Proteins interacting via a short-range attractive potential have been shown to serve as ideal model systems to study the influence of such an attraction on the equilibrium and non-equilibrium phase behavior of colloidal suspensions. Their size of only a few nm, their monodispersity, and the possibility to tune the attractive well depth simply by temperature, make these proteins ideal for such studies. Here we report on a critical re-examination of the different scenarios proposed for the interplay between phase separation and dynamical arrest in colloidal suspensions. We have used aqueous solutions of the globular protein lysozyme as a model system for colloids with a tunable short-ranged attraction. We were able to demonstrate that temperature quenches into the spinodal region and below an arrest temperature lead to the formation of a bicontinuous network, where the dense phase undergoes dynamical arrest once it reaches the glass line at this temperature. Microscopically, this corresponds to a coexistence of a dilute fluid with a dense percolated glass phase. Finally, deep quenches below the glass line result in the formation of a homogeneous glass phase. These measurements have allowed us for the first time to quantitatively locate the glass line in the unstable region below the spinodal, and thus provide a new test ground for computer simulations and theoretical calculations in the current attempt to understand and generalize dynamical arrest in soft matter.