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PSIP1 not only enhances integrase’s strand transfer activity and protects it from proteasomal degradation but also influences integration site selection and even modulates aspects of viral latency through interactions with other host factors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in viral integration, PSIP1 acts as a transcriptional coactivator and epigenetic reader whose activities extend to regulation of gene expression, alternative splicing, DNA repair, and oncogenic transcription. The two alternatively spliced isoforms—p75 and the shorter p52—mediate distinct functions: p75 serves as an adaptor that links transcription factors (such as MLL and menin) and chromatin-associated proteins (including PogZ and JPO2) to chromatin, thereby influencing leukemogenic gene programs and stress‐response pathways, whereas p52 directly interacts with splicing factors (for example, Srsf1) via its PWWP domain and modulates alternative splicing in active genes marked by H3K36 methylation. Further, PSIP1 participates in the repair of DNA double‐strand breaks by facilitating recruitment of proteins like CtIP, and its interactions can be competitively modulated by peptides designed to block binding to viral integrase. 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