title: Primary structure polymorphism at amino acid residue 72 of human p53.
abstract: We analyzed p53 cDNA and genomic clones from a variety of normal and transformed cells. Sequence analysis of these clones revealed that amino acid residue 72 can be an arginine, proline, or cysteine. This single codon difference results in electrophoretically distinct forms of human p53 seen in normal and transformed cells.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002471:Cell Transformation, Neoplastic / Q000235:genetics; D006801:Humans; D051379:Mice; D009363:Neoplasm Proteins / Q000235:genetics*; D009369:Neoplasms / Q000235:genetics; D009374:Neoplasms, Experimental / Q000235:genetics; D010750:Phosphoproteins / Q000235:genetics*; D011110:Polymorphism, Genetic; D016159:Tumor Suppressor Protein p53
chemical_list: D009363:Neoplasm Proteins; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53