Proteins controlling mineralization in vivo are diverse, suggesting that there are various ways by which mineralization can be directed in bioinspired approaches. While well-defined three-dimensional (3D) structures occur in biomineralization proteins, the design of synthetic, soluble, bioinspired macromolecules with specific, reproducible, and predictable 3D arrangements of mineral-interacting functions poses an ultimate challenge. Thus, the question of how certain arrangements of such functions on protein surfaces influence mineralization and in what ways specific alterations subsequently affect this process remains elusive. Here we used genetically engineered ubiquitin (Ub) proteins in order to overcome the limitations of generic bioinspired additive systems. By advancing existing protocols, we introduced an unnatural amino acid and subsequently mineral-interacting functions via selective-pressure incorporation and click chemistry, respectively, without affecting the Ub secondary structure. Indeed, as-obtained Ub with three phosphate functions at defined positions shows unique effects based on a yet-unmatched capability toward the stabilization of a film of a dense liquid mineral phase visible even with the naked eye and its transformation into amorphous nanoparticles and afterward crystals with complex shapes. We thereby demonstrate that Ub designer proteins pose a unique new generation of crystallization additives where the 3D arrangement of mineral-interacting functions can be designed at will, promising their future use for programmable, target-oriented mineralization control.