PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32850820-9	2020	Manipulation of DAG levels by overexpression of the DAG kinase Dgk1, impacted localization of the DAG probe and affected fitness of the triple mutant.	Diglycerides	16-19	diacylglycerol kinase	Saccharomyces cerevisiae S288C	63-67
12604233-5	2003	Recently, we reported that the solubility of 11beta-HSD 1 could be increased by substitution of hydrophobic amino acid residues with arginine without affecting activity.	Arginine	133-141	diacylglycerol kinase	Saccharomyces cerevisiae S288C	45-57
32850820-9	2020	Manipulation of DAG levels by overexpression of the DAG kinase Dgk1, impacted localization of the DAG probe and affected fitness of the triple mutant.	Diglycerides	52-55	diacylglycerol kinase	Saccharomyces cerevisiae S288C	63-67
32058036-0	2020	Triglyceride deficiency and diacylglycerol kinase1 activity lead to the upregulation of mevalonate pathway in yeast: A study for the development of potential yeast platform for improved production of triterpenoid.	Mevalonic Acid	88-98	diacylglycerol kinase	Saccharomyces cerevisiae S288C	28-50
32058036-0	2020	Triglyceride deficiency and diacylglycerol kinase1 activity lead to the upregulation of mevalonate pathway in yeast: A study for the development of potential yeast platform for improved production of triterpenoid.	Triterpenes	200-212	diacylglycerol kinase	Saccharomyces cerevisiae S288C	28-50
28673963-7	2017	Loss of the DGK1-encoded diacylglycerol kinase, which converts diacylglycerol to phosphatidate, partially suppressed the pah1Delta-mediated induction of Cho1 and PSS activity.	Diglycerides	25-39	diacylglycerol kinase	Saccharomyces cerevisiae S288C	12-16
29649282-7	2018	In another yeast mutant that lacks both PAH1 and DGK1 (encodes diacylglycerol kinase converting diacylglycerol to PA), which has a normal nuclear membrane but maintains similar lipid compositional changes as in pah1Delta cells, BMV replicated as efficiently as in pah1Delta cells, suggesting that the altered lipid composition was responsible for the enhanced BMV replication.	Diglycerides	63-77	diacylglycerol kinase	Saccharomyces cerevisiae S288C	49-53
30910690-7	2020	The pah1Delta phenotypes requiring Dgk1 diacylglycerol kinase exemplify the importance of the phosphatidate level in the misregulation of cellular processes.	phosphatidate	94-107	diacylglycerol kinase	Saccharomyces cerevisiae S288C	35-39
28673963-7	2017	Loss of the DGK1-encoded diacylglycerol kinase, which converts diacylglycerol to phosphatidate, partially suppressed the pah1Delta-mediated induction of Cho1 and PSS activity.	phosphatidate	81-94	diacylglycerol kinase	Saccharomyces cerevisiae S288C	12-16
28673963-7	2017	Loss of the DGK1-encoded diacylglycerol kinase, which converts diacylglycerol to phosphatidate, partially suppressed the pah1Delta-mediated induction of Cho1 and PSS activity.	pah1delta	121-130	diacylglycerol kinase	Saccharomyces cerevisiae S288C	12-16
28276191-3	2017	Furthermore, DAG and PA can be interconverted by the DAG kinase Dgk1 and the PA phosphatase Pah1.	Diglycerides	13-16	diacylglycerol kinase	Saccharomyces cerevisiae S288C	64-68
28276191-3	2017	Furthermore, DAG and PA can be interconverted by the DAG kinase Dgk1 and the PA phosphatase Pah1.	Phosphatidic Acids	21-23	diacylglycerol kinase	Saccharomyces cerevisiae S288C	64-68
28276191-6	2017	Deleting DGK1 alone caused a marked increase in vacuole fusion that was attributed to elevated DAG levels.	Diglycerides	95-98	diacylglycerol kinase	Saccharomyces cerevisiae S288C	9-13
28276191-8	2017	Together these data show that Dgk1 function can act as a negative regulator of vacuole fusion through the production of PA at the cost of depleting DAG and reducing Ypt7 activity.	Phosphatidic Acids	120-122	diacylglycerol kinase	Saccharomyces cerevisiae S288C	30-34
28276191-8	2017	Together these data show that Dgk1 function can act as a negative regulator of vacuole fusion through the production of PA at the cost of depleting DAG and reducing Ypt7 activity.	Diglycerides	148-151	diacylglycerol kinase	Saccharomyces cerevisiae S288C	30-34
