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M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:25242552, PubMed:26318451). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May also regulate alternative splice site selection (PubMed:20167602). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (By similarity). Also recognizes and binds m6A on other RNA molecules (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (PubMed:27602518). Also recognizes and binds m6A-containing single-stranded DNA (PubMed:32663306). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (By similarity). Independently of its N6-methyladenosine-containing RNA reader activity, it regulates PPARG stability by preventing its interaction with the E3 ubiquitin ligase ARIH2, thereby protecting it from ubiquitin-mediated proteasomal degradation and contributing to brown adipose tissue (BAT) development and energy homeostasis (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"E9Q5K9"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9QY02"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12755701"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19282290"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26876937"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28984244"}],"value":"Interacts with SRSF1 (By similarity). Interacts with SRSF2 (By similarity). Interacts with SRSF3 (PubMed:26876937, PubMed:28984244). Interacts with SRSF7 (By similarity). Interacts with SRSF10 (PubMed:26876937). Interacts with CPSF6 (By similarity). Interacts with KHDRBS1/SAM68 (By similarity). Interacts with TRA2B (By similarity). Interacts with KHDRBS3 (By similarity). Interacts with EMD (PubMed:12755701). Interacts with RBMX (PubMed:19282290). Interacts with ZCCHC8 (PubMed:28984244). Interacts (via its intrinsically disordered region) with PPARG; the interaction prevents PPARG from its ubiquitin-mediated proteasomal degradation (By 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