EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   2.7.11.15 | more |
domain structure |
Bos taurus |
? |
- |
? |
| 2.7.11.15 | more |
beta-ARK interacts rapidly with a high affinity binding site present in salt-stripped rat liver microsomal membranes, modulation of binding of enzyme |
Bos taurus |
? |
- |
? |
| 2.7.11.15 | more |
mechanism and significance of the PH-domain function |
Bos taurus |
? |
- |
? |
| 2.7.11.15 | more |
phosphorylates G protein coupled receptors in an agonist-dependent manner |
Bos taurus |
? |
- |
? |
| 2.7.11.15 | more |
role of the PH domain, ligand binding characteristics of the PH domain, distinct role for each ligand, i.e. betagamma subunits of G proteins and phosphatidylinositol 4,5-bisphosphate, in enzyme-mediated receptor phosphorylation |
Bos taurus |
? |
- |
? |
| 2.7.11.15 | more |
beta-ARK 1 phosphorylates beta2-AR and other G protein-coupled receptors, substrate recognition mechanism, consensus sequence required for substrates, 3-dimensional model structure of the catalytic domain, residues 188-436 |
Homo sapiens |
? |
- |
? |
| 2.7.11.15 | more |
not: alpha1-adrenergic receptor |
Bos taurus |
? |
- |
? |
| 2.7.11.15 | more |
not: casein, histones |
Mus musculus |
? |
- |
? |
| 2.7.11.15 | more |
rhodopsin kinase, EC 2.7.11.14, is also capable of beta-adrenergic receptor phosphorylation |
Bos taurus |
? |
- |
? |
| 2.7.11.15 | more |
very poor substrates: casein, phosvitin |
Bos taurus |
? |
- |
? |
