BRENDA - Enzyme Database
show all sequences of 3.1.3.67

A new role for PTEN in regulating transient receptor potential canonical channel 6-mediated Ca2+ entry, endothelial permeability, and angiogenesis

Kini, V.; Chavez, A.; Mehta, D.; J. Biol. Chem. 285, 33082-33091 (2010)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
thrombin
transiently increases PTEN lipid phosphatase activity by about 2.5fold within 1 min, which remains elevated for 5 min
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
C124S
the PTEN mutant lacks phosphatase activity, but is not altered in TRPC6 activity
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
Homo sapiens
-
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
pulmonary artery endothelial cell
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
-
715544
Homo sapiens
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
-
-
-
?
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
thrombin
transiently increases PTEN lipid phosphatase activity by about 2.5fold within 1 min, which remains elevated for 5 min
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C124S
the PTEN mutant lacks phosphatase activity, but is not altered in TRPC6 activity
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
Homo sapiens
-
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
pulmonary artery endothelial cell
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
-
715544
Homo sapiens
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
-
-
-
?
General Information
General Information
Commentary
Organism
malfunction
thrombin transiently increases PTEN lipid phosphatase activity, while pretreatment of HPAE cells with bpV(pic) slightly reduces basal PTEN activity.Thrombin fails to induce PTEN activity in cells pretreated with bpV(pic). Inhibiting PTEN activity also decreases Akt phosphorylation, inhibiting PTEN phosphatase activity has no effect on thrombin-induced Ca2+ entry
Homo sapiens
physiological function
phosphatase and tensin homologue is a dual lipidprotein phosphatase that catalyzes the conversion of phosphoinositol 3,4,5-triphosphate to phosphoinositol 4,5-bisphosphate and thereby inhibits PI3K-Akt-dependent cell proliferation, migration, and tumor vascularization. But PTEN is indicated to play a role beyond suppressing PI3K signaling, it also plays a role in regulating Ca2+ entry through transient receptor potential canonical channel 6, TRPC6, that does not require PTEN phosphatase activity, overview. PTEN tail-domain residues 394-403 permit PTEN to associate with TRPC6. The inflammatory mediator thrombin promotes this association. Deletion of PTEN residues 394-403 prevents TRPC6 cell surface expression and Ca2+ entry, regulation, overview
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
malfunction
thrombin transiently increases PTEN lipid phosphatase activity, while pretreatment of HPAE cells with bpV(pic) slightly reduces basal PTEN activity.Thrombin fails to induce PTEN activity in cells pretreated with bpV(pic). Inhibiting PTEN activity also decreases Akt phosphorylation, inhibiting PTEN phosphatase activity has no effect on thrombin-induced Ca2+ entry
Homo sapiens
physiological function
phosphatase and tensin homologue is a dual lipidprotein phosphatase that catalyzes the conversion of phosphoinositol 3,4,5-triphosphate to phosphoinositol 4,5-bisphosphate and thereby inhibits PI3K-Akt-dependent cell proliferation, migration, and tumor vascularization. But PTEN is indicated to play a role beyond suppressing PI3K signaling, it also plays a role in regulating Ca2+ entry through transient receptor potential canonical channel 6, TRPC6, that does not require PTEN phosphatase activity, overview. PTEN tail-domain residues 394-403 permit PTEN to associate with TRPC6. The inflammatory mediator thrombin promotes this association. Deletion of PTEN residues 394-403 prevents TRPC6 cell surface expression and Ca2+ entry, regulation, overview
Homo sapiens
Other publictions for EC 3.1.3.67
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Keum
Phosphoinositide 5- and 3-pho ...
Danio rerio
Proc. Natl. Acad. Sci. USA
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2016
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731861
Shearn
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Mus musculus
Free Radic. Biol. Med.
65
680-692
2013
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732083
Ijuin
Regulation of insulin signalin ...
Mus musculus
J. Biol. Chem.
287
6991-6999
2012
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732809
Kurokawa
3'Phosphatase activity toward ...
Ciona intestinalis, Homo sapiens
Proc. Natl. Acad. Sci. USA
109
10089-10094
2012
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732810
Hsu
Structural basis for substrate ...
Legionella pneumophila
Proc. Natl. Acad. Sci. USA
109
13567-13572
2012
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715544
Kini
A new role for PTEN in regulat ...
Homo sapiens
J. Biol. Chem.
285
33082-33091
2010
1
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716688
Langlois
The PTEN phosphatase controls ...
Homo sapiens
PLoS ONE
5
e15742
2010
1
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2
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690780
Rankin
PTEN downregulates p75NTR expr ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
379
721-725
2009
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691598
Semba
Phosphatase activity of nuclea ...
Homo sapiens
Cancer Lett.
274
143-150
2009
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694916
Rahdar
A phosphorylation-dependent in ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
106
480-485
2009
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6
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705669
Fan
PTEN inhibits BMI1 function in ...
Homo sapiens
Mol. Cancer
8
98
2009
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690927
Redfern
PTEN phosphatase selectively b ...
Homo sapiens
Biochemistry
47
2162-2171
2008
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691607
Dey
The protein phosphatase activi ...
Mus musculus
Cancer Res.
68
1862-1871
2008
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692556
Qiu
Phosphatase and tensin homolog ...
Homo sapiens, Mus musculus
Hepatology
48
1799-1809
2008
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693117
Feng
Par-3-mediated junctional loca ...
Canis lupus
J. Biol. Chem.
283
23440-23449
2008
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694494
Knobbe
The roles of PTEN in developme ...
Mus musculus
Oncogene
27
5398-5415
2008
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31
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694495
Leslie
Understanding PTEN regulation: ...
Homo sapiens
Oncogene
27
5464-5476
2008
2
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1
2
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681020
Hoshino
Phosphatase PTEN is inactivate ...
Bos taurus
J. Cell. Biochem.
100
515-526
2007
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2
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682679
Gajewski
Expression, generation, and pu ...
Rattus norvegicus
Protein Expr. Purif.
55
334-342
2007
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1
1
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677869
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PTEN and SHIP2 phosphoinositid ...
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The PTEN phosphatase is essent ...
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PTEN: Tumour suppressor, multi ...
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650758
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Analysis of PTEN/MMAC1 alterat ...
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Overexpression of PTEN/MMAC1 a ...
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Functional evaluation of PTEN ...
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651205
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Cell cycle arrest by the PTEN ...
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Phosphorylation of the PTEN ta ...
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The PTEN lipid phosphatase dom ...
Homo sapiens
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653397
Paramio
PTEN tumour suppressor is link ...
Homo sapiens
Oncogene
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653616
Georgescu
The tumor-suppressor activity ...
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653626
Ramaswamy
Regulation of G1 progression b ...
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653630
Sun
PTEN modulates cell cycle prog ...
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Protein kinase B (PKB/Akt) act ...
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The tumor suppressor, PTEN/MMA ...
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Purification and characterizat ...
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