Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.67 - phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC3.1.3.67
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Requires Mg2+. Does not dephosphorylate inositol 4,5-bisphosphate. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4,5)P4 to Ins(1,4,5)P3
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phosphatase and tensin homolog, phosphatase and tensin homologue, pten/mmac1, pten phosphatase, voltage-sensing phosphatase, pten/mmac, pi 3-phosphatase, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase, voltage-sensing phosphoinositide phosphatase, mmac1/tep1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase
-
-
-
-
phosphatase and tensin homolog
phosphatase and tensin homologue
-
-
phosphatase and tensin homologue deleted on chromosome 10
-
-
PI 3-phosphatase
-
-
PTEN phosphatase
-
-
PTEN/MMAC
-
-
PTEN/MMAC1
-
-
TPIP
-
human VSP ortholog of Ciona intestinalis. Enzyme also possesses 5'-phosphatase activity. Substrate specificity of the VSP changes with membrane potential
tumor suppressor PREN
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
phospho-group transfer
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 3-phosphohydrolase
Requires Mg2+. Does not dephosphorylate inositol 4,5-bisphosphate. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4,5)P4 to Ins(1,4,5)P3
CAS REGISTRY NUMBER
COMMENTARY hide
210488-47-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
show the reaction diagram
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
inositol 1,3,4,5-tetrakisphosphate + H2O
inositol 1,4,5-trisphosphate + phosphate
show the reaction diagram
phosphatidylinositol 3,4,5-triphosphate + H2O
phosphatidylinositol 4,5-biphosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol 3,4,5-triphosphate + H2O
phosphatidylinositol 4,5-bisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidyl inositol 4,5-bisphosphate + phosphate
show the reaction diagram
phosphatidylinositol 3,4-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
phosphatidylinositol 3-phosphate + H2O
phosphatidylinositol + phosphate
show the reaction diagram
-
at 20% of the activity with phosphatidylinositol-3,4,5-trisphosphate
-
?
Phosphatidylinositol-3,4,5-trisphosphate + H2O
Phosphatidyl inositol-4,5-bisphosphate + phosphate
show the reaction diagram
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-4,5-bisphosphate + phosphate
show the reaction diagram
phosphatidylinositol-3,4-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
-
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
-
?
phosphatidylinostitol 3,4-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
-
at 20% of the activity with phosphatidylinositol-3,4,5-trisphosphate
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate
show the reaction diagram
-
dual-specific phosphatase
-
-
?
phosphatidylinositol 3,4,5-triphosphate + H2O
phosphatidylinositol 4,5-bisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidyl inositol 4,5-bisphosphate + phosphate
show the reaction diagram
Phosphatidylinositol-3,4,5-trisphosphate + H2O
Phosphatidyl inositol-4,5-bisphosphate + phosphate
show the reaction diagram
-
it is possible that the enzyme acts in vivo as a phosphoinositide 3-phosphatase by regulating phosphatidylinositol-3,4,5-trisphosphate levels
-
?
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-4,5-bisphosphate + phosphate
show the reaction diagram
phosphatidylinositol-3,4-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
-
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
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
-
H2O2 reversibly inhibits PTEN activity by covalently linking Cys-71 to Cys-124, inhibition partially reverses by inclusion of 100 mM dithiothreitol to the buffer
reactive oxygen species
-
oxidation of the active site cysteine by reactive oxygen species inhibits PTEN
-
additional information
-
PTEN function is very frequently lost during the development of epithelial-derived tumors, and many such tumors are believed to undergo a form of epithelial to mesenchymal transition before these metastasize
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acidic lipids
-
acidic lipids, and phosphatidylinositol 4,5-bisphosphate in particular, cause a conformational change within the enzyme and allosteric activation
-
phosphatidylinositol 4,5-biphosphate
-
Enhances PTEN phosphatase activity by inducing conformational change by binding to the PTEN N-terminal domain. Binding constants are in accord with enzyme kinetic measurements showing that phosphatidylinositol 4,5-bisphosphate enhances phosphatidylinositol 3,4,5-triphosphate hydrolysis more effectively than phosphatidylserine, and the binding constant of phosphatidylinositol 4,5-biphosphate of 8.14 microM is in general agreement with the phosphatidylinositol 4,5-bisphosphate concentration requires to activate the PTEN phosphatase. The magnitude of this binding constant indicates that PTEN-phosphatidylinositol 4,5-bisphosphate interactions are physiologically relevant since the effective cellular concentration of phosphatidylinositol 4,5-bisphosphate is thought to be 10 microM, and local phosphatidylinositol 4,5-bisphosphate concentrations are likely to reach even higher levels. Increasing the phosphatidylserine concentration to 25 mol results in stronger binding, but even for these higher surface charge densities, binding constant is still lower than the corresponding values for the phosphatidylcholine/phosphatidylinositol 4,5-bisphosphate vesicle system.
