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  • Title: Phosphoserine in peptide substrates can specify casein kinase II action.
    Author: Hrubey TW, Roach PJ.
    Journal: Biochem Biophys Res Commun; 1990 Oct 15; 172(1):190-6. PubMed ID: 2171517.
    Abstract:
    Casein kinase II is a ubiquitous serine/threonine protein kinase which utilizes acidic amino acid residues as recognition determinants in its substrates, the motif -S/T-X-X-D/E- being particularly important. To test whether a phosphoserine residue can act as a substrate determinant, a peptide was synthesized, containing the sequence -S-X-X-S, which was not phosphorylated by casein kinase II. However, upon phosphorylation at the +3 position, the peptide became a substrate for casein kinase II. With another peptide, a positive influence of more distal phosphorylations was found. The results indicate the potential for casein kinase II to participate in hierarchal phosphorylation schemes.
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