Full text data of LSM6
LSM6
[Confidence: low (only semi-automatic identification from reviews)]
U6 snRNA-associated Sm-like protein LSm6
Note: presumably soluble (membrane word is not in UniProt keywords or features)
U6 snRNA-associated Sm-like protein LSm6
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62312
ID LSM6_HUMAN Reviewed; 80 AA.
AC P62312; Q4W5J5; Q9Y4Y8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN Name=LSM6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10369684; DOI=10.1093/emboj/18.12.3451;
RA Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B.;
RT "Sm and Sm-like proteins assemble in two related complexes of deep
RT evolutionary origin.";
RL EMBO J. 18:3451-3462(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP IDENTIFICATION IN THE LSM2-LSM8 COMPLEX.
RX PubMed=10523320; DOI=10.1093/emboj/18.20.5789;
RA Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., Luehrmann R.;
RT "A doughnut-shaped heteromer of human Sm-like proteins binds to the
RT 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in
RT vitro.";
RL EMBO J. 18:5789-5802(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE LSM1-LSM7 COMPLEX.
RX PubMed=12515382;
RA Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.;
RT "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes
RT Dcp1/2 and Xrnl in distinct cytoplasmic foci.";
RL RNA 8:1489-1501(2002).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of LSm protein complexes, which are involved
CC in RNA processing and may function in a chaperone-like manner,
CC facilitating the efficient association of RNA processing factors
CC with their substrates. Component of the cytoplasmic LSM1-LSM7
CC complex, which is thought to be involved in mRNA degradation by
CC activating the decapping step in the 5'-to-3' mRNA decay pathway.
CC Component of the nuclear LSM2-LSM8 complex, which is involved in
CC splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple
CC snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP,
CC spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds
CC directly to the 3'-terminal U-tract of U6 snRNA and plays a role
CC in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP
CC complexes. LSM2-LSM8 probably also is involved degradation of
CC nuclear pre-mRNA by targeting them for decapping, and in
CC processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity).
CC -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex, which
CC consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component
CC of the heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8. The LSm subunits form a seven-
CC membered ring structure with a doughnut shape.
CC -!- INTERACTION:
CC P62310:LSM3; NbExp=3; IntAct=EBI-373310, EBI-348239;
CC Q9Y4Y9:LSM5; NbExp=4; IntAct=EBI-373310, EBI-373007;
CC Q9UK45:LSM7; NbExp=4; IntAct=EBI-373310, EBI-348372;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ238098; CAB45869.1; -; mRNA.
DR EMBL; AF182292; AAD56230.1; -; mRNA.
DR EMBL; AK312126; BAG35062.1; -; mRNA.
DR EMBL; AC097372; AAY41032.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05029.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05030.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05031.1; -; Genomic_DNA.
DR EMBL; BC016026; AAH16026.1; -; mRNA.
DR RefSeq; NP_009011.1; NM_007080.2.
DR UniGene; Hs.190520; -.
DR ProteinModelPortal; P62312; -.
DR SMR; P62312; 7-74.
DR DIP; DIP-31128N; -.
DR IntAct; P62312; 15.
DR MINT; MINT-4100591; -.
DR STRING; 9606.ENSP00000296581; -.
DR PhosphoSite; P62312; -.
DR DMDM; 61227727; -.
DR PaxDb; P62312; -.
DR PeptideAtlas; P62312; -.
DR PRIDE; P62312; -.
DR DNASU; 11157; -.
DR Ensembl; ENST00000296581; ENSP00000296581; ENSG00000164167.
DR Ensembl; ENST00000502781; ENSP00000422392; ENSG00000164167.
DR Ensembl; ENST00000504181; ENSP00000420929; ENSG00000164167.
DR Ensembl; ENST00000515311; ENSP00000427036; ENSG00000164167.
DR GeneID; 11157; -.
DR KEGG; hsa:11157; -.
DR UCSC; uc003ikq.4; human.
DR CTD; 11157; -.
DR GeneCards; GC04P147097; -.
DR HGNC; HGNC:17017; LSM6.
DR HPA; HPA045079; -.
DR MIM; 607286; gene.
DR neXtProt; NX_P62312; -.
DR PharmGKB; PA128394584; -.
DR eggNOG; COG1958; -.
DR HOVERGEN; HBG052369; -.
DR InParanoid; P62312; -.
DR KO; K12625; -.
DR OMA; VMYISAD; -.
DR OrthoDB; EOG7HXCTK; -.
DR PhylomeDB; P62312; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; LSM6; -.
DR GenomeRNAi; 11157; -.
DR NextBio; 42433; -.
DR PRO; PR:P62312; -.
DR Bgee; P62312; -.
DR CleanEx; HS_LSM6; -.
DR Genevestigator; P62312; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR010920; LSM_dom.
DR InterPro; IPR001163; Ribonucl_LSM.
DR InterPro; IPR006649; Ribonucl_LSM_euk/arc.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; Spliceosome;
KW tRNA processing.
FT CHAIN 1 80 U6 snRNA-associated Sm-like protein LSm6.
FT /FTId=PRO_0000125575.
FT MOD_RES 59 59 N6-acetyllysine.
SQ SEQUENCE 80 AA; 9128 MW; 21167891FDE804F1 CRC64;
MSLRKQTPSD FLKQIIGRPV VVKLNSGVDY RGVLACLDGY MNIALEQTEE YVNGQLKNKY
GDAFIRGNNV LYISTQKRRM
//
ID LSM6_HUMAN Reviewed; 80 AA.
