{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Blatnik AJ"],"funding":["Ohio State Pre-accelerator Award","Cure SMA Fellowship","Center for RNA Biology","NINDS NIH HHS","NIH HHS","NIGMS NIH HHS"],"pagination":["gkaf794"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12359035"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(15)"],"pubmed_abstract":["Sm-ring assembly is important for the biogenesis, stability, and function of uridine-rich small nuclear RNAs (U snRNAs) involved in pre-messenger RNA (mRNA) splicing and histone pre-mRNA processing. Sm-ring assembly is cytoplasmic and dependent upon the Sm-site sequence and structural motif, ATP, and Survival motor neuron (SMN) protein complex. While RNAs other than U snRNAs were previously shown to associate with Sm proteins, whether this association follows Sm-ring assembly requirements is unknown. We systematically identified Sm-sites within the human and mouse transcriptomes and assessed whether these sites can accept Sm-rings. In addition to snRNAs, Sm-sites are highly prevalent in the 3' untranslated regions of long mRNAs. RNA immunoprecipitation experiments confirm that Sm-site cont"],"journal":["Nucleic acids research"],"pubmed_title":["Sm-site containing mRNAs can accept Sm-rings and are downregulated in Spinal Muscular Atrophy."],"pmcid":["PMC12359035"],"funding_grant_id":["R35-GM149298","R01 NS123736","T32-GM141955","R35-GM142580","T32 GM141955","R35 GM149298","5R01NS123736-04","R35 GM142580"],"pubmed_authors":["Singh G","Blatnik AJ","Slivka J","Pastore B","Embree CM","Sanjeev M","Burghes AHM","Tang W"],"additional_accession":[]},"is_claimable":false,"name":"Sm-site containing mRNAs can accept Sm-rings and are downregulated in Spinal Muscular Atrophy.","description":"Sm-ring assembly is important for the biogenesis, stability, and function of uridine-rich small nuclear RNAs (U snRNAs) involved in pre-messenger RNA (mRNA) splicing and histone pre-mRNA processing. Sm-ring assembly is cytoplasmic and dependent upon the Sm-site sequence and structural motif, ATP, and Survival motor neuron (SMN) protein complex. While RNAs other than U snRNAs were previously shown to associate with Sm proteins, whether this association follows Sm-ring assembly requirements is unknown. We systematically identified Sm-sites within the human and mouse transcriptomes and assessed whether these sites can accept Sm-rings. In addition to snRNAs, Sm-sites are highly prevalent in the 3' untranslated regions of long mRNAs. RNA immunoprecipitation experiments confirm that Sm-site cont","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-04-08T15:41:09.895Z","creation":"2026-04-08T05:10:30.654Z"},"accession":"S-EPMC12359035","cross_references":{"pubmed":["40823813"],"doi":["10.1093/nar/gkaf794"]}}