Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1-phosphatidyl-1D-myo-inositol
ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol-4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol-4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate
-
strong preference for phosphatidylinositol over 1-phosphatidyl-1D-myo-inositol-4-phosphate
-
-
?
ATP + phosphatidylinositol
?
-
strong preference for phosphatidylinositol over 1-phosphatidyl-1D-myo-inositol-4-phosphate
-
-
?
ATP + phosphatidylinositol
ADP + phosphatidylinositol 3-phosphate
ATP + phosphoinositides
ADP + ?
additional information
?
-
ATP + 1-phosphatidyl-1D-myo-inositol
ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
preferred substrate of enzyme form PI3K-C2beta
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol
ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
preferred substrate of enzyme form PI3K-C2beta
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol-4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol-4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol-4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
at 10% of the activity with phosphatidylinositol, phosphorylation only in presence of Mg2+, not in presence of Ca2+
-
?
ATP + 1-phosphatidyl-1D-myo-inositol-4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol-4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
?
ATP + phosphatidylinositol
ADP + phosphatidylinositol 3-phosphate
-
-
?
ATP + phosphatidylinositol
ADP + phosphatidylinositol 3-phosphate
-
-
-
?
ATP + phosphatidylinositol
ADP + phosphatidylinositol 3-phosphate
-
-
?
ATP + phosphatidylinositol
ADP + phosphatidylinositol 3-phosphate
-
-
-
?
ATP + phosphatidylinositol
ADP + phosphatidylinositol 3-phosphate
-
-
-
?
ATP + phosphatidylinositol
ADP + phosphatidylinositol 3-phosphate
-
-
-
?
ATP + phosphoinositides
ADP + ?
enzyme plays a role in cellular signalling pathways, e.g. the insulin signalling pathways acting via class Ia and PI3K-C2alpha isozymes synthesizing 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate and affecting the glucose metabolism, the enzyme antagonizes with phosphatases both regulating the signalling pathways together, the enzyme is also involved in insulin resistance in peripheral tissues, overview
-
-
?
ATP + phosphoinositides
ADP + ?
phosphorylation of the D-3 position on the inositol ring
-
-
?
ATP + phosphoinositides
ADP + ?
enzyme plays a role in cellular signalling pathways, e.g. the insulin signalling pathways acting via class Ia and PI3K-C2alpha isozymes synthesizing 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate and affecting the glucose metabolism, the enzyme antagonizes with phosphatases both regulating the signalling pathways together, the enzyme is also involved in insulin resistance in peripheral tissues, overview
-
-
?
ATP + phosphoinositides
ADP + ?
phosphorylation of the D-3 position on the inositol ring
-
-
?
ATP + phosphoinositides
ADP + ?
enzyme plays a role in cellular signalling pathways, e.g. the insulin signalling pathways acting via class Ia and PI3K-C2alpha isozymes synthesizing 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate and affecting the glucose metabolism, the enzyme antagonizes with phosphatases both regulating the signalling pathways together, the enzyme is also involved in insulin resistance in peripheral tissues, overview
-
-
?
ATP + phosphoinositides
ADP + ?
phosphorylation of the D-3 position on the inositol ring
-
-
?
additional information
?
-
no activity with phosphatidylinositol 4,5-diphosphate
-
-
?
additional information
?
-
-
the isozymes interact with and effect patterning of receptor signaling pathways, overview
-
-
?
additional information
?
-
-
the class II phosphoinositide 3-kinase C2.alpha. is activated by clathrin and regulates clathrin-mediated membrane trafficking
-
-
?
additional information
?
-
-
PI3K-C2alpha and PI3K-C2beta represent two downstream targets of the activated epidermal growth factor
-
-
?
additional information
?
-
enzyme regulation, overview
-
-
?
additional information
?
-
isozyme PI3K-C2alpha is a crucial survival factor for the cell
-
-
?
additional information
?
-
-
the isozymes activate different signalling cascades via stem cell factor SCF in overexpressing cancer cell lines, e.g. association with c-Met, IGF-IR, regulation, class II PI3K C2beta blocks both protein kinase and small lung cell carcinoma in reponse to stem cell factor, polypeptide growth factors induce the recruitment of class IA and II isozymes to phosphotyrosine-containing signalling complexes, detailed overview
-
-
?
additional information
?
-
PI3KC2alpha functions in vascular smooth muscle contraction, priming of neurosecretory granule exocytosis, insulin signalling and clathrin-mediated membrane trafficking.
-
-
?
additional information
?
-
PI3KC2alpha functions in vascular smooth muscle contraction, priming of neurosecretory granule exocytosis, insulin signalling and clathrin-mediated membrane trafficking.
-
-
?
additional information
?
-
PI3KC2alpha functions in vascular smooth muscle contraction, priming of neurosecretory granule exocytosis, insulin signalling and clathrin-mediated membrane trafficking.
-
-
?
additional information
?
-
PI3KC2beta functions in cell migration, and PTK receptor signalling
-
-
?
additional information
?
-
PI3KC2beta functions in cell migration, and PTK receptor signalling
-
-
?
additional information
?
-
PI3KC2beta functions in cell migration, and PTK receptor signalling
-
-
?
additional information
?
-
-
PI3KC2beta regulates the migration and survival of human tumor cells by distinct molecular mechanisms. Phosphoinositide 3-kinase C2beta regulates cytoskeletal organization and cell migration via Rac-dependent mechanisms
-
-
?
additional information
?
-
ATP and substrate binding of PI3K isozymes, overview
-
-
-
additional information
?
-
ATP and substrate binding of PI3K isozymes, overview
-
-
-
additional information
?
-
ATP and substrate binding of PI3K isozymes, overview
-
-
-
additional information
?
-
-
PI3K-C2alpha and PI3K-C2beta represent two downstream targets of the activated epidermal growth factor
-
-
?
additional information
?
-
-
the class II phosphoinositide 3-kinase C2.alpha. is activated by clathrin and regulates clathrin-mediated membrane trafficking
-
-
?
additional information
?
-
enzyme regulation, overview
-
-
?
additional information
?
-
-
TNFalpha and leptin stimulate the alpha-isoform of class II phosphoinositide 3-kinase
-
-
?
additional information
?
-
enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme is regulated by intracellular signalling mechanisms
-
-
?
additional information
?
-
ATP and substrate binding of PI3K isozymes, overview
-
-
-
additional information
?
-
ATP and substrate binding of PI3K isozymes, overview
-
-
-
additional information
?
-
ATP and substrate binding of PI3K isozymes, overview
-
-
-
additional information
?
-
no activity with phosphatidylinositol 4,5-diphosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
ATP + phosphoinositides
ADP + ?
additional information
?
-
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
-
-
?
ATP + phosphoinositides
ADP + ?
enzyme plays a role in cellular signalling pathways, e.g. the insulin signalling pathways acting via class Ia and PI3K-C2alpha isozymes synthesizing 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate and affecting the glucose metabolism, the enzyme antagonizes with phosphatases both regulating the signalling pathways together, the enzyme is also involved in insulin resistance in peripheral tissues, overview
-
-
?
ATP + phosphoinositides
ADP + ?
enzyme plays a role in cellular signalling pathways, e.g. the insulin signalling pathways acting via class Ia and PI3K-C2alpha isozymes synthesizing 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate and affecting the glucose metabolism, the enzyme antagonizes with phosphatases both regulating the signalling pathways together, the enzyme is also involved in insulin resistance in peripheral tissues, overview
-
-
?
ATP + phosphoinositides
ADP + ?
enzyme plays a role in cellular signalling pathways, e.g. the insulin signalling pathways acting via class Ia and PI3K-C2alpha isozymes synthesizing 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate and affecting the glucose metabolism, the enzyme antagonizes with phosphatases both regulating the signalling pathways together, the enzyme is also involved in insulin resistance in peripheral tissues, overview
-
-
?
additional information
?
