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
-
clinicopathological
-
pten-deficient
- adenocarcinoma
- colorectal
-
transwell
- hamartoma
- cowden
- caspase-3
- bcl-2
-
germline
- cyclin
- pik3ca
-
epithelial-mesenchymal
- lncrnas
-
nsclc
-
microrna-21
-
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
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Posttranslational Modification
Posttranslational Modification on EC 3.1.3.67 - phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
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phosphoprotein
ubiquitination
additional information
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carbonylation of PTEN increases significantly in ethanol-fed mice compared to pair-fed control animals, corresponding to decreased PTEN3-phosphatase activity
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exposure of bovine aortic endothelial cells to cyclic strain results in a time-dependent PTEN phosphorylation. Maximal phosphorylation occurres at 10 min after the cyclic strain stimulation by 2.21fold relative to static condition
phosphoprotein
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the 50-amino-acid C-terminal domain, the tail, is necessary for maintaining protein stability and it also acts to inhibit PTEN function. The tail-dependent regulation of stability and activity is linked to the phosphorylation of three residues, S380, T382, and T383 within the tail. Therefor, the tail is likely to mediate the regulation of PTEN function through phosphorylation
phosphoprotein
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C-terminal 51 amino acids contains a cluster of phosphorylation sites which regulates protein stability and function in cells, a phosphorylation-dependent intramolecular interaction regulates the membrane association and activity of the tumor suppressor PTEN, phosphorylation of the C-terminal cluster has an inhibitory effect on membrane association and activity
phosphoprotein
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phosphorylation of several serine and threonine residues in the C-terminus of the protein inhibits PTEN, e.g., suppressing of membrane association, nuclear localization, PDZ-binding, ubiquitination, degradation and phosphatase activity. The phosphorylation sites form 2 separable groups comprising a close cluster of 4 residues, Ser380, Thr382, Thr383 and Ser385, and a pair of residues slightly more N-terminal, Thr366 and Ser370. The 380-385 cluster sites all appear to be phosphorylated by protein kinase CK2.
phosphoprotein
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tyrosine residues, present in most examples of a rare subset of lung tumours, but not detected in the great majority. PTEN tyrosine phosphorylation may occur only in certain cell types and circumstances, or that only an extremely small proportion of the cellular PTEN becomes tyrosine phosphorylated
phosphoprotein
insertion of stoichiometric and site-specific phospho-Ser/Thr residues in the C-terminal tail of PTEN. No single phospho-modification of the Ser/Thr C-terminal cluster is dominant and each is partially additive in antagonizing catalysis. Conformational closure is influenced by the aggregate effect of multiple phospho-sites rather than dominated by a single phosphorylation site
phosphoprotein
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PTEN expression and PTEN phosphorylation are significantly increased in the livers of ethanol-fed mice
phosphoprotein
recombinant PTEN is phosphorylated in the infected insect cells at Ser-380, Thr-382, and Thr-383 at the C-terminal tail
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mono-ubiquitination-mediated PTEN stabilization is essential for its tumor suppression activity
ubiquitination
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regulation of activity, mono- and polyubiquitinated, PTEN has 2 canonical PEST motifs, a signature in many short-lived proteins degraded by ubiquitin-proteasome pathway, controlling of nuclear localization and PTEN stability