Primary structure polymorphism at amino acid residue 72 of human p53.

Molecular and cellular biology ·Vol. 7 ·No. 2 ·1987-02-00 ·Pages 961-3

Matlashewski GJ, Tuck S, Pim D, Lamb P, Schneider J, Crawford LV

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

Amino Acid Sequence Animals Cell Transformation, Neoplastic/genetics Humans Mice Neoplasm Proteins/genetics Neoplasms/genetics Neoplasms, Experimental/genetics Phosphoproteins/genetics Polymorphism, Genetic Tumor Suppressor Protein p53

Chemicals

Neoplasm Proteins Phosphoproteins Tumor Suppressor Protein p53

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Matlashewski G J

Tuck S

Pim D

Lamb P

Schneider J

Crawford L V

References (16)

16 references, click to expand

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Article Info

Journal

Molecular and cellular biology

Abbr.

Mol Cell Biol

ISSN

0270-7306

DOI

10.1128/mcb.7.2.961-963.1987

Published

1987-02-00

Pages

961-3

Language

English

Region

United States

NLM ID

8109087

PMCID

PMC365159

Subset

External Links

PubMed source DOI: 10.1128/mcb.7.2.961-963.1987 PMC Full Text View journal details

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Primary structure polymorphism at amino acid residue 72 of human p53.

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