2.3.1.50: serine C-palmitoyltransferase
This is an abbreviated version!
For detailed information about serine C-palmitoyltransferase, go to the full flat file.
Word Map on EC 2.3.1.50
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2.3.1.50
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sphingolipids
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ceramide
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myriocin
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sphingomyelin
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sphingosine
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sphingomyelinase
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neuropathy
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sphingoid
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cholesterol
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fumonisin
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glucosylceramide
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sphingosine-1-phosphate
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3-ketodihydrosphingosine
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corneum
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glycosphingolipids
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dihydroceramide
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dihydrosphingosine
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plp-dependent
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l-cycloserine
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ormdl3
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molecular biology
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sphingomonas
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paucimobilis
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transepidermal
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charcot-marie-tooth
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analysis
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ceramide-induced
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phytosphingosine
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medicine
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asmase
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aldimine
- 2.3.1.50
- sphingolipids
- ceramide
- myriocin
- sphingomyelin
- sphingosine
- sphingomyelinase
- neuropathy
-
sphingoid
- cholesterol
- fumonisin
- glucosylceramide
- sphingosine-1-phosphate
- 3-ketodihydrosphingosine
- corneum
- glycosphingolipids
- dihydroceramide
- dihydrosphingosine
-
plp-dependent
- l-cycloserine
-
ormdl3
- molecular biology
- sphingomonas
- paucimobilis
-
transepidermal
-
charcot-marie-tooth
- analysis
-
ceramide-induced
- phytosphingosine
- medicine
- asmase
-
aldimine
Reaction
Synonyms
3-oxosphinganine synthetase, acyl-CoA:serine C-2 acyltransferase decarboxylating, LCB1, LCB2, LCB2a, LCB2b, More, palmitoyltransferase, serine, serine palmitoyl transferase, serine palmitoyltransferase, serine palmitoyltransferase 1, serine palmitoyltransferase a, serine-palmitoyl transferase, serine-palmitoyltransferase, SPT, SPT1, SPT2, SPT3, SPTase, SPTLC1, SPTLC2, ssSPT, ssSPTa, Tsc3
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 2.3.1.50 - serine C-palmitoyltransferase
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glycoprotein
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the small activating subunits of serine palmitoyltransferase, ssSPTs, are glycoproteins and are part of the enzyme complex
phosphoprotein
additional information
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carrier lipid during extraction required for activity
E2RKV3
phosphorylation of serine palmitoyltransferase long chain-1 (SPTLC1) on tyrosine 164 by the fusion kinase ABL inhibits the SPTLC1 enzyme activity. ABL-mediated phosphorylation of SPTLC1 affects its endoplasmic reticulum localization
phosphoprotein
phosphorylation of serine palmitoyltransferase long chain-1 (SPTLC1) on tyrosine 164 by the fusion kinase BCR-ABL inhibits the SPTLC1 enzyme activity. Inhibition of BCR-ABL kinase using either imatinib or shRNA-mediated silencing leads to the activation of SPTLC1 and to increased apoptosis in both K562 and LAMA-84 cells. ABL-mediated phosphorylation of SPTLC1 affects its endoplasmic reticulum localization
phosphoprotein
the enzyme is phosphorylated at S284 regulating its substrate specificity