3.1.3.67: phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
This is an abbreviated version!
For detailed information about phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase, go to the full flat file.
Word Map on EC 3.1.3.67
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3.1.3.67
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3-kinase
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rapamycin
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mtor
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tumorigenesis
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prostate
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metastasis
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endothelial
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luciferase
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glioblastoma
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tumour
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glioma
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carcinogenesis
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endometrial
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clinicopathological
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pten-deficient
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adenocarcinoma
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colorectal
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transwell
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hamartoma
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cowden
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caspase-3
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bcl-2
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germline
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cyclin
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pik3ca
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epithelial-mesenchymal
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lncrnas
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nsclc
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microrna-21
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phosphatidylinositol-3-kinase
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tumor-suppressor
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pten-induced
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her2
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phospho-akt
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pink1
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pi3k-akt
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4,5-bisphosphate
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macrocephaly
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her2-positive
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hamartomatous
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endometrioid
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ptdins3,4,5p3
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phosphatidylinositol-4,5-bisphosphate
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phosphoinositide-3-kinase
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phosphoinositide-dependent
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trastuzumab
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phosphoinositide-3
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analysis
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drug development
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everolimus
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diagnostics
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medicine
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mirna-21
- 3.1.3.67
- 3-kinase
- rapamycin
- mtor
- tumorigenesis
- prostate
- metastasis
- endothelial
- luciferase
- glioblastoma
- tumour
- glioma
- carcinogenesis
- endometrial
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clinicopathological
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pten-deficient
- adenocarcinoma
- colorectal
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transwell
- hamartoma
- cowden
- caspase-3
- bcl-2
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germline
- cyclin
- pik3ca
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epithelial-mesenchymal
- lncrnas
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nsclc
-
microrna-21
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phosphatidylinositol-3-kinase
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tumor-suppressor
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pten-induced
- her2
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phospho-akt
- pink1
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pi3k-akt
- 4,5-bisphosphate
- macrocephaly
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her2-positive
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hamartomatous
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endometrioid
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ptdins3,4,5p3
- phosphatidylinositol-4,5-bisphosphate
- phosphoinositide-3-kinase
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phosphoinositide-dependent
- trastuzumab
-
phosphoinositide-3
- analysis
- drug development
-
everolimus
- diagnostics
- medicine
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mirna-21
Reaction
Synonyms
1-phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase, MMAC1/TEP1, phosphatase and tensin homolog, phosphatase and tensin homologue, phosphatase and tensin homologue deleted on chromosome 10, phosphatidylinositol 3,4,5-trisphosphate-specific phosphatase, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase, PI 3-phosphatase, PTEN, PTEN phosphatase, PTEN/MMAC, PTEN/MMAC1, SidF, TPIP, tumor suppressor PREN, voltage-sensing phosphatase, Voltage-sensing phosphoinositide phosphatase, VSP
ECTree
3.1.3.67 phosphatidylinositol-3,4,5-trisphosphate 3-phosphataseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.1.3.67 - phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
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?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
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dual-specific phosphatase
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?
D-myo-phosphatidylinositol 3,4,5-trisphosphate + H2O
D-myo-phosphatidylinositol 4,5-bisphosphate + phosphate
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?
phosphatidylinositol 3,4,5-triphosphate + H2O
phosphatidylinositol 4,5-bisphosphate + phosphate
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidyl inositol 4,5-bisphosphate + phosphate
Phosphatidylinositol-3,4,5-trisphosphate + H2O
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the enzyme may play a critical role in the inositolphospholipid 3-kinase signalling
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?
Phosphatidylinositol-3,4,5-trisphosphate + H2O
Phosphatidyl inositol-4,5-bisphosphate + phosphate
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-4,5-bisphosphate + phosphate
phosphatidylinositol-3,4-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
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tumor suppressor function. Dephosphorylation of the second-messenger phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-diphosphate and, by doing so, to antagonize the phosphoinositide 3-kinase pathway
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?
phosphatidylinositol 3,4,5-triphosphate + H2O
phosphatidylinositol 4,5-bisphosphate + phosphate
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?
phosphatidylinositol 3,4,5-triphosphate + H2O
phosphatidylinositol 4,5-bisphosphate + phosphate
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?
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidyl inositol 4,5-bisphosphate + phosphate
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tumor suppressor function. Dephosphorylation of the second-messenger phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-diphosphate and, by doing so, to antagonize the phosphoinositide 3-kinase pathway
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?
