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Information on EC 2.7.1.174 - diacylglycerol kinase (CTP)
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2.7.1.174 diacylglycerol kinase (CTP)IUBMB Comments
Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP.
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The enzyme appears in viruses and cellular organisms
Synonyms
dgk1p, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CTP-dependent DAG kinase
CTP-dependent diacylglycerol kinase
DAG kinase
DGK1
Dgk1p
diacylglycerol kinase (CTP dependent)
-
-
-
-
additional information
CTP-dependent diacylglycerol kinase
-
-
-
-
DAG kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
CTP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP.
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CAS REGISTRY NUMBER
COMMENTARY
60382-71-0
cf. EC 2.7.1.107
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Dgk1p-derived phosphatidate accumulates on the nuclear membrane
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Dgk1p-derived phosphatidate accumulates on the nuclear membrane
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity
-
-
?
CTP + 1,2-dioleoyl-sn-glycerol
CDP + 1,2-dioleoyl-sn-glycerol 3-phosphate
the CTP transferase domain is sufficient for diacylglycerol kinase activity
-
-
?
CTP + 1,2-dioleoyl-sn-glycerol
CDP + 1,2-dioleoyl-sn-glycerol 3-phosphate
the CTP transferase domain is sufficient for diacylglycerol kinase activity
-
-
?
dCTP + 1,2-diacyl-sn-glycerol
dCDP + 1,2-diacyl-sn-glycerol 3-phosphate
both a substrate and competitive inhibitor
-
-
?
dCTP + 1,2-diacyl-sn-glycerol
dCDP + 1,2-diacyl-sn-glycerol 3-phosphate
both a substrate and competitive inhibitor
-
-
?
additional information
?
-
Dgk1p does not function as a CDP-DAG synthase in vivo
-
-
?
additional information
?
-
-
Dgk1p does not function as a CDP-DAG synthase in vivo
-
-
?
additional information
?
-
the enzyme is a bona fide substrate of casein kinase II and its phosphorylation stimulates enzyme activity
-
-
-
additional information
?
-
the enzyme is a bona fide substrate of casein kinase II and its phosphorylation stimulates enzyme activity
-
-
-
additional information
?
-
Dgk1p does not function as a CDP-DAG synthase in vivo
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Dgk1p-derived phosphatidate accumulates on the nuclear membrane
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
Dgk1p-derived phosphatidate accumulates on the nuclear membrane
-
?
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity
-
-
?
additional information
?
-
Dgk1p does not function as a CDP-DAG synthase in vivo
-
-
?
additional information
?
-
-
Dgk1p does not function as a CDP-DAG synthase in vivo
-
-
?
additional information
?
-
Dgk1p does not function as a CDP-DAG synthase in vivo
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
the enzyme requires Ca2+ or Mg2+ ions for activity. Maximum DAG kinase activity obtained with 1 mM Ca2+ ions is slightly greater than the maximum activity obtained with 10 mM Mg2+ ions
Mg2+
the enzyme requires Ca2+ or Mg2+ ions for activity. Maximum DAG kinase activity obtained with 1 mM Ca2+ ions is slightly greater than the maximum activity obtained with 10 mM Mg2+ ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
inhibition kinetics, overview. No inhibition by monoacylglycerol
additional information
the enzyme is inhibited by sphingoid bases
-
additional information
-
the enzyme is inhibited by sphingoid bases
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
diacylglycerol kinase activity is stimulated by major membrane phospholipids, overview
-
additional information
-
diacylglycerol kinase activity is stimulated by major membrane phospholipids, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
the enzyme exhibits positive cooperative kinetics with respect to diacylglycerol and saturation kinetics with respect to CTP, kinetic analysis and modeling, overview
-
additional information
additional information
-
the enzyme exhibits positive cooperative kinetics with respect to diacylglycerol and saturation kinetics with respect to CTP, kinetic analysis and modeling, overview
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
surface dilution kinetic model, overview, positive cooperative kinetics with respect to the surface concentration of 1,2-dioleoyl-sn-glycerol
