LSM7: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''U6 snRNA-associated Sm-like protein LSm7''' is a [[protein]] that in humans is encoded by the ''LSM7'' [[gene]].<ref name="pmid10523320">{{cite journal | vauthors = Achsel T, Brahms H, Kastner B, Bachi A, Wilm M, Lührmann R | 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 = The EMBO Journal | volume = 18 | issue = 20 | pages = 5789–802 | date = Oct 1999 | pmid = 10523320 | pmc = 1171645 | doi = 10.1093/emboj/18.20.5789 }}</ref><ref name="pmid12515382">{{cite journal | vauthors = 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 | date = Dec 2002 | pmid = 12515382 | pmc = 1370355 | doi = 10.1017/S1355838202021726}}</ref><ref name="entrez"/>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- 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 = LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)
| HGNCid = 20470
| Symbol = LSM7
| AltSymbols =; YNL147W
| OMIM = 607287
| ECnumber = 
| Homologene = 6781
| MGIid = 1913344
| GeneAtlas_image1 = PBB_GE_LSM7_204559_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017070 |text = U6 snRNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0000398 |text = nuclear mRNA splicing, via spliceosome}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}} {{GNF_GO|id=GO:0016071 |text = mRNA metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51690
    | Hs_Ensembl = ENSG00000130332
    | Hs_RefseqProtein = NP_057283
    | Hs_RefseqmRNA = NM_016199
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 2272522
    | Hs_GenLoc_end = 2279479
    | Hs_Uniprot = Q9UK45
    | Mm_EntrezGene = 66094
    | Mm_Ensembl = ENSMUSG00000064317
    | Mm_RefseqmRNA = XM_903539
    | Mm_RefseqProtein = XP_908632
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 77796432
    | Mm_GenLoc_end = 77796881
    | Mm_Uniprot = Q9CQQ8
  }}
}}
'''LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)''', also known as '''LSM7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LSM7 LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51690| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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: LSM7 LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51690| accessdate = }}</ref>
{{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: LSM7 LSM7 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51690| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
LSM7 has been shown to [[Protein-protein interaction|interact]] with [[TACC1]]<ref name=pmid14603251>{{cite journal | vauthors = Conte N, Delaval B, Ginestier C, Ferrand A, Isnardon D, Larroque C, Prigent C, Séraphin B, Jacquemier J, Birnbaum D | title = TACC1-chTOG-Aurora A protein complex in breast cancer | journal = Oncogene | volume = 22 | issue = 50 | pages = 8102–16 | date = Nov 2003 | pmid = 14603251 | doi = 10.1038/sj.onc.1206972 }}</ref><ref name=pmid12165861>{{cite journal | vauthors = Conte N, Charafe-Jauffret E, Delaval B, Adélaïde J, Ginestier C, Geneix J, Isnardon D, Jacquemier J, Birnbaum D | title = Carcinogenesis and translational controls: TACC1 is down-regulated in human cancers and associates with mRNA regulators | journal = Oncogene | volume = 21 | issue = 36 | pages = 5619–30 | date = Aug 2002 | pmid = 12165861 | doi = 10.1038/sj.onc.1205658 }}</ref> and [[LSM2]].<ref name=pmid15231747>{{cite journal | vauthors = Lehner B, Sanderson CM | title = A protein interaction framework for human mRNA degradation | journal = Genome Research | volume = 14 | issue = 7 | pages = 1315–23 | date = Jul 2004 | pmid = 15231747 | pmc = 442147 | doi = 10.1101/gr.2122004 }}</ref><ref name=pmid14667819>{{cite journal | vauthors = Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM | 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 | date = Jan 2004 | pmid = 14667819 | doi = 10.1016/S0888-7543(03)00235-0 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 = The Journal of Biological Chemistry | volume = 275 | issue = 34 | pages = 26370–5 | date = Aug 2000 | pmid = 10851237 | doi = 10.1074/jbc.M003299200 }}
