Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1 (By similarity). Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. The phosphatase activity has been shown in vitro. Coactivates SIX1. Seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity. May be involved in development of the eye. May play a role in mediating the induction and differentiation of cranial placodes. H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate Binds 1 Mg(2+) ion per subunit. Interacts with SIX1 and DACH1, and probably SIX2, SIX4 and SIX5. Localizes at sites of DNA damage at double-strand breaks (DSBs). Expressed in branchial arches, CNS and developing eye. Ser-203 phosphorylation is required for localization at sites of DNA damage and directing interaction with H2AX. Belongs to the HAD-like hydrolase superfamily. EYA family. According to PubMed:14628042 also shows serine/threonine protein phosphatase activity.