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Information on EC 2.7.1.138 - ceramide kinase and Organism(s) Homo sapiens and UniProt Accession Q8TCT0
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2.7.1.138 ceramide kinaseSpecify your search results
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- 2.7.1.138
- ceramide-1-phosphate
- sphingolipids
- 1-phosphate
- sphingosine-1-phosphate
- ceramidase
-
pleckstrin
-
cerkl
- medicine
-
ceramide-induced
- analysis
- diagnostics
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
ceramide kinase, hcerk, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CERK
-
acylsphingosine kinase
-
-
-
-
CERK
-
-
kinase, acylsphingosine (phosphorylating)
-
-
-
-
additional information
-
the enzyme belongs to the subfamily of diacylglyceride kinases DAGKs
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + ceramide = ADP + ceramide 1-phosphate
the secondary hydroxy group is not required for substrate recognition, preference for the D-erythro isomer, the enzyme is specific for th phosphorylation of the 1-hydroxy group
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Phosphorylation
Phosphorylation
-
-
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:ceramide 1-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY
123175-68-8
-
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
ATP + D-erythro-N-hexanoyl-sphinganine
ADP + D-erythro-N-hexanoyl-sphinganine 1-phosphate
-
-
-
?
ATP + D-erythro-N-hexanoyl-sphingenine
ADP + D-erythro-N-hexanoyl-sphingenine 1-phosphate
-
-
-
?
ATP + hexadecanoylceramide
ADP + hexadecanoylceramide 1-phosphate
C8 acyl chain, slightly higher activity than with natural ceramide
-
?
ATP + hexanoylceramide
ADP + hexanoylceramide 1-phosphate
C6 acyl chain, similar activity than with natural ceramide, very low activity with C2-ceramide and C6-dihydroceramide, no activity with C2-dihydroceramide
-
?
ATP + N-acetyl-D-erythro-sphingenine
ADP + N-acetyl-D-erythro-sphingenine 1-phosphate
-
-
-
?
ATP + N-acetyl-sphingenine
ADP + N-acetyl-sphingenine 1-phosphate
-
-
-
?
ATP + N-hexanoyl-1-O-hexadecyl-2-deoxy-2-amino-sn-glycerol
ADP + ?
-
-
-
?
ATP + N-hexanoyl-D-erythro-sphingenine
ADP + N-hexanoyl-D-erythro-sphingenine 1-phosphate
best substrate
-
-
?
ATP + N-hexanoyl-sphingenine
ADP + N-hexanoyl-sphingenine 1-phosphate
-
-
-
?
ATP + octanoylceramide
ADP + octanoylceramide 1-phosphate
C8 acyl chain, higher activity than with natural ceramide
-
?
ATP + octanoyldihydroceramide
ADP + octanoyldihydroceramide 1-phosphate
C8 acyl chain, slightly higher activity than with natural ceramide
-
?
N-(6-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)hexanoyl)-D-erythro-sphingosine + ATP
N-(6-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)hexanoyl)-D-erythro-sphingosine 1-phosphate + ADP
C6-ceramide
-
-
?
N-(7-(4-nitrobenzo-2-oxa-1,3-diazole))-6-aminocaproyl-D-erythro-sphingosine + ATP
N-(7-(4-nitrobenzo-2-oxa-1,3-diazole))-6-aminocaproyl-D-erythro-sphingosine 1-phosphate + ADP
NBD-ceramide
NBD-ceramide 1-phosphate
-
?
N-(8-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)octanoyl)-D-erythro-sphingosine + ATP
N-(8-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)octanoyl)-D-erythro-sphingosine 1-phosphate + ADP
C8-ceramide
-
-
?
alpha-OH-C24:0 phytoceramide + ATP
alpha-OH-C24:0 phytoceramide 1-phosphate + ADP
-
-
-
-
?
alpha-OH-D-erythro-C6:0 ceramide + ATP
alpha-OH-D-erythro-C6:0 ceramide 1-phosphate + ADP
-
-
-
-
?
ATP + 3-O-methyl C16:0 ceramide
ADP + 3-O-methyl C16:0 ceramide 1-phosphate
-
very low activity
-
-
?
ATP + C8-dihydroceramide
ADP + C8-dihydroceramide 1-phosphate
-
high activity
-
-
?
ATP + D-erythro-C6:0 ceramide
ADP + D-erythro-C6:0 ceramide 1-phosphate
-
very low activity
-
-
?
ATP + D-eythro-C10:0 ceramide
ADP + D-eythro-C10:0 ceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C12:0 ceramide
ADP + D-eythro-C12:0 ceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C14:0 ceramide
ADP + D-eythro-C14:0 ceramide 1-phosphate
-
best substrate
-
-
?
ATP + D-eythro-C16:0 (R)-alpha-hydroxyceramide
ADP + D-eythro-C16:0 (R)-alpha-hydroxyceramide 1-phosphate
-
low activity
-
-
?
ATP + D-eythro-C16:0 (S)-alpha-hydroxyceramide
ADP + D-eythro-C16:0 (S)-alpha-hydroxyceramide 1-phosphate
-
very low activity
-
-
?
ATP + D-eythro-C16:0 dehydroceramide
ADP + D-eythro-C16:0 dehydroceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C16:0 dihydroceramide
ADP + D-eythro-C16:0 dihydroceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C16:0 urea ceramide
ADP + D-eythro-C16:0 urea ceramide 1-phosphate
-
low activity, no activity with L-e-C16:0 urea ceramide
-
-
?
ATP + D-eythro-C16:0-cis ceramide
ADP + D-eythro-C16:0-cis ceramide 1-phosphate
-
low activity
-
-
?
ATP + D-eythro-C18:0 phytoceramide
ADP + D-eythro-C18:0 phytoceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C20:0 ceramide
ADP + D-eythro-C20:0 ceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C24:0 ceramide
ADP + D-eythro-C24:0 ceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C24:1 ceramide
ADP + D-eythro-C24:1 ceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C8:0 ceramide
ADP + D-eythro-C8:0 ceramide 1-phosphate
-
low activity
-
-
?