| citations =
* {{cite journal | vauthors = Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y | title = Protein-protein interaction panel using mouse full-length cDNAs | journal = Genome Research | volume = 11 | issue = 10 | pages = 1758–65 | date = Oct 2001 | pmid = 11591653 | pmc = 311163 | doi = 10.1101/gr.180101 }}
*{{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 | vauthors = Eystathioy T, Peebles CL, Hamel JC, Vaughn JH, Chan EK | title = Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera | journal = Arthritis and Rheumatism | volume = 46 | issue = 3 | pages = 726–34 | date = Mar 2002 | pmid = 11920408 | doi = 10.1002/art.10220 }}
*{{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 | vauthors = Conte N, Charafe-Jauffret E, Delaval B, Adélaïde J, Ginestier C, Geneix J, Isnardon D, Jacquemier J, Birnbaum D | title = Carcinogenesis and translational controls: TACC1 is down-regulated in human cancers and associates with mRNA regulators | journal = Oncogene | volume = 21 | issue = 36 | pages = 5619–30 | date = Aug 2002 | pmid = 12165861 | doi = 10.1038/sj.onc.1205658 }}
*{{cite journal | author=Suzuki H, Fukunishi Y, Kagawa I, ''et al.'' |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758-65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 }}
* {{cite journal | vauthors = Conte N, Delaval B, Ginestier C, Ferrand A, Isnardon D, Larroque C, Prigent C, Séraphin B, Jacquemier J, Birnbaum D | title = TACC1-chTOG-Aurora A protein complex in breast cancer | journal = Oncogene | volume = 22 | issue = 50 | pages = 8102–16 | date = Nov 2003 | pmid = 14603251 | doi = 10.1038/sj.onc.1206972 }}
*{{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 | vauthors = Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM | 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 | date = Jan 2004 | pmid = 14667819 | doi = 10.1016/S0888-7543(03)00235-0 }}
*{{cite journal | author=Conte N, Charafe-Jauffret E, Delaval B, ''et al.'' |title=Carcinogenesis and translational controls: TACC1 is down-regulated in human cancers and associates with mRNA regulators. |journal=Oncogene |volume=21 |issue= 36 |pages= 5619-30 |year= 2002 |pmid= 12165861 |doi= 10.1038/sj.onc.1205658 }}
* {{cite journal | vauthors = Lehner B, Sanderson CM | title = A protein interaction framework for human mRNA degradation | journal = Genome Research | volume = 14 | issue = 7 | pages = 1315–23 | date = Jul 2004 | pmid = 15231747 | pmc = 442147 | doi = 10.1101/gr.2122004 }}
*{{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 | vauthors = Stanĕk D, Neugebauer KM | title = Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer | journal = The Journal of Cell Biology | volume = 166 | issue = 7 | pages = 1015–25 | date = Sep 2004 | pmid = 15452143 | pmc = 2172029 | doi = 10.1083/jcb.200405160 }}
*{{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=Conte N, Delaval B, Ginestier C, ''et al.'' |title=TACC1-chTOG-Aurora A protein complex in breast cancer. |journal=Oncogene |volume=22 |issue= 50 |pages= 8102-16 |year= 2003 |pmid= 14603251 |doi= 10.1038/sj.onc.1206972 }}
*{{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  | author=Grimwood J, Gordon LA, Olsen A, ''et al.'' |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529-35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 }}
*{{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 | author=Stanĕk D, Neugebauer KM |title=Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer. |journal=J. Cell Biol. |volume=166 |issue= 7 |pages= 1015-25 |year= 2004 |pmid= 15452143 |doi= 10.1083/jcb.200405160 }}
*{{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 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
{{gene-19-stub}}

Latest revision as of 18:11, 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

n/a

RefSeq (protein)

n/a

n/a

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

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. ↑ 3.0 3.1 "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


Retrieved from "https://www.wikidoc.org/index.php?title=LSM7&oldid=1418874"