27834677-5	2016	When phosphate groups were globally reduced using nonspecific alkaline phosphatase, Triton X-100-solubilized membranes from DGK1-overexpressing cells showed a 7.7-fold reduction in DAG kinase activity; the reduced enzyme activity could be increased 5.5-fold by treatment with CKII.	Octoxynol	84-96	diacylglycerol kinase	Saccharomyces cerevisiae S288C	124-128
27834677-0	2016	Phosphorylation of Dgk1 Diacylglycerol Kinase by Casein Kinase II Regulates Phosphatidic Acid Production in Saccharomyces cerevisiae.	Phosphatidic Acids	76-93	diacylglycerol kinase	Saccharomyces cerevisiae S288C	19-23
27834677-1	2016	In the yeast Saccharomyces cerevisiae, Dgk1 diacylglycerol (DAG) kinase catalyzes the CTP-dependent phosphorylation of DAG to form phosphatidic acid (PA).	Diglycerides	44-58	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
27834677-1	2016	In the yeast Saccharomyces cerevisiae, Dgk1 diacylglycerol (DAG) kinase catalyzes the CTP-dependent phosphorylation of DAG to form phosphatidic acid (PA).	Cytidine Triphosphate	86-89	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
27834677-1	2016	In the yeast Saccharomyces cerevisiae, Dgk1 diacylglycerol (DAG) kinase catalyzes the CTP-dependent phosphorylation of DAG to form phosphatidic acid (PA).	Diglycerides	60-63	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
27834677-1	2016	In the yeast Saccharomyces cerevisiae, Dgk1 diacylglycerol (DAG) kinase catalyzes the CTP-dependent phosphorylation of DAG to form phosphatidic acid (PA).	Phosphatidic Acids	131-148	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
27834677-1	2016	In the yeast Saccharomyces cerevisiae, Dgk1 diacylglycerol (DAG) kinase catalyzes the CTP-dependent phosphorylation of DAG to form phosphatidic acid (PA).	Phosphatidic Acids	150-152	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
27834677-5	2016	When phosphate groups were globally reduced using nonspecific alkaline phosphatase, Triton X-100-solubilized membranes from DGK1-overexpressing cells showed a 7.7-fold reduction in DAG kinase activity; the reduced enzyme activity could be increased 5.5-fold by treatment with CKII.	Phosphates	5-14	diacylglycerol kinase	Saccharomyces cerevisiae S288C	124-128
27834677-6	2016	Dgk1(1-77) expressed heterologously in Escherichia coli was phosphorylated by CKII on a serine residue, and its phosphorylation was dependent on time as well as on the concentrations of CKII, ATP, and Dgk1(1-77).	Serine	88-94	diacylglycerol kinase	Saccharomyces cerevisiae S288C	0-4
27834677-6	2016	Dgk1(1-77) expressed heterologously in Escherichia coli was phosphorylated by CKII on a serine residue, and its phosphorylation was dependent on time as well as on the concentrations of CKII, ATP, and Dgk1(1-77).	Adenosine Triphosphate	192-195	diacylglycerol kinase	Saccharomyces cerevisiae S288C	0-4
27834677-7	2016	We used site-specific mutagenesis, coupled with phosphorylation analysis and phosphopeptide mapping, to identify Ser-45 and Ser-46 of Dgk1 as the CKII target sites, with Ser-46 being the major phosphorylation site.	Serine	124-127	diacylglycerol kinase	Saccharomyces cerevisiae S288C	134-138
27834677-7	2016	We used site-specific mutagenesis, coupled with phosphorylation analysis and phosphopeptide mapping, to identify Ser-45 and Ser-46 of Dgk1 as the CKII target sites, with Ser-46 being the major phosphorylation site.	Serine	124-127	diacylglycerol kinase	Saccharomyces cerevisiae S288C	134-138
27834677-9	2016	In addition, the phosphorylation-deficient mutations decreased Dgk1 function in PA production and in eliciting pah1Delta phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity.	Phosphatidic Acids	80-82	diacylglycerol kinase	Saccharomyces cerevisiae S288C	63-67
27834677-9	2016	In addition, the phosphorylation-deficient mutations decreased Dgk1 function in PA production and in eliciting pah1Delta phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity.	pah1delta	111-120	diacylglycerol kinase	Saccharomyces cerevisiae S288C	63-67
