phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase
Aspergillus awamori acid protein phosphatase
phosphopyruvate dehydrogenase phosphatase
branched-chain alpha-keto acid dehydrogenase phosphatase
3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase
phosphoprotein phosphatase (phosphotyrosine)
PTEN: sometimes taking it off can be better than putting it on.
A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast.
P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase.
Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association.
Structural assets of a tumor suppressor.
Analysis of the cellular functions of PTEN using catalytic domain and C-terminal mutations: differential effects of C-terminal deletion on signalling pathways downstream of phosphoinositide 3-kinase.
The Cold Spring Harbor Laboratory meeting on tyrosine phosphorylation and cell signaling. Cold Spring Harbor, NY, USA, May 12-16, 1999.
Stabilization and productive positioning roles of the C2 domain of PTEN tumor suppressor.
Antagonism of PI 3-kinase-dependent signalling pathways by the tumour suppressor protein, PTEN.
Regulation of PTEN binding to MAGI-2 by two putative phosphorylation sites at threonine 382 and 383.
The murine orthologue of the Golgi-localized TPTE protein provides clues to the evolutionary history of the human TPTE gene family.
PTEN 2, a Golgi-associated testis-specific homologue of the PTEN tumor suppressor lipid phosphatase.
Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway.
The myotubularin family: from genetic disease to phosphoinositide metabolism.
Some protein tyrosine phosphatases target in part to lipid rafts and interact with caveolin-1.
PTEN: The down side of PI 3-kinase signalling.
PHOSPHORYLATION OF THR-366; SER-370 AND SER-385
Direct identification of PTEN phosphorylation sites.
Membrane-binding and activation mechanism of PTEN.
The C-terminal of this enzyme, which seems to be phosphorylated, is not included in the PDB structure. According to the literature [4], Cys124, Arg130 and Asp92 are catalytic residues. Asp92 acts as a general acid, to protonate the leaving, phonolic oxgen atom. As the catalytic domain of this enzyme is homologous to dual specificity protein phosphatase 3 (Swiss-prot;P51452; S00458 in EzCatDB), the catalytic mechanism can be similar to that. In the protein phosphatase 3, Ser131 facilitates the reaction by interacting with the thiol group of Cys124. The corresponding residue, Thr131 also seems to interact with Cys124 in this enzyme structure (PDB; 1d5r).