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidyl inositol 4,5-bisphosphate + phosphate
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dephosphorylating
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?
Phosphatidylinositol-3,4,5-trisphosphate + H2O
Phosphatidyl inositol-4,5-bisphosphate + phosphate
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it is possible that the enzyme acts in vivo as a phosphoinositide 3-phosphatase by regulating phosphatidylinositol-3,4,5-trisphosphate levels
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?
Phosphatidylinositol-3,4,5-trisphosphate + H2O
Phosphatidyl inositol-4,5-bisphosphate + phosphate
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PTEN regulates the phosphatidylinositol-3,4,5-trisphosphate and Akt signaling pathway and consequently modulates two critical cellular processes: cell cycle progression and cell survival
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?
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-4,5-bisphosphate + phosphate
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lipid phosphatase activity of PTEN is critical for its tumor suppressor function and the enzyme negatively regulates the phosphatidylinositol 3'-kinase-protein kinase B pathway
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?
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-4,5-bisphosphate + phosphate
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PTEN/MMAC is a tumor suppressor that dephosphorylates phosphatidylinositol-3,4,5-trisphosphate, an intermediate in the PI 3-K/Akt signaling pathway
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?
additional information
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the Par-3/PDZ3-PTEN binding is required for the enrichment of PTEN at the junctional membranes of Madin-Darby canine kidney cells, the junctional membrane-localized PTEN is specifically required for the polarization of Madin-Darby canine kidney cells
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additional information
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the regulatory function of PTEN in cell polarity is specifically mediated by its interaction with Par-3, the junctional membrane localization of PTEN depends on this specific Par-3/PDZ3-PTEN tail peptide interaction
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additional information
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germline PTEN mutations are associated with several dominant growth disorders. The growth regulatory function is primarily mediated via its lipid phosphatase activity, which specifically reduces the cellular levels of phosphatidylinositol 3,4,5-trisphosphate. This activity antagonizes the effects of activated phosphatidylinositol 3-kinase in the nutritionally controlled insulin receptor pathway, thereby reducing protein synthesis and restraining cell and organismal growth, while also regulating other biological processes, such as fertility and ageing. PTEN also plays a role as specialized cytoskeletal regulator, which, for example, is involved in directional movement of some migratory cells and may be important in metastasis
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additional information
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phosphatase-independent domains of PTEN markedly reduce the invasive potential of glioma cells, defining a structural role for PTEN that regulates cell motility distinct of the PKB/Akt pathway
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additional information
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protein phosphatase activity may contribute to the cell cycle inhibitory and thereby tumor suppresive function of PTEN
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additional information
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PTEN is a tumor suppressor inactivated in a variety of cancers such as glioblastoma and endometrial and prostate carcinoma. It acts as a phosphatidylinositol 3,4,5-triphosphate phosphatase antagonizing the activity of the phosphatidylinositol 3-OH kinase. The C-terminal region of PTEN contains secondary structure elements that are essential for the tumor-suppressor function of the protein
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additional information
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PTEN might regulate cell-cycle progression by blocking activation of downstream targets of phosphatidylinositol 3-kinase such as the protooncogene Akt. PTEN is capable of inhibiting wild-type Akt kinase activity in cells
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additional information
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PTEN tumour suppressor is linked to the cell cycle control through the retinoblastoma protein
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additional information
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the enzyme plays a role in regulating the activity of the phosphatidylinositol 3-kinase pathway in malignant cells
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additional information
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N-terminal domain of PTEN binds anionic lipids via nonspecific electrostatic interactions
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additional information
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nuclear PTEN is not the same as cytoplasmic PTEN, nuclear PTEN has diverse roles particularly in chromosome stability, DNA repair, cell cycle arrest and cellular stability
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additional information
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overexpression of PTEN modulates the basal activities of both phosphoinositide 3 kinase-AKT and mitogen-activated protein kinase-extracellular signal-regulated kinase cascades
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additional information
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PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a tumor suppressor that is mutated or deleted in a variety of human tumors, and even loss of only one PTEN gene profoundly affects carcinogenesis
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additional information
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PTEN acts to suppress cell growth, proliferation and survival, and in a more cell-specific manner, PTEN plays a role in the establishment of polarity and inhibits the migration of several mammalian cell types
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additional information
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PTEN binds synergistically phosphatidylinositol 4,5-biphosphate and phosphatidylserine
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additional information
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PTEN encodes a phosphatidylinositol phosphate phosphatase specific for the 3-position of the inositol ring, it influences many biological processes in both developing and adult organisms
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additional information
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PTEN exists in a high activity state when it binds transiently at membrane surfaces containing its substrate and other lipids, such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine
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additional information
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PTEN regulates basal activities of the phosphoinositide 3-kinase-AKT8 virus oncogene cellular homolog and extracellular signal-regulated kinase cascades, independent of insulin stimulation
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additional information
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PTEN tumor suppressor negatively regulates the phosphatidylinositol 3-kinase-AKT pathway
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additional information
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PTEN, one of the most important tumor suppressors, must associate with the plasma membrane to maintain appropriate steady-state levels of phosphatidylinositol 3,4,5-triphosphate
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additional information
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the membrane binding of PTEN requires phosphatidylinositol 4,5-bisphosphate
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additional information
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the PTEN tumor suppressor is a lipid and protein phosphatase that inhibits phosphoinositide 3-kinase-dependent signalling by dephosphorylating phosphatidylinositol 3,4,5-trisphosphate
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additional information
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the PTEN phosphatase acts on phosphatidylinositol 3,4,5-triphosphates resulting from phosphatidylinositol 3-kinase activation
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additional information
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depending on the cell type, PTEN is important for proper development, cell fate and cell function, as well as for protection from tumorigenesis
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additional information
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loss of PTEN in the liver creates a state in which the phosphatidylinositol-3 kinase pathway is constitutively active, leading to chronic suppression of apolipoprotein B 100 and mitogen-activated protein resulting in reduced very low-density lipoprotein assembly and hepatic secretion of triglyceride
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additional information
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lung-specific deletion of PTEN after birth results in bronchiolar and alveolar epithelial hyperplasia
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additional information
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most of the tumor suppressor function of PTEN has been attributed to its ability to dephosphorylate the second messenger, phosphatidylinositol 3,4,5-triphosphate, resulting in the biological control of the phosphatidylinositol 3-kinase/protein kinase B pathway
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additional information
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PTEN activity may control the stability and cellular availability of newly synthesized hepatic apolipoprotein B100 at least partially through modulation of microsomal triglyceride transfer protein
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additional information
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PTEN acts as an major tumor suppressor gene that is inacitvated in a wide variety of cancers
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additional information
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PTEN controls FYN kinase activity through its protein phosphatase function in glioma cells
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additional information
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PTEN controls vitronectin-mediated migration through its protein phosphatase activity in glioma cells
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additional information
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PTEN inactivation in pancreas results in increases insulin sensitivity and hypoglycemia and may result in cystic changes of this organ due to mucinous metaplasia. Thus, PTEN is important for the physiological function of the pancreas as well as for the conservation of normal organ structure
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additional information
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PTEN is critical for insulin regulation and liver homeostasis under physiological conditions, and plays an important role in suppressing the devlopment of hepatic adenomas and hepatocellular carcinomas
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additional information
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PTEN is required for both maturation and activation of natural killer cells
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additional information
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PTEN liver-specific knockout mice have fatty liver, increased triglyceride content and reduced apolipoprotein B protein mass
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additional information
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PTEN negatively regulates the phosphorylation of the important cellsurvival kinase Akt
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additional information
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PTEN plays a role in controlling seum insulin and resistin levels, which in turn regulate insulin sensitivity and AMP kinase activity in the liver
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additional information
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PTEN plays a role in embryogenesis and in maintenance of the normal physiological functions of many organ systems
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additional information
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PTEN plays an important role for protection from both epithelial as well as melanocytic tumor formation in the skin
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additional information
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PTEN regulates hepatic lipogenesis, microsomal triglyceride transfer protein and the secretion of apolipoprotein B-containing lipoproteins
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additional information
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PTEN signaling in Pimc neurons in the hypothlamus is vital for the regulation of food uptake and body weight
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additional information
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the protein phosphatase activity of PTEN regulates src family kinases and controls glioma migration
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additional information
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PTEN directly downregulates neurotophin receptor (p75NTR) expression by decreasing DNA-binding activity of transcription factor Sp1
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additional information
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PTEN is a dual specificity phosphatase capable of dephosphorylating both lipid and protein substrates
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