27834677-10	2016	This work demonstrates that the CKII-mediated phosphorylation of Dgk1 regulates its function in the production of PA.	Phosphatidic Acids	114-116	diacylglycerol kinase	Saccharomyces cerevisiae S288C	65-69
26980090-8	2016	As proof of concept the correlation between 11beta-HSD1 inhibition and fluorescent output signals was successfully tested with increasing concentrations of carbenoxolone and tanshinone IIA, two known 11beta-HSD1 inhibitors.	Carbenoxolone	156-169	diacylglycerol kinase	Saccharomyces cerevisiae S288C	200-211
26980090-2	2016	At the peripheral level the concentration of active glucocorticoids is mainly regulated by the 11beta-hydroxysteroid dehydrogenase 1 (11beta-HSD1) enzyme, involved in the conversion of cortisone into the biologically active hormone cortisol.	Cortisone	185-194	diacylglycerol kinase	Saccharomyces cerevisiae S288C	95-145
26980090-2	2016	At the peripheral level the concentration of active glucocorticoids is mainly regulated by the 11beta-hydroxysteroid dehydrogenase 1 (11beta-HSD1) enzyme, involved in the conversion of cortisone into the biologically active hormone cortisol.	Hydrocortisone	232-240	diacylglycerol kinase	Saccharomyces cerevisiae S288C	95-145
26980090-8	2016	As proof of concept the correlation between 11beta-HSD1 inhibition and fluorescent output signals was successfully tested with increasing concentrations of carbenoxolone and tanshinone IIA, two known 11beta-HSD1 inhibitors.	Carbenoxolone	156-169	diacylglycerol kinase	Saccharomyces cerevisiae S288C	44-55
26980090-8	2016	As proof of concept the correlation between 11beta-HSD1 inhibition and fluorescent output signals was successfully tested with increasing concentrations of carbenoxolone and tanshinone IIA, two known 11beta-HSD1 inhibitors.	tanshinone	174-188	diacylglycerol kinase	Saccharomyces cerevisiae S288C	44-55
26980090-8	2016	As proof of concept the correlation between 11beta-HSD1 inhibition and fluorescent output signals was successfully tested with increasing concentrations of carbenoxolone and tanshinone IIA, two known 11beta-HSD1 inhibitors.	tanshinone	174-188	diacylglycerol kinase	Saccharomyces cerevisiae S288C	200-211
23133385-6	2012	In addition, by using relevant yeast genetic backgrounds we examined several L. pneumophila effectors expected to be involved in phospholipids biosynthesis and identified an effector (LpdA) that contains a phospholipase-D (PLD) domain which caused lethal effect only in a dgk1 deletion mutant of yeast.	lpda	184-188	diacylglycerol kinase	Saccharomyces cerevisiae S288C	272-276
23970552-1	2013	In the yeast Saccharomyces cerevisiae, the DGK1-encoded diacylglycerol kinase catalyzes the CTP-dependent phosphorylation of diacylglycerol to form phosphatidate.	Cytidine Triphosphate	92-95	diacylglycerol kinase	Saccharomyces cerevisiae S288C	43-47
23970552-1	2013	In the yeast Saccharomyces cerevisiae, the DGK1-encoded diacylglycerol kinase catalyzes the CTP-dependent phosphorylation of diacylglycerol to form phosphatidate.	Diglycerides	56-70	diacylglycerol kinase	Saccharomyces cerevisiae S288C	43-47
23970552-1	2013	In the yeast Saccharomyces cerevisiae, the DGK1-encoded diacylglycerol kinase catalyzes the CTP-dependent phosphorylation of diacylglycerol to form phosphatidate.	phosphatidate	148-161	diacylglycerol kinase	Saccharomyces cerevisiae S288C	43-47
23970552-7	2013	In the presence of cerulenin, an inhibitor of de novo fatty acid synthesis, the dgk1Delta mutant expressing DGK1(reb1) exhibited a significant defect in growth as well as in the synthesis of phospholipids from triacylglycerol mobilization.	Cerulenin	19-28	diacylglycerol kinase	Saccharomyces cerevisiae S288C	108-112
23970552-7	2013	In the presence of cerulenin, an inhibitor of de novo fatty acid synthesis, the dgk1Delta mutant expressing DGK1(reb1) exhibited a significant defect in growth as well as in the synthesis of phospholipids from triacylglycerol mobilization.	Fatty Acids	54-64	diacylglycerol kinase	Saccharomyces cerevisiae S288C	108-112
