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PRDMs exhibit unique dualities: (a) PR domain\/ZNF arrays\u2014their structure combines a SET\u2010like domain known as a<jats:italic>PR domain,<\/jats:italic>typically found in methyltransferases, with a variable array of<jats:italic>C2H2 zinc fingers (ZNF)<\/jats:italic>characteristic of DNA\u2010binding transcription factors; (b) transcriptional activators\/repressors\u2014their physiological function is context\u2010 and cell\u2010dependent; mechanistically, some PRDMs have a PKMT activity and directly catalyze histone lysine methylation, while others are rather pseudomethyltransferases and act by recruiting transcriptional cofactors; (c) oncogenes\/tumor suppressors\u2014their pathological function depends on the specific PRDM isoform expressed during tumorigenesis. This duality is well known as the \u2018Yin and Yang\u2019 of PRDMs and involves a complex regulation of alternative splicing or alternative promoter usage, to generate full\u2010length or PR\u2010deficient isoforms with opposing functions in cancer. 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