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PMID:8463208

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Citation

McLaughlin, S and Dixon, JE (1993) Alternative splicing gives rise to a nuclear protein tyrosine phosphatase in Drosophila. J. Biol. Chem. 268:6839-42

Abstract

A novel Drosophila protein tyrosine phosphatase gene (dPTP61F) undergoes alternative splicing to encode two non-receptor-like proteins of 61,000 daltons. This splice selection occurs at the 3' end of the message, altering the carboxyl termini of the encoded proteins. These carboxyl-terminal sequences govern the targeting of each protein tyrosine phosphatase either to a cytoplasmic membrane or to the nucleus. The catalytic activity of the two protein products is indistinguishable, suggesting that substrate specificity is modulated by the protein's subcellular location.

Links

PubMed

Keywords

Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Cell Line; Cell Nucleus/enzymology; DNA; Drosophila; Fluorescent Antibody Technique; Humans; Molecular Sequence Data; Phosphorylation; Protein Tyrosine Phosphatases/genetics; Protein Tyrosine Phosphatases/metabolism; Sequence Homology, Amino Acid

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


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References

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