might be crucial in the genesis and development of several pathologies.

DNA/RNA

Note DGKA gene is highly expressed in thymus, spleen, testis and lung (Sanjuan et al., 2001). DGKA displays alternative splicing; numerous splice variants are predicted, including truncated forms of the protein as well as RNAs with introns retained (Martínez-Moreno et al., 2012). The expression of some of these transcripts might be related to certain pathologies (Batista et al., 2013).
 
  Figure 1. The DGKA gene is located at chromosome 12. It contains 24 exons and the translation initiator ATG is located at Exon 2.
Figure 2. Putative regulatory elements in the DGKA gene. Transcription initiation sites are indicated (arrows). The +1 position was assigned in the Inr element. Putative binding sites for transcription factors are indicated by rectangles; FoxO sites are gray (Adapted from Martinez-Moreno et al., 2012).
Transcription The DGKA gene encodes a protein of 80 KDa. Presence of regulatory regions in the gene was early suggested to restrain the expression of DGKA to certain tissues (Fujikawa et al., 1993). DGKA gene displays alternative use of promoter regions, in homology with the mouse gene at least two alternative promoters likely exist. The regulatory gene region contain several binding motifs for transcription factors including FoxO, p53, Egr, Smad, etc, which allow the coupling of DGKA expression with several signaling pathways. Identification of DGKA as a gene regulated by FoxO has contributed to explain its transcriptional downregulation in response to antigen stimulation and interleukin 2 (IL2) (Martinez-Moreno et al., 2012).

Protein

Note The protein encoded by the DGKA gene (2.7.1.107) belongs to the eukaryotic diacylglycerol kinase family. It attenuates the second messenger diacylglycerol, that activates C1-containing proteins like members of the classical and novel PKCs, PKD, RasGRP and chimaerin families. It also produces phosphatidic acid, another lipid mediator that participates in the resynthesis of phosphatidylinositols and activates different proteins like mTOR or atypical PKCs.
 