D-erythro-C12:0 ceramide + ATP
D-erythro-C12:0 ceramide 1-phosphate + ADP
-
-
-
-
?
D-erythro-C14:0 ceramide + ATP
D-erythro-C14:0 ceramide 1-phosphate + ADP
-
-
-
-
?
D-erythro-C16:0 ceramide + ATP
D-erythro-C16:0 ceramide 1-phosphate + ADP
-
used for kinetic analysis of ceramide kinase activity
-
-
?
D-erythro-C2:0 ceramide + ATP
D-erythro-C2:0 ceramide 1-phosphate + ADP
-
-
-
-
?
D-erythro-C2:0 dihydroceramide + ATP
D-erythro-C2:0 dihydroceramide 1-phosphate + ADP
-
-
-
-
?
D-erythro-C6:0 ceramide + ATP
D-erythro-C6:0 ceramide 1-phosphate + ADP
-
-
-
-
?
D-erythro-C6:0 dihydroceramide + ATP
D-erythro-C6:0 dihydroceramide 1-phosphate + ADP
-
-
-
-
?
N-(12-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)dodecanoyl)-D-erythro-sphingosine + ATP
N-(12-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)dodecanoyl)-D-erythro-sphingosine 1-phosphate + ADP
-
C12-NBD ceramide
-
-
?
N-(6-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)hexanoyl)-D-erythro-sphingosine + ATP
N-(6-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)hexanoyl)-D-erythro-sphingosine 1-phosphate + ADP
-
C6-NBD ceramide
-
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
no activity sphingosine, D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine and phyto-sphingosine
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
in vitro substrate delivery of short chain ceramides requires bovine serum albumin, and a mixed micellar form consisting of octylglucoside and cardiolipin for long chain ceramides, choice of delivery system is important for in vitro activity
-
-
?
ATP + N-hexadecanoyl-sphingenine
ADP + N-hexadecanoyl-sphingenine 1-phosphate
-
-
-
?
ATP + N-hexadecanoyl-sphingenine
ADP + N-hexadecanoyl-sphingenine 1-phosphate
very low activity
-
-
?
C2-ceramide + ATP
C2-ceramide 1-phosphate + ADP
C2-Cer is a potent inducer of cell death in CerK-expressing cells
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
CERK plays a role in cell signalling
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
involvement in inflammatory processes and cell growth
-
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
-
-
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
-
ceramide 1-phosphate is a lipid signalling molecule involved in regulation of many physiological processes related to cell proliferation, apoptosis, and inflammation, most of them in concert with sphingosine 1-phosphate, ceramide 1-phosphate might act via extracellular cell surface receptors or intracellularly as second messenger
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
-
synthesis of the sphingolipid signaling molecule
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
no activity with 1,2-diacylglycerol
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
stereospecific ceramide substrate recognition, the C4-5 trans double bond is important for substrate recognition, a minimum of 12C-acyl chain is required for activity
-
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
the enzyme is specific for the cramide backbone, acylation of amino group in position 2 is required
-
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
the pleckstrin homology domain is essential for activity, binding of liposomes
-
-
?
ATP + D-eythro-C16:0 ceramide
ADP + D-eythro-C16:0 ceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C16:0 ceramide
ADP + D-eythro-C16:0 ceramide 1-phosphate
-
high activity
-
-
?
ATP + D-eythro-C18:0 ceramide
ADP + D-eythro-C18:0 ceramide 1-phosphate
-
-
-
-
?
ATP + D-eythro-C18:0 ceramide
ADP + D-eythro-C18:0 ceramide 1-phosphate
-
high activity
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
-
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
ceramide is a key mediator of cellular apoptosis
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
ceramide kinase is a critical mediator of eicosanoid synthesis, and its product, ceramide 1-phosphate, is required for the production of prostaglandins in response to several inflammatory agonists, CERK requires ceramide actively transported to the trans-Golgi network via ceramide transport protein CERT
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
ceramide kinase is important for cellular proliferation and survival, activation of cytosolic phospholipase A2, mast cell degranulation, and phagocytosis
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
CERK and C1P are playing significant biological roles in cell-signaling cascades
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
CerK has important roles in leukocyte functions, including the role in degranulation of mast cells and the phagocytosis of polymorphonuclear leukocytes
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
increased ceramide 1-phosphate during phagocytosis enhances phagocytosis and phagolysosome formation in COS-1 cells expressing hCERK
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
key enzyme for controlling ceramide levels
-
-
?
additional information
?
-
2-amino-1-hexadecanol, 1-O-hexadecyl-2-deoxy-2-amino-sn-glycerol, N-tetradecanoyl-2(R)-pyrrolidine-methanol, N-tetradecanoyl-(R)-serine, N-tetradecanoyl-3-hydroxypyrrolidin, N-tetradecanoyl-4-amino-1-butanol, N-tetradecanoyl-3-amino-1-propanol, N-tetradecanoyl-(S)-serine, N-tetradecanoyl-2-benzylserine, N-tetradecanoyl3-phenylserine, N-tetradecanoyl-3-amino-tyrosine, N-tetradecanoyl-1-amino-2-naphthol-4-sulfonic acid, N-tetradecanoyl-3-hydroxy-anthranilic acid, N-tetradecanoyl-4-aminophenol, N-tetradecanoyl-diethanolamine, N-tetradecanoyl-ethanolamine, and N-tetradecanoyl-(S)-phenylalaninol are no substrates
-
-
?
additional information
?
