EC Number   |
Protein Variants |
Reference |
|---|
   2.7.11.15 | C221V |
site-directed mutagenesis, mutant GRK2 activity is slightly increased compared to the wild-type enzyme, the requirement for initial ligand-induced internalization of a G protein-coupled receptor with subsequent rounds of internalization is different for the mutant GRK2 compared to the wild-type enzyme |
662417 |
| 2.7.11.15 | D110A |
site-directed mutagenesis, GRK2 mutant deficient in Galphaq/11 binding |
662363 |
| 2.7.11.15 | D110A |
the expression of the D110A mutant in COS7-transfected cells fails to desensitize the histamine H2 receptor |
725436 |
| 2.7.11.15 | D110A |
the Galphaq binding site mutant of GRK 2 inhibits the inositol phosphate signal significantly less than wild-type GRK2, the mutant GRK 2 D110A still inhibitS inositol phosphate formation by 22.35 |
686401 |
| 2.7.11.15 | D110A |
the mutant shows impaired binding to Galphaq proteins, mutant GRK2 inhibits ERK phosphorylation similar to the wild-type enzyme when co-expressed with CCR2B in HEK-293 cells |
662818 |
| 2.7.11.15 | D110A |
the point mutation within the RH domain abrogates GRK2 sequestration of activated GTP-boundGalphaq/11 |
674729 |
| 2.7.11.15 | D110A/K220R |
double mutant has a disrupted RGS (regulator of G protein signalling) function. Although double mutant coimmunoprecipitates with the histamine H2 receptor, it reverses GRK2K220R-mediated histamine H2 receptor desensitization |
725436 |
| 2.7.11.15 | D110A/K220R |
site-directed mutagenesis, inactive GRK2 mutant deficient in Galphaq/11 binding |
662363 |
| 2.7.11.15 | D110A/K220R |
the mutant inhibits the inositol phosphate signal significantly less than wild-type GRK2, but does not differ significantly from wild-type GRK2 in its ability to inhibit calcium-sensing receptor signaling |
686401 |
| 2.7.11.15 | D110A/K220R |
the mutant, which exhibits no RH or kinase activity, is completely defective in its ability to attenuate M33 signaling |
674729 |
