UHRF1 and UHRF2 are multiple‐domain epigenetic proteins that share a high degree of sequence similarity. These proteins play a very important role in histone modification and DNA methylation. Although both proteins contain a TTD and a PHD domain, the TTD domain of UHRF2 contains a unique ~35 amino acid long region that is highly basic called the “stretch”. This region was analyzed for the possibility of being a disordered region using the Sypro Orange Thermofluor assay. We found that UHRF2 TTD‐PHD has a lower melting temperature than UHRF2 TTD‐PHD without the stretch. It was also found that at higher salt concentrations, the melting temperature of UHRF2 TTD‐PHD increases, likely due to the disordered “stretch” region becoming stabilized. This data provides support towards the model that the stretch region is disordered and regulates protein stability.