Matches in Nanopublications for { ?s ?p "Their minimum consensus sequence Hyd-X-R-X-X-(S/T) (where Hyd is any hydrophobic amino acid), determined through peptide studies, provides only a rough template common to many protein kinases (11). Additional specificity is provided by residues adjacent to the phosphorylation site of the substrate, producing differences in substrate preference among these kinases. The differences can have important transcriptional implications; for example, although all three can phosphorylate CREB on the activating site Ser-133, only CaMKII phosphorylates an additional inhibitory site, Ser-142 (13). " ?g. }
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- _5 value "Their minimum consensus sequence Hyd-X-R-X-X-(S/T) (where Hyd is any hydrophobic amino acid), determined through peptide studies, provides only a rough template common to many protein kinases (11). Additional specificity is provided by residues adjacent to the phosphorylation site of the substrate, producing differences in substrate preference among these kinases. The differences can have important transcriptional implications; for example, although all three can phosphorylate CREB on the activating site Ser-133, only CaMKII phosphorylates an additional inhibitory site, Ser-142 (13). " provenance.
- _5 value "Their minimum consensus sequence Hyd-X-R-X-X-(S/T) (where Hyd is any hydrophobic amino acid), determined through peptide studies, provides only a rough template common to many protein kinases (11). Additional specificity is provided by residues adjacent to the phosphorylation site of the substrate, producing differences in substrate preference among these kinases. The differences can have important transcriptional implications; for example, although all three can phosphorylate CREB on the activating site Ser-133, only CaMKII phosphorylates an additional inhibitory site, Ser-142 (13). " provenance.
- _5 value "Their minimum consensus sequence Hyd-X-R-X-X-(S/T) (where Hyd is any hydrophobic amino acid), determined through peptide studies, provides only a rough template common to many protein kinases (11). Additional specificity is provided by residues adjacent to the phosphorylation site of the substrate, producing differences in substrate preference among these kinases. The differences can have important transcriptional implications; for example, although all three can phosphorylate CREB on the activating site Ser-133, only CaMKII phosphorylates an additional inhibitory site, Ser-142 (13). " provenance.
- _5 value "Their minimum consensus sequence Hyd-X-R-X-X-(S/T) (where Hyd is any hydrophobic amino acid), determined through peptide studies, provides only a rough template common to many protein kinases (11). Additional specificity is provided by residues adjacent to the phosphorylation site of the substrate, producing differences in substrate preference among these kinases. The differences can have important transcriptional implications; for example, although all three can phosphorylate CREB on the activating site Ser-133, only CaMKII phosphorylates an additional inhibitory site, Ser-142 (13). " provenance.