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Literature summary for 2.7.1.137 extracted from
- Phosphatidylinositol 3-kinase: a key regulator in adherens junction formation and function (2009), Front. Biosci., 14, 510-522.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| beta-catenin | tyrosine-phopshorylated | Homo sapiens | |
| beta-catenin | tyrosine-phopshorylated | Canis lupus familiaris | |
| c-Src | - |
Homo sapiens | |
| c-Src | - |
Canis lupus familiaris | |
| Dlg | tyrosine-phopshorylated | Homo sapiens | |
| Dlg | tyrosine-phopshorylated | Canis lupus familiaris | |
| additional information | the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. Interaction of docking proteins via the p85 subunit of PI3K | Homo sapiens | |
| additional information | the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. Interaction of docking proteins via the p85 subunit of PI3K | Canis lupus familiaris |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | a mutant with a deletion in the binding site of the p110 catalytic subunit is dominant negative | Homo sapiens |
| additional information | a mutant with a deletion in the binding site of the p110 catalytic subunit is dominant negative | Canis lupus familiaris |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| LY294002 | - |
Canis lupus familiaris |  |
| LY294002 | - |
Homo sapiens | |
| Wortmannin | - |
Canis lupus familiaris | |
| Wortmannin | - |
Homo sapiens | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | PI3K associates with E-cadherin and part of the E-cadherin signaling complex, which is intergrated into the plasma membrane, complex formation, overview | Homo sapiens | - |
- |
| additional information | PI3K associates with E-cadherin and part of the E-cadherin signaling complex, which is intergrated into the plasma membrane, complex formation, overview | Canis lupus familiaris | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1-phosphatidyl-1D-myo-inositol | Homo sapiens | catalyzed by class I and III, and probably by class II enzymes, overview. PI3K is part of the plasma membrane E-cadherin signaling complex | ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol | Canis lupus familiaris | catalyzed by class I and III, and probably by class II enzymes, overview. PI3K is part of the plasma membrane E-cadherin signaling complex | ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
? | |
| additional information | Homo sapiens | the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. PI3K, stimulated by E-cadherin adhesion, activates PKB/Akt | ? | - |
? | |
| additional information | Canis lupus familiaris | the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. PI3K, stimulated by E-cadherin adhesion, activates PKB/Akt | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Canis lupus familiaris | - |
- |
- |
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| endothelial cell | - |
Homo sapiens | - |
| enterocyte | - |
Homo sapiens | - |
| epidermis | - |
Homo sapiens | - |
| epithelium | - |
Homo sapiens | - |
| keratinocyte | - |
Homo sapiens | - |
| mammary gland | - |
Homo sapiens | - |
| MDCK cell | - |
Canis lupus familiaris | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 1-phosphatidyl-1D-myo-inositol | - |
Homo sapiens | ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol | - |
Canis lupus familiaris | ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol | catalyzed by class I and III, and probably by class II enzymes, overview. PI3K is part of the plasma membrane E-cadherin signaling complex | Homo sapiens | ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
? | |
| ATP + 1-phosphatidyl-1D-myo-inositol | catalyzed by class I and III, and probably by class II enzymes, overview. PI3K is part of the plasma membrane E-cadherin signaling complex | Canis lupus familiaris | ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
? | |
| additional information | the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. PI3K, stimulated by E-cadherin adhesion, activates PKB/Akt | Homo sapiens | ? | - |
? | |
| additional information | the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. PI3K, stimulated by E-cadherin adhesion, activates PKB/Akt | Canis lupus familiaris | ? | - |
? | |
| additional information | the enzyme also catalyzes the reactions of EC 2.7.1.68, 1-phosphatidylinositol-4-phosphate 5-kinase, and EC 2.7.1.67, 1-phosphatidylinositol 4-kinase | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PI3K | - |
Homo sapiens |
| PI3K | - |
Canis lupus familiaris |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Homo sapiens | |
| ATP | - |
Canis lupus familiaris | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | Tiam1-mediated Rac1 activation and E-cadherin-mediated cell-cell adhesion are dependent on PI3K activity, regulation, overview. The signaling hierarchy leads from PI3K to Tiam1 to Rac to the actin cytoskeleton resulting in adherens junction formation. PI3K is involved in E-cadherin-dependent regulation of epithelial cell differentiation and polarity | Homo sapiens |
| physiological function | Tiam1-mediated Rac1 activation and E-cadherin-mediated cell-cell adhesion are dependent on PI3K activity, regulation, overview. The signaling hierarchy leads from PI3K to Tiam1 to Rac to the actin cytoskeleton resulting in adherens junction formation. PI3K is involved in E-cadherin-dependent regulation of epithelial cell differentiation and polarity | Canis lupus familiaris |
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