thrombin
-
transiently increases PTEN lipid phosphatase activity by about 2.5fold within 1 min, which remains elevated for 5 min
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25.6
4-nitrophenyl phosphate
-
-
0.0989
Inositol 1,3,4,5-tetrakisphosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary astrocyte, expression of wild-type enzyme
Manually annotated by BRENDA team
-
decreased enzyme in colorectal cancer
Manually annotated by BRENDA team
-
tissue from patients with sporadic gastric carcinoma
Manually annotated by BRENDA team
-
expression of mutant forms of PTEN
Manually annotated by BRENDA team
-
human embryonic kidney cell
Manually annotated by BRENDA team
-
infiltrative glioma cell line
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
the disruption of the PTEN/MMAC1 gene is not a frequent event in neuroblastoma. This disruption may be responsible for malignant progression in only a limited proportion of cases of neuroblastoma
Manually annotated by BRENDA team
-
papillomavirus-infected laryngeal papillomas overexpress PTEN/MMAC1
Manually annotated by BRENDA team
-
derived from testis cDNA
Manually annotated by BRENDA team
-
gastric cancer cell, PTEN negative and phospho-Akt-positive
Manually annotated by BRENDA team
-
glioblastoma-astrocytoma, epithelial-like cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
additional information
-
loss of PTEN expression in HCT116 and CT26, but not in Caco-2/15, leads to an increase in their metastatic potential following tail-vein injections in mice
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTEN_HUMAN
403
0
47166
Swiss-Prot
other Location (Reliability: 2)
TPTE2_HUMAN
522
3
61112
Swiss-Prot
other Location (Reliability: 1)
F6KCZ4_HUMAN
403
0
47165
TrEMBL
other Location (Reliability: 2)
A0A386NCS8_HUMAN
403
0
47219
TrEMBL
other Location (Reliability: 2)
A0A6G6A825_HUMAN
475
0
55011
TrEMBL
other Location (Reliability: 5)
A0A1V0DNR7_HUMAN
549
0
62491
TrEMBL
Mitochondrion (Reliability: 4)
F6KCZ5_HUMAN
403
0
47164
TrEMBL
other Location (Reliability: 2)
A0A2R4SE35_HUMAN
79
0
9089
TrEMBL
other Location (Reliability: 2)
A0A2P0XNP6_HUMAN
61
0
6921
TrEMBL
other Location (Reliability: 1)
F6KD02_HUMAN
403
0
47098
TrEMBL
other Location (Reliability: 2)
F6KCZ3_HUMAN
403
0
47111
TrEMBL
other Location (Reliability: 3)
F6KD01_HUMAN
403
0
47166
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the PTEN C-tail and a segment in the N-terminal region of the catalytic domain directly interact
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
-
inhibiton of PTEN
phosphoprotein
ubiquitination
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A121P
-
inactive mutant enzyme
C105F
-
inactive mutant enzyme
C124R
-
inactive mutant enzyme
C124S
C136Y
-
inactive mutant enzyme
C71Y
-
inactive mutant enzyme
D107Y
-
inactive mutant enzyme
D331G
-
mutant enzyme with partial activity
D92A
-
catalytically inert mutant enzyme, retains partial ability to induce cells to accumulate in G1
DELTA1-15
-
phosphatidylinositol 4,5-biphosphate has no effect on binding of PTEN16-403
DELTA352-403
-
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
F342N
-
mutant enzyme with partial activity
F347L
-
mutant enzyme with partial activity
G129E
G129R
G165R
-
inactive mutant enzyme
G20E
-
mutant enzyme with partial activity
G251C
-
inactive mutant enzyme
H123Y
-
mutant enzyme lacking phosphatase activity is ineffective in blocking the cell cycle of MCF-7 cells
H129R
-
mutant enzyme lacking phosphatase activity is ineffective in blocking the cell cycle of MCF-7 cells
H61R
-
inactive mutant enzyme
H93Y
-
inactive mutant enzyme
K13E
-
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
K289E
-
mutant enzyme with partial activity
L112P
-
inactive mutant enzyme
L112R
-
inactive mutant enzyme
L345Q
-
inactive mutant enzyme
L42R
-
activity is comparable with or even higher than that of wild-type enzyme
M134L
-
mutant enzyme with partial activity
PTEN1-274
-
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
-
