LSM1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''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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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)
| HGNCid = 20472
| Symbol = LSM1
| AltSymbols =; CASM; YJL124C
| OMIM = 607281
| ECnumber = 
| Homologene = 40945
| MGIid = 1914457
| GeneAtlas_image1 = PBB_GE_LSM1_203534_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0031202 |text = RNA splicing factor activity, transesterification mechanism}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 27257
    | Hs_Ensembl = ENSG00000175324
    | Hs_RefseqProtein = NP_055277
    | Hs_RefseqmRNA = NM_014462
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 38140034
    | Hs_GenLoc_end = 38152995
    | Hs_Uniprot = O15116
    | Mm_EntrezGene = 67207
    | Mm_Ensembl = ENSMUSG00000037296
    | Mm_RefseqmRNA = XM_357867
    | Mm_RefseqProtein = XP_357867
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 27251136
    | Mm_GenLoc_end = 27269520
    | Mm_Uniprot = Q544C9
  }}
}}
'''LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)''', also known as '''LSM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LSM1 LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27257| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[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" />
{{PBB_Summary
| section_title =
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: LSM1 LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27257| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{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. }}
| citations =
*{{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, Sugiyama H, Fujii Y, ''et al.'' |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=  }}
*{{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, Graber MW, Chapman JM, ''et al.'' |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=  }}
*{{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  | author=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 }}
*{{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, Brahms H, Kastner B, ''et al.'' |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 }}
*{{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  | author=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=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, Peebles CL, Hamel JC, ''et al.'' |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 }}
*{{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 | author=Takahashi S, Suzuki S, Inaguma S, ''et al.'' |title=Down-regulation of Lsm1 is involved in human prostate cancer progression. |journal=Br. J. Cancer |volume=86 |issue= 6 |pages= 940-6 |year= 2002 |pmid= 11953827 |doi= 10.1038/sj.bjc.6600163 }}
*{{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, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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=Ingelfinger D, Arndt-Jovin DJ, Lührmann 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 |year= 2003 |pmid= 12515382 |doi=  }}
*{{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, Semple JI, Brown SE, ''et al.'' |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=  }}
*{{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  | author=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 }}
*{{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, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{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, Venkatesan K, Hao T, ''et al.'' |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 }}
*{{cite journal  | author=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 }}
*{{cite journal  | author=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 }}
*{{cite journal  | author=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 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:10, 2 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 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.
  2. ↑ 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. ↑ 3.0 3.1 "Entrez Gene: LSM1 LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae)".

Further reading


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