-
-
2-amino-1-hexadecanol, 1-O-hexadecyl-2-deoxy-2-amino-sn-glycerol, N-tetradecanoyl-2(R)-pyrrolidine-methanol, N-tetradecanoyl-(R)-serine, N-tetradecanoyl-3-hydroxypyrrolidin, N-tetradecanoyl-4-amino-1-butanol, N-tetradecanoyl-3-amino-1-propanol, N-tetradecanoyl-(S)-serine, N-tetradecanoyl-2-benzylserine, N-tetradecanoyl3-phenylserine, N-tetradecanoyl-3-amino-tyrosine, N-tetradecanoyl-1-amino-2-naphthol-4-sulfonic acid, N-tetradecanoyl-3-hydroxy-anthranilic acid, N-tetradecanoyl-4-aminophenol, N-tetradecanoyl-diethanolamine, N-tetradecanoyl-ethanolamine, and N-tetradecanoyl-(S)-phenylalaninol are no substrates
-
-
?
additional information
?
-
activity of CerK in cells is measured by the formation of NBD-C1P from a substrate NBD-ceramide
-
-
-
additional information
?
-
-
the enzyme does not play a role in neutrophil priming, the enzyme regulates the activity and translocalization of cytosolic phospholipase isozyme A2alpha, overview, the enzyme is involved in prostaglandin biosynthesis, i.e. intracellular arachidonic acid production, which is blocked by enzyme gene silencing
-
-
?
additional information
?
-
-
the enzyme is a critical mediator of eicosanoid synthesis
-
-
?
additional information
?
-
-
no activity with GTP, no activity with sphingosine and sphinganine, and with diacylglycerol
-
-
?
additional information
?
-
-
substrate specificity and stereochemistry, overview, methylation of the primary hydroxyl group results in loss of activity, the enzyme can use both ceramides with long saturated and long unsaturated fatty acyl chains
-
-
?
additional information
?
-
-
does not bind to lysophosphatidic acid, lysophosphocholine, sphingosine 1-phosphate, phosphatidylethanolamine, phosphatidylcholine, phosphatidic acid, or phosphatidylserine
-
-
?
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
ATP + N-hexadecanoyl-sphingenine
ADP + N-hexadecanoyl-sphingenine 1-phosphate
-
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
CERK plays a role in cell signalling
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
involvement in inflammatory processes and cell growth
-
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
-
ceramide 1-phosphate is a lipid signalling molecule involved in regulation of many physiological processes related to cell proliferation, apoptosis, and inflammation, most of them in concert with sphingosine 1-phosphate, ceramide 1-phosphate might act via extracellular cell surface receptors or intracellularly as second messenger
-
?
ATP + ceramide
ADP + ceramide 1-phosphate
-
-
synthesis of the sphingolipid signaling molecule
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
ceramide is a key mediator of cellular apoptosis
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
ceramide kinase is a critical mediator of eicosanoid synthesis, and its product, ceramide 1-phosphate, is required for the production of prostaglandins in response to several inflammatory agonists, CERK requires ceramide actively transported to the trans-Golgi network via ceramide transport protein CERT
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
ceramide kinase is important for cellular proliferation and survival, activation of cytosolic phospholipase A2, mast cell degranulation, and phagocytosis
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
CERK and C1P are playing significant biological roles in cell-signaling cascades
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
CerK has important roles in leukocyte functions, including the role in degranulation of mast cells and the phagocytosis of polymorphonuclear leukocytes
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
increased ceramide 1-phosphate during phagocytosis enhances phagocytosis and phagolysosome formation in COS-1 cells expressing hCERK
-
-
?
ceramide + ATP
ceramide 1-phosphate + ADP
-
key enzyme for controlling ceramide levels
-
-
?
additional information
?
-
-
the enzyme does not play a role in neutrophil priming, the enzyme regulates the activity and translocalization of cytosolic phospholipase isozyme A2alpha, overview, the enzyme is involved in prostaglandin biosynthesis, i.e. intracellular arachidonic acid production, which is blocked by enzyme gene silencing
-
-
?
additional information
?
-
-
the enzyme is a critical mediator of eicosanoid synthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
Mg2+
Mg2+
the recombinant enzyme is highly dependent on Mg2+, at 3 mM MgCl2, preferred divalent cation
Ca2+
-
required for activity, 60 nM - 3 mM, 20fold linear increase in activity, progressive loss of activity at higher concentrations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1alpha,25-dihydroxyvitamin D3
enzyme activity decreases by approximately 40% in the presence of the hormone
3,3-cholamidopropyl-dimethylammonio-1-propanesulfonate
almost complete inhibition at high concentrations
all-trans retinoic acid
inhibits ceramide kinase transkription in neuroblastoma cells
N-ethyl-maleimide
thiol modifiying agent stops CerK acitivity, demonstrating that CerK contains exposed cysteine residues important for enzymatic activity
N-[2-(benzoylamino)-6-benzothiazolyl]-tricyclo[3.3.1.13,7] decane-1-carboxamide
NVP-231, a potent inhibitor of CerK
-
NVP-231
diamino-benzothiazole derivative, potent inhibitor, no inhibition with its analog NVP-995
octyl-beta-D-glucopyranoside
almost complete inhibition at high concentrations
ZK191784
enzyme activity decreases by approximately 25% in the presence of the hormone analogue
2,5-dihydroxy-3-[[(4aS,8aS)-2,5,5,8a-tetramethyl-3,4,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]methyl]cyclohexa-2,5-diene-1,4-dione
-
K1, novel F-12509A olefin isomer, inhibitor decreases ceramide 1-phosphate levels without changing other lipids such as ceramide and sphingomyelin
adamantane-1-carboxylic acid (2-benzoylamino-benzothiazol-6-yl)amide
-
NVP-231, a potent, specific, and reversible CerK inhibitor that competitively inhibits binding of ceramide to CerK
siRNA
-
downregulation of CerK with siRNA targeted against Cerk reduced cellular proliferation within 48 hours
-
additional information
no inhibition by ceramide analogues containing a carboxy group, i.e. N-acylated amino acids
-
additional information
-
no inhibition by ceramide analogues containing a carboxy group, i.e. N-acylated amino acids