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
-
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
R130G
-
inactive mutant enzyme
R130L
-
inactive mutant enzyme
R130Q
-
inactive mutant enzyme
R173C
-
inactive mutant enzyme
R173H
-
inactive mutant enzyme
R173P
-
inactive mutant enzyme
S10N
-
activity is comparable with or even higher than that of wild-type enzyme
S170N
-
inactive mutant enzyme
S170R
-
inactive mutant enzyme
S227F
-
mutant enzyme with partial activity
S380A
S383A
-
PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity
T382A
T383A
-
greater catalytic activity than an unphosphorylated, bacterially expressed wild type enzyme
T385A
-
PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity
T401I
-
activity is comparable with or even higher than that of wild-type enzyme
V133I
-
inactive mutant enzyme
V343E
-
inactive mutant enzyme
V369G
-
activity is comparable with or even higher than that of wild-type enzyme
Y155C
-
inactive mutant enzyme
Y16C
-
inactive mutant enzyme
Y174N
-
inactive mutant enzyme
Y27S
-
inactive mutant enzyme
Y68H
-
inactive mutant enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the 50-amino-acid C-terminal domain, the tail, is necessary for maintaining protein stability
-
the PDZ-binding domain binds to several proteins, including MAGI-2 and MAST205, these interactions appear to enhance the stability of PTEN, as interference with either these binding partners or the ability of PTEN to bind them greatly reduces stability. A protein named PICT-1 (protein interacting with the C-tail-1) interacts with the C-terminus of PTEN, promoting both phosphorylation and stability of PTEN
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Poly-His tag proteins are purified with a HisTrap HP kit using buffers with 10 mM mercaptoethanol, enzymes are further purified with a gel filtration column in 100 mM NaCl, 10 mM Tris, pH 7.4, and 1 mM dithiothreitol. Final purification is done with a anion exchange column in 10 mM Tris, pH 7.4 with a linear gradient from 50-600 mM NaCl.
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenovirus expressing PTEN wild-type, encoding full-length human wild-type PTEN cDNA and AdPTENC/S, encoding a dominant negative human PTEN cDNA mutant (cysteine 124 changed to serine within the catalytic domain) are used for the transduction of cell cultures, overexpression of PTEN and its mutant
-
cDNA is subcloned into bicistronic pIRES vector, which also codes for GFP expression and transiently transfected into the following cell lines: HaCaT, MCA3D, NIH 3T3, 3T3 Ki ras and 3T3 v-src
-
cytosolic domain (amino acids 215–522) is used for analysis
-
expression in Escherichia coli
-
fusion of a C-terminal truncated PTEN (amino acids 1-378) to Mycobacterium xenopi GyrA intein, and chitin-binding domain
overexpressed in MCF-7 breast cancer cell line
-
PTEN-null U87 cells are transiently transfected with either wild-type PTEN-green fluorescent protein or PTEN-alanine substituted-green fluorescent protein. U87 cells expressing PH-AKT1-green fluorescent protein are co-transfected with either wildtype PTEN or PTEN-alanine substituted enzyme. Whereas two cells co-expressing wild-type PTEN and PH-AKT1-green fluorescent protein fails to respond to epidermal growth factor stimulation, all PTEN-alanine substituted proteins co-transfected cells fail to respond. HeLa cells are transiently co-transfected with cyan fluorescent protein-FKBP-inositol polyphosphate-5-phosphatase and PTEN-C124S-alanine substituted-yellow fluorescent protein. Expression of PTEN-C124Salanine substituted-yellow fluorescent protein in HeLa cells.
-
The cDNA encoding full-length 1-403 PTEN is cloned into the NdeI and XhoI sites of the pET30b vector, thereby introducing a poly-His tag at the C-terminus. Point mutations are introduced with the Quick-Change site-directed mutagenesis kit. Deletion mutant 16-403 is prepared by PCR with the Phusion DNA polymerase. PTEN proteins are expressed in Escherichia coli BL21 (DE3) cells.
