|<< MOD_PLK <<||Menu||>> MOD_SPalmitoyl_2 >>|
|Functional site class:||MAPK Phosphorylation Site|
|Functional site description:||Site at which MAP Kinase phosphorylates substrates|
|Description:|| (S/T)P Site at which Pro-directed kinases such as P38 MAP Kinase phosphorylate Ser/Thr in various signal transduction pathways. These kinases require a docking motif to be activated so the site is not meaningful of itself.
MAP Kinase homologues are found widely in eukaryota, including protozoa, but experimental data is from higher eukaryotes, mainly metazoa.
|Pattern:||...([ST])P.. (Probability: 0.0154332)|
|Present in taxons:||Drosophila melanogaster Eukaryota Vertebrata|
So-called proline-directed kinases phosphorylate a Ser/Thr residue preceding a Pro residue. This low specificity site is recognised by a large family of MAP and CDK-like kinases. However, the kinases achieve their target substrate specificity through separate docking motifs which are also required to activate the kinase enzymatic function. A docking motif should be present in a candidate substrate sequence - or any (S/T)P motifs are unlikely to be meaningful. For example the P38 MAP kinase is activated by motifs approximating to (R/K)XXXX#X# where # is a hydrophobic residue (Chang et al. (2002) 12086621) and ERK kinase is also activated by FxFP-like motifs (Fantz et al. (2001) 11371562).
(click table headers for sorting)