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
A23187
-
calcium ionophore, 216% activation of ceramide kinase in A549 lung adenocarcinoma cells
interleukin-1 beta
-
187% activation of ceramide kinase in A549 lung adenocarcinoma cells
-
additional information
-
the enzyme is induced by the calcium triggers interleukin-1beta and IgE/Ag due to calcium mobilization
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
N-(6-((7-nitro-2-1,3-benzoxadiazol-4-yl)amino)hexanoyl)-D-erythro-sphingosine
-
-
0.042
ATP
assay mixture is composed of 0.88 mM ceramide, 1 mM cardiolipin, 1.5% beta-octylglucoside, 0.2 mM diethylenetriaminepenta-acetic acid, 20 mM MOPS, pH 7.2, 50 mM NaCl, 10 mM dithiothreitol, 2 mM EGTA, 3 mM CaCl2 and 0.5 mM ATP, at 30°C
0.052
ATP
assay mixture is composed of 0.88 mM ceramide, 1 mM cardiolipin, 1.5% beta-octylglucoside, 0.2 mM diethylenetriaminepenta-acetic acid, 20 mM MOPS, pH 7.2, 50 mM NaCl, 10 mM dithiothreitol, 2 mM EGTA, 3 mM CaCl2 and 0.5 mM ATP, at 30°C
0.194
ceramide
assay mixture is composed of 0.88 mM ceramide, 1 mM cardiolipin, 1.5% beta-octylglucoside, 0.2 mM diethylenetriaminepenta-acetic acid, 20 mM MOPS, pH 7.2, 50 mM NaCl, 10 mM dithiothreitol, 2 mM EGTA, 3 mM CaCl2 and 0.5 mM ATP, at 30°C
0.205
ceramide
assay mixture is composed of 0.88 mM ceramide, 1 mM cardiolipin, 1.5% beta-octylglucoside, 0.2 mM diethylenetriaminepenta-acetic acid, 20 mM MOPS, pH 7.2, 50 mM NaCl, 10 mM dithiothreitol, 2 mM EGTA, 3 mM CaCl2 and 0.5 mM ATP, at 30°C
additional information
additional information
kinetics of recombinant enzymes
-
additional information
additional information
-
kinetics of recombinant enzymes
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000012
adamantane-1-carboxylic acid (2-benzoylamino-benzothiazol-6-yl)amide
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.92 - 5.4
recombinant enzyme in CHO cell extract, substrate N-C6-D-erythro-sphingenine
additional information
additional information
enzyme activity is decreased during all-trans retinoic acid-induced neuronal differentiation of SH-SY5Y cells, all-trans retinoic acid reduces CERK protein and mRNA level in a time- and concentration-dependent manner, all-trans retinoic acid reduces cellular enzyme product ceramide 1-phosphate to 60% of control cells
additional information
-
enzyme activity is decreased during all-trans retinoic acid-induced neuronal differentiation of SH-SY5Y cells, all-trans retinoic acid reduces CERK protein and mRNA level in a time- and concentration-dependent manner, all-trans retinoic acid reduces cellular enzyme product ceramide 1-phosphate to 60% of control cells
additional information
-
assay development utilizing Triton X-100 mixed micelles with cardiolipin, beta-octylglucoside, and diethylene pentaacetic acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
very high expression level in resting and low expression level in activated CD4+ cell, resting CD8+ cells, resting, CD14+ cells, higher expression level in resting and low expression level in activated CD19+ cells
additional information
CERK expression is associated with an increased risk of recurrence in women with breast cancer
-
CerK mRNA expression and activity decreased during macrophagelike cell differentiation of HL-60 cells
additional information
in nerve growth factor (NGF)-treated cells, HA-tagged CerK is mainly localized in punctuate structures, possibly endosomes and/or vesicles, in the cytoplasm in both the bottom and nucleus phases, and HA-tagged CerK exists in the extended neurites observed in the bottom phase
additional information
-
the enzyme is expressed in all or nearly all tissues and cell types
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
phosphorylation of ceramide by CERK at the cytoplasmic surface of the trans-Golgi network
-
CERK and localizes to the caveolar microdomains during phagocytosis
additional information
CERK also contains nuclear localization/export signals and traffics to the plasma membrane via microtubule-driven vesicles in response to hyperosmotic shock
microtubule-driven vesicles that traffic between the Golgi complex and the plasma membrane
-
bound to, probably via the pleckstrin homology domain of the enzyme
additional information
truncation of the PH domain either from the N-terminus or C-terminus results in disruption of the PH domain fold and loss of wild type ceramide kinase localization
-
additional information
-
subcellular localization may be dependent on the cell type
-
additional information
-
the enzyme is involved in vesicular trafficking and subcellular translocation involving its pleckstrin homology domain, the enzyme co-localizes with its substrate, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
cells lacking acid sphingomyelinase (ASM) have decreased ceramide 1-phosphate production following TNF-alpha treatment, suggesting that ASM may be acting upstream of CERK. Effect of CERK knockdown on lipid levels of ceramide 1-phosphate, ceramide, and sphingosine, overview. Knockdown of CERK in the presence of ASM overexpression led to a decrease in CCL5 levels on the protein and message levels
malfunction
knockdown of CerK and overexpression of HA-tagged CerK down- and upregulated the formation of ceramide-1-phosphate (C1P), respectively. When knockdown or overexpression of CerK is performed, Ca2+-induced release of [3H] noradrenaline is reduced or enhanced, respectively, but neurite extension is not modified. A limited change in cellular sphingolipid levels by knockdown of CerK. The levels of ceramide, sphingomyelin, and monohexosylceramide, including their total levels and levels of their subspecies with irrespective of N-acyl chain lengths, and those of sphingosine, sphingomyelin 1-phosphate, and their dihydro-forms are not affected by the CerK knockdown in PC12 cells
metabolism
functional role of the ASM/CERK pathway in cancer cell migration, and of the ASM/CERK signaling axis in cytokines associated with EMT, cell migration, and invasiveness
metabolism
involvement of the lysosome pathway in CerK levels and ceramide 1-phosphate formation
physiological function
enzyme plays an important role in cellular events such as cell growth and inflammation
physiological function