-
additional information
additional information
-
surface dilution kinetic model, overview, positive cooperative kinetics with respect to the surface concentration of 1,2-dioleoyl-sn-glycerol
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130
DAG kinase in the membrane fraction of galactose-grown cells, pH 7.5, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein
brenda
-
integral membrane protein
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
mutations decrease phosphatidate levels decrease nuclear membrane growth in pah1DELTA cells, the inactivation of Pah1p leads to nuclear growth. A dgk1DLETA strain expressing a mutant DGK1 allele in which residue 177 is changed to alanine does not display any CTP-dependent DAG kinase activity
malfunction
a Reb1p-binding site mutation abolishes the DGK1-mediated nuclear/endoplasmic reticulum membrane expansion
malfunction
-
mutations decrease phosphatidate levels decrease nuclear membrane growth in pah1DELTA cells, the inactivation of Pah1p leads to nuclear growth. A dgk1DLETA strain expressing a mutant DGK1 allele in which residue 177 is changed to alanine does not display any CTP-dependent DAG kinase activity
-
metabolism
phosphatidate metabolism is a critical factor determining nuclear structure by regulating nuclear membrane biogenesis, DGK1 rescues the lethality of dephosphorylated PAH1
metabolism
the enzyme in conjunction with Pah1 phosphatidic acid phosphatase controls the levels of phosphatidic acid and diacylglycerol for the synthesis of triacylglycerol and membrane phospholipids, the growth of the nuclear/endoplasmic reticulum membrane, and the formation of lipid droplets
metabolism
-
phosphatidate metabolism is a critical factor determining nuclear structure by regulating nuclear membrane biogenesis, DGK1 rescues the lethality of dephosphorylated PAH1
-
metabolism
-
the enzyme in conjunction with Pah1 phosphatidic acid phosphatase controls the levels of phosphatidic acid and diacylglycerol for the synthesis of triacylglycerol and membrane phospholipids, the growth of the nuclear/endoplasmic reticulum membrane, and the formation of lipid droplets
-
physiological function
Dgk1p is a unique diacylglycerol kinase that uses CTP, instead of ATP, to generate phosphatidate. The unconventional diacylglycerol kinase regulates phospholipid synthesis and nuclear membrane growth, detailed overview. DGK1 counteracts the activity of PAH1 at the nuclear envelope by controlling phosphatidate levels. Phosphatidate metabolism is a critical factor determining nuclear structure by regulating nuclear membrane biogenesis. DGK1 rescues the lethality of dephosphorylated PAH1
physiological function
in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity. DGK1 counteracts the PAH1-encoded PA phosphatase
physiological function
the enzyme catalyzes the CTP-dependent phosphorylation of diacylglycerol to form phosphatidate, and in conjunction with PAH1-encoded phosphatidate phosphatase, it controls the levels of phosphatidate and diacylglycerol for phospholipid synthesis, membrane growth, and lipid droplet formation. A functional level of diacylglycerol kinase is regulated by the Reb1p transcription factor. Reb1p specifically binds the consensus recognition sequence (CGGGTAA, -166 to -160) in the DGK1 promoter. Diacylglycerol kinase is regulated at the level of transcription. The expression of diacylglycerol kinase is induced by the Reb1p transcription factor, and the resulting activity increase is essential for the enzyme function in phospholipid synthesis. The DGK1-encoded DAG kinase activity causes the accumulation of phosphatidic acid at the nuclear/endoplasmicreticulum membrane when the phospholipid is not hydrolyzed by PAH1-encoded phosphatidic acid phosphatase
physiological function
-
Dgk1p is a unique diacylglycerol kinase that uses CTP, instead of ATP, to generate phosphatidate. The unconventional diacylglycerol kinase regulates phospholipid synthesis and nuclear membrane growth, detailed overview. DGK1 counteracts the activity of PAH1 at the nuclear envelope by controlling phosphatidate levels. Phosphatidate metabolism is a critical factor determining nuclear structure by regulating nuclear membrane biogenesis. DGK1 rescues the lethality of dephosphorylated PAH1
-
physiological function
-
