3.1.3.67: phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
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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
-
clinicopathological
-
pten-deficient
- adenocarcinoma
- colorectal
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transwell
- hamartoma
- cowden
- caspase-3
- bcl-2
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germline
- cyclin
- pik3ca
-
epithelial-mesenchymal
- lncrnas
-
nsclc
-
microrna-21
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phosphatidylinositol-3-kinase
-
tumor-suppressor
-
pten-induced
- her2
-
phospho-akt
- pink1
-
pi3k-akt
- 4,5-bisphosphate
- macrocephaly
-
her2-positive
-
hamartomatous
-
endometrioid
-
ptdins3,4,5p3
- phosphatidylinositol-4,5-bisphosphate
- phosphoinositide-3-kinase
-
phosphoinositide-dependent
- trastuzumab
-
phosphoinositide-3
- analysis
- drug development
-
everolimus
- diagnostics
- medicine
-
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
results (
results (Engineering
Engineering on EC 3.1.3.67 - phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
380-385A
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in endothelial cells transfected with 380-385A (mutation on the PTEN phosphorylation site) phosphatidylinositol 3,4,5-trisphosphate immunofluorescence intensity is than in wildtype or G129R transfected cells. Phosphatidylinositol 3,4,5-trisphosphate intensity in endothelial cells transfected with 380385A is weak but gradually increases to a maximum at 240 min after cyclic strain stimulation by 1.48fold relative to static condition
G129R
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in endothelial cells transfected with G129R, that lacks both protein and lipid phosphatase activities, phosphatidylinositol 3,4,5-trisphosphate immunofluorescence intensity is higher than transfection with wildtype PTEN. phosphatidylinositol 3,4,5-trisphosphate immunofluorescence in endothelial cells transfected with G129R rapidly increases and is maximum at 60 min after cyclic strain stimulation by 2.14fold relative to static condition
DELTA394-403
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removal of the last 10 residues of PTEN leads to the complete diffusion of PTEN in MDCK cells, failing to restore the junctional localization of phosphatidylinositol 4,5-bisphosphate
C124S
D92A
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catalytically inert mutant enzyme, retains partial ability to induce cells to accumulate in G1
DELTA1-15
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phosphatidylinositol 4,5-biphosphate has no effect on binding of PTEN16-403
DELTA352-403
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truncated enzyme binds strongly to the plasma membrane, an effect that is reversed by co-expression of the remainder of the molecule, PTEN 352-403
G129E
G129R
H123Y
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mutant enzyme lacking phosphatase activity is ineffective in blocking the cell cycle of MCF-7 cells
H129R
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mutant enzyme lacking phosphatase activity is ineffective in blocking the cell cycle of MCF-7 cells
K13E
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the binding of the PTEN mutant K13E, which is a tumor-derived mutation that renders PTEN inactive, is not affected by phosphatidylinositol 4,5-biphosphate
PTEN1-274
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when produced as glutathione S-transferase fusion protein, the protein is defective in catalyzing the release of phosphate from either a phosphate-labeled poly(Glu4-Tyr1) substrate or inositol 1,3,4,5-tetrakisphosphate
PTEN1-336
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when produced as glutathione S-transferase fusion protein, the protein is defective in catalyzing the release of phosphate from either a phosphate-labeled poly(Glu4-Tyr1) substrate or inositol 1,3,4,5-tetrakisphosphate
PTENDELTA274-342
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when produced as glutathione S-transferase fusion protein, the protein is defective in catalyzing the release of phosphate from either a phosphate-labeled poly(Glu4-Tyr1) substrate or inositol 1,3,4,5-tetrakisphosphate
S380A
S383A
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PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity
T382A
T383A
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greater catalytic activity than an unphosphorylated, bacterially expressed wild type enzyme
T385A
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PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity
T401I
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activity is comparable with or even higher than that of wild-type enzyme
V369G
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activity is comparable with or even higher than that of wild-type enzyme
G129E
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protein phosphatase-active, lipid phosphatase inactive mutant, expression of G129E mutant of PTEN in U-87MG cells has no effect on the phosphorylation status of protein kinase B, the mutant displays 7% of wildtype lipid phosphatidylinositol 3,4,5-trisphosphate-phosphatase activitiy and 65% wild type protein phosphatase activitiy in glioma cells
R130M
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kinase dead mutant, expression of R130M mutant of PTEN in U-87MG cells has no effect on the phosphorylation status of protein kinase B, the mutant displays 5% of wildtype lipid phosphatidylinositol 3,4,5-trisphosphate-phosphatase activitiy and 12% of wild-type protein phosphatase activitiy in glioma cells
C124S
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PTEN mutant is devoid of phosphatase activity and fails to modulate p75NTR expression, indicating that phosphatase activity is required for PTEN regulation of neurotophin receptor p75NTR
G129E
