Proteins are vital molecules for biological processes—for regulation and structure. Notably, proteins are prone to degradation due to environmental factors like radiation. Radiation elicits reactive oxygen species (ROS) that accumulate as oxidative stress. Hence, it is suggested that the damage suppressor (Dsup) protein, the protein responsible for the extremotolerant ability of tardigrades should be utilized as a therapeutic agent for protection and cell longevity. One of the recommended targets is the BRCA1 protein, which functions for tumor suppression and is susceptible to degradation. Using AlphaFold for protein modeling, HADDOCK and PRODIGY for protein-protein docking and scoring, and STRING to establish a protein-protein interaction network to screen relative proteins of BRCA1 that can be docked with Dsup and possibly affected pathways and functions because of the interaction. The researchers generated a complex model of the Dsup protein of Ramazzottius varieornatus and the Dsup-like protein of Hypsibius exemplaris with the BRCA1 protein of Homo sapiens. The potential optimal binding site of the Dsup on the BRCA1 is a semi-flexible region. The PPI network was established, and ATR, ATM, RAD50, RAD51, MSH2, MYC, and RB1 were suggested for future docking studies with Dsup. The probable affected pathway is organ system cancer and the BRCA1-DNA and BRCA1-Nucleic acid-dependent function. In conclusion, the Dsup and BRCA1 association is possible. These findings contribute to the potential application of Dsup to medicine and human space endeavors. However, further investigation of extensive molecular dynamics analysis and experimental validation such as in vivo and in vitro is recommended.