We have theoretically studied the uptake of a nonuniformly charged biomolecule suitable for representing a globular protein or a drug by a charged hydrogel carrier in the presence of a 1:1 electrolyte. On the basis of the analysis of a physical interaction Hamiltonian including monopolar, dipolar, and Born (self-energy) contributions derived from linear electrostatic theory of the unperturbed homogeneous hydrogel, we have identified five different sorption states of the system, from complete repulsion of the molecule to its full sorption deep inside the hydrogel, passing through metastable and stable surface adsorption states. The results are summarized in state diagrams that also explore the effects of varying the electrolyte concentration, the sign of the net electric charge of the biomolecule, and the role of including excluded-volume (steric) or hydrophobic biomolecule-hydrogel interactions. We show that the dipole moment of the biomolecule is a key parameter controlling the spatial distribution of the globules. In particular, biomolecules with a large dipole moment tend to be adsorbed at the external surface of the hydrogel, even if like-charged, whereas uniformly charged biomolecules tend to partition toward the internal core of an oppositely charged hydrogel. Hydrophobic attraction shifts the states toward the internal sorption of the biomolecule, whereas steric repulsion promotes surface adsorption for oppositely charged biomolecules or for the total exclusion of likely charged ones. Our results establish a guideline for the spatial partitioning of proteins and drugs in hydrogel carriers, tunable by the hydrogel charge, pH, and salt concentration.