ceramide kinase/ceramide 1-phosphate axis acts as molecular effector of the anti-proliferative action of 1alpha,25-dihydroxyvitamin D3 and its analogues. The inhibition of ceramide kinase by specific gene silencing or pharmacological inhibition, drastically reduces cell proliferation. 1alpha,25-Dihydroxyvitamin D3 and structural analogue ZK191784 treatment induce a significant decrease in ceramide kinase expression and ceramide 1-phosphate content, and an increase of ceramide. The treatment of SH-SY5Y cells with ZK159222, antagonist of 1alpha,25-dihydroxyvitamin D3 receptor, trichostatin A, inhibitor of histone deacetylases, and COUP-TFI-siRNA prevents the decrease of ceramide kinase expression elicited by 1alpha,25-dihydroxyvitamin D3 supporting the involvement of VDR/COUP-TFI/histone deacetylase complex in ceramide kinase regulation
physiological function
ceramide kinase promotes tumor cell survival and mammary tumor recurrence. Ceramide kinase is required for mammary tumor recurrence following HER2/neu pathway inhibition and is spontaneously upregulated during tumor recurrence in multiple genetically engineered mouse models for breast cancer. CERK expression is associated with an increased risk of recurrence in women with breast cancer, Cerk promotes tumor cell survival in vivo
physiological function
CERK is required for eicosanoid biosynthesis in response to mechanical insult. Simulation of mechanical trauma of a wound demonstrates steadily increasing levels of arachidonic acid in a time-dependent manner reflected in scratch-induced eicosanoid levels. Proper migration of fi broblasts is one of the necessary steps of wound healing, requirement for the CERK-derived ceramide 1-phosphate in the proper healing response of wounds
physiological function
phosphorylated sphingolipids ceramide-1-phosphate and sphingosine-1-phosphate are key regulators of cell growth, survival, migration, and inflammation. Ceramide 1-phosphate produced by ceramide kinase is an activator of group IVA cytosolic phospholipase A2alpha (cPLA2alpha), the rate-limiting releaser of arachidonic acid used for pro-inflammatory eicosanoid production, which contributes to disease pathogenesis in asthma/airway hyper-responsiveness, cancer, atherosclerosis, and thrombosis. To modulate eicosanoid action and avoid the damaging effects of chronic inflammation, cells require efficient targeting, trafficking, and presentation of ceramide 1-phosphate to specific cellular sites. Nonvesicular trafficking by a ceramide-1-phosphate transfer protein, CPTP, regulates eicosanoids, mechanism, overview. CPTP prevents excess ceramide-1-phosphate accumulation after production by CERK, thereby regulating cPLA2alpha action, diminishing arachidonic acid release and downstream generation of pro-inflammatory eicosanoids
physiological function
ceramide kinase (CerK) phosphorylates ceramide to ceramide-1-phosphate (C1P). The activity of CerK is regulated by post-translational modifications including phosphorylation, CerK has a role in neuronal functions
physiological function
TNF-alpha induces the formation of ceramide 1-phosphate (C-1-P) in a CERK-dependent manner. Silencing of CERK blocks CCL5 production in response to TNF-alpha. ASM and CERK induce a highly concordant program of cytokine production and both are required for migration of breast cancer cells. ASM can produce ceramide which is then converted to ceramide 1-phosphate by CERK, and that ceramide 1-phosphate is required for production of CCL5 and several cytokines and chemokines, with roles in cell migration. Enzyme CERK is required for CCL5 production and sufficient to induce CCL5 in MCF-7 breast cancer cells
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). CERK1_HUMAN
537
0
59977
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
subdomain structure of the enzyme, possessing a pleckstrin homology domain, a DAGK-like catalytic domain, and a Ca2+/calmodulin binding domain
additional information
-
the enzyme possesses an N-terminal pleckstrin homology PH domain, residues 32-121, and a C-terminal region which contains a Ca2+/calmodulin binding domain, residues 378-455, that flanks the catalytic domain, residues 124-433, the enzyme also contains 5 sequences stretches C1-C5 typical for lipid kinases
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
ubiquitination
levels of CerK are downregulated by the ubiquitin/proteasome and lysosome pathways and the former pathway-sensitive pool of CerK is suggested to be linked with exocytosis in PC12 cells
lipoprotein
-
the enzyme is myristoylated at the N-terminus within the pleckstrin homology PH domain, required for activity
phosphoprotein
phosphorylation of serine residues at positions 340 and 408, putative additional phosphorylation site at serine 427 lying in the calcium/calmodulin domain, preventing phosphorylation at S340 results in CERK instability
phosphoprotein
activity of CerK is regulated by post-translational modifications including phosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C347A
C351A
C354A
DELTA1-123
production by site-directed mutagenesis, localization in cytosol
DELTA124-537
production by site-directed mutagenesis, resulted in almost complete accumulation in the nucleus
DELTA219-496
production by site-directed mutagenesis, localization in cytosol and nucleus
DELTA340-537
production by site-directed mutagenesis, significant accumulation into the nucleus, existence of nuclear export signals in the C-terminal part of enzyme, traditional nuclear export signals 511-IEVRVHCQLVRL-522 in the CC3 domain and a class 2 nuclear export signals 347-CRAGCFVC-354 between the CC1 and the CC2 domains
DELTA454-537
production by site-directed mutagenesis, localization in cytosol and nucleus
DELTA514-537
production by site-directed mutagenesis, nuclear localization of ceramide kinase
DELTA520-537
production by site-directed mutagenesis, localization is mostly cytosolic but is also detected in the nucleus
DELTA525-537
production by site-directed mutagenesis, both localization and cellular activity are lost
DELTA528-537
production by site-directed mutagenesis, no effect of localization and activity when assaying at the cellular level with exogenously added substrate, activity is lost after cell lysis in vitro
DELTA533-537
production by site-directed mutagenesis, no effect of localization and activity
S340A