-
Wild type and mutant cDNA is subcloned in the vector pcDNA3.1 to generate expression vectors, transduction of recombinant PTEN and PTEN mutant into TMK-1 cells. Recombinant PTEN effectively downregulates phospho-Akt levels as well as the LY294002 phosphatidylinositol 3-kinase inhibitor
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
treatment with flavonoid paeonol concentrations of 50 and 100 microM causes a significant downregulation of vascular endothelial growth factor VEGF, hypoxia inducible factor HIF-1alpha, and proteins of the phosphatidylinositol-3-kinase/Akt pathway
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
putative biomarker, nuclear localization of PTEN is important for intestinal differentiation of gastric carcinomas, the loss of cytoplasmatic PTEN expression is correlated with poor gastric carcinoma prognosis
drug development
-
This study is a direct evidence for a model in which PTEN switches between open and closed states and phosphorylation favors the closed conformation, thereby regulating localization and function. Small molecules targeting these interactions can potentially serve as therapeutic agents in antagonizing Ras or phosphoinositide 3-kinase-driven tumors.
medicine
paeonol effectively enhances the sensitivity of ovarian cancer cells to radiation by significantly altering regulation of the proteins of the PI3K/Akt pathway, in addition to downregulating VEGF and HIF-1alpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moritake, H.; Horii, Y.; Kuroda, H.; Sugimoto, T.
Analysis of PTEN/MMAC1 alteration in neuroblastoma
Cancer Genet. Cytogenet.
125
151-155
2001
Homo sapiens
Manually annotated by BRENDA team
Maier, D.; Jones, G.; Li, X.; Schonthal, A.H.; Gratzl, O.; Van Meir, E.G.; Merlo, A.
The PTEN lipid phosphatase domain is not required to inhibit invasion of glioma cells
Cancer Res.
59
5479-5482
1999
Homo sapiens
Manually annotated by BRENDA team
Zhang, P.; Steinberg, B.M.
Overexpression of PTEN/MMAC1 and decreased activation of Akt in human papillomavirus-infected laryngeal papillomas
Cancer Res.
60
1457-1462
2000
Homo sapiens
Manually annotated by BRENDA team
Han, S.Y.; Kato, H.; Kato, S.; Suzuki, T.; Shibata, H.; Ishii, S.; Shiiba, K.I.; Matsuno, S.; Kanamaru, R.; Ishioka, C.
Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay
Cancer Res.
60
3147-3151
2000
Homo sapiens
Manually annotated by BRENDA team
Haas-Kogan, D.; Shalev, N.; Wong, M.; Mills, G.; Yount, G.; Stokoe, D.
Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC
Curr. Biol.
8
1195-1198
1998
Homo sapiens
Manually annotated by BRENDA team
Hlobilkova, A.; Guldberg, P.; Thullberg, M.; Zeuthen, J.; Lukas, J.; Bartek, J.
Cell cycle arrest by the PTEN tumor suppressor is target cell specific and may require protein phosphatase activity
Exp. Cell Res.
256
571-577
2000
Homo sapiens
Manually annotated by BRENDA team
Goberdhan, D.C.I.; Wilson, C.
PTEN: Tumour suppressor, multifunctional growth regulator and more
Hum. Mol. Genet.
12
R239-R248
2003
Homo sapiens
-
Manually annotated by BRENDA team
Maehama, T.; Dixon, J.E.
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
J. Biol. Chem.
273
13375-13378
1998
Homo sapiens
Manually annotated by BRENDA team
Vazquez, F.; Ramaswamy, S.; Nakamura, N.; Sellers, W.R.
Phosphorylation of the PTEN tail regulates protein stability and function
Mol. Cell. Biol.
20
5010-5018
2000
Homo sapiens
Manually annotated by BRENDA team
Paramio, J.M.; Navarro, M.; Segrelles, C.; Gomez-Casero, E.; Jorcano, J.L.
PTEN tumour suppressor is linked to the cell cycle control through the retinoblastoma protein
Oncogene
18
7462-7468
1999
Homo sapiens
Manually annotated by BRENDA team
Georgescu, M.M.; Kirsch, K.H.; Akagi, T.; Shishido, T.; Hanafusa, H.
The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region
Proc. Natl. Acad. Sci. USA
96
10182-10187
1999
Homo sapiens
Manually annotated by BRENDA team
Ramaswamy, S.; Nakamura, N.; Vazquez, F.; Batt, D.B.; Perera, S.; Roberts, T.M.; Sellers, W.R.
Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway
Proc. Natl. Acad. Sci. USA
96
2110-2115
1999
Homo sapiens
Manually annotated by BRENDA team
Vinciguerra, M.; Foti, M.
PTEN and SHIP2 phosphoinositide phosphatases as negative regulators of insulin signalling
Arch. Physiol. Biochem.
112
89-104
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Redfern, R.E.; Redfern, D.; Furgason, M.L.; Munson, M.; Ross, A.H.; Gericke, A.
PTEN phosphatase selectively binds phosphoinositides and undergoes structural changes
Biochemistry
47
2162-2171
2008
Homo sapiens
Manually annotated by BRENDA team
Semba, S.; Satake, S.; Matsushita, M.; Yokozaki, H.
Phosphatase activity of nuclear PTEN is required for CDX2-mediated intestinal differentiation of gastric carcinoma
Cancer Lett.
274
143-150
2009
Homo sapiens
Manually annotated by BRENDA team
Qiu, W.; Federico, L.; Naples, M.; Avramoglu, R.K.; Meshkani, R.; Zhang, J.; Tsai, J.; Hussain, M.; Dai, K.; Iqbal, J.; Kontos, C.D.; Horie, Y.; Suzuki, A.; Adeli, K.
Phosphatase and tensin homolog (PTEN) regulates hepatic lipogenesis, microsomal triglyceride transfer protein, and the secretion of apolipoprotein B-containing lipoproteins
Hepatology
48
1799-1809
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Leslie, N.R.; Batty, I.H.; Maccario, H.; Davidson, L.; Downes, C.P.
Understanding PTEN regulation: PIP2, polarity and protein stability
Oncogene
27
5464-5476
2008
Homo sapiens
Manually annotated by BRENDA team
Rahdar, M.; Inoue, T.; Meyer, T.; Zhang, J.; Vazquez, F.; Devreotes, P.N.
A phosphorylation-dependent intramolecular interaction regulates the membrane association and activity of the tumor suppressor PTEN
Proc. Natl. Acad. Sci. USA
106
480-485
2009
Homo sapiens
Manually annotated by BRENDA team
Fan, C.; He, L.; Kapoor, A.; Rybak, A.P.; De Melo, J.; Cutz, J.C.; Tang, D.
PTEN inhibits BMI1 function independently of its phosphatase activity
Mol. Cancer
8
98
2009
Homo sapiens
Manually annotated by BRENDA team
Kini, V.; Chavez, A.; Mehta, D.
A new role for PTEN in regulating transient receptor potential canonical channel 6-mediated Ca2+ entry, endothelial permeability, and angiogenesis
J. Biol. Chem.
285
33082-33091
2010
Homo sapiens
Manually annotated by BRENDA team
Langlois, M.J.; Bergeron, S.; Bernatchez, G.; Boudreau, F.; Saucier, C.; Perreault, N.; Carrier, J.C.; Rivard, N.
The PTEN phosphatase controls intestinal epithelial cell polarity and barrier function: role in colorectal cancer progression
PLoS ONE
5
e15742
2010
Homo sapiens
Manually annotated by BRENDA team
Kurokawa, T.; Takasuga, S.; Sakata, S.; Yamaguchi, S.; Horie, S.; Homma, K.J.; Sasaki, T.; Okamura, Y.
3'Phosphatase activity toward phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2] by voltage-sensing phosphatase (VSP)
Proc. Natl. Acad. Sci. USA
109
10089-10094
2012
Ciona intestinalis, Homo sapiens
Manually annotated by BRENDA team
Zhou, H.M.; Sun, Q.X.; Cheng, Y.
Paeonol enhances the sensitivity of human ovarian cancer cells to radiotherapy-induced apoptosis due to downregulation of the phosphatidylinositol-3-kinase/Akt/phosphatase and tensin homolog pathway and inhibition of vascular endothelial growth factor
Exp. Ther. Med.
14
3213-3220
2017
Homo sapiens (P60484)
Manually annotated by BRENDA team
Chen, Z.; Dempsey, D.R.; Thomas, S.N.; Hayward, D.; Bolduc, D.M.; Cole, P.A.
Molecular features of phosphatase and tensin homolog (PTEN) regulation by C-terminal phosphorylation
J. Biol. Chem.
291
14160-14169
2016
Homo sapiens (P60484)
Manually annotated by BRENDA team