  Figure 3. Distribution of conserved and specific regions in DGKA. C1, conserved protein kinase C-type 1 regions. Y218, Tyrosine phosphorylated by c-Abl. Y335, Tyrosine phosphorylated by Src and Lck. PPP Pro-rich region proposed to interact with Src.
Description -The diacylglycerol kinases (DGK) are a family of signaling proteins that modulate diacylglycerol levels by catalyzing its conversion to phosphatidic acid (Merida et al., 2008). DGK belongs to a superfamily that also includes the recently identified bacterial DgkB as well as the sphingosine kinase (SPK) and ceramide kinase (CERK) families. Proteins in this superfamily share a common catalytic domain (DAGKc: Pfam00781).
-In addition to the catalytic region, all DGK family members have at least two protein kinase C-like type 1 (C1) domains that, except for the first C1 domain in DGKB and DGKG, lack the key residues that define a canonical phorbol ester/DAG-binding C1 domain (Shindo et al., 2003).
- Mammals express ten DGK isoforms grouped into five subtypes; each DGK subtype has distinct regulatory motifs that suggest the existence of diverse regulatory mechanisms and/or participation in different signaling complexes.
- Diacylglycerol Kinase alpha (DGKA) together with the beta (DGKB) and gamma (DGKG) isoforms represent the type I DGK, whose signature is the presence at the N-terminal region of a recoverin-like domain (RVH) and a tandem of EF hand motifs, characteristic of Ca2+-binding proteins.
Expression - DGKA is the only DGK isoform particularly enriched in the thymus and peripheral T lymphocytes. DGKA levels are tightly coupled to the differentiation and proliferation state of T lymphocytes. Quiescent, naïve T lymphocytes express high levels of DGKA that decrease rapidly in response to antigenic and IL2-derived signals (Martinez-Moreno et al., 2012). DGKA was identified as an anergy-induced gene (Macian et al., 2002). Anergy represents an unresponsive state in T cells that is vital in immune system homeostasis and constitutes a means for avoiding response to self and thus, for preventing autoimmunity. Tumors also induce anergic-non responsive states in T cells. In agreement with this finding, DGKA-overexpressing lymphocytes are "anergic" and no longer respond to antigenic stimuli (Zha et al., 2006). On the contrary, T cells from DGKA deficient mice are resistant to anergy induction (Olenchock et al., 2006).
- Recent studies have characterized miR-297 as a highly cytotoxic microRNA expressed in glioblastoma, with minimal cytotoxicity to normal astrocytes. DGKA is shown to be a miR-297 target with a critical role in miR-297 toxicity. These studies identify miR-297 as a novel and physiologic regulator of cancer cell survival, largely through targeting of DGKA (Kefas et al., 2013).
Localisation - DGKA is a cytosolic enzyme that translocates to the membrane to phosphorylate diacylglycerol. The N-terminal region of DGKA, encompassing the Ca2+ regulatory elements has a negative regulatory role in enzyme activation and receptor-induced membrane localization, as shown by enhanced activity and constitutive plasma membrane localization of a mutant lacking this region (Sanjuan et al., 2001). In addition to Ca2+ generation, activation of Tyr kinases is required for membrane stabilization of DGKA (Sanjuan et al., 2001). Tyr335 in the human sequence, located at the hinge between the C1 and the catalytic domains, was recently identified as an Lck-dependent DGKA phosphorylation site in T lymphocytes (Merino et al., 2008).
- Membrane localization of DGKA in non-T cells requires Src-family tyrosine kinase activity and involves the association of DGKA with Src via a proline-rich sequence (Baldanzi et al., 2008). DGKA membrane localization and activation is required for cell motility, proliferation and angiogenesis, acting as a rheostat that sets the thresholds required for growth factor-induced migratory signals.
- Recent reports have suggested nuclear localization for DGKA following serum starvation and demonstrated that DGKA relocates back to the cytosol in response to serum re-addition. Serum-induced export requires c-Abl mediated Tyr-218 phosphorylation (Matsubara et al., 2012).
Function - The best characterized function for DGKA as a negative modulator of diacylglycerol-based signaling has been demonstrated in T lymphocytes. DGKA acts as a "switch-off" signal for Ras activation, mediated by localization to the membrane of Ras-GRP1 a GDP-exchanger for Ras with a DAG-binding domain (Sanjuan et al., 2001; Sanjuan et al., 2003).
- Contrary to its negative contribution to T cell responses, high DGKA expression in tumors appears to have a positive role in neoplastic transformation. DGKA-dependent PA generation contributes to melanoma survival through activation of the NFKB pathway (Yanagisawa et al., 2007).
- DGKA mediated PA generation has been reported to participate in tumor migration and invasion. Generation of PA downstream of DGKA is essential to facilitate the Rab coupling protein (RCP)- mediated integrin recycling that is required for tumor cell invasion (Rainiero et al., 2012).
 

Mutations

Note V379I mutation in DGKA identified as a putative driver mutation for pancreatic cancer.

Implicated in

Note
  
Entity Lymphoma
Note DGKA was found to be constitutively activated in nucleophosmin/anaplastic lymphoma kinase (NPM / ALK) fusion in malignant lymphomas, where inhibition of DGKA significantly reduced tumor growth (Bacchiocchi et al., 2005).
  
  
Entity Melanoma
Note DGKA has been implicated in suppression of TNF-alpha induced apoptosis of human melanoma cells via NF-KB (Yanagisawa et al., 2005).
  
  
Entity Hepatocellular carcinoma
Note DGKA is absent in hepatocytes but it is expressed in different hepatocellular carcinoma cell lines. DGKA is found expressed in cancerous tissue but not in the adjacent non-cancerous hepatocytes. High DGKA expression associates with high Ki67 expression and a high rate of HCC recurrence (p=0.033) following surgery. In multivariate analyses, high DGKA expression is found as an independent factor for determining HCC recurrence after surgery (Takeishi et al., 2012).
  
  
Entity Pancreatic carcinoma
Note Using CHASM (Cancer-specific High-throughput Annotation of Somatic Mutations) V379I mutation in DGKA was found as a putative driver mutation for pancreatic cancer (Carter et al., 2010).
  
  
Entity Glioblastoma
Note Recent studies have described DGKA as an important component of malignant transformation in glioblastoma (Dominguez et al., 2013). Impaired DGKA activity through siRNA targeting or the use of small-molecule inhibitors induced caspase-mediated apoptosis in glioblastoma cells, but lacked toxicity in noncancerous cells.
  
