| Accession: | |
|---|---|
| Functional site class: | MAPK Phosphorylation Site |
| Functional site description: | Site at which MAP Kinase phosphorylates substrates. |
| ELM Description: | (S/T)P site at which Pro-directed kinases such as P38 MAP Kinase phosphorylate a Ser/Thr residue in various signal transduction pathways. These kinases require a docking motif to be activated, so the site is not meaningful by itself. MAP Kinase homologues are found widely in eukaryotes, including protozoa, but experimental data is from higher eukaryotes, mainly Metazoa. |
| Pattern: | ...([ST])P.. |
| Pattern Probability: | 0.0154332 |
| Present in taxons: | Drosophila melanogaster Eukaryota Vertebrata |
| Interaction Domain: |
Pkinase (PF00069)
Protein kinase domain
(Stochiometry: 1 : 1)
|
 Abstract |
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 motif is unlikely to be meaningful. For example, the P38 MAP kinase is activated by motifs approximating to [RK]XXXX#X# where # is a hydrophobic residue (Chang,2002) and ERK kinase is also activated by FxFP-like motifs (Fantz,2001). |
5 GO-Terms:
38 Instances for MOD_ProDKin_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Please cite:
ELM-the Eukaryotic Linear Motif resource-2024 update.
(PMID:37962385)
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement