LSM7

LSM7 homolog, U6 small nuclear RNA and mRNA degradation associated
Identifiers
Symbols	LSM7 ; YNL147W
External IDs	OMIM: 607287 MGI: 1913344 HomoloGene: 6781 GeneCards: LSM7 Gene
Gene ontology Molecular function • protein binding • U6 snRNA binding Cellular component • spliceosomal complex • small nucleolar ribonucleoprotein complex • cytosol Biological process • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay • mRNA splicing, via spliceosome • gene expression • exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	51690	66094
Ensembl	ENSG00000130332	ENSMUSG00000035215
UniProt	Q9UK45	Q9CQQ8
RefSeq (mRNA)	NM_016199	NM_025349
RefSeq (protein)	NP_057283	NP_079625
Location (UCSC)	Chr 19: 2.32 – 2.33 Mb	Chr 10: 80.85 – 80.86 Mb
PubMed search

U6 snRNA-associated Sm-like protein LSm7 is a protein that in humans is encoded by the LSM7 gene.^[1][2][3]

Function

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]^[3]

Interactions

LSM7 has been shown to interact with TACC1^[4][5] and LSM2.^[6][7]

References

1. Achsel T, Brahms H, Kastner B, Bachi A, Wilm M, Lührmann R (Oct 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". The EMBO Journal 18 (20): 5789–802. doi:10.1093/emboj/18.20.5789. PMC 1171645. PMID 10523320.
2. Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T (Dec 2002). "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.
3. "Entrez Gene: LSM7 LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)".
4. Conte N, Delaval B, Ginestier C, Ferrand A, Isnardon D, Larroque C, Prigent C, Séraphin B, Jacquemier J, Birnbaum D (Nov 2003). "TACC1-chTOG-Aurora A protein complex in breast cancer". Oncogene 22 (50): 8102–16. doi:10.1038/sj.onc.1206972. PMID 14603251.
5. Conte N, Charafe-Jauffret E, Delaval B, Adélaïde J, Ginestier C, Geneix J, Isnardon D, Jacquemier J, Birnbaum D (Aug 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.
6. Lehner B, Sanderson CM (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
7. Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (Jan 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.

Further reading

• Friesen WJ, Dreyfuss G (Aug 2000). "Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN)". The Journal of Biological Chemistry 275 (34): 26370–5. doi:10.1074/jbc.M003299200. PMID 10851237.
• Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y (Oct 2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Research 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
• Eystathioy T, Peebles CL, Hamel JC, Vaughn JH, Chan EK (Mar 2002). "Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera". Arthritis and Rheumatism 46 (3): 726–34. doi:10.1002/art.10220. PMID 11920408.
• Conte N, Charafe-Jauffret E, Delaval B, Adélaïde J, Ginestier C, Geneix J, Isnardon D, Jacquemier J, Birnbaum D (Aug 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.
• Conte N, Delaval B, Ginestier C, Ferrand A, Isnardon D, Larroque C, Prigent C, Séraphin B, Jacquemier J, Birnbaum D (Nov 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, Counsell D, Campbell RD, Sanderson CM (Jan 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 (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Stanĕk D, Neugebauer KM (Sep 2004). "Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer". The Journal of Cell Biology 166 (7): 1015–25. doi:10.1083/jcb.200405160. PMC 2172029. PMID 15452143.