BAIT

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 (Acetylation)

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

Structural and Mechanistic Insights into the Regulation of the Fundamental Rho Regulator RhoGDIα by Lysine Acetylation.

Kuhlmann N, Wroblowski S, Knyphausen P, de Boor S, Brenig J, Zienert AY, Meyer-Teschendorf K, Praefcke GJ, Nolte H, Krueger M, Schacherl M, Baumann U, James LC, Chin JW, Lammers M

Rho proteins are small GTP/GDP-binding proteins primarily involved in cytoskeleton regulation. Their GTP/GDP cycle is often tightly connected to a membrane/cytosol cycle regulated by the Rho guanine nucleotide dissociation inhibitor α (RhoGDIα). RhoGDIα has been regarded as a housekeeping regulator essential to control homeostasis of Rho proteins. Recent proteomic screens showed that RhoGDIα is extensively lysine-acetylated. Here, we present the ... [more]

J. Biol. Chem. Mar. 11, 2016; 291(11);5484-99 [Pubmed: 26719334]

Throughput

  • Low Throughput

Additional Notes

  • K178 most strongly acetylated, along with K43

Curated By

  • BioGRID