23970552-7	2013	In the presence of cerulenin, an inhibitor of de novo fatty acid synthesis, the dgk1Delta mutant expressing DGK1(reb1) exhibited a significant defect in growth as well as in the synthesis of phospholipids from triacylglycerol mobilization.	Phospholipids	191-204	diacylglycerol kinase	Saccharomyces cerevisiae S288C	108-112
23970552-7	2013	In the presence of cerulenin, an inhibitor of de novo fatty acid synthesis, the dgk1Delta mutant expressing DGK1(reb1) exhibited a significant defect in growth as well as in the synthesis of phospholipids from triacylglycerol mobilization.	Triglycerides	210-225	diacylglycerol kinase	Saccharomyces cerevisiae S288C	108-112
24563465-10	2014	That Pah1p abundance was stabilized in pah1Delta mutant cells expressing catalytically inactive forms of Pah1p and dgk1Delta mutant cells with induced expression of DGK1-encoded diacylglycerol kinase indicated that alteration in phosphatidate and/or diacylglycerol levels might be the signal that triggers Pah1p degradation.	Diglycerides	178-192	diacylglycerol kinase	Saccharomyces cerevisiae S288C	165-169
21708942-8	2011	Deletion of the DGK1-encoded diacylglycerol kinase, which counteracts PA phosphatase in controlling PA content, suppressed the defect in lipid droplet formation in the pah1Delta mutant.	Protactinium	70-72	diacylglycerol kinase	Saccharomyces cerevisiae S288C	16-20
18458075-3	2008	Two screens for novel regulators of phosphatidate led to the identification of DGK1.	phosphatidate	36-49	diacylglycerol kinase	Saccharomyces cerevisiae S288C	79-83
21071438-0	2011	DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae.	Phospholipids	60-72	diacylglycerol kinase	Saccharomyces cerevisiae S288C	0-4
21071438-2	2011	In this work, we provide evidence that DGK1-encoded diacylglycerol kinase activity is required to convert triacylglycerol-derived diacylglycerol to phosphatidate for phospholipid synthesis.	Triglycerides	106-121	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
21071438-2	2011	In this work, we provide evidence that DGK1-encoded diacylglycerol kinase activity is required to convert triacylglycerol-derived diacylglycerol to phosphatidate for phospholipid synthesis.	Diglycerides	52-66	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
21071438-2	2011	In this work, we provide evidence that DGK1-encoded diacylglycerol kinase activity is required to convert triacylglycerol-derived diacylglycerol to phosphatidate for phospholipid synthesis.	phosphatidate	148-161	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
21071438-2	2011	In this work, we provide evidence that DGK1-encoded diacylglycerol kinase activity is required to convert triacylglycerol-derived diacylglycerol to phosphatidate for phospholipid synthesis.	Phospholipids	166-178	diacylglycerol kinase	Saccharomyces cerevisiae S288C	39-43
18458075-4	2008	We show that Dgk1p is a unique diacylglycerol kinase that uses CTP, instead of ATP, to generate phosphatidate.	Cytidine Triphosphate	63-66	diacylglycerol kinase	Saccharomyces cerevisiae S288C	13-18
18458075-4	2008	We show that Dgk1p is a unique diacylglycerol kinase that uses CTP, instead of ATP, to generate phosphatidate.	Adenosine Triphosphate	79-82	diacylglycerol kinase	Saccharomyces cerevisiae S288C	13-18
18458075-4	2008	We show that Dgk1p is a unique diacylglycerol kinase that uses CTP, instead of ATP, to generate phosphatidate.	phosphatidate	96-109	diacylglycerol kinase	Saccharomyces cerevisiae S288C	13-18
18458075-5	2008	DGK1 counteracts the activity of PAH1 at the nuclear envelope by controlling phosphatidate levels.	phosphatidate	77-90	diacylglycerol kinase	Saccharomyces cerevisiae S288C	0-4
18458075-6	2008	Overexpression of DGK1 causes the appearance of phosphatidate-enriched membranes around the nucleus and leads to its expansion, without proliferating the cortical endoplasmic reticulum membrane.	phosphatidate	48-61	diacylglycerol kinase	Saccharomyces cerevisiae S288C	18-22
