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XB-ART-24987
J Biol Chem 1991 Mar 15;2668:5249-55.
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Purification and characterization of ribosomal protein S6 kinase I from Xenopus eggs.

Erikson E , Maller JL .


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Ribosomal protein S6 kinase I has been purified from unfertilized Xenopus eggs to near homogeneity as a Mr = 90,000 protein. S6 kinase I is phosphorylated when activated in vivo and can be phosphorylated by mitogen-activated protein kinase in vitro. The purified enzyme is inactivated upon treatment with protein phosphatase 2A. Immunological data and analysis of substrate specificity demonstrate that S6 kinase I is related to, but distinct from, the previously characterized S6 kinase II. Both enzymes are members of the ribosomal protein S6 kinase (rsk) gene family.

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Species referenced: Xenopus
Genes referenced: ptpa rps6ka1 rps6ka3