-
-
the isozymes interact with and effect patterning of receptor signaling pathways, overview
-
-
?
additional information
?
-
-
the class II phosphoinositide 3-kinase C2.alpha. is activated by clathrin and regulates clathrin-mediated membrane trafficking
-
-
?
additional information
?
-
-
PI3K-C2alpha and PI3K-C2beta represent two downstream targets of the activated epidermal growth factor
-
-
?
additional information
?
-
enzyme regulation, overview
-
-
?
additional information
?
-
isozyme PI3K-C2alpha is a crucial survival factor for the cell
-
-
?
additional information
?
-
-
the isozymes activate different signalling cascades via stem cell factor SCF in overexpressing cancer cell lines, e.g. association with c-Met, IGF-IR, regulation, class II PI3K C2beta blocks both protein kinase and small lung cell carcinoma in reponse to stem cell factor, polypeptide growth factors induce the recruitment of class IA and II isozymes to phosphotyrosine-containing signalling complexes, detailed overview
-
-
?
additional information
?
-
PI3KC2alpha functions in vascular smooth muscle contraction, priming of neurosecretory granule exocytosis, insulin signalling and clathrin-mediated membrane trafficking.
-
-
?
additional information
?
-
PI3KC2alpha functions in vascular smooth muscle contraction, priming of neurosecretory granule exocytosis, insulin signalling and clathrin-mediated membrane trafficking.
-
-
?
additional information
?
-
PI3KC2alpha functions in vascular smooth muscle contraction, priming of neurosecretory granule exocytosis, insulin signalling and clathrin-mediated membrane trafficking.
-
-
?
additional information
?
-
PI3KC2beta functions in cell migration, and PTK receptor signalling
-
-
?
additional information
?
-
PI3KC2beta functions in cell migration, and PTK receptor signalling
-
-
?
additional information
?
-
PI3KC2beta functions in cell migration, and PTK receptor signalling
-
-
?
additional information
?
-
-
PI3KC2beta regulates the migration and survival of human tumor cells by distinct molecular mechanisms. Phosphoinositide 3-kinase C2beta regulates cytoskeletal organization and cell migration via Rac-dependent mechanisms
-
-
?
additional information
?
-
-
PI3K-C2alpha and PI3K-C2beta represent two downstream targets of the activated epidermal growth factor
-
-
?
additional information
?
-
-
the class II phosphoinositide 3-kinase C2.alpha. is activated by clathrin and regulates clathrin-mediated membrane trafficking
-
-
?
additional information
?
-
enzyme regulation, overview
-
-
?
additional information
?
-
-
TNFalpha and leptin stimulate the alpha-isoform of class II phosphoinositide 3-kinase
-
-
?
additional information
?
-
enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme is regulated by intracellular signalling mechanisms
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide
(5Z)-5-[[5-(4-fluoro-2-hydroxyphenyl)furan-2-yl]methylidene]-1,3-thiazolidine-2,4-dione
1,2-bis-(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid
-
i.e. BAPTA-AM, a cell-penetrating Ca2+-chelator
2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid
2-amino-N-[(1S)-1-[8-[(1-methyl-1H-pyrazol-4-yl)ethynyl]-1-oxo-2-phenyl-1,2-dihydroisoquinolin-3-yl]ethyl]pyrazolo[1,5-a]pyrimidine-3-carboxamide
2-methyl-1-[[2-methyl-3-(trifluoromethyl)phenyl]methyl]-6-(morpholin-4-yl)-1H-benzimidazole-4-carboxylic acid
3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide
3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol
4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one
5-[2,6-bis(morpholin-4-yl)pyrimidin-4-yl]-4-(trifluoromethyl)pyridin-2-amine
6-[5-(2,2-dimethylpropane-1-sulfonyl)pyridin-3-yl]-8-fluoro[1,2,4]triazolo[1,5-a]pyridin-2-amine
8-[(1R)-1-(3,5-difluoroanilino)ethyl]-N,N-dimethyl-2-(morpholin-4-yl)-4-oxo-4H-1-benzopyran-6-carboxamide
calpeptin
-
inhibits proteolytic activation of enzyme form PI3K C2beta in brush border plasma membranes
Isoflurane
ISO, inhibits KCl-stimulated PI3K-C2alpha membrane translocation
Mn2+
3.5 mM, instead of Mg2+, almost complete inhibition
N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide
N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide
N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide
N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide
Nonidet P-40
0.5%, almost complete inhibition
sevoflurane
SEVO, inhibits KCl-stimulated PI3K-C2alpha membrane translocation
-
Triton X-100
0.5%, almost complete inhibition
[6-(2-amino-1,3-benzoxazol-5-yl)imidazo[1,2-a]pyridin-3-yl](morpholin-4-yl)methanone
(2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide
-
(2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide
-
(5Z)-5-[[5-(4-fluoro-2-hydroxyphenyl)furan-2-yl]methylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[[5-(4-fluoro-2-hydroxyphenyl)furan-2-yl]methylidene]-1,3-thiazolidine-2,4-dione
-
2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid
-
2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid
-
2-amino-N-[(1S)-1-[8-[(1-methyl-1H-pyrazol-4-yl)ethynyl]-1-oxo-2-phenyl-1,2-dihydroisoquinolin-3-yl]ethyl]pyrazolo[1,5-a]pyrimidine-3-carboxamide
-
2-amino-N-[(1S)-1-[8-[(1-methyl-1H-pyrazol-4-yl)ethynyl]-1-oxo-2-phenyl-1,2-dihydroisoquinolin-3-yl]ethyl]pyrazolo[1,5-a]pyrimidine-3-carboxamide
-
2-methyl-1-[[2-methyl-3-(trifluoromethyl)phenyl]methyl]-6-(morpholin-4-yl)-1H-benzimidazole-4-carboxylic acid
-
2-methyl-1-[[2-methyl-3-(trifluoromethyl)phenyl]methyl]-6-(morpholin-4-yl)-1H-benzimidazole-4-carboxylic acid
-
3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide
-
3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide
-
3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol
-
3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol
-
4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one
-
4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one
-
5-[2,6-bis(morpholin-4-yl)pyrimidin-4-yl]-4-(trifluoromethyl)pyridin-2-amine
-
5-[2,6-bis(morpholin-4-yl)pyrimidin-4-yl]-4-(trifluoromethyl)pyridin-2-amine
-
6-[5-(2,2-dimethylpropane-1-sulfonyl)pyridin-3-yl]-8-fluoro[1,2,4]triazolo[1,5-a]pyridin-2-amine
-
6-[5-(2,2-dimethylpropane-1-sulfonyl)pyridin-3-yl]-8-fluoro[1,2,4]triazolo[1,5-a]pyridin-2-amine
-
8-[(1R)-1-(3,5-difluoroanilino)ethyl]-N,N-dimethyl-2-(morpholin-4-yl)-4-oxo-4H-1-benzopyran-6-carboxamide
-
8-[(1R)-1-(3,5-difluoroanilino)ethyl]-N,N-dimethyl-2-(morpholin-4-yl)-4-oxo-4H-1-benzopyran-6-carboxamide
-
adipokines
block insulin signalling via PI3K isozymes
-
adipokines
block insulin signalling via PI3K isozymes
-
Caffeine
might inhibit the enzyme
Caffeine
might inhibit the enzyme
ceramide
selective inhibition of PI3KC2beta
ceramide
selective inhibition of PI3KC2beta
cytokines
block insulin signalling via PI3K isozymes
-
cytokines
block insulin signalling via PI3K isozymes
-
dactolisib
-
duvelisib
-
GDC-0941
-
LY294002
-
IC50: 0.019 mM, maximal inhibition at 1 mM
LY294002
a PI3K inhibitor, inhibits KCl-elicited rapid and sustained contraction of rat aortic smooth muscle
N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide
-
N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide
-
N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide
-
N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide
-
N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide
-
N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide
-
N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide
-
N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide
-
naringenin
might inhibit the enzyme
naringenin
might inhibit the enzyme
Wortmannin
IC50: 11 nM
Wortmannin
-
IC50: 420 nM, maximal inhibition at 10 mM
Wortmannin
class I isozyme inhibitor, isozyme PI3K-C2alpha is resistant to inhibition
Wortmannin
low inhibition
Wortmannin
class I isozyme inhibitor, isozyme PI3K-C2alpha is resistant to inhibition
Wortmannin
low inhibition
Wortmannin
-
phosphoinositide 3-kinase C2beta
Wortmannin
-
a pan-PI3K inhibitor
ZSTK474
-
[6-(2-amino-1,3-benzoxazol-5-yl)imidazo[1,2-a]pyridin-3-yl](morpholin-4-yl)methanone
-
[6-(2-amino-1,3-benzoxazol-5-yl)imidazo[1,2-a]pyridin-3-yl](morpholin-4-yl)methanone
-
additional information
-
introduction of phosphatidylserine, produces an 8fold decrease in Vmax for ATP using phosphatidylinositol. Without phosphatidylserine, phosphatidylinositol 4-phosphate produces non-linear enzyme kinetics
-
additional information
enzyme is regulated by several feedback inhibition possibilities in the insulin signalling pathway, overview
-
additional information
no or poor inhibition by buparlisib, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, and N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide; no or poor inhibition by GDC-0941, (2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide, 2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid, idelalisib, N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide, N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide, 4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one, dactolisib, ZSTK474, AZD 3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide; no or poor inhibition by NVP-BYL719/buparlisib, 5-fluoro-3-phenyl-2-[(1S)-1-[(9H-purin-6-yl)amino]propyl]quinazolin-4(3H)-one, 3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, 3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
additional information
no or poor inhibition by buparlisib, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, and N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide; no or poor inhibition by GDC-0941, (2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide, 2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid, idelalisib, N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide, N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide, 4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one, dactolisib, ZSTK474, AZD 3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide; no or poor inhibition by NVP-BYL719/buparlisib, 5-fluoro-3-phenyl-2-[(1S)-1-[(9H-purin-6-yl)amino]propyl]quinazolin-4(3H)-one, 3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, 3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
additional information
no or poor inhibition by buparlisib, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, and N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide; no or poor inhibition by GDC-0941, (2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide, 2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid, idelalisib, N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide, N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide, 4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one, dactolisib, ZSTK474, AZD 3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide; no or poor inhibition by NVP-BYL719/buparlisib, 5-fluoro-3-phenyl-2-[(1S)-1-[(9H-purin-6-yl)amino]propyl]quinazolin-4(3H)-one, 3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, 3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
additional information
enzyme is regulated by several feedback inhibition possibilities in the insulin signalling pathway, overview
-
additional information
no or poor inhibition by buparlisib, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, and N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide; no or poor inhibition by buparlisib, idelalisib, 3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, 3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide, N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide; no or poor inhibition by GDC-0941, (2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide, 2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid, idelalisib, N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide, N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide, 4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one, dactolisib, ZSTK474, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
additional information
no or poor inhibition by buparlisib, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, and N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide; no or poor inhibition by buparlisib, idelalisib, 3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, 3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide, N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide; no or poor inhibition by GDC-0941, (2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide, 2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid, idelalisib, N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide, N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide, 4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one, dactolisib, ZSTK474, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
additional information
no or poor inhibition by buparlisib, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, and N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide; no or poor inhibition by buparlisib, idelalisib, 3-[4-(morpholin-4-yl)pyrido[3',2':4,5]furo[3,2-d]pyrimidin-2-yl]phenol, (8S)-2-[(3R)-3-methylmorpholin-4-yl]-9-(3-methyl-2-oxobutyl)-8-(trifluoromethyl)-6,7,8,9-tetrahydro-4H-pyrimido[1,2-a]pyrimidin-4-one, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, 3-amino-N-[3-(3,5-dimethoxyanilino)pyrazin-2-yl]benzene-1-sulfonamide, N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide; no or poor inhibition by GDC-0941, (2S)-N1-[4-methyl-5-[3-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl]pyrrolidine-1,2-dicarboxamide, 2-([(1R)-1-[7-methyl-2-(morpholin-4-yl)-4-oxo-4H-pyrido[1,2-a]pyrimidin-9-yl]ethyl]amino)benzoic acid, idelalisib, N-(7,8-dimethoxy-2,3-dihydroimidazo[1,2-c]quinazolin-5-yl)pyridine-3-carboxamide, N-(5-[4-chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl]-4-methyl-1,3-thiazol-2-yl)acetamide, 4-[(3-chloro-4-fluorophenyl)methyl]-6-[(Z)-(4-oxo-2-sulfanylidene-1,3-thiazolidin-5-ylidene)methyl]-2H-1,4-benzoxazin-3(4H)-one, dactolisib, ZSTK474, AZD3147, 5-[4-[(methanesulfonyl)methyl]-6-(morpholin-4-yl)pyrimidin-2-yl]-1H-indole, gedatolisib, 4'-(cyclopropylmethyl)-N2-(pyridin-4-yl)[4,5'-bipyrimidine]-2,2'-diamine, 1-([2-[(2-chloropyridin-4-yl)amino]-4'-(cyclopropylmethyl)[4,5'-bipyrimidin]-2'-yl]amino)-2-methylpropan-2-ol, SAR405, (2S)-2-amino-1-(4-[4-[2-(difluoromethyl)-1H-benzimidazol-1-yl]-6-(morpholin-4-yl)-1,3,5-triazin-2-yl]piperazin-1-yl)-3-phenylpropan-1-one, N-[4-(morpholin-4-yl)-2-[3-[(naphthalene-2-sulfonyl)amino]phenyl]quinazolin-6-yl]acetamide, N-[2-[3-[(benzenesulfonyl)amino]phenyl]-4-(morpholin-4-yl)quinazolin-6-yl]acetamide, N-(3-[[3-(2-chloro-5-methoxyanilino)quinoxalin-2-yl]sulfamoyl]phenyl)-2-methylalaninamide, N-[3-(3,5-dimethoxyanilino)quinoxalin-2-yl]-4-fluorobenzene-1-sulfonamide, and N-[3-(2-chloro-5-hydroxyanilino)pyrazin-2-yl]benzenesulfonamide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
adipocyte
brenda
-
moderate expression of PI3K-C2alpha andPI3K-C2beta
brenda
-
brenda
-
moderate expression of PI3K-C2alpha
brenda
-
brenda
-
-
brenda
-
brenda
isozyme PI3K-C2beta is overexpressed in human breast cancer cell lines
brenda
-
low amount of isozyme p85, isozyme PI3K-C2beta and isozyme PI3K-C2alpha in bronchial epithelium
brenda
-
moderate expression of PI3K-C2alpha and PI3K-C2beta
brenda
-
of Fallopian tube, moderate expression of PI3K-C2alpha and weak expression of PI3K-C2beta
brenda
-
-
brenda
-
PI3K-C2alpha
brenda
-
moderate expression of PI3K-C2alpha and weak expression of PI3K-C2beta
brenda
high expression level of PI3KC2beta
brenda
-
isozyme PI3K-C2alpha, high amount of isozyme p85, and low amount of isozyme PI3K-C2beta
brenda
-
isozyme PI3K-C2alpha in smooth muscle layer, mononuclear cells, and lining epithelium, isozyme p85 and isozyme PI3K-C2beta in lining epithelium and mononuclear cells
brenda
-
strong expression of PI3K-C2alpha
brenda
-
brenda
-
brenda
-
-
brenda
-
strong expression of PI3K-C2alpha and moderate expression of PI3K-C2beta
brenda
-
isozyme p85, isozyme PI3K-C2beta and isozyme PI3K-C2alpha in alveolar macrophages
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
moderate expression of PI3K-C2alpha
brenda
-
non-myelinated, moderate expression of PI3K-C2beta
brenda
-
-
brenda
-
-
brenda
-
brenda
-
moderate expression of PI3K-C2alpha and PI3K-C2beta
brenda
expression at low level
brenda
-
brenda
-
brenda
-
isozyme PI3K-C2alpha inbasal epithelium and fibromuscular stroma, no isozyme PI3K-C2beta and isozyme p85
brenda
-
-
brenda
-
-
brenda
expression at low level
brenda
-
isozyme p85 in Langerhans cells, dermal macrophages, and in low amounts in sebaceous glands, hair follicles, and sweat gland, isozyme PI3K-C2beta and isozyme PI3K-C2alpha in dermal macrophages, low amount of isozyme PI3K-C2alpha in sweat gland
brenda
-
different cell lines overexpress different isozymes, e.g. cell lines H-69, HC-33, H-510, H-1045, and H-209
brenda
-
strong expression of PI3K-C2beta
brenda
-
brenda
-
isozyme PI3K-C2beta and isozyme PI3K-C2alpha, and high amount of isozyme p85 in peptic cells
brenda
-
brenda
-
isozyme PI3K-C2alpha in cervical smooth muscle, no isozyme PI3K-C2beta and isozyme p85
brenda
-
isozyme p85 in proliferative endometrium and in low amounts in secretory endometrium, isozyme PI3K-C2alpha in myometrium, no isozyme PI3K-C2beta
brenda
-
-
brenda
-
carcinoma-derived cell
brenda
-
carcinoma-derived cell
-
brenda
-
brenda
-
brenda
-
low amount of isozyme PI3K-C2alpha in myoepithelial cells and lactiferous ducts, no isozyme PI3K-C2beta and isozyme p85
brenda
PI3KC2gamma
brenda
non-neoplastic breast tissues
brenda
-
brenda
-
isozyme p85, isozyme PI3K-C2beta and isozyme PI3K-C2alpha in colonocytes
brenda
-
-
brenda
-
brenda
-
glomerular, PI3K-C2alpha
brenda
-
strong expression of PI3K-C2beta
brenda
-
high amounts of isozyme p85 and isozyme PI3K-C2beta
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
macrophage
brenda
expression at low level
brenda
-
mRNA is undetectable in kidney
brenda
-
isozyme p85 in glomerular macrophages, macula densa, and collecting tubules, high amount of isozyme PI3K-C2alpha in glomerular tuft, low amount of isozyme PI3K-C2beta and isozyme PI3K-C2alpha in proximal, distal, and collecting tubules
brenda
-
mRNA is undetectable in kidney
-
brenda
-
-
brenda
-
isozyme PI3K-C2alpha in bile ducts, no isozyme PI3K-C2beta and isozyme p85
brenda
PI3KC2gamma
brenda
exclusively expressed in liver
brenda
PI3K-IIgamma mRNA expression is confined to the liver throughout the development with much higher expression in adult liver than in fetal liver. Expression increases during liver regeneration after partial hepatectomy. PI3K-gamma may function mainly in highly differentiated hepatic cells
brenda
-
in the nuclear matrix harvested 20 h after partial hepatectomy, an increase in immunoprecipitable PI3K-C2beta activity is observed
brenda
-
brenda
-
weak expression of PI3K-C2alpha and PI3K-C2beta in germinal centre mononuclear cells, moderate expression of PI3K-C2alpha and PI3K-C2beta in tissue macrophages, strong expression of PI3K-C2alpha in polymorphonuclear leucocytes, weak expression of PI3K-C2alpha and moderate expression of PI3K-C2beta in medulla mononuclear cells, no expression in lymphoid follicles
brenda
-
isozyme p85 in medulla, germinal centre mononuclear cells, low amount in polymorphnuclear leucocytes, and high amount in tissue macrophages, isozyme PI3K-C2alpha and isozyme PI3K-C2beta in medulla, tissue macrophages, and germinal centre mononuclear cells, high amount of isozyme PI3K-C2alpha in polymorphnuclear leucocytes
brenda
PI3K-C2beta is highly expressed in lymph-nodes metastases compared to matching primary tumors
brenda
-
dermal, moderate expression of PI3K-C2alpha and PI3K-C2beta
brenda
-
glomerular, moderate expression of PI3K-C2beta
brenda
-
PI3K-C2alpha and PI3K-C2beta
brenda
-
isozyme PI3K-C2beta
brenda
-
cell culture
brenda
-
cell culture, cell line J774.2
brenda
-
-
brenda
-
brenda
-
moderate expression of PI3K-C2alpha and strong expression of PI3K-C2beta
brenda
-
all isozymes
brenda
-
brenda
PI3K class IIbeta (PI3KC2beta) and its regulator intersectin 1 (ITSN1) are highly expressed in primary neuroblastoma tumors and cell lines
brenda
-
-
brenda
-
isozyme p85, low amount of isozyme PI3K-C2beta and isozyme PI3K-C2alpha in follicular cells
brenda
-
-
-
brenda
-
brenda
-
moderate expression of PI3K-C2alpha and PI3K-C2beta
brenda
low enzyme expression
brenda
-
high amount of isozyme p85 in acini, isozyme PI3K-C2alpha in acini and ducts, no isozyme PI3K-C2beta
brenda
-
-
brenda
highest expression in thymus and placenta
brenda
-
-
-
brenda
-
fibromuscular stroma, moderate expression of PI3K-C2alpha
brenda
PI3KC2gamma
brenda
-
moderate expression of PI3K-C2alpha and weak expression of PI3K-C2beta
brenda
-
isozyme PI3K-C2alpha, high amount of isozyme p85, and low amount of isozyme PI3K-C2beta in enterocytes, isozyme p85 in Paneth cells
brenda
-
bronchial and cervical, moderate expression of PI3K-C2alpha
brenda
-
isozyme PI3K-C2alpha
brenda
-
strong expression of PI3K-C2alpha in red pulp splenic sinusoids, weak expression of PI3K-C2alpha and moderate expression of PI3K-C2beta in red pulp mononuclear cells, no expression in white pulp
brenda
-
isozyme p85, isozyme PI3K-C2beta and isozyme PI3K-C2alpha in red pulp
brenda
-
-
brenda
-
high content of isozyme p85 and isozyme PI3K-C2beta in spermatogenic cells, high content of isozyme PI3K-C2alpha in Leydig cells, isozyme p85 and PI3K-C2beta in Leydig cells
brenda
-
-
-
brenda
-
monocyte
brenda
-
monocyte
-
brenda
highest expression in thymus and placenta
brenda
high activity of PI3KC2beta
brenda
-
-
brenda
-
monocyte
brenda
monocyte
brenda
-
monocyte
-
brenda
-
brenda
HUVEC
brenda
-
moderate expression of PI3K-C2alpha and weak expression of PI3K-C2beta
brenda
-
isozyme PI3K-C2alpha in muscularis and transitional epithelium, isozyme p85 and isozyme PI3K-C2beta in transitional epithelium
brenda
additional information
-
isozyme expression pattern and phenotype, Drk adaptor protein might be involved in localization of the isozymes, overview
brenda
additional information
-
immunohistological analysis, no expression of isozymes in endocrine pancreas, thyroid, or parathyroid, topographical expression of class IA and class II isozymes in normal human tissues is consistent with a role in differentiation
brenda
additional information
widely expressed, but not ubiquitous
brenda
additional information
widely expressed, but not ubiquitous
