C-terminal A-band: is thought to act as a protein-ruler and possesses kinase activity.

Therefore, it is an effective method of turning 'on' and 'off' kinase activity.

With a very poor intrinsic kinase activity, they were long thought to be inactive, until their catalytic activity was finally demonstrated in recent years.

It results in the occlusion of the catalytic site and full shutdown of kinase activity.

The kinase activity of the fusion protein is inhibited by crizotinib.

This demonstrates that Rad3 has a biochemical activity in addition to its catalytic kinase activity.

Tyr-857 has therefore been assigned a role in positive regulation of kinase activity.

GRKs regulate also cellular responses independent of their kinase activity.

The effect comes from outside of the cell membrane and does not depend on G-proteins or kinase activity inside the cell.

Full kinase activity requires an activating phosphorylation on a threonine adjacent to the active site.