LSM7
From Wikipedia, the free encyclopedia
LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)
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Identifiers | ||||||||||||||
Symbol(s) | LSM7; YNL147W | |||||||||||||
External IDs | OMIM: 607287 MGI: 1913344 HomoloGene: 6781 | |||||||||||||
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RNA expression pattern | ||||||||||||||
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) |
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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: . 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: . 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: . 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: . 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: . 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: . 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: . 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: . PMID 15057824.
- Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi: . 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: . 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: . PMID 15489334.