brenda
additional information
widely expressed, but not ubiquitous
brenda
additional information
PI3KC2alpha is broadly expressed in human cells
brenda
additional information
PI3KC2alpha is broadly expressed in human cells
brenda
additional information
PI3KC2alpha is broadly expressed in human cells
brenda
additional information
isozyme PI3KC2alpha is widely expressed in mammalian cells
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
three enzymes belong to the class II subfamily, PI3K-C2alpha, beta, and gamma
evolution
PI3K enzyme sequence comparisons
malfunction
agonist-induced 3-phosphorylated phosphoinositide production and cellular activation are normal in PI3KC2alpha-deficient platelets. PI3KC2alpha deficiency exacerbates bleeding and impairs thrombosis. Phenotype of Pik3c2alpha-/- mice. PI3KC2alpha deficiency alters platelet and megakaryocyte internal membrane structures, overview. PI3KC2alpha deficiency causes unstable platelet thrombi and enhances shear-dependent platelet adhesion
malfunction
downregulation of PI3K-C2beta in breast cancer cell lines reduces colony formation, induces cell cycle arrest and inhibits tumor growth, in particular in an estrogen-dependent in vivo xenograft. PI3K-C2beta inhibits breast cancer cell invasion in vitro and breast cancer metastasis in vivo
malfunction
inhibition of MEK/ERK activation as well as downregulation of PI3K-C2beta does not affect cell proliferation while specifically inhibiting cell invasion
malfunction
-
PI3K-C2alpha knockdown decreases the FceRI-triggered release of a lysosomal enzyme, namely beta-hexosaminidase, protein levels of PI3K-C2beta are not significantly affected by the shRNAs. siRNA against PI3K-C2beta impairs the FceRI-induced increase in intracellular Ca2+ and degranulation. Release of NPY-mRFP, a reporter of the regulated exocytosis of mast cells is increased by PI3K-C2alpha overexpression and is impaired in the PI3K-C2alpha-deficient cells
malfunction
PI3KC2beta-silencing inhibits early stages of neuroblastoma tumorigenic growth, but does not alter apoptotic or endocytic pathways, and silencing of the enzyme's regulator intersectin 1, ITSN1, also dramatically reduces the tumorigenic potential of neuroblastoma cells. Overexpression of PI3KC2beta rescues the anchorage-independent growth of ITSN1-silenced cells suggesting that PI3KC2beta mediates ITSN1's function in neuroblastoma cells. Silencing ITSN1 or PI3KC2beta decreases AKT activation in neuroblastoma cells
malfunction
TGFbeta1 stimulated nuclear accumulation of p-Smad2 is markedly suppressed by PI3K-C2alpha knockdown. Effect of PI3K-C2alpha knockdown on the co-localization of TGFbeta1 receptors and SARA. PI3K-C2alpha knockdown does not affect the numbers of either SARA-positive or EEA1-positive vesicles in nonstimulated cells but abolished TGFbeta1-induced increase in SARA- and EEA1-double positive early endosomes
malfunction
different deficiency types of PI3KC2alpha can cause different phenotypes, including stunted growth, decreased survival, renal abnormalities, embryonic lethality, decreased retinal angiogenesis, impaired revascularization following ischemic injury, and impaired platelet function during thrombosis. Mouse models of PI3KC2alpha deficiency. While homozygosity for kinase-dead PI3KC2alpha is embryonic lethal, heterozygous PI3KC2alpha KI mice are viable and fertile, with no significant histopathological findings. Male heterozygous mice show early onset leptin resistance, with a defect in leptin signaling in the hypothalamus, correlating with a mild, age-dependent obesity, insulin resistance, and glucose intolerance
malfunction
downregulation of PI3KC2beta results the inhibition of early stage neuroblastoma formation. Serum-dependent lamellipodia formation has been significantly reduced in cells lacking PI3KC2beta. Selective inhibition of PI3KC2beta with ceramide has been shown to diminish PI3KC2beta-dependent lamellipodia formation, reducing ovarian cancer cell mobility. Blocking of PI3KC2? pathway results in the impairment of SKOV3 cell migration. Depletion of PI3KC2beta can increase resistance of cells to chemotherapeutics
malfunction
effects of LY294002, sevoflurane (SEVO) and isoflurane (ISO) on KCl-elicited PI3KC2alpha mediated vasoconstriction in rat aortic smooth muscle, overview. PI3K inhibitor LY294002 inhibits PI3K-C2alpha membrane translocation in response to KCl. SEVO and ISO inhibit KCl-stimulated MLC phosphorylation, PI3K-C2alpha and Rock-II, but not PI3K p85, membrane translocation in a concentration-dependent manner in rat aorta
malfunction
global deficiency of PI3KC2gamma causes a phenotype of hyperlipidemia, adiposity, and insulin resistance
malfunction
heterozygous kinase-dead inactivating mutation of PI3KC2gamma causes a phenotype of decreased circulating insulin levels, increased glucose tolerance, and protection against steatosis. Inhibition of PI3KC2beta significantly reduced ovarian cancer metastasis in mice
malfunction
ITSN1 knockdown dramatically reduces the localization of PI3K-C2beta at actin patches and at clathrin-coated structures
malfunction
knockdown of PI3K-C2alpha inhibits internalization of cell surface molecules
malfunction
PI3KC2alpha mRNA is downregulated in islets from type 2 diabetic patients compared to nondiabetic individuals. PI3KC2alpha plays a sex-dependent role in the modulation of hypothalamic leptin action and systemic glucose homeostasis
malfunction
PI3KCb and PI3KC2a mRNA levels re significantly lower in insulin + wortmannin group than those in single insulin group
metabolism
-
involvement of PI3K-C2alpha in the antigen-induced degranulation pathway
metabolism
insulin treatment shows no significant effect on GDH activity and mRNA expression of PI3KCa, PI3KCd, PI3KCg, PI3KC2b, PI3KC3 and eEF2 both in the in vivo and in vitro studies. Among seven PI3K members, PI3KCb and PI3KC2a are more sensitive to the insulin signaling pathway, and insulin stimulates hepatic protein synthesis in yellow catfish through PI3K signaling pathway
metabolism
knockdown studies of endogenous PI3K isoforms and clathrin heavy chain (CHC) mediated by small interfering RNA (siRNA) demonstrate that the class II PI3K PI3K-C2alpha and PI3K-C2beta, but not the class I or III PI3K, are required for pinocytosis, based on an evaluation of fluorescein-5-isothiocyanate (FITC)-dextran uptake in endothelial cells. Pinocytosis is partially dependent on both clathrin and dynamin, and both PI3K-C2alpha and PI3K-C2beta are required for clathrin-mediated, but not clathrin-nonmediated, FITC-dextran uptake at the step leading up to its delivery to early endosomes. PI3K-C2alpha and PI3K-C2beta play differential, indispensable roles in clathrin-mediated pinocytosis
physiological function
class II phosphoinositide 3-kinase C2beta regulates a novel signaling pathway involved in breast cancer progression. Isozyme PI3K-C2beta regulates breast cancer cell growth in vitro and in vivo, PI3K-C2beta expression in breast tissues is correlated with the proliferative status of the tumor. Analsis of the mechanism of the PI3K-C2beta-dependent regulation of cell cycle progression and cell growth revealed that PI3K-C2beta regulates cyclin B1 protein levels through modulation of microRNA miR-449a levels. PI3K-C2beta may represent a key molecular switch that regulates a rate-limiting step in breast tumor progression and therefore it may be targeted to limit breast cancer spread. PI3K-C2beta regulates cyclin B1 expression through modulation of miR-449a, miR-449a levels are downregulated in primary human breast cancer samples, and cyclin B1/miR-449a expression through modulation of LEF1/beta catenin pathway in MDA-MB-231 cells. PI3K-C2beta regulates senescence via miR-449 regulation