by site directed mutagenesis, using of Triton X-100 as lysis buffer results in 15% activity decrease in the mutant protein compared with the wild type enzyme, when octylglucoside is used instead of Triton X-100 for cell lysis, activity is reduced in the S340A mutant protein which reaches only 15% of wild type activity
S340D
by site directed mutagenesis, intermediate recovery of 16% is observed for the mutant protein
S427A
by site directed mutagenesis, activity in the S427A mutant protein amounts to only 30% of that of wild type enzyme
S427D
by site directed mutagenesis, mutant protein displays 50% of wild type activity
CERKL
-
the point mutant enzyme CERKL does not phosphorylate ceramide or diacylglycerol and is localized in the nucleus
G2A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
additional information
C347A
by site-directed mutagenesis, mutation severely impairs localization at the Golgi complex resulting in cytosolic accumulation instead
C351A
by site-directed mutagenesis, mutation severely impairs localization at the Golgi complex resulting in cytosolic accumulation instead
additional information
a truncated mutant enzyme, lacking the first 115 amno acids, is not active and fails to be located in the plasma membrane
additional information
-
a truncated mutant enzyme, lacking the first 115 amno acids, is not active and fails to be located in the plasma membrane
additional information
knockdown of CERK in MCF-7 cells by specific siRNA
additional information
knockdown of CerK is performed with shRNA to silence CerK (shCerK, target sequence GTT (TATCGAGTCAAGAAAT)). Establishment of a stable CerK-knockdown cell line (shCerK) and a HA-tagged CerK expressing cell line using a retroviral vector. Serum withdrawal causes ubiquitination of HA-tagged CerK protein and downregulates both HA-tagged CerK protein and ceramide 1-phosphate formation within 6 h, and these downregulations are abolished by co-treatments with NGF or proteasome inhibitors such as MG132 and clasto-lactacystin. Treatment with the proteasome inhibitors increases HA-tagged CerK in puncture structures, possibly endosomes and/or vesicles, in cells. Treatment with the lysosome inhibitors reduces serum withdrawal-induced downregulation of HA-tagged CerK protein but not ceramide 1-phosphate formation. When knockdown or overexpression of CerK is performed, Ca2+-induced release of [3H] noradrenaline is reduced or enhanced, respectively, but neurite extension is not modified. There is a positive correlation between noradrenaline release and formation of ceramide 1-phosphate and/or HA-tagged CerK levels in NGF- and clasto-lactacystin-treated cells
additional information
-
siRNA to the gene encoding the enzyme for downregulation blocks arachidonic acid release and subsequent prostaglandin E2 production after stimulation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
ceramide kinase is extremely sensitive to oxidation, 1 mM dithiothreitol stabilizes
-
640967
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
30°C, 50 mM Tris/HCl, pH 7.5, 270 mM sucrose, 1 mM EDTA, 1 mM EGTA, 5 mM tris(hydroxypropyl)phosphine, 1% Triton X-100, 20 min, 50% decrease of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
as a C-terminal fusion to maltose binding protein, MBP-Cerk was purified on amylose resin
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, overexpression of human CerK in COS-1 and RBL-2H3 cells
expression in SF9 insect cell and transfection of FLAG-tagged or GFP-tagged wild type and mutant CerK proteins in COS-1 cell
recombinant expression of HA-tagged enzyme CerK in PC-12 cells, A-549cells, and HEK-293 T cells, quantitative real-time PCR analysis of CerK mRNA
recombinant full-length hCERK is obtained from baculovirus-infected Sf9 cells as a glutathione-S-transferase fusion
stable expression of human CerK in COS-1 cell, named COS-CerK cell, and RBL-2H3 cell
DNA and amino acid sequence determination, expression in HeLa and COS-1 cells, expression of GFP-tagged enzyme in HUVEC and COS-1 cells
-
expression of C-terminally FLAG-tagged and of EGFP-tagged wild-type and mutant enzymes in COS-1 cells
-
expression of green fluorescent protein-tagged human ceramide kinase in CHO-W11A cells, the increase in ceramide 1-phosphate formation by transfection with the vector for human ceramide kinase significantly enhances the Ca2+-ionophore A23187-induced release of arachidonic acid via cytosolic phospholipase A2alpha activation in CHO cells
-
overexpression in HeLa cells, expression of His6-tagged enzyme in Spodoptera frugiperda Sf9 insect cells using the baculovirus infection system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
all-trans retinoic acid inhibits ceramide kinase transkription during neuronal differentiation of a human neuroblastoma cell line SH-SY5Y, inhibition of the transcriptional activity of the 5'-promoter of ceramide kinase. Retinol does not reduce CERK protein and mRNA level
Cerk is rapidly upregulated in tumor cells following HER2/neu downregulation or treatment with adriamycin
expression of the enzyme, after 24 h of treatment with 1alpha,25-dihydroxyvitamin D3 or its analogue ZK191784, is reduced by approximately 40 and 60%, respectively
ceramide kinase expression shows no association with age, lymph node status and tumor size
-
higher expression in estrogen receptor negative breast tumors, gene expression of ceramide kinase is associated with prognosis in breast cancer, high ceramide kinase expression is correlated with ErbB2 status
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
enzymatic assay to quantify mass levels of long chain ceramides in cellular lipid extracts
medicine
the enzyme is a therapeutical target in breast cancer treatment due to its functional role in breast cancer recurrence
diagnostics
-
putative prognostic marker in breast cancer, estrogen receptor negative patients with high ceramide kinase expression had a worse prognosis then those with low expression
medicine
medicine
-
potentially important therapeutic target in oncology and inflammation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kolesnick, R.N.; Hemer, M.R.
Characterization of a ceramide kinase activity from human leukemia (HL-60) cells. Separation from diacylglycerol kinase activity
J. Biol. Chem.
265
18803-18808
1990
Homo sapiens
Bajjalieh, S.; Batchelor, R.
Ceramide kinase
Methods Enzymol.
