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{{ | '''U6 snRNA-associated Sm-like protein LSm1''' is a [[protein]] that in humans is encoded by the ''LSM1'' [[gene]].<ref name="pmid12515382">{{cite journal |vauthors=Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T | title = The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci | journal = RNA | volume = 8 | issue = 12 | pages = 1489–501 |date=Jan 2003 | pmid = 12515382 | pmc = 1370355 | doi = 10.1017/S1355838202021726 }}</ref><ref name="pmid11953827">{{cite journal |vauthors=Takahashi S, Suzuki S, Inaguma S, Cho YM, Ikeda Y, Hayashi N, Inoue T, Sugimura Y, Nishiyama N, Fujita T, Ushijima T, Shirai T | title = Down-regulation of Lsm1 is involved in human prostate cancer progression | journal = Br J Cancer | volume = 86 | issue = 6 | pages = 940–6 |date=Apr 2002 | pmid = 11953827 | pmc = 2364150 | doi = 10.1038/sj.bjc.6600163 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LSM1 LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27257| accessdate = }}</ref> | ||
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== Function == | |||
[[LSm|Sm-like protein]]s 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]].<ref name="entrez" /> | |||
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==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{cite journal | author=Shimizu Y |title=Lineage- and differentiation stage-specific expression of LSM-1 (LPAP), a possible substrate for CD45, in human hematopoietic cells |journal=Am. J. Hematol. |volume=54 |issue= 1 |pages= 1–11 |year= 1997 |pmid= 8980254 |doi=10.1002/(SICI)1096-8652(199701)54:1<1::AID-AJH1>3.0.CO;2-1 |name-list-format=vanc| author2=Sugiyama H | author3=Fujii Y | display-authors=3 | last4=Sasaki | first4=K. | last5=Inoue | first5=K. | last6=Ogawa | first6=H. | last7=Tamaki | first7=H. | last8=Miyake | first8=S. | last9=Oji | first9=Y. }} | |||
*{{cite journal | author=Schweinfest CW |title=CaSm: an Sm-like protein that contributes to the transformed state in cancer cells |journal=Cancer Res. |volume=57 |issue= 14 |pages= 2961–5 |year= 1997 |pmid= 9230209 |doi= |name-list-format=vanc| author2=Graber MW | author3=Chapman JM | display-authors=3 | last4=Papas | first4=TS | last5=Baron | first5=PL | last6=Watson | first6=DK }} | |||
*{{cite journal | author=Shimizu Y | *{{cite journal |vauthors=Salgado-Garrido J, Bragado-Nilsson E, Kandels-Lewis S, Séraphin B |title=Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin |journal=EMBO J. |volume=18 |issue= 12 |pages= 3451–62 |year= 1999 |pmid= 10369684 |doi= 10.1093/emboj/18.12.3451 | pmc=1171424 }} | ||
*{{cite journal | author=Schweinfest CW | *{{cite journal | author=Achsel T |title=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 |journal=EMBO J. |volume=18 |issue= 20 |pages= 5789–802 |year= 1999 |pmid= 10523320 |doi= 10.1093/emboj/18.20.5789 | pmc=1171645 |name-list-format=vanc| author2=Brahms H | author3=Kastner B | display-authors=3 | last4=Bachi | first4=A | last5=Wilm | first5=M | last6=Lührmann | first6=R }} | ||
*{{cite journal | | *{{cite journal |vauthors=Friesen WJ, Dreyfuss G |title=Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN) |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26370–5 |year= 2000 |pmid= 10851237 |doi= 10.1074/jbc.M003299200 }} | ||
*{{cite journal | author=Achsel T | *{{cite journal | author=Eystathioy T |title=Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera |journal=Arthritis Rheum. |volume=46 |issue= 3 |pages= 726–34 |year= 2002 |pmid= 11920408 |doi= 10.1002/art.10220 |name-list-format=vanc| author2=Peebles CL | author3=Hamel JC | display-authors=3 | last4=Vaughn | first4=John H. | last5=Chan | first5=Edward K. L. }} | ||
*{{cite journal | | *{{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }} | ||
*{{cite journal | author=Eystathioy T | *{{cite journal | author=Lehner B |title=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 |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=10.1016/S0888-7543(03)00235-0 |name-list-format=vanc| author2=Semple JI | author3=Brown SE | display-authors=3 | last4=Counsell | first4=Damian | last5=Campbell | first5=R.Duncan | last6=Sanderson | first6=Christopher M }} | ||
*{{cite journal |vauthors=Lehner B, Sanderson CM |title=A Protein Interaction Framework for Human mRNA Degradation |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 | pmc=442147 }} | |||
*{{cite journal | author=Strausberg RL | *{{cite journal | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }} | ||
*{{cite journal | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |name-list-format=vanc| author2=Venkatesan K | author3=Hao T | display-authors=3 | last4=Hirozane-Kishikawa | first4=Tomoko | last5=Dricot | first5=Amélie | last6=Li | first6=Ning | last7=Berriz | first7=Gabriel F. | last8=Gibbons | first8=Francis D. | last9=Dreze | first9=Matija }} | |||
*{{cite journal | author=Lehner B | *{{cite journal |vauthors=Wichroski MJ, Robb GB, Rana TM |title=Human Retroviral Host Restriction Factors APOBEC3G and APOBEC3F Localize to mRNA Processing Bodies |journal=PLoS Pathog. |volume=2 |issue= 5 |pages= e41 |year= 2006 |pmid= 16699599 |doi= 10.1371/journal.ppat.0020041 | pmc=1458959 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Chu CY, Rana TM |title=Translation Repression in Human Cells by MicroRNA-Induced Gene Silencing Requires RCK/p54 |journal=PLoS Biol. |volume=4 |issue= 7 |pages= e210 |year= 2006 |pmid= 16756390 |doi= 10.1371/journal.pbio.0040210 | pmc=1475773 }} | ||
*{{cite journal | author=Gerhard DS | *{{cite journal |vauthors=Streicher KL, Yang ZQ, Draghici S, Ethier SP |title=Transforming function of the LSM1 oncogene in human breast cancers with the 8p11−12 amplicon |journal=Oncogene |volume=26 |issue= 14 |pages= 2104–14 |year= 2007 |pmid= 17001308 |doi= 10.1038/sj.onc.1210002 | pmc=2435249 }} | ||
*{{cite journal | author=Rual JF | |||
*{{cite journal | | |||
*{{cite journal | | |||
*{{cite journal | | |||
}} | |||
{{refend}} | {{refend}} | ||
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{{gene-8-stub}} |
Latest revision as of 18:10, 2 September 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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U6 snRNA-associated Sm-like protein LSm1 is a protein that in humans is encoded by the LSM1 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). 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.[3]
References
- ↑ 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.
- ↑ 3.0 3.1 "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. 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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