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FEBS Lett. 1996 Dec 16;399(3):339-43.

Amino acid sequence of a novel protein phosphatase 1 binding protein (R5) which is related to the liver- and muscle-specific glycogen binding subunits of protein phosphatase 1.

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Medical Research Council Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Scotland, UK.


A full-length cDNA encoding a novel human protein phosphatase 1 (PP1) binding subunit of molecular mass 36 kDa, termed PPP1R5, was sequenced. PPP1R5 shows 42% identity to the glycogen binding subunit (G(L)) of PP1 from rat liver and 28% identity to the N-terminal region of the glycogen binding subunit (G(M)) of PP1 from human skeletal muscle. Like G(L), PPP1R5 modulates the specificity of PP1, but it differs from G(L) in being present in a wide variety of tissues, besides liver. The amino acid sequence and properties of PPP1R5 indicate that it is not subject to the same modes of covalent and allosteric regulation by hormones as are G(M) and G(L).

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