18458076-1	2008	The Saccharomyces cerevisiae DGK1 gene encodes a diacylglycerol kinase enzyme that catalyzes the formation of phosphatidate from diacylglycerol.	phosphatidate	110-123	diacylglycerol kinase	Saccharomyces cerevisiae S288C	29-33
18458076-1	2008	The Saccharomyces cerevisiae DGK1 gene encodes a diacylglycerol kinase enzyme that catalyzes the formation of phosphatidate from diacylglycerol.	phosphatidate	110-123	diacylglycerol kinase	Saccharomyces cerevisiae S288C	49-70
18458076-1	2008	The Saccharomyces cerevisiae DGK1 gene encodes a diacylglycerol kinase enzyme that catalyzes the formation of phosphatidate from diacylglycerol.	Diglycerides	49-63	diacylglycerol kinase	Saccharomyces cerevisiae S288C	29-33
18458076-7	2008	The DGK1-encoded enzyme had a pH optimum at 7.0-7.5, required Ca(2+) or Mg(2+) ions for activity, was potently inhibited by N-ethylmaleimide, and was labile at temperatures above 40 degrees C. The enzyme exhibited positive cooperative (Hill number = 2.5) kinetics with respect to diacylglycerol (apparent K(m) = 6.5 mol %) and saturation kinetics with respect to CTP (apparent K(m) = 0.3 mm).	magnesium ion	72-78	diacylglycerol kinase	Saccharomyces cerevisiae S288C	4-8
18458076-7	2008	The DGK1-encoded enzyme had a pH optimum at 7.0-7.5, required Ca(2+) or Mg(2+) ions for activity, was potently inhibited by N-ethylmaleimide, and was labile at temperatures above 40 degrees C. The enzyme exhibited positive cooperative (Hill number = 2.5) kinetics with respect to diacylglycerol (apparent K(m) = 6.5 mol %) and saturation kinetics with respect to CTP (apparent K(m) = 0.3 mm).	Ethylmaleimide	124-140	diacylglycerol kinase	Saccharomyces cerevisiae S288C	4-8
18458076-7	2008	The DGK1-encoded enzyme had a pH optimum at 7.0-7.5, required Ca(2+) or Mg(2+) ions for activity, was potently inhibited by N-ethylmaleimide, and was labile at temperatures above 40 degrees C. The enzyme exhibited positive cooperative (Hill number = 2.5) kinetics with respect to diacylglycerol (apparent K(m) = 6.5 mol %) and saturation kinetics with respect to CTP (apparent K(m) = 0.3 mm).	Diglycerides	280-294	diacylglycerol kinase	Saccharomyces cerevisiae S288C	4-8
18458076-7	2008	The DGK1-encoded enzyme had a pH optimum at 7.0-7.5, required Ca(2+) or Mg(2+) ions for activity, was potently inhibited by N-ethylmaleimide, and was labile at temperatures above 40 degrees C. The enzyme exhibited positive cooperative (Hill number = 2.5) kinetics with respect to diacylglycerol (apparent K(m) = 6.5 mol %) and saturation kinetics with respect to CTP (apparent K(m) = 0.3 mm).	Cytidine Triphosphate	363-366	diacylglycerol kinase	Saccharomyces cerevisiae S288C	4-8
18458076-9	2008	Diacylglycerol kinase activity was stimulated by major membrane phospholipids and was inhibited by CDP-diacylglycerol and sphingoid bases.	Phospholipids	64-77	diacylglycerol kinase	Saccharomyces cerevisiae S288C	0-21
18458076-9	2008	Diacylglycerol kinase activity was stimulated by major membrane phospholipids and was inhibited by CDP-diacylglycerol and sphingoid bases.	Cytidine Diphosphate Diglycerides	99-117	diacylglycerol kinase	Saccharomyces cerevisiae S288C	0-21
18458076-9	2008	Diacylglycerol kinase activity was stimulated by major membrane phospholipids and was inhibited by CDP-diacylglycerol and sphingoid bases.	sphingoid bases	122-137	diacylglycerol kinase	Saccharomyces cerevisiae S288C	0-21
17825335-6	2007	We used recombinant yeast-expressed 11beta-HSD1 with NADP(H)-regenerating systems for examining the products obtained after incubation with 7alpha-Adiol, 7beta-Adiol or 7-oxo-Adiol.	7alpha-adiol	140-152	diacylglycerol kinase	Saccharomyces cerevisiae S288C	36-47
17825335-6	2007	We used recombinant yeast-expressed 11beta-HSD1 with NADP(H)-regenerating systems for examining the products obtained after incubation with 7alpha-Adiol, 7beta-Adiol or 7-oxo-Adiol.	7beta-adiol	154-165	diacylglycerol kinase	Saccharomyces cerevisiae S288C	36-47