EC Number   |
Posttranslational Modification |
Reference  |
|---|
   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 | more |
no autophosphorylation of beta-ARK 1 |
645028 |
| 2.7.11.15 | phosphoprotein |
GRK2 is phosphorylated by MAP kinase at S670 |
661202 |
| 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 | phosphoprotein |
GRK2 is phosphorylated by c-Src kinase, ERK1 and ERK2, protein kinase C, and PKA, overview |
661455 |
| 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 | 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 | phosphoprotein |
regulation of GRKs by other kinases, such as PKA, PKC, ERK1 and ERK2, e.g. GRK2 is phosphorylated at Ser670 by ERK1 or ERK2, phosphorylation of the beta-adrenergic receptor-activated GRK2 by c-SRC at tyrosine residues mediated by binding of beta-arrestin, which rapidly activates the GPCR phosphorylation activity of GRK2 and its degradation via the ubiquitine/proteosome pathway, overview |
662911 |
