PTEN

(phosphatase and tensin homolog (mutated in multiple advanced cancers 1))

 

  • Alias                                 (According to NCBI)

 
  • BZS,
  • MGC11227,
  • MHAM,
  • MMAC1,
  • PTEN1,
  • TEP1
  • MMAC1 phosphatase and tensin homolog deleted on chromosome 10;
  • mutated in multiple advanced cancers 1;
  • phosphatase and tensin homolog
  • Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue.
  • Location: 10q23.3
  • Size: 105338 bp
  • exons: 9
  • DNA sequence (Human): NC_000010.9

  • CGH (10q23.3):  Losses (%) -7.8   Gain (%) 2.2  

  • Mutations and SNPs (According to HGMD and SNP)

 

 
  • m-RNA                       (According to NCBI and CGAP)

 

  • mRNA sequence (Human):  NM_000314.4

  • Size: 5572 bp

  • cDNA libraries:

  • Size:403 amino acids: 47166 Da
  • Catalytic activity:

    Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate.

    A phosphoprotein + H(2)O = a protein + phosphate.

    Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.

  • Subcellular location:

  • Protein domains Cytoplasm.

     

  • Protein sequence (Human): P60484

  • Homologous genes:  265

  • 2D PAGE:

  • 3D Structure:  1D5R

  • PTM: PTEN (Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit and promote PDZ-binding.)

 

                        

  • Protein interactions: PTEN
  • Clinical                            (According to OMIM, PubMed)