in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity. DGK1 counteracts the PAH1-encoded PA phosphatase
-
additional information
Dgk1p contains a CTP transferase domain that is present in the SEC59-encoded dolichol kinase and CDS1-encoded CDP-diacylglycerol synthase enzymes
additional information
-
Dgk1p contains a CTP transferase domain that is present in the SEC59-encoded dolichol kinase and CDS1-encoded CDP-diacylglycerol synthase enzymes
additional information
role of phospholipid metabolism in nuclear/ER membrane structure
additional information
-
role of phospholipid metabolism in nuclear/ER membrane structure
additional information
-
role of phospholipid metabolism in nuclear/ER membrane structure
-
additional information
-
Dgk1p contains a CTP transferase domain that is present in the SEC59-encoded dolichol kinase and CDS1-encoded CDP-diacylglycerol synthase enzymes
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DGK1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
218
5
24397
Swiss-Prot
other Location (Reliability: 5)
DGK1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
290
4
32840
Swiss-Prot
other Location (Reliability: 2)
DGK1_ASHGO
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
317
4
35399
Swiss-Prot
other Location (Reliability: 1)
A0A8J5BRN0_9ASCO
281
6
30496
TrEMBL
Mitochondrion (Reliability: 4)
W1QAD7_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
326
4
36761
TrEMBL
other Location (Reliability: 2)
A0A8J5CHI6_9ASCO
281
6
30385
TrEMBL
Mitochondrion (Reliability: 3)
A0A3G2SAQ6_9BASI
329
4
36533
TrEMBL
Mitochondrion (Reliability: 3)
A0A0F8CPY4_CERFI
286
8
31503
TrEMBL
other Location (Reliability: 4)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Dgk1p contains a CTP transferase domain, the CTP transferase domain is sufficient for diacylglycerol kinase activity
additional information
-
Dgk1p contains a CTP transferase domain, the CTP transferase domain is sufficient for diacylglycerol kinase activity
additional information
-
Dgk1p contains a CTP transferase domain, the CTP transferase domain is sufficient for diacylglycerol kinase activity
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
the enzyme is phosphorylated by casein kinase II at serine residues Ser45 and Ser46. The casein kinase II-mediated phosphorylation of the enzyme regulates its function in the production of phosphatidic acid. The enzyme is inhibited by dephosphorylation with alkaline phosphatase
phosphoprotein
-
the enzyme is phosphorylated by casein kinase II at serine residues Ser45 and Ser46. The casein kinase II-mediated phosphorylation of the enzyme regulates its function in the production of phosphatidic acid. The enzyme is inhibited by dephosphorylation with alkaline phosphatase
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D177A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
G184A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a loss of diacylglycerol kinase activity
K77A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing an almost complete loss of diacylglycerol kinase activity
R76A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
S44A
the mutation does not affect phosphorylation of the enzyme
S44A/S45A/S46A
the mutations abolish the stationary phase-dependent stimulation of enzyme activity. The phosphorylation-deficient mutations decrease enzyme function in phosphatidic acid production and in eliciting pah1DELTA phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity
S46A
the mutation abolishes the stationary phase-dependent stimulation of enzyme activity. The phosphorylation-deficient mutation decreases enzyme function in phosphatidic acid production and in eliciting pah1DELTA phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity
S5A
the mutation does decreases phosphorylation of the enzyme by about 40% compared to the wild type enzyme
S44A/S45A/S46A
-
the mutations abolish the stationary phase-dependent stimulation of enzyme activity. The phosphorylation-deficient mutations decrease enzyme function in phosphatidic acid production and in eliciting pah1DELTA phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity
-
S46A
-
the mutation abolishes the stationary phase-dependent stimulation of enzyme activity. The phosphorylation-deficient mutation decreases enzyme function in phosphatidic acid production and in eliciting pah1DELTA phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity
-
S5A
-
the mutation does decreases phosphorylation of the enzyme by about 40% compared to the wild type enzyme
-
D177A
-
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
-
G184A
-
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a loss of diacylglycerol kinase activity
-
K77A
-
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing an almost complete loss of diacylglycerol kinase activity
-
R76A
-
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
-
additional information
additional information
construction of DGK1 truncation mutants. The DELTA66 and DELTA70 truncations remove most of the N-terminal hydrophilic region of Dgk1p, whereas the DELTA77 truncation removes the entire N-terminal hydrophilic region plus the first two residues contained within the CTP transferase domain, the later mutant is inactive, the other two show reduced activity compared to the wild-type enzyme
additional information
-
construction of DGK1 truncation mutants. The DELTA66 and DELTA70 truncations remove most of the N-terminal hydrophilic region of Dgk1p, whereas the DELTA77 truncation removes the entire N-terminal hydrophilic region plus the first two residues contained within the CTP transferase domain, the later mutant is inactive, the other two show reduced activity compared to the wild-type enzyme
additional information
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. Deletion of DGK1 returns the phosphatidate and phosphatidylethanolamine levels of the pah1DELTA cells to normal
additional information
-
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. Deletion of DGK1 returns the phosphatidate and phosphatidylethanolamine levels of the pah1DELTA cells to normal
additional information
-
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. Deletion of DGK1 returns the phosphatidate and phosphatidylethanolamine levels of the pah1DELTA cells to normal
-
additional information
-
construction of DGK1 truncation mutants. The DELTA66 and DELTA70 truncations remove most of the N-terminal hydrophilic region of Dgk1p, whereas the DELTA77 truncation removes the entire N-terminal hydrophilic region plus the first two residues contained within the CTP transferase domain, the later mutant is inactive, the other two show reduced activity compared to the wild-type enzyme
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, the enzyme preparation is completely stable for at least 3 months of storage at, and is stable to several cycles of freezing and thawing
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene DGK1, the DGK1 promoter is substituted with the inducible GAL1/10 promoter in the low copy YCplac111 and high copy YEplac181 vectors, expression of wild-type and mutant enzymes, induction of wild-type DGK1 gene expression from high copy number plasmid YEplac181-GAL1/10-DGK1 results in a massive increase in DAG kinase activity. Temperature sensitivity of dgk1DELTA cells overexpressing DGK1 and its mutant alleles
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of diacylglycerol kinase is induced by the Reb1p transcription factor, Reb1p directly interacts with the Reb1p-binding sequence in the DGK1 promoter
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, G.S.; OHara, L.; Siniossoglou, S.; Carman, G.M.
Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase
J. Biol. Chem.
283
20443-20453
2008
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742 (Q12382)
brenda
Han, G.S.; OHara, L.; Carman, G.M.; Siniossoglou, S.
An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth
J. Biol. Chem.
283
20433-20442
2008
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742 (Q12382)
brenda
Qiu, Y.; Fakas, S.; Han, G.S.; Barbosa, A.D.; Siniossoglou, S.; Carman, G.M.
Transcription factor Reb1p regulates DGK1-encoded diacylglycerol kinase and lipid metabolism in Saccharomyces cerevisiae
J. Biol. Chem.
288
29124-29133
2013
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae
brenda
Qiu, Y.; Hassaninasab, A.; Han, G.S.; Carman, G.M.
Phosphorylation of Dgk1 diacylglycerol kinase by casein kinase II regulates phosphatidic acid production in Saccharomyces cerevisiae
J. Biol. Chem.
291
26455-26467
2016
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae BY4741 (Q12382)
brenda
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