In contrast, Th2‐CD4+ T cells may subvert Th1 responses, providing a microenvironment conducive to tumor progression.[52, 53] Additionally, MAGEA6 has been implicated in modulating protein ubiquitination by enhancing the activity of E3 ubiquitin ligases, leading to the ubiquitination and degradation of AMPK.[31] Our study builds on this by demonstrating that MAGEA6 interacts with the deubiquitinase USP10, inhibiting the ubiquitination and degradation of YY1 protein, further emphasizing its significant role in ubiquitination regulation. Here, USP10 is linked to neoplasm.