LSM1

LSM1
Identifiers
Aliases	LSM1, CASM, YJL124C, LSM1 homolog, mRNA degradation associated
External IDs	OMIM: 607281 MGI: 1914457 HomoloGene: 40945 GeneCards: LSM1
Gene location (Human)
Chr.	Chromosome 8 (human)[1]
End	38,176,730 bp[1]
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)[2]
End	25,803,975 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• GO:0001948 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; • cell 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 nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; • histone mRNA catabolic process; • nuclear-transcribed mRNA catabolic process; • RNA metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	27257
	67207
	ENSG00000175324
	ENSMUSG00000037296
	O15116
	Q8VC85
	NM_014462
	NM_026032
	NP_055277
	NP_080308
	Wikidata
View/Edit Human	View/Edit Mouse

U6 snRNA-associated Sm-like protein LSm1 is a protein that in humans is encoded by the LSM1 gene.[5][6][7]

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.[7]

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References

GRCh38: Ensembl release 89: ENSG00000175324 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000037296 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T (Jan 2003). "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci". RNA. 8 (12): 1489–501. doi:10.1017/S1355838202021726. PMC 1370355. PMID 12515382.
Takahashi S, Suzuki S, Inaguma S, Cho YM, Ikeda Y, Hayashi N, Inoue T, Sugimura Y, Nishiyama N, Fujita T, Ushijima T, Shirai T (Apr 2002). "Down-regulation of Lsm1 is involved in human prostate cancer progression". Br J Cancer. 86 (6): 940–6. doi:10.1038/sj.bjc.6600163. PMC 2364150. PMID 11953827.
"Entrez Gene: LSM1 LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)".

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. 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. doi:10.1038/nature04209. PMID 16189514.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000175324 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000037296 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid12515382-5] Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T (Jan 2003). "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci". RNA. 8 (12): 1489–501. doi:10.1017/S1355838202021726. PMC 1370355. PMID 12515382.

[pmid11953827-6] Takahashi S, Suzuki S, Inaguma S, Cho YM, Ikeda Y, Hayashi N, Inoue T, Sugimura Y, Nishiyama N, Fujita T, Ushijima T, Shirai T (Apr 2002). "Down-regulation of Lsm1 is involved in human prostate cancer progression". Br J Cancer. 86 (6): 940–6. doi:10.1038/sj.bjc.6600163. PMC 2364150. PMID 11953827.

[entrez-7] "Entrez Gene: LSM1 LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)".

LSM1

Function

References

Further reading