一种新型蛋白磷酸酶1结合蛋白（R5）的氨基酸序列，该蛋白与蛋白磷酸酶1的肝脏和肌肉特异性糖原结合亚基相关。

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.

作者信息

Doherty M J, Young P R, Cohen P T

机构信息

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

出版信息

FEBS Lett. 1996 Dec 16;399(3):339-43. doi: 10.1016/s0014-5793(96)01357-9.

DOI:10.1016/s0014-5793(96)01357-9

PMID:8985175

Abstract

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).

摘要

对一个编码分子量为36 kDa的新型人类蛋白磷酸酶1（PP1）结合亚基的全长cDNA进行了测序，该亚基称为PPP1R5。PPP1R5与大鼠肝脏PP1的糖原结合亚基（G(L)）有42%的同源性，与人类骨骼肌PP1的糖原结合亚基（G(M)）的N端区域有28%的同源性。与G(L)一样，PPP1R5调节PP1的特异性，但它与G(L)的不同之处在于，除肝脏外，它还存在于多种组织中。PPP1R5的氨基酸序列和特性表明，它不像G(M)和G(L)那样受到激素相同模式的共价和变构调节。