LSM1

U6 snRNA-associated Sm-like protein LSm1 is a protein that in humans is encoded by the LSM1 gene.

LSM1
Identifiers
Aliases	LSM1, CASM, YJL124C, LSM1 homolog, mRNA degradation associated
External IDs	OMIM: 607281 MGI: 1914457 HomoloGene: 40945 GeneCards: LSM1
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 A2 Start 26,275,316 bp End 26,294,003 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland hair follicle right ventricle renal medulla saphenous vein cardia monocyte vena cava external globus pallidus body of tongue Top expressed in renal corpuscle medullary collecting duct facial motor nucleus medial ganglionic eminence neural tube ectoderm otic placode endocardial cushion barrel cortex primitive streak More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding RNA cap binding pre-mRNA binding mRNA binding RNA binding Cellular component cytosol P-body messenger ribonucleoprotein complex axon neuronal cell body dendrite nucleus cytoplasm mRNA cap binding complex Lsm1-7-Pat1 complex Biological process negative regulation of neuron differentiation deadenylation-dependent decapping of nuclear-transcribed mRNA RNA splicing, via transesterification reactions mRNA processing stem cell population maintenance RNA splicing exonucleolytic catabolism of deadenylated mRNA histone mRNA catabolic process nuclear-transcribed mRNA catabolic process RNA metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27257 67207 Ensembl n/a ENSMUSG00000037296 UniProt O15116 Q8VC85 RefSeq (mRNA) NM_014462 NM_026032 RefSeq (protein) NP_055277 NP_080308 Location (UCSC) n/a Chr 8: 26.28 – 26.29 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

Sm-like proteins were identified in a variety of organisms based on sequence homology with the Sm protein family (see SNRPD2). Sm-like proteins contain the Sm sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing.

Further reading

• Shimizu Y, Sugiyama H, Fujii Y, et al. (1997). "Lineage- and differentiation stage-specific expression of LSM-1 (LPAP), a possible substrate for CD45, in human hematopoietic cells". Am. J. Hematol. 54 (1): 1–11. doi:10.1002/(SICI)1096-8652(199701)54:1<1::AID-AJH1>3.0.CO;2-1. PMID 8980254.
• Schweinfest CW, Graber MW, Chapman JM, et al. (1997). "CaSm: an Sm-like protein that contributes to the transformed state in cancer cells". Cancer Res. 57 (14): 2961–5. PMID 9230209.
• Salgado-Garrido J, Bragado-Nilsson E, Kandels-Lewis S, Séraphin B (1999). "Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin". EMBO J. 18 (12): 3451–62. doi:10.1093/emboj/18.12.3451. PMC 1171424. PMID 10369684.
• Achsel T, Brahms H, Kastner B, et al. (1999). "A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro". EMBO J. 18 (20): 5789–802. doi:10.1093/emboj/18.20.5789. PMC 1171645. PMID 10523320.
• Friesen WJ, Dreyfuss G (2000). "Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN)". J. Biol. Chem. 275 (34): 26370–5. doi:10.1074/jbc.M003299200. PMID 10851237.
• Eystathioy T, Peebles CL, Hamel JC, et al. (2002). "Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera". Arthritis Rheum. 46 (3): 726–34. doi:10.1002/art.10220. PMID 11920408.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Wichroski MJ, Robb GB, Rana TM (2006). "Human Retroviral Host Restriction Factors APOBEC3G and APOBEC3F Localize to mRNA Processing Bodies". PLOS Pathog. 2 (5): e41. doi:10.1371/journal.ppat.0020041. PMC 1458959. PMID 16699599.
• Chu CY, Rana TM (2006). "Translation Repression in Human Cells by MicroRNA-Induced Gene Silencing Requires RCK/p54". PLOS Biol. 4 (7): e210. doi:10.1371/journal.pbio.0040210. PMC 1475773. PMID 16756390.
• Streicher KL, Yang ZQ, Draghici S, Ethier SP (2007). "Transforming function of the LSM1 oncogene in human breast cancers with the 8p11−12 amplicon". Oncogene. 26 (14): 2104–14. doi:10.1038/sj.onc.1210002. PMC 2435249. PMID 17001308.