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Information on EC 3.1.3.67 - phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and Organism(s) Rattus norvegicus and UniProt Accession O54857
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3.1.3.67 phosphatidylinositol-3,4,5-trisphosphate 3-phosphataseIUBMB 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
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Word Map
- 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
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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-
-
-
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
210488-47-4
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SUBSTRATE
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
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidyl inositol 4,5-bisphosphate + phosphate
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-
-
?
phosphatidylinositol-3,4-bisphosphate + H2O
phosphatidylinositol-4-monophosphate + phosphate
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-
-
?
additional information
?
-
-
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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-
?
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
additional information
?
-
-
PTEN directly downregulates neurotophin receptor (p75NTR) expression by decreasing DNA-binding activity of transcription factor Sp1
-
-
?
additional information
?
-
-
PTEN is a dual specificity phosphatase capable of dephosphorylating both lipid and protein substrates
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Laminin
-
laminin medium induces PTEN upregulation decreases transcription factor Sp1-binding activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). O54857_RAT
403
0
47118
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
recombinant PTEN is phosphorylated in the infected insect cells at Ser-380, Thr-382, and Thr-383 at the C-terminal tail
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C124S
-
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant PTEN is purified to near homogeneity using four sequential column chromatographic steps: a diethylaminoethyl (DEAE) Sepharose anion exchange column, a bio-gel hydroxyapatite HT (HAP) column, a Mono-S cation exchange column, and a Mono-Q anion exchange column
treatment with alkaline phosphatase fully dephosphorylates the phosphorylation sites. Unphosphorylated PTEN and alkaline phosphatase can be separated by ion exchange column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PTEN is ligated into the pBacPAK9 baculovirus transfer vector. Sf9 cells are infected with the recombinant PTEN baculovirus
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
availability of the phosphorylated and unphosphorylated forms of recombinant PTEN permits future investigations into the three-dimensional structures of the phosphorylated and unphosphorylated forms of PTEN, and the role of phosphorylation in regulating PTEN activity, phospholipid- and protein-binding affinities
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gajewski, J.E.; Bird, M.J.; Crowhurst, M.O.; Sio-Seng Lio, D.; Liu, J.; Wettenhall, R.E.; Zhu, H.J.; Cheng, H.C.
Expression, generation, and purification of unphosphorylated and phospho-Ser-380/Thr-382/Thr-383 form of recombinant PTEN phosphatase
Protein Expr. Purif.
55
334-342
2007
Rattus norvegicus (O54857)
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