LSM1

Protein-coding gene in the species Homo sapiens
LSM1
Identifiers
AliasesLSM1, CASM, YJL124C, LSM1 homolog, mRNA degradation associated
External IDsOMIM: 607281; MGI: 1914457; HomoloGene: 40945; GeneCards: LSM1; OMA:LSM1 - orthologs
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[1]
Chromosome 8 (mouse)
Genomic location for LSM1
Genomic location for LSM1
Band8|8 A2Start26,275,316 bp[1]
End26,294,003 bp[1]
RNA expression pattern
Bgee
HumanMouse (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

  • epithelium of lens

  • facial motor nucleus

  • medial ganglionic eminence

  • embryo

  • neural tube

  • ectoderm

  • epiblast

  • otic vesicle
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
SpeciesHumanMouse
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/aChr 8: 26.28 – 26.29 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

U6 snRNA-associated Sm-like protein LSm1 is a protein that in humans is encoded by the LSM1 gene.[4][5][6]

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.[6]

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037296 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ 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.
  5. ^ 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.
  6. ^ a b "Entrez Gene: LSM1 LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)".

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.


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