  
Entity Lung cancer
Note Survival trees in a study involving the expression profiles of 3588 genes in 211 lung adenocarcinoma patients identified DGKA as a marker for good survival in a group of advanced-stage patients with remarkably good survival outcome (Berrar et al., 2005).
  
  
Entity X-linked proliferative disease
Note Studies have reported DGKA inhibition by the adaptor protein SAP (Baldanzi et al., 2011). Loss-of-function SAP mutations cause X-linked lymphoproliferative disease (XLP), an immune disorder characterized by a deregulated immune response to Epstein-Barr virus, susceptibility to lymphoma and defective antibody production. Impaired regulation of DGKA activity in SAP-deficient lymphocytes may contribute to their defective TCR-induced responses, suggesting that pharmacological inhibition of DGKA could be useful in the treatment of certain manifestations of XLP.
  
  
Entity CD8 tumor infiltrates
Note DGKA was found to be more highly expressed in CD8-tumor infiltrates T cells (TILs) in renal carcinoma that in circulating CD8 cells (Prinz et al., 2012). Low dose treatment of TILs with IL2 reduced DGKA protein levels, improved stimulation-induced ERK and AKT phosphorylation, and increased the number of degranulating CD8-TILs. DGKA inhibition could be a novel strategy to enhance anti-tumor CD8 T cells response and may help prevent inactivation of adoptively transferred T cells improving therapeutic efficacy.
  
  
Entity Localized aggressive periodontitis (LAP)
Note Localized aggressive periodontitis (LAP) is a familial disorder characterized by destruction of the supporting structures of dentition. Microarray and kinetic-PCR analysis revealed diminished RNA expression of DGKA in neutrophils from LAP patients compared with asymptomatic individuals (Gronert et al., 2004).
  

Bibliography

Activation of alpha-diacylglycerol kinase is critical for the mitogenic properties of anaplastic lymphoma kinase.
Bacchiocchi R, Baldanzi G, Carbonari D, Capomagi C, Colombo E, van Blitterswijk WJ, Graziani A, Fazioli F.
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SAP-mediated inhibition of diacylglycerol kinase α regulates TCR-induced diacylglycerol signaling.
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Alternative Splicing Generates a Diacylglycerol Kinase α (DGKα) Transcript That Acts as a Dominant Negative Modulator of Superoxide Production in Localized Aggressive Periodontitis.
Batista EL Jr, Kantarci AI, Hasturk H, Van Dyke TE.
J Periodontol. 2013 Oct 30.
PMID 24171497
 
Survival trees for analyzing clinical outcome in lung adenocarcinomas based on gene expression profiles: identification of neogenin and diacylglycerol kinase alpha expression as critical factors.
Berrar D, Sturgeon B, Bradbury I, Downes CS, Dubitzky W.
J Comput Biol. 2005 Jun;12(5):534-44.
PMID 15952876
 
Prioritization of driver mutations in pancreatic cancer using cancer-specific high-throughput annotation of somatic mutations (CHASM).
Carter H, Samayoa J, Hruban RH, Karchin R.
Cancer Biol Ther. 2010 Sep 15;10(6):582-7. Epub 2010 Oct 1.
PMID 20581473
 
Diacylglycerol kinase α is a critical signaling node and novel therapeutic target in glioblastoma and other cancers.
Dominguez CL, Floyd DH, Xiao A, Mullins GR, Kefas BA, Xin W, Yacur MN, Abounader R, Lee JK, Wilson GM, Harris TE, Purow BW.
Cancer Discov. 2013 Jul;3(7):782-97. doi: 10.1158/2159-8290.CD-12-0215. Epub 2013 Apr 4.
PMID 23558954
 
Isolation and characterization of the human diacylglycerol kinase gene.
Fujikawa K, Imai S, Sakane F, Kanoh H.
Biochem J. 1993 Sep 1;294 ( Pt 2):443-9.
PMID 8396913
 
