BAIT

MTOR

FRAP, FRAP1, FRAP2, RAFT1, RAPT1
mechanistic target of rapamycin (serine/threonine kinase)
GO Process (30)
GO Function (9)
GO Component (11)
Homo sapiens
PREY

EP300

KAT3B, RSTS2, p300, RP1-85F18.1
E1A binding protein p300
GO Process (29)
GO Function (15)
GO Component (3)

Gene Ontology Cellular Component

Homo sapiens

Biochemical Activity (Phosphorylation)

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

mTORC1 Phosphorylates Acetyltransferase p300 to Regulate Autophagy and Lipogenesis.

Wan W, You Z, Xu Y, Zhou L, Guan Z, Peng C, Wong CCL, Su H, Zhou T, Xia H, Liu W

Acetylation is increasingly recognized as one of the major post-translational mechanisms for the regulation of multiple cellular functions in mammalian cells. Acetyltransferase p300, which acetylates histone and non-histone proteins, has been intensively studied in its role in cell growth and metabolism. However, the mechanism underlying the activation of p300 in cells remains largely unknown. Here, we identify the homeostatic sensor ... [more]

Mol. Cell Oct. 19, 2017; 68(2);323-335.e6 [Pubmed: 29033323]

Throughput

  • Low Throughput

Additional Notes

  • Phosphorylation sites identified by MS: Ser2271, Ser2279, Ser2291, and Ser2315

Curated By

  • BioGRID