EC Number |
Posttranslational Modification |
Reference |
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2.7.11.15 | more |
GRK2 is ubiquinated after being tyrosine phosphorylated leading to its proteolytic degradation via the ubiquitine/proteasome pathway, regulation overview |
662911 |
2.7.11.15 | more |
mechanisms of regulation of GRK protein stability and degradation, e.g. via ubiquination or protease cleavage, overview |
661455 |
2.7.11.15 | more |
mechanisms of regulation of GRK protein stability and degradation, e.g. via ubiquitination or protease cleavage, overview |
661455 |
2.7.11.15 | more |
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 |