A molecular defect in intracellular lipid signaling in human neutrophils in localized aggressive periodontal tissue damage.
Gronert K, Kantarci A, Levy BD, Clish CB, Odparlik S, Hasturk H, Badwey JA, Colgan SP, Van Dyke TE, Serhan CN.
J Immunol. 2004 Feb 1;172(3):1856-61.
PMID 14734770
 
A miR-297/hypoxia/DGK-α axis regulating glioblastoma survival.
Kefas B, Floyd DH, Comeau L, Frisbee A, Dominguez C, Dipierro CG, Guessous F, Abounader R, Purow B.
Neuro Oncol. 2013 Dec;15(12):1652-63. doi: 10.1093/neuonc/not118. Epub 2013 Oct 24.
PMID 24158111
 
Transcriptional mechanisms underlying lymphocyte tolerance.
Macian F, Garcia-Cozar F, Im SH, Horton HF, Byrne MC, Rao A.
Cell. 2002 Jun 14;109(6):719-31.
PMID 12086671
 
FoxO-dependent regulation of diacylglycerol kinase α gene expression.
Martinez-Moreno M, Garcia-Lievana J, Soutar D, Torres-Ayuso P, Andrada E, Zhong XP, Koretzky GA, Merida I, Avila-Flores A.
Mol Cell Biol. 2012 Oct;32(20):4168-80. Epub 2012 Aug 13.
PMID 22890845
 
c-Abl tyrosine kinase regulates serum-induced nuclear export of diacylglycerol kinase α by phosphorylation at Tyr-218.
Matsubara T1, Ikeda M, Kiso Y, Sakuma M, Yoshino K, Sakane F, Merida I, Saito N, Shirai Y.
J Biol Chem. 2012 Feb 17;287(8):5507-17. doi: 10.1074/jbc.M111.296897. Epub 2011 Dec 23.
PMID 22199356
 
Diacylglycerol kinases: at the hub of cell signalling.
Merida I, Avila-Flores A, Merino E.
Biochem J. 2008 Jan 1;409(1):1-18. (REVIEW)
PMID 18062770
 
Lck-dependent tyrosine phosphorylation of diacylglycerol kinase alpha regulates its membrane association in T cells.
Merino E, Avila-Flores A, Shirai Y, Moraga I, Saito N, Merida I.
J Immunol. 2008 May 1;180(9):5805-15.
PMID 18424699
 
Disruption of diacylglycerol metabolism impairs the induction of T cell anergy.
Olenchock BA, Guo R, Carpenter JH, Jordan M, Topham MK, Koretzky GA, Zhong XP.
Nat Immunol. 2006 Nov;7(11):1174-81. Epub 2006 Oct 8.
PMID 17028587
 
High DGK-α and disabled MAPK pathways cause dysfunction of human tumor-infiltrating CD8+ T cells that is reversible by pharmacologic intervention.
Prinz PU, Mendler AN, Masouris I, Durner L, Oberneder R, Noessner E.
J Immunol. 2012 Jun 15;188(12):5990-6000. doi: 10.4049/jimmunol.1103028. Epub 2012 May 9.
PMID 22573804
 
Diacylglycerol kinase α controls RCP-dependent integrin trafficking to promote invasive migration.
Rainero E, Caswell PT, Muller PA, Grindlay J, McCaffrey MW, Zhang Q, Wakelam MJ, Vousden KH, Graziani A, Norman JC.
J Cell Biol. 2012 Jan 23;196(2):277-95. doi: 10.1083/jcb.201109112.
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T cell activation in vivo targets diacylglycerol kinase alpha to the membrane: a novel mechanism for Ras attenuation.
Sanjuan MA, Pradet-Balade B, Jones DR, Martinez-A C, Stone JC, Garcia-Sanz JA, Merida I.
J Immunol. 2003 Mar 15;170(6):2877-83.
PMID 12626538
 
Synthesis and phorbol ester binding of the cysteine-rich domains of diacylglycerol kinase (DGK) isozymes. DGKgamma and DGKbeta are new targets of tumor-promoting phorbol esters.
Shindo M, Irie K, Masuda A, Ohigashi H, Shirai Y, Miyasaka K, Saito N.
J Biol Chem. 2003 May 16;278(20):18448-54. Epub 2003 Mar 5.
PMID 12621060
 
