2.7.1.91: sphingosine kinase
This is an abbreviated version!
For detailed information about sphingosine kinase, go to the full flat file.
Word Map on EC 2.7.1.91
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2.7.1.91
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sphingosine-1-phosphate
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1-phosphate
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sphingolipids
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ceramide
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endothelial
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sirnas
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necrosis
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agonist
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metastasis
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artery
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erk
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phospholipase
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fingolimod
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fibrosis
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lymphocyte
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protein-coupled
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sphingomyelinase
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tnf
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pulmonary
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leukemia
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sphingomyelin
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anti-apoptotic
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s1p-induced
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stat3
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pertussis
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mapks
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pro-apoptotic
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mitogen
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sclerosis
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pkc
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rheostat
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signal-regulated
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caspase-3
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pro-survival
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platelet-derived
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lysophospholipids
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cardioprotective
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phytosphingosine
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drug development
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lymphopenia
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egress
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glucosylceramide
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medicine
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fumonisins
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s1p-mediated
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dihydroceramide
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mitogenesis
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pdgf-induced
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ceramide-induced
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lysophosphatidic
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fcepsilonri
- 2.7.1.91
- sphingosine-1-phosphate
- 1-phosphate
- sphingolipids
- ceramide
- endothelial
- sirnas
- necrosis
- agonist
- metastasis
- artery
- erk
- phospholipase
- fingolimod
- fibrosis
- lymphocyte
-
protein-coupled
- sphingomyelinase
- tnf
- pulmonary
- leukemia
- sphingomyelin
-
anti-apoptotic
-
s1p-induced
- stat3
- pertussis
- mapks
-
pro-apoptotic
-
mitogen
- sclerosis
- pkc
-
rheostat
-
signal-regulated
- caspase-3
-
pro-survival
-
platelet-derived
- lysophospholipids
-
cardioprotective
- phytosphingosine
- drug development
- lymphopenia
-
egress
- glucosylceramide
- medicine
- fumonisins
-
s1p-mediated
- dihydroceramide
-
mitogenesis
-
pdgf-induced
-
ceramide-induced
-
lysophosphatidic
- fcepsilonri
Reaction
Synonyms
dihydrosphingosine kinase, kinase, dihydrosphingosine (phosphorylating), kinase, sphingosine (phosphorylating), More, SGK, SK, SK-1, SK-2, SK1, SK2, sphinganine kinase, sphingoid base kinase, sphingosine kinase, sphingosine kinase 1, sphingosine kinase 2, sphingosine kinase type 1, sphingosine kinase type 2, sphingosine kinase-1, sphingosine kinase-2, SPHK, SPHK-1, SPHK1, SPHK1a, SPHK1b, SPHK2, SPK
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Subunits
Subunits on EC 2.7.1.91 - sphingosine kinase
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monomer
additional information
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relationship to diacylglyceride kinases, NAD+ kinases and 6-phosphofructokinases
additional information
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structure analysis of the 2 isozymes, schematic map, the enzyme contains 5 sequences stretches C1-C5 typical for lipid kinases, but the enzyme does not contain distinct domains for catalysis or substrate binding, overview
additional information
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isoform Sk1 interacts with four-and-a-half LIM only protein FHL-2. Overexpression of FHL-2 in endothelial cells inhibits VEGF-induced Sk1 activity, phosphatidylinositol 3-kinase activity, and phosphorylation of Akt and eNOS. Overexpression of FHL-2 has no effect on sphinganine 1-phosphate induced Akt phosphorylation. VEGF stimulation decreases the binding of FHL-2 and Sk1. Depletion of FHL-2 by siRNA increases endothelial cell migration accompanied with Sk1 and Akt activation
additional information
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isoform SK1 interacts with subunit 7 of cytosolic chaperonin CCT, i.e. chaperonin containing t-complex polypeptide, also called TRiC for TCP-1 ring complex, a hexadecameric chaperonin that binds unfolded polypeptides. Other CCT/TRiC subunits also associate with SK1 in HEK293T cell lysates in an ATP-sensitive manner. CCT/TRiC binds specifically to newly translated SK1. Depletion of functional CCT/TRiC through the use of RNA interference in HeLa cells or temperature sensitive CCT mutants reduces cellular SK1 activity
additional information
oligomeric protein containing noncooperative catalytic sites, the allosteric site exerts an autoinhibition of the catalytic site
additional information
the SphK1 structure reveals a two-domain architecture in which its catalytic site is located in the cleft between the two domains and a hydrophobic lipid-binding pocket is buried in the C-terminal domain, structure comparisons with Staphylococcus aureus DgkB, PDB ID 2QVL, and Archaeoglobus fulgidus NAD kinase, PDB ID 1ZOZ
additional information
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the SphK1 structure reveals a two-domain architecture in which its catalytic site is located in the cleft between the two domains and a hydrophobic lipid-binding pocket is buried in the C-terminal domain, structure comparisons with Staphylococcus aureus DgkB, PDB ID 2QVL, and Archaeoglobus fulgidus NAD kinase, PDB ID 1ZOZ