The translocation process of a globular protein (Ubiquitin) across a cylindrical nanopore is studied via molecular dynamics simulations. The Ubiquitin is described by simplified native-centric model to investigate the influence of protein structural properties on translocation mechanism. A complete thermodynamical and kinetic characterization of the process is obtained by studying the statistics of blockage times, the mobility and translocation probability as a function of the pulling force F acting in the pore. The transport dynamics occurs when the force exceeds a critical threshold Fc depending on a free-energy barrier that Ubiquitin has to overcome in order to slide along the channel. Such a barrier results from competition of the unfolding energy and the entropy associated to the confinement effects of the pore. We implement appropriate umbrella sampling simulations to compute the free energy profile as a function of the position of Ubiquitin center of mass inside the channel (reaction coordinate). This free-energy is then used to construct a one dimensional phenomenological model in the reaction coordinate which explains and reproduces the behaviour of the observables during the translocation.