2.7.1.138: ceramide kinase
This is an abbreviated version!
For detailed information about ceramide kinase, go to the full flat file.
Word Map on EC 2.7.1.138
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2.7.1.138
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ceramide-1-phosphate
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sphingolipids
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1-phosphate
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sphingosine-1-phosphate
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ceramidase
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pleckstrin
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cerkl
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medicine
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ceramide-induced
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analysis
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diagnostics
- 2.7.1.138
- ceramide-1-phosphate
- sphingolipids
- 1-phosphate
- sphingosine-1-phosphate
- ceramidase
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pleckstrin
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cerkl
- medicine
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ceramide-induced
- analysis
- diagnostics
Reaction
Synonyms
acylsphingosine kinase, ceramide kinase, CERK, DCERK protein, hCERK, kinase, acylsphingosine (phosphorylating), More
ECTree
2.7.1.138 ceramide kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.138 - ceramide kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C347A
C351A
C354A
CERKL
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the point mutant enzyme CERKL does not phosphorylate ceramide or diacylglycerol and is localized in the nucleus
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
G2A
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
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
E8A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
F429R
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site-directed mutagenesis, weak binding of calmodulin compared to the wild-type enzyme
F431R
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site-directed mutagenesis, no binding of calmodulin in contrary to the wild-type enzyme
G2A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
L10A
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site-directed mutagenesis, 99% reduced activity compared to the wild-type enzyme, substrate affinity and activation by Ca2+ are unaffected, mutation within the pleckstrin homology domain
L10I
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site-directed mutagenesis, 71% reduced activity compared to the wild-type enzyme, substrate affinity and activation by Ca2+ are unaffected, mutation within the pleckstrin homology domain
L422R
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site-directed mutagenesis, similar binding of calmodulin compared to the wild-type enzyme
L435R
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site-directed mutagenesis, no binding of calmodulin in contrary to the wild-type enzyme
P9A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
S12A
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site-directed mutagenesis, the mutant shows unaltered 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
generation of an Arabidopsis thaliana cell-death mutant, accelerated cell death5 (acd5), which accumulates ceramides and exhibits spontaneous cell death late in development. NaCl enhances disease resistance and suppresses cell death in ceramide kinase mutants. The effect of NaCl is partly dependent on the antagonistic interaction between endogenous abscisic acid (ABA) and salicylic acid (SA). The intact ABA pathway may not be required for this effect. The response of the acd5 mutant to abiotic stress shows that the mutants do not have the cell-death phenotype. 300 mM NaCl suppresses the cell-death phenotype of the acd5 mutant without inhibiting plant growth. NaCl treatment inhibits sphingolipid accumulation in the acd5 mutant and alters the endogenous levels of SA and ABA
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
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a truncated mutant enzyme, lacking the first 115 amno acids, is not active and fails to be located in the plasma membrane
additional information
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siRNA to the gene encoding the enzyme for downregulation blocks arachidonic acid release and subsequent prostaglandin E2 production after stimulation
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
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construction of an enzyme mutant which shows loss of activity but contains the calmodulin binding motif, expression of the mutant inhibits Ca2+-dependent ceramide 1-phosphate formation
additional information
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construction of N-terminally truncated mutants lacking the first 7, 12, or 76 amino acid residues, respectively, mutant DELTAN7 is still active while mutants DELTAN12 and DELTAN76 are catalytically inactive
additional information
generation of CERK-/- knockout mice and enzyme silencing by siRNA
additional information
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generation of CERK-/- knockout mice and enzyme silencing by siRNA
additional information
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generation of CERK-/- knockout mice and enzyme silencing by siRNA
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