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Literature summary extracted from

  • Fukushima, T.; Nedachi, T.; Akizawa, H.; Akahori, M.; Hakuno, F.; Takahashi, S.
    Distinct modes of activation of phosphatidylinositol 3-kinase in response to cyclic adenosine 3',5'-monophosphate or insulin-like growth factor I play different roles in regulation of cyclin D1 and p27Kip1 in FRTL-5 cells (2008), Endocrinology, 149, 3729-3742.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.137 cAMP PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1 Rattus norvegicus
2.7.1.137 IGF-I PI 3-kinase is activated in response to cAMP or IGF-I. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1 Rattus norvegicus
2.7.1.153 cAMP PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1 Rattus norvegicus
2.7.1.153 IGF-I PI 3-kinase is activated in response to cAMP or IGF-I. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1 Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.137 LY294002
-
 Rattus norvegicus
2.7.1.153 LY294002
-
 Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.137 Mg2+
-
 Rattus norvegicus
2.7.1.153 Mg2+
-
 Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.137 ATP + 1-phosphatidyl-1D-myo-inositol Rattus norvegicus
-
 ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.137 Rattus norvegicus
-
-
-
2.7.1.153 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.137 FRTL-5 cell thyroid follicular cell line Rattus norvegicus
-
2.7.1.153 FRTL-5 cell thyroid follicular cell line Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.137 ATP + 1-phosphatidyl-1D-myo-inositol
-
 Rattus norvegicus ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 ?
2.7.1.137 ATP + 1-phosphatidyl-1D-myo-inositol substrate from bovine liver Rattus norvegicus ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
 ?
2.7.1.137 additional information 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 ?
-
 ?
2.7.1.153 ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
 Rattus norvegicus ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
 ?
2.7.1.153 ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
 Rattus norvegicus ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
-
 ?
2.7.1.153 additional information 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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.137 heterodimer 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
2.7.1.153 heterodimer 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

Synonyms

EC Number Synonyms Comment Organism
2.7.1.137 PI 3-kinase
-
 Rattus norvegicus
2.7.1.137 PI3K
-
 Rattus norvegicus
2.7.1.153 PI 3-kinase
-
 Rattus norvegicus
2.7.1.153 PI3K
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.137 25
-
 assay at Rattus norvegicus
2.7.1.153 25
-
 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.137 7.5
-
 assay at Rattus norvegicus
2.7.1.153 7.5
-
 assay at Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.137 ATP
-
 Rattus norvegicus
2.7.1.153 ATP
-
 Rattus norvegicus

General Information

EC Number General Information Comment Organism
2.7.1.137 physiological function PI 3-kinase activated in response to cAMP or IGF-I stimulus plays important roles in increasing the translation rate or mRNA levels of cyclin D1, respectively. Activation of PI 3-kinase in response to cAMP or IGF-I are essential for marked increases in G1 CDK activities and DNA synthesis. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1 Rattus norvegicus
2.7.1.153 physiological function PI 3-kinase activated in response to cAMP or IGF-I stimulus plays important roles in increasing the translation rate or mRNA levels of cyclin D1, respectively. Activation of PI 3-kinase in response to cAMP or IGF-I are essential for marked increases in G1 CDK activities and DNA synthesis. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1 Rattus norvegicus