title: Phosphorylation of p53 in normal and simian virus 40-transformed NIH 3T3 cells.
abstract: We observed six major tryptic phosphopeptides in p53 from simian virus 40-transformed and normal NIH 3T3 cells. Analyses of the phosphopeptides indicated that serines 37, 310 and/or 312, 389 and one or more of serines 7, 9, 12, 18, and 23 were phosphorylated. Phosphorylation of serines 310 and/or 312 was twofold higher in the simian virus 40-transformed cells as compared with that in normal NIH 3T3 cells.
authors.affiliation: Molecular Biology and Virology Laboratory, Salk Institute for Biological Studies, San Diego, California 92138.
authors.forename: D W
authors.initials: DW
authors.lastname: Meek
authors.forename: W
authors.initials: W
authors.lastname: Eckhart
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002472:Cell Transformation, Viral; D002918:Chymotrypsin; D051379:Mice; D009363:Neoplasm Proteins / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D013539:Simian virus 40 / Q000235:genetics; D014357:Trypsin; D016159:Tumor Suppressor Protein p53
chemical_list: D009363:Neoplasm Proteins; D010446:Peptide Fragments; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53; D010768:Phosphoserine; D002918:Chymotrypsin; D014357:Trypsin