Title : Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain.

Pub. Date : 1991 Aug 5

PMID : 1650359






3 Functional Relationships(s)
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1 The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain. Serine myristoylated alanine rich protein kinase C substrate Homo sapiens
2 The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain. Serine myristoylated alanine rich protein kinase C substrate Homo sapiens
3 Thus, the phosphorylation site domain peptide of the MARCKS protein is a high affinity substrate for protein kinase C in vitro; the cognate peptide containing no serines is a potent but not completely specific inhibitor of both protein kinase C and its catalytic fragment. Serine myristoylated alanine rich protein kinase C substrate Homo sapiens