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However, the PTMs of H2A.B and their functional implications are unknown. Here, we demonstrate that the Amino terminus of H2A.B serves as a central hub for a diverse range of gene regulatory protein-protein interactions, orchestrated by phosphorylation and arginine methylation. This includes a mechanism whereby non\u2013chromatin-bound H2A.B associates with SWI\/SNF, which limits its access to the genome. Last, we identify phosphorylated H2A.B as a previously uncharacterized marker of active RNA polymerase II transcription start sites. These findings elucidate a central role for H2A.B in genome regulation and highlight the importance of its PTMs in modulating its multifunctional roles.<\/jats:p>","DOI":"10.1126\/sciadv.adx1568","type":"journal-article","created":{"date-parts":[[2025,7,25]],"date-time":"2025-07-25T17:58:38Z","timestamp":1753466318000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":3,"title":["Nonchromatin regulatory functions of the histone variant H2A.B in SWI\/SNF genomic deposition"],"prefix":"10.1126","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1608-3846","authenticated-orcid":true,"given":"Xuanzhao","family":"Jiang","sequence":"first","affiliation":[{"name":"The John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, 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