BAIT

PPP2R1A

PP2A-Aalpha, PP2AAALPHA, PR65A
protein phosphatase 2, regulatory subunit A, alpha
Homo sapiens
PREY

AKT1

AKT, CWS6, PKB, PKB-ALPHA, PRKBA, RAC, RAC-ALPHA
v-akt murine thymoma viral oncogene homolog 1
GO Process (73)
GO Function (12)
GO Component (6)

Gene Ontology Biological Process

Homo sapiens

Biochemical Activity (Dephosphorylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

An ATP-site on-off switch that restricts phosphatase accessibility of Akt.

Lin K, Lin J, Wu WI, Ballard J, Lee BB, Gloor SL, Vigers GP, Morales TH, Friedman LS, Skelton N, Brandhuber BJ

The protein serine-threonine kinase Akt undergoes a substantial conformational change upon activation, which is induced by the phosphorylation of two critical regulatory residues, threonine 308 and serine 473. Paradoxically, treating cells with adenosine 5'-triphosphate (ATP)-competitive inhibitors of Akt results in increased phosphorylation of both residues. We show that binding of ATP-competitive inhibitors stabilized a conformation in which both phosphorylated sites ... [more]

Sci Signal May. 08, 2012; 5(223);ra37 [Pubmed: 22569334]

Throughput

  • Low Throughput

Curated By

  • BioGRID