MARIA JAVEED2025-11-212025-11-212022https://escholar.umt.edu.pk/handle/123456789/11292ADAM32 is a disintegrin and metalloproteinase domain containing protein 32. This gene generates a member of the disintegrin class of proteins that is associated with membranes. Several metabolic pathways, including inflammation, tumor growth, fertilization, and brain development, are influenced by the members of this family. In this study, the ADAM32 was both structurally and functionally annotated, and Insilco methods were used to predict the effects of amino acid substitutions on biological functions, analysis of protein molecules in light of evolutionary relationships, pathogenicity predictions, secondary structure analysis of proteins, evaluations of the protein's quality, and protein-protein docking. The findings of this investigation demonstrated that the ADAM32 variations are pathogenic, harmful, or destructive. A protein known as SPAG17 has a higher binding affinity with ADAM32 than other proteins, according to protein-protein docking research. The homology modelling approach was used to create three-dimensional structure. Additionally, the proper annotation will contribute to the characterization of ADAM32 and expand our understanding of its biological functions.enThesis