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PTEN mutant which is lipid phosphatase dead but which retains protein phosphatase activity, significantly reduces the expression of p75NTR, suggesting that it is the protein phosphatase activity of PTEN that is able to regulate neurotophin receptor p75NTR expression
additional information
C124S
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adenovirus encoding a dominant negative human PTEN cDNA is used for the transduction of cell cultures
C124S
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mutant PTEN-C124S-A4-YFP lacks lipid and protein phosphatase activity, great localization to the plasma membrane than other mutants
C124S
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the PTEN mutant lacks phosphatase activity, but is not altered in TRPC6 activity
G129E
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mutant enzyme associated with Cowdens disease has protein phosphatase activity yet is defective in dephosphorylating inositol 1,3,4,5-tetrakisphosphate in vitro and fails to arrest cells in G1
G129E
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mutant enzyme is selectively deficient in the lipid phosphatase activity but still blocks the cell cycle of MCF-7 cells
G129E
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transduction of recombinant PTEN in to TMK-1 cells promotes nuclear localization with increased mRNA levels of CDX2 and intestinal claudins, whereas the G129 dead phosphatase mutant has no effect
S380A
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greater catalytic activity than an unphosphorylated, bacterially expressed wild type enzyme
S380A
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PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity
T382A
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greater catalytic activity than an unphosphorylated, bacterially expressed wild type enzyme
T382A
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PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity
additional information
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PTEN overexpression in MCF-7 breast cancer cell line prevents ERK1/2 phosphorylation in response to insulin. Inhibition of ERK1/2 activation is not only caused by a reduction in PtdIns(3,4,5)P3 level but also by a decreased association of Shc with Grb2/Sos complex and Ras activation
additional information
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lentiviral infection of PTEN shRNA significantly inhibited Caco-2/15 cell polarization, functional differentiation and brush border development
additional information
deletion of the C-terminal portion of SidF including the two transmembrane motifs changes its localization to the cell periphery
additional information
deletion of the putative transmembrane domains does not affect its enzymatic activity
additional information
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adipose tissue-specific depletion of PTEN in mice results in improved glucose tolerance and insulin sensitivity rendering mice resistant to streptozotocin-induced diabetes. Increased recruitment of Glut4 transporters at the plasma membrane of adipocytes,whereas the contrary is observed in muscle of the same animals. Decreased expression of resistin is shown
additional information
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CA1 synapses in hippocampal slices from PTEN-deficient mice exhibit activity-induced long-term potentiation of synaptic transmission but are resistant to long-term depression. PTEN reduces phosphatidylinositol-3-kinase activity and pharmacological inhibition of phosphatidylinositol-3-kinase restores long-term depression of synaptic transmission in PTEN-deficient mice, suggesting that inhibition of phosphatidylinositol-3-kinase is necessary for induction of long term depression
additional information
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deletion of one PTEN allele in insulin receptor substrate 2 (IRS2) in mice is able to restore pancreatic beta-cell function, peripheral insulin sensitivity, glucose tolerance and significantly increases life span of the animals, indicating that PTEN controls insulin sensitivity in peripheral tissues and pancreatic beta-cell growth and function
additional information
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liver-specific deletion of PTEN in mice results in enhanced insulin sensitivity, hypoinsulinemia, hypoleptinemia and overall improved glucose tolerance. Adult mice lacking PTEN in liver also develop hepatomegaly syndromes, steatohepatitis and hepatocellular carcinomas
additional information
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muscle-specific depletion of PTEN in mice results in improved glucose metabolism in animals with diabetes and insulin resistance. Elevated fasting glucose levels are prevented and insulin sensitivity and glucose tolerance in high-fat fed animals are improved. Insulin stimulated Akt-activation is enhanced. PTEN depletion in muscle is not associated with increased tumorigenesis
additional information
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overexpresion of catalytically inactive or dominant-negative PTEN mutants in 3T1-L1 adipocytes show that it is the lipid phosphatase activity of PTEN which is required to downregulate Akt/PKB signaling and glucose uptake in response to insulin
additional information
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PTEN downregulation in 3T1-L1 adipocytes by small interfering RNAs enhances Akt/PKB activation and glucose uptake in response to insulin
additional information
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PTEN null mutations in mice are lethal at embryonic stages and even a 50% reduction in PTEN expression leads to increased tumorigenesis
additional information
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PTEN overexpression in 3T1-L1 adipocytes causes inhibition of insulin-induced PtdIns(3,4)P2 and PtdIns(3,4,5)P3 production, Akt/PKB activation, GLUT4 translocation to the cell membrane and glucose uptake
