Given the small size of the protein, lyophylization has a good chance to work.  Especially if the protein is loosely folded or unstructured and does not have a strong tendency to agregate. The best is to try and check on gel filtration that the rehydrated protein has the expected behavior. Freezing could also work but may require some buffer optimization - for example addition of glycerol.

Lyophylization can be done provided that its structure is not influenced by dehydration  or salts if any 

Cédric Leyrat  Sir will it affect the In vitro phosphorylated  protein?

I don't see why the phosphorylation should be affected by the lyophylization.