Multiple structural and functional annotations based in-silico characterization of Q9BRX8 protein

Numerous proteins found in humans are poorly understood because there is a dearth of experimental evidence. Hypothetical proteins (HPs) or uncharacterized proteins are the terms used to describe these proteins. In this work, one of these proteins, Q9BRX8, is investigated using in-silico or bioinformatics tools to reveal its significant properties. In this regard, NCBI for the sequence retrieval, ProtParam tool for analysis of physiochemical properties, SOPMA for secondary structure prediction, SWISS-Model for homology modelling, STRING for protein-protein interaction and HDOCK for protein-protein docking analysis among other tools, were incorporated. The physiochemical characteristics indicated that Q9BRX8, which has an instability score of 32.57, is a stable protein. It was identified in other cellular compartments, such as the cytosol, mitochondria, etc., where it may be betrothed in a variety of cellular functions, according to the sub-cellular localization studies. In addition, its secondary structure consists of high percentage of alpha helices (44.10%), among other components. Additionally, it was discovered through protein-protein interactions that this protein belongs to FAM213A family suggesting that it may function as antioxidant and affect bone resorption among other crucial functions. While, molecular docking analysis indicated that Q9BRX8 had a larger degree of similarity with the HLA-G protein, scoring -332.53kcal/mol. It can be hypothesized that the functions of Q9BRX8 and the HLA-G may be associated as a result of this similarity.