<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Blatnik AJ</submitter><funding>Ohio State Pre-accelerator Award</funding><funding>Cure SMA Fellowship</funding><funding>Center for RNA Biology</funding><funding>NINDS NIH HHS</funding><funding>NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>gkaf794</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12359035</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>53(15)</volume><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</pubmed_abstract><journal>Nucleic acids research</journal><pubmed_title>Sm-site containing mRNAs can accept Sm-rings and are downregulated in Spinal Muscular Atrophy.</pubmed_title><pmcid>PMC12359035</pmcid><funding_grant_id>R35-GM149298</funding_grant_id><funding_grant_id>R01 NS123736</funding_grant_id><funding_grant_id>T32-GM141955</funding_grant_id><funding_grant_id>R35-GM142580</funding_grant_id><funding_grant_id>T32 GM141955</funding_grant_id><funding_grant_id>R35 GM149298</funding_grant_id><funding_grant_id>5R01NS123736-04</funding_grant_id><funding_grant_id>R35 GM142580</funding_grant_id><pubmed_authors>Singh G</pubmed_authors><pubmed_authors>Blatnik AJ</pubmed_authors><pubmed_authors>Slivka J</pubmed_authors><pubmed_authors>Pastore B</pubmed_authors><pubmed_authors>Embree CM</pubmed_authors><pubmed_authors>Sanjeev M</pubmed_authors><pubmed_authors>Burghes AHM</pubmed_authors><pubmed_authors>Tang W</pubmed_authors></additional><is_claimable>false</is_claimable><name>Sm-site containing mRNAs can accept Sm-rings and are downregulated in Spinal Muscular Atrophy.</name><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</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-04-08T15:41:09.895Z</modification><creation>2026-04-08T05:10:30.654Z</creation></dates><accession>S-EPMC12359035</accession><cross_references><pubmed>40823813</pubmed><doi>10.1093/nar/gkaf794</doi></cross_references></HashMap>