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Comparative Study
. 1992 Dec 15;189(2):1223-30.
doi: 10.1016/0006-291x(92)92335-u.

Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase

Affiliations
Comparative Study

Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase

M Takekawa et al. Biochem Biophys Res Commun. .

Abstract

We have cloned and characterized a human cDNA encoding a new member of the family of cytosolic type protein-tyrosine-phosphatase (PTP), designated as PTPG1, from an adult colon tissue cDNA library by using the PCR product as probe. We obtained 5 cDNA clones, which cover the predicted open reading frame encoding a 88-kDa protein composed of 780 amino acids, and it had no apparent signal or transmembrane sequences, suggesting that it is a cytosolic protein. The N-terminal region had a PTP catalytic domain that is 30-40% identical to previously reported human PTPs. This revealed that the enzyme composes an additional family of human PTPs. PTPG1 was characterized by a long non-enzymatic domain located at the C-terminus, including PEST sequences which are characteristic for short half-life proteins in eukaryotes. Northern blot analysis of PTPG1 mRNA showed a 4.6-kb transcript that was detected in a wide variety of cell lines to suggest its extensive expression.

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