We investigate the universal scaling of protein fluctuation dynamics with a site-specific diffusive model of protein motion, which predicts an initial subdiffusive regime in the configurational relaxation. The long-time dynamics of proteins is controlled by an activated regime. We argue that the hierarchical free energy barriers set the time scales of biological processes and establish an upper limit to the size of single protein domains. We find it compelling that the scaling behavior for the protein dynamics is in close agreement with the Kardar-Parisi-Zhang scaling exponents.