Diacylglycerol kinase alpha enhances hepatocellular carcinoma progression by activation of Ras-Raf-MEK-ERK pathway.
Takeishi K, Taketomi A, Shirabe K, Toshima T, Motomura T, Ikegami T, Yoshizumi T, Sakane F, Maehara Y.
J Hepatol. 2012 Jul;57(1):77-83. doi: 10.1016/j.jhep.2012.02.026. Epub 2012 Mar 14.
PMID 22425622
 
Diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation.
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PMID 17276726
 
T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-alpha.
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Citation

This paper should be referenced as such :
Merida, I ; Avila-Flores, A
DGKA (diacylglycerol kinase, alpha 80kDa)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(8):545-549.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/DGKAID40299ch12q13.html


External links

Nomenclature
HGNC (Hugo)DGKA   2849
Cards
AtlasDGKAID40299ch12q13
Entrez_Gene (NCBI)DGKA  1606  diacylglycerol kinase alpha
AliasesDAGK; DAGK1; DGK-alpha
GeneCards (Weizmann)DGKA
Ensembl hg19 (Hinxton)ENSG00000065357 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000065357 [Gene_View]  chr12:55931162-55954023 [Contig_View]  DGKA [Vega]
ICGC DataPortalENSG00000065357
TCGA cBioPortalDGKA
AceView (NCBI)DGKA
Genatlas (Paris)DGKA
WikiGenes1606
SOURCE (Princeton)DGKA
Genetics Home Reference (NIH)DGKA
Genomic and cartography
GoldenPath hg38 (UCSC)DGKA  -     chr12:55931162-55954023 +  12q13.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)DGKA  -     12q13.2   [Description]    (hg19-Feb_2009)
EnsemblDGKA - 12q13.2 [CytoView hg19]  DGKA - 12q13.2 [CytoView hg38]
Mapping of homologs : NCBIDGKA [Mapview hg19]  DGKA [Mapview hg38]
OMIM125855   
Gene and transcription
Genbank (Entrez)AF064767 AF064768 AF064769 AF064770 AF064771
RefSeq transcript (Entrez)NM_001345 NM_001351033 NM_001351034 NM_001351035 NM_001351036 NM_001351037 NM_001351038 NM_001351039 NM_001351040 NM_201444 NM_201445 NM_201554
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)DGKA
Cluster EST : UnigeneHs.524488 [ NCBI ]
CGAP (NCI)Hs.524488
Alternative Splicing GalleryENSG00000065357
Gene ExpressionDGKA [ NCBI-GEO ]   DGKA [ EBI - ARRAY_EXPRESS ]   DGKA [ SEEK ]   DGKA [ MEM ]
Gene Expression Viewer (FireBrowse)DGKA [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1606
GTEX Portal (Tissue expression)DGKA
Protein : pattern, domain, 3D structure
UniProt/SwissProtP23743   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP23743  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP23743
Splice isoforms : SwissVarP23743
Catalytic activity : Enzyme2.7.1.107 [ Enzyme-Expasy ]   2.7.1.1072.7.1.107 [ IntEnz-EBI ]   2.7.1.107 [ BRENDA ]   2.7.1.107 [ KEGG ]   
PhosPhoSitePlusP23743
Domaine pattern : Prosite (Expaxy)DAGK (PS50146)    EF_HAND_1 (PS00018)    EF_HAND_2 (PS50222)    ZF_DAG_PE_1 (PS00479)    ZF_DAG_PE_2 (PS50081)   
Domains : Interpro (EBI)DAG_kinase_typeI_N    Diacylglycerol_kin_accessory    Diacylglycerol_kinase_cat_dom    EF-hand-dom_pair    EF_Hand_1_Ca_BS    EF_hand_dom    NAD/diacylglycerol_kinase    PE/DAG-bd   
Domain families : Pfam (Sanger)C1_1 (PF00130)    DAG_kinase_N (PF14513)    DAGK_acc (PF00609)    DAGK_cat (PF00781)   
Domain families : Pfam (NCBI)pfam00130    pfam14513    pfam00609    pfam00781   
Domain families : Smart (EMBL)C1 (SM00109)  DAGKa (SM00045)  DAGKc (SM00046)  EFh (SM00054)  
Conserved Domain (NCBI)DGKA
DMDM Disease mutations1606
Blocks (Seattle)DGKA
PDB (SRS)1TUZ   
PDB (PDBSum)1TUZ   
PDB (IMB)1TUZ   
PDB (RSDB)1TUZ   
Structural Biology KnowledgeBase1TUZ   