physiological function
isozyme phosphatidylinositol 3-kinase class II alpha is required for transforming growth factor beta-induced Smad signaling in endothelial cells, but not in smooth muscle cells or epithelial cells. TGFbeta1-induced phosphorylation and nuclear translocation of Smad2/3 are dependent on class II PI3K-C2alpha. C2alpha is required for SARA-Smad2/3 complex formation
physiological function
isozyme PI3K-C2beta regulates mitogen-activated protein kinase kinase (MEK1/2) and extracellular signal-regulated kinase (ERK1/2) activation in prostate cancer (PCa) cells. MEK/ERK and isozyme PI3K-C2beta are required for PCa cell invasion but not proliferation. MEK/ERK and PI3K-C2beta are not required for PCa cell proliferation. PI3K-C2beta but not MEK/ERK regulates PCa cell migration as well as expression of the transcription factor Slug. PI3K-C2beta regulates FBS-induced PCa cell migration in a mechanism that does not appear to involve MEK/ERK activation
physiological function
phosphatidylinositol 3-kinase class 2 beta isoform, PI3KC2beta, contributes to neuroblastoma tumorigenesis. Activation of the PI3K target AKT is frequent in neuroblastoma and correlates with poor prognosis
physiological function
-
PI3K-C2beta regulates the FceRI-stimulated activation of the KCa3.1 channel and the FceRI-induced Ca2+ influx and degranulation in BMMCs. PI3K-C2alpha regulates the FceRI-triggered degranulation by a mechanism different from that induced by PI3K-C2beta. PI3KC2alpha and PI3K-C2beta share different roles in the FceRI-regulated degranulation pathway
physiological function
PI3KC2alpha is important for mouse platelet function in vivo and plays an important role in regulating endothelial cell barrier function and vasculogenesis. Role for PI3KC2alpha in regulating the internal membrane reserve structure of megakaryocytes (demarcation membrane system) and platelets (open canalicular system) that results in dysregulated platelet adhesion under haemodynamic shear stress. Important role for PI3KC2alpha in regulating shear-dependent platelet adhesion via regulation of membrane structure, rather than acute signalling
physiological function
class II phosphoinositide 3-kinase alpha-isoform (PI3K-C2alpha) is involved in regulating KCl-induced vascular smooth muscle contraction. PI3K-C2alpha mediates part of sevoflurane (SEVO)- and isoflurane (ISO)-mediated vasodilation in rat aorta
physiological function
class II phosphoinositide 3-kinases PI3K-C2alpha and PI3K-C2beta differentially regulate clathrin-dependent pinocytosis in human vascular endothelial cells. Pinocytosis is partially dependent on both clathrin and dynamin, and both PI3K-C2alpha and PI3K-C2beta are required for clathrin-mediated, but not clathrin-nonmediated, FITC-dextran uptake at the step leading up to its delivery to early endosomes. PI3K-C2alpha and PI3K-C2beta play differential, indispensable roles in clathrin-mediated pinocytosis
physiological function
class II phosphoinositide 3-kinases PI3K-C2alpha and PI3K-C2beta differentially regulate clathrin-dependent pinocytosis in human vascular endothelial cells. Pinocytosis is partially dependent on both clathrin and dynamin, and both PI3K-C2alpha and PI3K-C2beta are required for clathrin-mediated, but not clathrin-nonmediated, FITC-dextran uptake at the step leading up to its delivery to early endosomes. PI3K-C2alpha and PI3K-C2beta play differential, indispensable roles in clathrin-mediated pinocytosis. Endogenous ITSN1 is required for the formation of actin patches and recruitment of PI3K-C2beta to the clathrin-coated structures. mCherry-C2beta overexpression stimulates pinocytosis through the mechanisms involving GFP-ITSN1-mediated recruitment of mCherry-C2beta
physiological function
importance of PI3KC2beta in ovarian cancer cell migration
physiological function
PI3KC2alpha has a role in glucose transport and secretion. Possible role of PI3KC2alpha in carcinogenesis, possible involvement of PI3KC2alpha in breast cancer development, and potential involvement of PI3KC2alpha in tumor angiogenesis favoring lung cancer and melanoma. Role for PI3KC2alpha in platelet function. PI3KC2alpha regulates a basal pool of PtdIns3P in platelets that may lead to impaired regulation of the platelet's cytoskeletal-membrane system
physiological function
PI3KC2beta plays an essential role in neuroblastoma development by mediating functions of ITSN1 and by stabilizing metylocytomatosis viral oncogene (MYCN), an oncogene found in 20% of neuroblastoma cases and a marker for poor prognosis. Correlation between PI3KC2beta expression levels and esophageal squamous-cell carcinoma (ESCC) metastasis. PI3KC2beta is involved in the regulation of cell invasion in PCa cells, partly by activation of MEK/ERK pathways and partly by regulation of cell migration through regulation of Slug protein. This protein is essential for epithelial-mesenchymal transition (EMT), a process which enables cells to gain migratory and invasive properties. PI3KC2beta has no influence on PCa cell proliferation. But it plays crucial roles in cell motility, migration, and invasion. PI3KC2beta is involved in the regulation of cell migration and invasion in different cancers. Implication of PI3KC2beta in metastasis has been demonstrated in breast, prostate, and ovarian cancers. The enzyme has a key role in lamellipodia formation in ovarian cancer SKOV3 cells, allowing for the increase in cell motility. A specific role for this enzyme in ovarian cancer cell motility and, as a consequence, in cancer metastasis. Importance of PI3KC2beta in ovarian cancer cell migration. Overexpression of PI3KC2beta has been also found to enhance migration of A-431 epidermoid carcinoma cells, HeLa and ovarian cancer cells, whereas overexpression of the negative PI3KC2beta is able to reduce this process. Possible mechanism of contribution of PI3KC2beta in cancer cell migration and metastasis included PIK3C2B is regulated by miR-515-5p, which plays a role in the control of cancer cell migration and metastasis. Overexpression of miR-515-5p downregulates PIK3C2B, among others, binding directly to its 3'-UTR region
physiological function
PIK3C2G, the gene encoding PI3KC2gamma, acts mainly as a tumor suppressor gene. Low PI3KC2gamma expression influences colorectal cancer (CRC) development, with low copy number of PIK3C2G associated with a 2.5fold increase in the risk of death
additional information
PI3KC2beta catalytic site structure, overview
additional information
PI3KC2beta catalytic site structure, overview
additional information
PI3KC2beta catalytic site structure, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
-
?
-
x * 190000, calculation from nucleotide sequence
?
x * 182000, calculation from nucleotide sequence
?
x * 110000, catalytic subunit, + x * 85000, catalytically inactive adaptor subunit
?
-
x * 190000, calculation from nucleotide sequence
-
?
-
x * 110000, catalytic subunit, + x * 85000, catalytically inactive adaptor subunit
-
?
-
x * 170000, calculation from nucleotide sequence
?
x * 110000, catalytic subunit, + x * 85000, catalytically inactive adaptor subunit
?
x * 170972, calculation from nucleotide sequence
?
