Allosteric regulation of proteins is widely present in biological systems as an efficient way of function control.Existing theoretical models can only explain the regulation mechanisms in a limited number of proteins.Currently,it is still impossible to predict the specific allosteric regulation mechanism that a protein of interest uses,and difficult to design allosteric effector molecules targeting specific functions.We have developed methods for protein allosteric site prediction for cases with large conformational changes or with no obvious conformational changes.By using an elastic network model,we found that residues in allosteric site are highly correlated with those in the functional site.