311
207-215
2000
Homo sapiens, Rattus norvegicus
Sugiura, M.; Kono, K.; Liu, H.; Shimizugawa, T.; Minekura, H.; Spiegel, S.; Kohama, T.
Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization
J. Biol. Chem.
277
23294-23300
2002
Homo sapiens (Q8TCT0), Homo sapiens
Bektas, M.; Jolly, P.S.; Milstien, S.; Spiegel, S.
A specific ceramide kinase assay to measure cellular levels of ceramide
Anal. Biochem.
320
259-265
2003
Homo sapiens (Q8TCT0), Homo sapiens
Pettus, B.J.; Bielawska, A.; Spiegel, S.; Roddy, P.; Hannun, Y.A.; Chalfant, C.E.
Ceramide kinase mediates cytokine- and calcium ionophore-induced arachidonic acid release
J. Biol. Chem.
278
38206-38213
2003
Homo sapiens
Carre, A.; Graf, C.; Stora, S.; Mechtcheriakova, D.; Csonga, R.; Urtz, N.; Billich, A.; Baumruker, T.; Bornancin, F.
Ceramide kinase targeting and activity determined by its N-terminal pleckstrin homology domain
Biochem. Biophys. Res. Commun.
324
1215-1219
2004
Homo sapiens
Yokota, H.; Yatomi, Y.; Mashige, F.; Nakahara, K.
Expression of ceramide kinase in hematopoietic cells
Eur. J. Haematol.
73
307-308
2004
Homo sapiens
Baumruker, T.; Bornancin, F.; Billich, A.
The role of sphingosine and ceramide kinases in inflammatory responses
Immunol. Lett.
96
175-185
2005
Homo sapiens
Wijesinghe, D.S.; Massiello, A.; Subramanian, P.; Szulc, Z.; Bielawska, A.; Chalfant, C.E.
Substrate specificity of human ceramide kinase
J. Lipid Res.
46
2706-2716
2005
Homo sapiens
Van Overloop, H.; Gijsbers, S.; Van Veldhoven, P.P.
Further characterization of mammalian ceramide kinase. Substrate delivery and (stereo)specificity, tissue distribution and subcellular localization studies
J. Lipid Res.
47
268-283
2006
Mus musculus, Rattus norvegicus, Homo sapiens (Q8TCT0), Homo sapiens
Kim, T.J.; Mitsutake, S.; Igarashi, Y.
The interaction between the pleckstrin homology domain of ceramide kinase and phosphatidylinositol 4,5-bisphosphate regulates the plasma membrane targeting and ceramide 1-phosphate levels
Biochem. Biophys. Res. Commun.
342
611-617
2006
Homo sapiens
Inagaki, Y.; Mitsutake, S.; Igarashi, Y.
Identification of a nuclear localization signal in the retinitis pigmentosa-mutated RP26 protein, ceramide kinase-like protein
Biochem. Biophys. Res. Commun.
343
982-987
2006
Homo sapiens
Graf, C.; Rovina, P.; Tauzin, L.; Schanzer, A.; Bornancin, F.
Enhanced ceramide-induced apoptosis in ceramide kinase overexpressing cells
Biochem. Biophys. Res. Commun.
354
309-314
2007
Homo sapiens, Homo sapiens (Q8TCT0)
Rovina, P.; Jaritz, M.; Hoefinger, S.; Graf, C.; Devay, P.; Billich, A.; Baumruker, T.; Bornancin, F.
A critical beta6-beta7 loop in the pleckstrin homology domain of ceramide kinase
Biochem. J.
400
255-265
2006
Homo sapiens (Q8TCT0)
Van Overloop, H.; Denizot, Y.; Baes, M.; Van Veldhoven, P.P.
On the presence of C2-ceramide in mammalian tissues: possible relationship to etherphospholipids and phosphorylation by ceramide kinase
Biol. Chem.
388
315-324
2007
Homo sapiens
Mitra, P.; Maceyka, M.; Payne, S.G.; Lamour, N.; Milstien, S.; Chalfant, C.E.; Spiegel, S.
Ceramide kinase regulates growth and survival of A549 human lung adenocarcinoma cells
FEBS Lett.
581
735-740
2007
Homo sapiens, Mus musculus
Lamour, N.F.; Stahelin, R.V.; Wijesinghe, D.S.; Maceyka, M.; Wang, E.; Allegood, J.C.; Merrill, A.H.; Cho, W.; Chalfant, C.E.
Ceramide kinase uses ceramide provided by ceramide transport protein: localization to organelles of eicosanoid synthesis
J. Lipid Res.
48
1293-1304
2007
Homo sapiens
Don, A.S.; Rosen, H.
A fluorescent plate reader assay for ceramide kinase
Anal. Biochem.
375
265-271
2008
Homo sapiens
Graf, C.; Rovina, P.; Bornancin, F.
A secondary assay for ceramide kinase inhibitors based on cell growth inhibition by short-chain ceramides
Anal. Biochem.
384(1)
166-169
2008
Homo sapiens (Q8TCT0)
Munagala, N.; Nguyen, S.; Lam, W.; Lee, J.; Joly, A.; McMillan, K.; Zhang, W.
Identification of small molecule ceramide kinase inhibitors using a homogeneous chemiluminescence high throughput assay
Assay Drug Dev. Technol.
5
65-74
2007
Homo sapiens
Lidome, E.; Graf, C.; Jaritz, M.; Schanzer, A.; Rovina, P.; Nikolay, R.; Bornancin, F.
A conserved cysteine motif essential for ceramide kinase function
Biochimie
90
1560-1565
2008
Homo sapiens (Q8TCT0), Homo sapiens
Lamour, N.F.; Chalfant, C.E.
Ceramide kinase and the ceramide-1-phosphate/cPLA2alpha interaction as a therapeutic target
Curr. Drug Targets
9
674-682
2008
Homo sapiens
Saxena, S.; Banerjee, M.; Shirumalla, R.K.; Ray, A.
