CATH Classification

Domain Context

CATH Clusters

Superfamily 2.60.40.1110
Functional Family Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Enzyme Information

3.1.3.16
Protein-serine/threonine phosphatase.
based on mapping to UniProt P60484
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
-!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
3.1.3.67
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase.
based on mapping to UniProt P60484
Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate.
-!- Does not dephosphorylate inositol 4,5-bisphosphate. -!- This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3,4,5)P(4) to Ins(1,4,5)P(3).
3.1.3.48
Protein-tyrosine-phosphatase.
based on mapping to UniProt P60484
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
-!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.

UniProtKB Entries (1)

P60484
PTEN_HUMAN
Homo sapiens
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

PDB Structure

PDB 5BZZ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Redox Modulation of PTEN Phosphatase Activity by Hydrogen Peroxide and Bisperoxidovanadium Complexes.
Lee, C.U., Hahne, G., Hanske, J., Bange, T., Bier, D., Rademacher, C., Hennig, S., Grossmann, T.N.
Angew.Chem.Int.Ed.Engl.