EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.7.1.137 | more |
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 |
? |
- |
? |
2.7.1.137 | more |
Vps34, p150, Beclin 1, Atg14, and UVRAG form two distinct class III phosphatidylinositol 3-kinase complexes, overview. Atg14 interacts with Beclin 1 and Vps34 but not with UVRAG, the coiled-coil region of Atg14 required for binding with Vps34 and Beclin 1 is essential for autophagy |
Homo sapiens |
? |
- |
? |
2.7.1.137 | more |
a p110alpha/beta-subunit binds to a p85 regulatory subunit, and this heterodimer is recruited to the membrane through the association with phosphotyrosyl proteins, leading to production of phosphatidylinositol 3,4,5-triphosphate, PIP3, followed by activation of downstream signal pathway(s) |
Rattus norvegicus |
? |
- |
? |
2.7.1.137 | more |
PI3-kinase activity is not required for starvation-induced Atg14 puncta formation |
Homo sapiens |
? |
- |
? |
2.7.1.137 | more |
PI3K binds PD1 peptide, a 12-residue proline-rich peptide HSKRPLPPLPSL, and PD1R peptide, at the SH3 domain with type I ligand orientation of the bound peptide with an extended conformation where the central portion forms a left-handed type II polyproline, PPII, helix. The residue at anchor position P-3 is a tyrosine |
Homo sapiens |
? |
- |
? |
2.7.1.137 | more |
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 |
? |
- |
? |
2.7.1.137 | more |
PI3K binds to the V-ATPase subunit B2 (VHA-B2) in vitro and in vivo |
Arabidopsis thaliana |
? |
- |
? |
2.7.1.137 | more |
wild-type Risk1 binds preferentially to PIs (i.e., phosphatidylinositol [PI], phosphatidylinositol 4-phosphate [PI(4)P], phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], and phosphatidylserine [PS]) over other lipids such as phosphatidylethanolamine (PE), phosphatidylcholine (PC), diacylglycerol (DAG), cholesterol, or sphingomyelin. Class III PI3Ks convert PI to phosphatidylinositol 3-phosphate [PI(3)P] |
Rickettsia typhi |
? |
- |
- |
2.7.1.137 | more |
nerve growth factor inhibits Na+/H+ exchange and formula absorption through parallel phosphatidylinositol 3-kinase-mTOR and ERK pathways in thick ascending limb |
Rattus norvegicus Sprague-Dawley |
? |
- |
? |
2.7.1.137 | more |
wild-type Risk1 binds preferentially to PIs (i.e., phosphatidylinositol [PI], phosphatidylinositol 4-phosphate [PI(4)P], phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], and phosphatidylserine [PS]) over other lipids such as phosphatidylethanolamine (PE), phosphatidylcholine (PC), diacylglycerol (DAG), cholesterol, or sphingomyelin. Class III PI3Ks convert PI to phosphatidylinositol 3-phosphate [PI(3)P] |
Rickettsia typhi ATCC VR-144 |
? |
- |
- |