Candida auris is a recently found pathogenic yeast that causes systemic infections, showing a high mortality rate. In addition, C. auris has been found to be difficult to remove from the environment of health care settings, among other causes due to its high resistance to stress conditions. Moreover, the reactive oxygen species that cause the oxidative stress are also used by our immune cells to kill the microorganisms. Considering this, our research group has studied the proteomic changes that are associated to the presence of high oxidative stress conditions (8 mM H2O2) in the fungus C. auris. Thirteen spots were found to be overexpressed between normal and oxidative stress conditions; four were specific points only detected under oxidative stress and nine were overexpressed in this condition. Fifteen proteins were identified in this spots. The four spots detected as specifically expressed corresponded to the proteins ubiquitin-activating enzyme e1 (Uba1), elongation factor 3 (Cef3), leucine—tRNA ligase (Cdc60), an uncharacterized protein (A0A2H0ZCS4), and thioredoxin-dependent peroxiredoxin (Tsa1b). The uncharacterized protein had the same amino acid sequence as the formyltetrahydrofolate synthetase (Fau1) found in another C. auris strain. On the other hand, the nine spots detected as overexpressed corresponded to the proteins mitochondrial C-1-tetrahydrofolate (Mis1), Fau1, 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase (Met6), 40S ribosomal protein S6 (Rps6), 60S ribosomal protein L8 (Rpl8), 40S ribosomal protein S4 (Rps4), elongation factor 1-α (Tef1), ATP synthase subunit β (Atp2), acetyl-CoA C-acetyltransferase (Erg10), mitochondrial aconitate hydratase (Aco1) and malate dehydrogenase (Mdh1).