BAIT

PTEN

10q23del, BZS, CWS1, DEC, GLM2, MHAM, MMAC1, PTEN1, TEP1
phosphatase and tensin homolog
GO Process (64)
GO Function (11)
GO Component (10)

Gene Ontology Biological Process

Homo sapiens
PREY

DLG1

DLGH1, SAP-97, SAP97, dJ1061C18.1.1, hdlg
discs, large homolog 1 (Drosophila)
GO Process (17)
GO Function (11)
GO Component (17)
Homo sapiens

Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

Publication

Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex.

Vazquez F, Grossman SR, Takahashi Y, Rokas MV, Nakamura N, Sellers WR

PTEN is a tumor suppressor protein that functions, in large part, by dephosphorylating the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate and by doing so antagonizing the action of phosphoinositide 3-kinase. PTEN structural domains include an N-terminal phosphatase domain, a lipid-binding C2 domain, and a 50-amino acid C-terminal tail that contains a PDZ binding sequence. We showed previously that phosphorylation of the ... [more]

J. Biol. Chem. Dec. 28, 2001; 276(52);48627-30 [Pubmed: 11707428]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PTEN DLG1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID