The PTEN phosphatase is found mutated in a diverse set of human cancers and is implicated in hereditary cancer disposition syndromes. PTEN can act on both peptide and phosphoinositide substrates (in vitro).
The structure of PTEN reveals a 2-domain arrangement, with the active site on the phosphatase domain and a second domain that has homology to C2 domains. C2 domains are associated with phospholipid membrane-binding activity in vitro, suggesting a role in substrate recruitment and orientation toward the active site.