-
x * 180000, enzyme form PI3K C2beta, SDS-PAGE
additional information
domain structure of the adaptor subunit containing a SH3 domain and 2 SH2 domains, three different isozymes of the catalytically subunits P110alpha, P110beta, and P110gamma determine the 3 isozymes alpha, beta, gamma of the enzyme, all P110 subunits can interact with the p85 adaptor subunit
additional information
class II PI3 kinase architecture, overview. PI3KC2alpha has a distinctive N-terminal region containing a clathrin-binding domain, but it lacks proline-rich sequence repeats found in PI3KC2beta
additional information
class II PI3 kinase architecture, overview. PI3KC2alpha has a distinctive N-terminal region containing a clathrin-binding domain, but it lacks proline-rich sequence repeats found in PI3KC2beta
additional information
class II PI3 kinase architecture, overview. PI3KC2alpha has a distinctive N-terminal region containing a clathrin-binding domain, but it lacks proline-rich sequence repeats found in PI3KC2beta
additional information
class II PI3 kinase architecture, overview. PI3KC2beta lacks a distinctive N-terminal region containing a clathrin-binding domain that is found in PI3KC2alpha
additional information
class II PI3 kinase architecture, overview. PI3KC2beta lacks a distinctive N-terminal region containing a clathrin-binding domain that is found in PI3KC2alpha
additional information
class II PI3 kinase architecture, overview. PI3KC2beta lacks a distinctive N-terminal region containing a clathrin-binding domain that is found in PI3KC2alpha
additional information
class II PI3 kinase architecture, overview. PI3KC2gamma lacks a distinctive N-terminal region containing a clathrin-binding domain that is found in PI3KC2alpha
additional information
class II PI3 kinase architecture, overview. PI3KC2gamma lacks a distinctive N-terminal region containing a clathrin-binding domain that is found in PI3KC2alpha
additional information
class II PI3 kinase architecture, overview. PI3KC2gamma lacks a distinctive N-terminal region containing a clathrin-binding domain that is found in PI3KC2alpha
additional information
-
domain structure of the adaptor subunit containing a SH3 domain and 2 SH2 domains, three different isozymes of the catalytically subunits P110alpha, P110beta, and P110gamma determine the 3 isozymes alpha, beta, gamma of the enzyme, all P110 subunits can interact with the p85 adaptor subunit
-
additional information
domain structure of the adaptor subunit containing a SH3 domain and 2 SH2 domains, three different isozymes of the catalytically subunits P110alpha, P110beta, and P110gamma determine the 3 isozymes alpha, beta, gamma of the enzyme, all P110 subunits can interact with the p85 adaptor subunit
additional information
class II PI3 kinase architecture, overview
additional information
class II PI3 kinase architecture, overview
additional information
class II PI3 kinase architecture, overview
additional information
-
class II PI3K enzymes are distinguished from other PI3K isoenzymes by the presence of two tandem domains at their C-termini, the first one is termed a Phox homology domain, which is revealed as a novel phosphoinositide-binding domain, whereas the second is the C2 domain, which is a phospholipid-binding domain that can confer Ca2+ sensitivity
additional information
the class II PI3Ks contain a ras-binding domain, a N-C2 domain, a PIK domain, a catalytic domain, a Phox-homology domain, and a C-C2 domain
additional information
the class II PI3Ks contain a ras-binding domain, a N-C2 domain, a PIK domain, a catalytic domain, a Phox-homology domain, and a C-C2 domain
additional information
-
the class II PI3Ks contain a ras-binding domain, a N-C2 domain, a PIK domain, a catalytic domain, a Phox-homology domain, and a C-C2 domain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Arcaro, A.; Zvelebil, M.J.; Wallasch, C.; Ullrich, A.; Waterfield, M.D.; Domin, J.
Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors
Mol. Cell. Biol.
20
3817-3830
2000
Homo sapiens, Homo sapiens PI3K-C2alpha
brenda
Arcaro, A.; Volinia, S.; Zvelebil, M.J.; Stein, R.; Watton, S.J.; Layton, M.J.; Gout, I.; Ahmadi, K.; Downward, J.; Waterfield, M.D.
Human phosphoinositide 3-kinase C2b, the role of calcium and the C2 domain in enzyme activity
J. Biol. Chem.
273
33082-33090
1998
Homo sapiens (O00750), Homo sapiens
brenda
Domin, J.; Pages, F.; Volinia, S.; Rittenhouse, S.E.; Zvelebil, M.J.; Stein, R.C.; Waterfield, M.D.
Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin
Biochem. J.
326
139-147
1997
Homo sapiens, Homo sapiens PI3K-C2alpha
-
brenda
Molz, L.; Chen, Y.W.; Hirano, M.; Williams, L.T.
CpK is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain
J. Biol. Chem.
271
13892-13899
1996
Mus musculus (Q61194), Drosophila melanogaster (Q7JNX6)
brenda
Virbasius, J.V.; Guilherme, A.; Czech, M.P.
Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain
J. Biol. Chem.
271
13304-13307
1996
Homo sapiens, Mus musculus, Homo sapiens PI3K-C2alpha
brenda
Brown, R.A.; Ho, L.K.; Weber-Hall, S.J.; Shipley, J.M.; Fry, M.J.
Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K
Biochem. Biophys. Res. Commun.
233
537-544
1997
Homo sapiens (O00750)
brenda
Misawa, H.; Ohtsubo, M.; Copeland, N.G.; Gilbert, D.J.; Jenkins, N.A.; Yoshimura, A.
Cloning and characterization of a novel class II phosphoinositide 3-kinase containing C2 domain
Biochem. Biophys. Res. Commun.
244
531-539
1998
Mus musculus (O70167), Mus musculus
brenda
Ono, F.; Nakagawa, T.; Saito, S.; Owada, Y.; Sakagami, H.; Goto, K.; Suzuki, M.; Matsuno, S.; Kondo, H.
A novel class II phosphoinositide 3-kinase predominantly expressed in the liver and its enhanced expression during liver regeneration
J. Biol. Chem.
273
7731-7736
1998
Rattus norvegicus (O70173)
brenda
Rozycka, M.; Lu, Y.J.; Brown, R.A.; Lau, M.R.; Shipley, J.M.; Fry, M.J.
cDNA cloning of a third human C2-domain-containing class II phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment of this gene (PIK3C2G) to 12p12
Genomics
54
569-574
1998
Homo sapiens (O75747), Homo sapiens
brenda
Ktori, C.; Shepherd, P.R.; O'Rourke, L.
TNF-alpha and leptin activate the alpha-isoform of class II phosphoinositide 3-kinase
Biochem. Biophys. Res. Commun.
306
139-143
2003
Mus musculus
brenda
Prior, I.A.; Clague, M.J.
Localization of a class II phosphatidylinositol 3-kinase, PI3KC2a, to clathrin-coated vesicles
Mol. Cell. Biol.
1
162-166
1999
Rattus norvegicus
brenda
Gaidarov, I.; Smith, M.E.K.; Domin, J.; Keen, J.H.
The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking
Mol. Cell
7
443-449
2001
Homo sapiens, Homo sapiens PI3K-C2alpha
brenda
Turner, S.J.; Domin, J.; Waterfield, M.D.; Ward, S.G.; Westwick, J.
The CC chemokine monocyte chemotactic peptide-1 activates both the class I p85/p110 phosphatidylinositol 3-kinase and the class II PI3K-C2alpha
J. Biol. Chem.
273
25987-25995
1998
Homo sapiens, Homo sapiens PI3K-C2alpha
brenda
Domin, J.; Gaidarov, I.; Smith, M.E.K.; Keen, J.H.; Waterfield, M.D.