SCOP (Structural Classification of Proteins)1TUZ   
CATH (Classification of proteins structures)1TUZ   
SuperfamilyP23743
Human Protein AtlasENSG00000065357
Peptide AtlasP23743
HPRD00517
IPIIPI00333143   IPI01026253   IPI00644617   IPI01020939   IPI00102417   IPI01018190   IPI00942306   IPI01021238   IPI01022058   IPI01021569   IPI01022018   IPI01026097   IPI01024741   IPI01024864   IPI01026484   IPI01026130   IPI01026340   
Protein Interaction databases
DIP (DOE-UCLA)P23743
IntAct (EBI)P23743
FunCoupENSG00000065357
BioGRIDDGKA
STRING (EMBL)DGKA
ZODIACDGKA
Ontologies - Pathways
QuickGOP23743
Ontology : AmiGONAD+ kinase activity  diacylglycerol kinase activity  diacylglycerol kinase activity  calcium ion binding  ATP binding  phospholipid binding  cytosol  plasma membrane  phosphatidic acid biosynthetic process  protein kinase C-activating G-protein coupled receptor signaling pathway  membrane  kinase activity  platelet activation  intracellular signal transduction  diacylglycerol metabolic process  glycerolipid metabolic process  lipid phosphorylation  
Ontology : EGO-EBINAD+ kinase activity  diacylglycerol kinase activity  diacylglycerol kinase activity  calcium ion binding  ATP binding  phospholipid binding  cytosol  plasma membrane  phosphatidic acid biosynthetic process  protein kinase C-activating G-protein coupled receptor signaling pathway  membrane  kinase activity  platelet activation  intracellular signal transduction  diacylglycerol metabolic process  glycerolipid metabolic process  lipid phosphorylation  
Pathways : KEGGGlycerolipid metabolism    Glycerophospholipid metabolism    Phosphatidylinositol signaling system   
REACTOMEP23743 [protein]
REACTOME PathwaysR-HSA-114508 [pathway]   
NDEx NetworkDGKA
Atlas of Cancer Signalling NetworkDGKA
Wikipedia pathwaysDGKA
Orthology - Evolution
OrthoDB1606
GeneTree (enSembl)ENSG00000065357
Phylogenetic Trees/Animal Genes : TreeFamDGKA
HOVERGENP23743
HOGENOMP23743
Homologs : HomoloGeneDGKA
Homology/Alignments : Family Browser (UCSC)DGKA
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerDGKA [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)DGKA
dbVarDGKA
ClinVarDGKA
1000_GenomesDGKA 
Exome Variant ServerDGKA
ExAC (Exome Aggregation Consortium)DGKA (select the gene name)
Genetic variants : HAPMAP1606
Genomic Variants (DGV)DGKA [DGVbeta]
DECIPHERDGKA [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisDGKA 
Mutations
ICGC Data PortalDGKA 
TCGA Data PortalDGKA 
Broad Tumor PortalDGKA
OASIS PortalDGKA [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICDGKA  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDDGKA
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch DGKA
DgiDB (Drug Gene Interaction Database)DGKA
DoCM (Curated mutations)DGKA (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)DGKA (select a term)
intoGenDGKA
NCG5 (London)DGKA
Cancer3DDGKA(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM125855   
Orphanet
MedgenDGKA
Genetic Testing Registry DGKA
NextProtP23743 [Medical]
TSGene1606
GENETestsDGKA
Target ValidationDGKA
Huge Navigator DGKA [HugePedia]
snp3D : Map Gene to Disease1606
BioCentury BCIQDGKA
ClinGenDGKA
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD1606
Chemical/Pharm GKB GenePA27310
Clinical trialDGKA
Miscellaneous
canSAR (ICR)DGKA (select the gene name)
Probes
Litterature
PubMed47 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineDGKA
EVEXDGKA
GoPubMedDGKA
iHOPDGKA
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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