Hydrogen deuterium exchange mass spectrometry (HDX-MS) was used to analyze how the mng-SHIP1-dCT construct interacts receptor-derived phosphotryrosine peptides (pY) to probe how these peptides regulate SHIP1 autoinhibition. This HDX-MS helped to identify intramolecular contacts involved in the regulation of SHIP1 autoinibition. Results from this HDX analyzing the dimeric mng-SHIP1 construct are used in tandem with previous results analyzing the monomeric mini-SHIP construct to confirm the same mechanism of autoinhibtion exists. These results help confirm autoinhibition of monomeric SHIP1 is indeed likely regulated by the same mechanism to that of dimeric SHIP1.