Related Experiment Video
Updated: Jun 26, 2026

Yeast As a Chassis for Developing Functional Assays to Study Human P53
Published on: August 4, 2019
Identification of new p53 acetylation sites in COS-1 cells
Anita Joubel1, Robert J Chalkley, Katalin F Medzihradszky
1Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517, USA.
Abstract:
The p53 tumor suppressor protein is a key regulator of cell cycle and death that is involved in many cell signaling pathways and is tightly regulated in mammalian cells. Post-translational modifications of p53 have been investigated previously mainly using antibodies. In this study, utilizing LC-MS/MS analysis, we have characterized p53 protein from COS-1 cells. Several already known post-translational modifications were observed, such as phosphorylation on serines 15, 33, 315, and 392 as well as acetylation on lysines 305, 370, 372, 373, 381, 382, and 386. Interestingly novel acetylation sites were identified at lysines 319 and 357. This study confirmed that p53 is a highly acetylated protein and revealed new acetylation sites that might aid the further understanding of p53 regulation.
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Abnormal Proliferation
Spreading of Chromatin Modifications
Writers
The writer is an enzyme that can...
Histone Variants at the Centromere
DNA Damage Can Stall the Cell Cycle