Ceramide kinase: a potential anti-inflammatory target?
Curr. Opin. Investig. Drugs
9
455-462
2008
Homo sapiens
Date, T.; Mitsutake, S.; Igarashi, Y.
Ceramide kinase expression is altered during macrophage-like cell differentiation of the leukemia cell line HL-60
In Vitro Cell. Dev. Biol. Anim.
43
321-323
2007
Homo sapiens
Hinkovska-Galcheva, V.; Clark, A.; VanWay, S.; Huang, J.B.; Hiraoka, M.; Abe, A.; Borofsky, M.; Kunkel, R.G.; Shanley, T.; Shayman, J.A.; Lanni, F.; Petty, H.R.; Boxer, L.A.
Ceramide kinase promotes Ca2+ signaling near IgG-opsonized targets and enhances phagolysosomal fusion in COS-1 cells
J. Lipid Res.
49
531-542
2008
Homo sapiens
Wijesinghe, D.S.; Lamour, N.F.; Gomez-Munoz, A.; Chalfant, C.E.
Ceramide kinase and ceramide-1-phosphate
Methods Enzymol.
434
265-292
2007
Homo sapiens
Graf, C.; Klumpp, M.; Habig, M.; Rovina, P.; Billich, A.; Baumruker, T.; Oberhauser, B.; Bornancin, F.
Targeting ceramide metabolism with a potent and specific ceramide kinase inhibitor
Mol. Pharmacol.
74
925-932
2008
Homo sapiens
Rovina, P.; Schanzer, A.; Graf, C.; Mechtcheriakova, D.; Jaritz, M.; Bornancin, F.
Subcellular localization of ceramide kinase and ceramide kinase-like protein requires interplay of their Pleckstrin Homology domain-containing N-terminal regions together with C-terminal domains
Biochim. Biophys. Acta
1791
1023-1030
2009
Homo sapiens (Q8TCT0)
Shimizu, M.; Tada, E.; Makiyama, T.; Yasufuku, K.; Moriyama, Y.; Fujino, H.; Nakamura, H.; Murayama, T.
Effects of ceramide, ceramidase inhibition and expression of ceramide kinase on cytosolic phospholipase A2alpha; additional role of ceramide-1-phosphate in phosphorylation and Ca2+ signaling
Cell. Signal.
21
440-447
2009
Homo sapiens
Ruckhaeberle, E.; Karn, T.; Rody, A.; Hanker, L.; Gaetje, R.; Metzler, D.; Holtrich, U.; Kaufmann, M.
Gene expression of ceramide kinase, galactosyl ceramide synthase and ganglioside GD3 synthase is associated with prognosis in breast cancer
J. Cancer Res. Clin. Oncol.
135
1005-1013
2009
Homo sapiens
Murakami, M.; Ito, H.; Hagiwara, K.; Yoshida, K.; Sobue, S.; Ichihara, M.; Takagi, A.; Kojima, T.; Tanaka, K.; Tamiya-Koizumi, K.; Kyogashima, M.; Suzuki, M.; Banno, Y.; Nozawa, Y.; Murate, T.
ATRA inhibits ceramide kinase transcription in a human neuroblastoma cell line, SH-SY5Y cells: The role of COUP-TFI
J. Neurochem.
112
511-520
2010
Homo sapiens (Q8TCT0), Homo sapiens
Chen, W.Q.; Graf, C.; Zimmel, D.; Rovina, P.; Krapfenbauer, K.; Jaritz, M.; Parker, P.J.; Lubec, G.; Bornancin, F.
Ceramide kinase profiling by mass spectrometry reveals a conserved phosphorylation pattern downstream of the catalytic site
J. Proteome Res.
9
420-429
2010
Homo sapiens (Q8TCT0)
Bini, F.; Frati, A.; Garcia-Gil, M.; Battistini, C.; Granado, M.; Martinesi, M.; Mainardi, M.; Vannini, E.; Luzzati, F.; Caleo, M.; Peretto, P.; Gomez-Munoz, A.; Meacci, E.
New signalling pathway involved in the anti-proliferative action of vitamin D3 and its analogues in human neuroblastoma cells. A role for ceramide kinase
Neuropharmacology
63
524-537
2012
Homo sapiens (Q8TCT0), Homo sapiens
Payne, A.W.; Pant, D.K.; Pan, T.C.; Chodosh, L.A.
Ceramide kinase promotes tumor cell survival and mammary tumor recurrence
Cancer Res.
74
6352-6363
2014
Homo sapiens (Q8TCT0), Homo sapiens
Wijesinghe, D.S.; Brentnall, M.; Mietla, J.A.; Hoeferlin, L.A.; Diegelmann, R.F.; Boise, L.H.; Chalfant, C.E.
Ceramide kinase is required for a normal eicosanoid response and the subsequent orderly migration of fibroblasts
J. Lipid Res.
55
1298-1309
2014
Mus musculus (Q8K4Q7), Homo sapiens (Q8TCT0), Homo sapiens, Mus musculus BALB/c (Q8K4Q7)
Simanshu, D.K.; Kamlekar, R.K.; Wijesinghe, D.S.; Zou, X.; Zhai, X.; Mishra, S.K.; Molotkovsky, J.G.; Malinina, L.; Hinchcliffe, E.H.; Chalfant, C.E.; Brown, R.E.; Patel, D.J.
Non-vesicular trafficking by a ceramide-1-phosphate transfer protein regulates eicosanoids
Nature
500
463-467
2013
Homo sapiens (Q8TCT0), Homo sapiens
Hori, M.; Gokita, M.; Yasue, M.; Honda, T.; Kohama, T.; Mashimo, M.; Nakamura, H.; Murayama, T.
Down-regulation of ceramide kinase via proteasome and lysosome pathways in PC12 cells by serum withdrawal its protection by nerve growth factor and role in exocytosis
Biochim. Biophys. Acta
1867
118714
2020
Homo sapiens (Q8TCT0)
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