2.7.11.15	additional information	GRK2 is ubiquinated after being tyrosine phosphorylated leading to its proteolytic degradation via the ubiquitine/proteasome pathway, regulation overview	662911	
2.7.11.15	additional information	mechanisms of regulation of GRK protein stability and degradation, e.g. via ubiquination or protease cleavage, overview	661455	
2.7.11.15	additional information	mechanisms of regulation of GRK protein stability and degradation, e.g. via ubiquitination or protease cleavage, overview	661455	
2.7.11.15	additional information	no autophosphorylation of beta-ARK 1	645028	
2.7.11.15	phosphoprotein	-	662401, 724779	
2.7.11.15	phosphoprotein	autophosphorylation, the site often depends more on structure than on primary sequence	490797	
2.7.11.15	phosphoprotein	enzyme appears to autophosphorylate	645001	
2.7.11.15	phosphoprotein	enzyme phosphorylation at Tyr-13, Try-86, and Try-92 by c-Src and phosphorylation at Ser-685 by protein kinase A are associated with increased enzyme activity, whereas phosphorylation at Ser-670 by CDK2/ERK1/2 negatively regulates enzyme activity	760331	
2.7.11.15	phosphoprotein	epinephrine-activated alpha2A-adrenergic receptor activates GRK2, interaction with GRK2 via the second and third intracellular loop of the receptor, determination of regions required for specific interaction and phosphorylation activity utilizing recombinant GST-tagged wild-type and several mutant alpha2A ARs, residues R225, R226, R218, K320, R322, and K358 are important, overview	662332	
2.7.11.15	phosphoprotein	GRK2 is activated by phosphorylation through c-Src, while phosphorylation by ERK inhibits GRK2	677232