HAX1 is a 32-kDa protein of unknown structure, involved in the regulation of apoptosis, cell migration and calcium homeostasis. It was also shown to bind mRNA. Scarcity of structural elements and the presence of a disordered region, inferred from HAX1 sequence, suggests that HAX1 is intrinsically disordered, and may have many protein-protein interactions. So far about 40 different proteins were characterized as HAX1 protein partners. In the present work, applying immunoaffinity chromatography coupled with mass spectrometry, we identified new candidates for HAX1 binding partners in cervical carcinoma cells. More than a half of these newly identified proteins represent RNA-binding proteins. There is also a big group of proteins, mostly mitochondrial, involved in cellular metabolism. These results imply that HAX1 has more protein partners than hitherto described. Subsequent analysis of these interactions may shed some light into molecular mechanisms of HAX1 functions, especially its involvement in mRNA processing and its role in protection against oxidative stress.