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While the canonical function of BMI\u20101 involves epigenetic repression, novel extranuclear functions have been recently reported. In the present study, we demonstrate that the phosphorylation of BMI\u20101 in diffuse intrinsic pontine glioma (DIPG) cells occurs in M phase and that it triggers simultaneous translocation of the phosphorylated BMI\u20101 to the cytoplasm. This translocation is mediated by the RanGTP\u2010dependent transporter CRM1, also known as exportin. Furthermore, we uncovered a previously unidentified nuclear export signal (NES) in the BMI\u20101 protein, suggesting an active transport type of modified BMI\u20101 mediated by CRM1. These findings associate BMI\u20101 phosphorylation with its trafficking in M phase. 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