Recent research suggests that the right open reading frame kinase 3 (RIOK3) protein is involved in mounting an anti-viral interferon (IFN) response to the Rift Valley Fever Virus. However, the underlying mechanism by which RIOK3 regulates the IFN response is unknown. A hypothesised mechanism for regulating RIOK3 is ubiquitination. Stx3 is a stable protein and numerous studies have been conducted on the ubiquitin binding site for Stx3 protein. Stx3 can therefore be used as a model to observe the binding of ubiquitin molecules to a protein, and this model allows the RIOK3 ubiquitin-binding site location to be confirmed. This investigation created a successful model to observe the binding of ubiquitin molecules to a protein. Stx3 protein was fluorescently labelled with Fluorescein isothiocyanate (FITC) florescence and a change of one fluorescently labelled species to two different fluorescently labelled species was able to be observed when ubiquitin was added to the solution. Using analytic ultracentrifugation (AUC) with the UltraScan4.0 program, the new species generated after the addition of ubiquitin demonstrated different sedimentation and diffusion coefficients, in addition to different molecular weights. However, this model requires further validation with repeated analysis for Stx3 and other known ubiquitin-binding proteins. After validation is complete, RIOK3 will be observed in this model system to confirm whether there is a ubiquitin-binding site on RIOK3.