LSM7

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LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)
Identifiers
Symbol(s) LSM7; YNL147W
External IDs OMIM: 607287 MGI1913344 HomoloGene6781
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 51690 66094
Ensembl ENSG00000130332 ENSMUSG00000064317
Uniprot Q9UK45 Q9CQQ8
Refseq NM_016199 (mRNA)
NP_057283 (protein)
XM_903539 (mRNA)
XP_908632 (protein)
Location Chr 19: 2.27 - 2.28 Mb Chr 10: 77.8 - 77.8 Mb
Pubmed search [1] [2]

LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae), also known as LSM7, is a human gene.[1]

Sm-like proteins were identified in a variety of organisms based on sequence homology with the Sm protein family (see SNRPD2; MIM 601061). 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.[supplied by OMIM][1]

[edit] References

[edit] Further reading

  • 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. 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. 
  • Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs.". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMID 11591653. 
  • 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. 
  • Conte N, Charafe-Jauffret E, Delaval B, et al. (2002). "Carcinogenesis and translational controls: TACC1 is down-regulated in human cancers and associates with mRNA regulators.". Oncogene 21 (36): 5619–30. doi:10.1038/sj.onc.1205658. PMID 12165861. 
  • 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. PMID 12477932. 
  • Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T (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. PMID 12515382. 
  • Conte N, Delaval B, Ginestier C, et al. (2003). "TACC1-chTOG-Aurora A protein complex in breast cancer.". Oncogene 22 (50): 8102–16. doi:10.1038/sj.onc.1206972. PMID 14603251. 
  • 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. PMID 14667819. 
  • Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824. 
  • Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMID 15231747. 
  • Stanĕk D, Neugebauer KM (2004). "Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer.". J. Cell Biol. 166 (7): 1015–25. doi:10.1083/jcb.200405160. PMID 15452143. 
  • 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. PMID 15489334.