Molecular cloning and characterization of a novel human protein phosphatase 2C cDNA (PP2C epsilon*).

Mol Biol Rep

State Key Laboratory of Genetic Engineering, Institute of Genetics, School of life Sciences, Fudan University, Shanghai 200433, People's Republic of China.

Published: September 2004

We have isolated a novel cDNA from the human fetal brain cDNA library with homology to the Mg2+ -dependent serine/threonine protein phosphatase 2C (PP2C) family. The cDNA is 3055 bp in length, and the predicted coding region encodes a 360-amino-acid protein, which shows 99% identity to the PP2C epsilon from rat and mouse. Then we term it human PP2C epsilon gene. The gene is mapped to chromosome 3q26.1 and contains 4 exons. RT-PCR analysis shows that the PP2C epsilon is widely expressed in human tissues and the expression levels in heart, placenta, lung, liver, kidney, and pancreas are relatively high.

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http://dx.doi.org/10.1023/b:mole.0000043624.96006.ebDOI Listing

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Molecular cloning and characterization of a novel human protein phosphatase 2C cDNA (PP2C epsilon*).

Mol Biol Rep

September 2004

State Key Laboratory of Genetic Engineering, Institute of Genetics, School of life Sciences, Fudan University, Shanghai 200433, People's Republic of China.

We have isolated a novel cDNA from the human fetal brain cDNA library with homology to the Mg2+ -dependent serine/threonine protein phosphatase 2C (PP2C) family. The cDNA is 3055 bp in length, and the predicted coding region encodes a 360-amino-acid protein, which shows 99% identity to the PP2C epsilon from rat and mouse. Then we term it human PP2C epsilon gene.

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