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|Functional site class:||PKA Phosphorylation site|
|Functional site description:||Motifs phosphorylated by a subset of AGC group kinases including PKA that all have similar sequence specificity.|
|Description:||The optimal phosphorylation site preference for PKA is RR.(ST) - Lysine in the basic sites may weaken the prefence. This site is also targeted by other basophilic kinases of the AGC group, including PKG and PKC isoforms. AGC group kinases do not tolerate Pro at position +1. Lys at the Arg positions may be allowed in some weaker sites. Some specificity determinants may be present at the less conserved non-basic sites.|
|Pattern:||[RK][RK].([ST])[^P].. (Probability: 0.0023151)|
|Present in taxons:||Eukaryota|
PKA belongs to the large set of related AGC kinases having a preference for phosphorylating basophilic sites. cAMP-dependent protein kinase A (PKA) is the major target for cAMP action in eukaryotic cells. The enzyme is allosterically activated by binding of cAMP to two regulatory ( R ) subunits which induces dissociation of two catalytic ( C ) subunits. The active kinase is then free to phosphorylate substrates on serine, or less commonly threonine residues in recognition motifs. The enzyme acts or a wide number of proteins involved in several biochemical processes. These include glucose metabolism (via activation and inactivation of glycogen phosphorylase b and glycogen synthase respectively), fatty acid synthesis (via acetyl-coA carboxylase), pyruvate oxidation (via pyruvate dehyrogenase complex).
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