The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles
J. Biol. Chem.
275
11943-11950
2000
Cricetulus griseus, Homo sapiens, Rattus norvegicus, Cricetulus griseus PI3K-C2alpha, Homo sapiens PI3K-C2alpha
brenda
Wheeler, M.; Domin, J.
Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: role of Grb2
Mol. Cell. Biol.
21
6660-6667
2001
Homo sapiens
brenda
El Sheikh, S.S.; Domin, J.; Tomtitchong, P.; Abel, P.; Stamp, G.; Lalani, E.N.
Topographical expression of class IA and class II phosphoinositide 3-kinase enzymes in normal human tissues is consistent with a role in differentiation
BMC Clin. Pathol.
3
4
2003
Homo sapiens
brenda
Shepherd, P.R.
Mechanisms regulating phosphoinositide 3-kinase signalling in insulin-sensitive tissues
Acta Physiol. Scand.
183
3-12
2005
Homo sapiens (O00443), Mus musculus (Q61194), Homo sapiens PI3K-C2alpha (O00443)
brenda
Kang, S.; Song, J.; Kang, J.; Kang, H.; Lee, D.; Lee, Y.; Park, D.
Suppression of the alpha-isoform of class II phosphoinositide 3-kinase gene expression leads to apoptotic cell death
Biochem. Biophys. Res. Commun.
329
6-10
2005
Homo sapiens (O00443)
brenda
Crljen, V.; Volinia, S.; Banfic, H.
Hepatocyte growth factor activates phosphoinositide 3-kinase C2beta in renal brush-border plasma membranes
Biochem. J.
365
791-799
2002
Rattus norvegicus
brenda
Arcaro, A.; Khanzada, U.K.; Vanhaesebroeck, B.; Tetley, T.D.; Waterfield, M.D.; Seckl, M.J.
Two distinct phosphoinositide 3-kinases mediate polypeptide growth factor-stimulated PKB activation
EMBO J.
21
5097-5108
2002
Homo sapiens
brenda
MacDougall, L.K.; Gagou, M.E.; Leevers, S.J.; Hafen, E.; Waterfield, M.D.
Targeted expression of the class II phosphoinositide 3-kinase in Drosophila melanogaster reveals lipid kinase-dependent effects on patterning and interactions with receptor signaling pathways
Mol. Cell. Biol.
24
796-808
2004
Drosophila melanogaster
brenda
Sindic, A.; Crljen, V.; Matkovic, K.; Lukinovic-Skudar, V.; Visnjic, D.; Banfic, H.
Activation of phosphoinositide 3-kinase C2 beta in the nuclear matrix during compensatory liver growth
Adv. Enzyme Regul.
46
280-287
2006
Rattus norvegicus
brenda
Falasca, M.; Maffucci, T.
Role of class II phosphoinositide 3-kinase in cell signalling
Biochem. Soc. Trans.
35
211-214
2007
Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Traer, C.J.; Foster, F.M.; Abraham, S.M.; Fry, M.J.
Are class II posphoinositide 3-kinases potential targets for anticancer therapies?
Bull. Cancer
93
E53-E58
2006
Homo sapiens (O00443), Homo sapiens (O00750), Homo sapiens (O75747)
brenda
Katso, R.M.; Pardo, O.E.; Palamidessi, A.; Franz, C.M.; Marinov, M.; De Laurentiis, A.; Downward, J.; Scita, G.; Ridley, A.J.; Waterfield, M.D.; Arcaro, A.
Phosphoinositide 3-kinase C2beta regulates cytoskeletal organization and cell migration via Rac-dependent mechanisms
Mol. Biol. Cell
17
3729-3744
2006
Homo sapiens
brenda
Russo, A.; Okur, M.N.; Bosland, M.; OBryan, J.P.
Phosphatidylinositol 3-kinase, class 2 beta (PI3KC2beta) isoform contributes to neuroblastoma tumorigenesis
Cancer Lett.
359
262-268
2015
Homo sapiens (O00750), Homo sapiens
brenda
Aki, S.; Yoshioka, K.; Okamoto, Y.; Takuwa, N.; Takuwa, Y.
Phosphatidylinositol 3-kinase class II alpha-isoform PI3K-C2alpha is required for transforming growth factor beta-induced Smad signaling in endothelial cells
J. Biol. Chem.
290
6086-6105
2015
Homo sapiens (O00443)
brenda
Mountford, J.K.; Petitjean, C.; Putra, H.W.; McCafferty, J.A.; Setiabakti, N.M.; Lee, H.; T?nnesen, L.L.; McFadyen, J.D.; Schoenwaelder, S.M.; Eckly, A.; Gachet, C.; Ellis, S.; Voss, A.K.; Dickins, R.A.; Hamilton, J.R.; Jackson, S.P.
The class II PI 3-kinase, PI3KC2alpha, links platelet internal membrane structure to shear-dependent adhesive function
Nat. Commun.
6
6535
2015
Mus musculus (Q61194)
brenda
Chikh, A.; Ferro, R.; Abbott, J.J.; Pineiro, R.; Buus, R.; Iezzi, M.; Ricci, F.; Bergamaschi, D.; Ostano, P.; Chiorino, G.; Lattanzio, R.; Broggini, M.; Piantelli, M.; Maffucci, T.; Falasca, M.
Class II phosphoinositide 3-kinase C2alpha regulates a novel signaling pathway involved in breast cancer progression
Oncotarget
7
18325-18345
2016
Homo sapiens (O00750), Homo sapiens
brenda
Nigorikawa, K.; Hazeki, K.; Guo, Y.; Hazeki, O.
Involvement of class II phosphoinositide 3-kinase ?-isoform in antigen-induced degranulation in RBL-2H3 cells.
PLoS ONE
9
e111698
2014
Rattus norvegicus
brenda
Mavrommati, I.; Cisse, O.; Falasca, M.; Maffucci, T.
Novel roles for class II phosphoinositide 3-kinase C2beta in signalling pathways involved in prostate cancer cell invasion
Sci. Rep.
6
23277
2016
Homo sapiens (O00750), Homo sapiens
brenda
Yang, S.; Wu, Q.; Huang, S.; Wang, Z.; Qi, F.
Sevoflurane and isoflurane inhibit KCl-induced Class II phosphoinositide 3-kinase alpha subunit mediated vasoconstriction in rat aorta
BMC Anesthesiol.
16
63
2016
Rattus norvegicus (D3ZTF6)
brenda
Zhuo, M.Q.; Pan, Y.X.; Wu, K.; Xu, Y.H.; Luo, Z.
Characterization and mechanism of phosphoinositide 3-kinases (PI3Ks) members in insulin-induced changes of protein metabolism in yellow catfish Pelteobagrus fulvidraco
Gen. Comp. Endocrinol.
247
34-45
2017
Tachysurus fulvidraco (A0A2I4KAQ4), Tachysurus fulvidraco (A0A2I4KAQ7), Tachysurus fulvidraco
brenda
Falasca, M.; Hamilton, J.R.; Selvadurai, M.; Sundaram, K.; Adamska, A.; Thompson, P.E.
Class II phosphoinositide 3-kinases as novel drug targets
J. Med. Chem.
60
47-65
2017
Mus musculus (E9QAN8), Mus musculus (O70167), Mus musculus (Q61194), Homo sapiens (O00443), Homo sapiens (O00750), Homo sapiens (O75747)
brenda
Aung, K.T.; Yoshioka, K.; Aki, S.; Ishimaru, K.; Takuwa, N.; Takuwa, Y.
The class II phosphoinositide 3-kinases PI3K-C2alpha and PI3K-C2beta differentially regulate clathrin-dependent pinocytosis in human vascular endothelial cells
J. Physiol. Sci.
69
263-280
2019
Homo sapiens (O00443), Homo sapiens (O00750), Homo sapiens
brenda