AC P62312; Q4W5J5; Q9Y4Y8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN Name=LSM6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10369684; DOI=10.1093/emboj/18.12.3451;
RA Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B.;
RT "Sm and Sm-like proteins assemble in two related complexes of deep
RT evolutionary origin.";
RL EMBO J. 18:3451-3462(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP IDENTIFICATION IN THE LSM2-LSM8 COMPLEX.
RX PubMed=10523320; DOI=10.1093/emboj/18.20.5789;
RA Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., Luehrmann R.;
RT "A doughnut-shaped heteromer of human Sm-like proteins binds to the
RT 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in
RT vitro.";
RL EMBO J. 18:5789-5802(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE LSM1-LSM7 COMPLEX.
RX PubMed=12515382;
RA Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.;
RT "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes
RT Dcp1/2 and Xrnl in distinct cytoplasmic foci.";
RL RNA 8:1489-1501(2002).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of LSm protein complexes, which are involved
CC in RNA processing and may function in a chaperone-like manner,
CC facilitating the efficient association of RNA processing factors
CC with their substrates. Component of the cytoplasmic LSM1-LSM7
CC complex, which is thought to be involved in mRNA degradation by
CC activating the decapping step in the 5'-to-3' mRNA decay pathway.
CC Component of the nuclear LSM2-LSM8 complex, which is involved in
CC splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple
CC snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP,
CC spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds
CC directly to the 3'-terminal U-tract of U6 snRNA and plays a role
CC in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP
CC complexes. LSM2-LSM8 probably also is involved degradation of
CC nuclear pre-mRNA by targeting them for decapping, and in
CC processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity).
CC -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex, which
CC consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component
CC of the heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8. The LSm subunits form a seven-
CC membered ring structure with a doughnut shape.
CC -!- INTERACTION:
CC P62310:LSM3; NbExp=3; IntAct=EBI-373310, EBI-348239;
CC Q9Y4Y9:LSM5; NbExp=4; IntAct=EBI-373310, EBI-373007;
CC Q9UK45:LSM7; NbExp=4; IntAct=EBI-373310, EBI-348372;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ238098; CAB45869.1; -; mRNA.
DR EMBL; AF182292; AAD56230.1; -; mRNA.
DR EMBL; AK312126; BAG35062.1; -; mRNA.
DR EMBL; AC097372; AAY41032.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05029.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05030.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05031.1; -; Genomic_DNA.
DR EMBL; BC016026; AAH16026.1; -; mRNA.
DR RefSeq; NP_009011.1; NM_007080.2.
DR UniGene; Hs.190520; -.
DR ProteinModelPortal; P62312; -.
DR SMR; P62312; 7-74.
DR DIP; DIP-31128N; -.
DR IntAct; P62312; 15.
DR MINT; MINT-4100591; -.
DR STRING; 9606.ENSP00000296581; -.
DR PhosphoSite; P62312; -.
DR DMDM; 61227727; -.
DR PaxDb; P62312; -.
DR PeptideAtlas; P62312; -.
DR PRIDE; P62312; -.
DR DNASU; 11157; -.
DR Ensembl; ENST00000296581; ENSP00000296581; ENSG00000164167.
DR Ensembl; ENST00000502781; ENSP00000422392; ENSG00000164167.
DR Ensembl; ENST00000504181; ENSP00000420929; ENSG00000164167.
DR Ensembl; ENST00000515311; ENSP00000427036; ENSG00000164167.
DR GeneID; 11157; -.
DR KEGG; hsa:11157; -.
DR UCSC; uc003ikq.4; human.
DR CTD; 11157; -.
DR GeneCards; GC04P147097; -.
DR HGNC; HGNC:17017; LSM6.
DR HPA; HPA045079; -.
DR MIM; 607286; gene.
DR neXtProt; NX_P62312; -.
DR PharmGKB; PA128394584; -.
DR eggNOG; COG1958; -.
DR HOVERGEN; HBG052369; -.
DR InParanoid; P62312; -.
DR KO; K12625; -.
DR OMA; VMYISAD; -.
DR OrthoDB; EOG7HXCTK; -.
DR PhylomeDB; P62312; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; LSM6; -.
DR GenomeRNAi; 11157; -.
DR NextBio; 42433; -.
DR PRO; PR:P62312; -.
DR Bgee; P62312; -.
DR CleanEx; HS_LSM6; -.
DR Genevestigator; P62312; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR010920; LSM_dom.
DR InterPro; IPR001163; Ribonucl_LSM.
DR InterPro; IPR006649; Ribonucl_LSM_euk/arc.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; Spliceosome;
KW tRNA processing.
FT CHAIN 1 80 U6 snRNA-associated Sm-like protein LSm6.
FT /FTId=PRO_0000125575.
FT MOD_RES 59 59 N6-acetyllysine.
SQ SEQUENCE 80 AA; 9128 MW; 21167891FDE804F1 CRC64;
MSLRKQTPSD FLKQIIGRPV VVKLNSGVDY RGVLACLDGY MNIALEQTEE YVNGQLKNKY
GDAFIRGNNV LYISTQKRRM
//
MIM
607286
*RECORD*
*FIELD* NO
607286
*FIELD* TI
*607286 LSM6 PROTEIN; LSM6
*FIELD* TX
DESCRIPTION
Sm-like proteins were identified in a variety of organisms based on
read moresequence homology with the Sm protein family (see SNRPD2; 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.
CLONING
In a search for human Sm-like proteins, Achsel et al. (1999)
fractionated proteins present in purified (U4/U6.U5) tri-snRNPs and
isolated 7 Sm-like proteins, which they named LSm2-LSm8. Using partial
peptide sequence for database searches, they identified and sequenced
EST clones. Using additional sequence obtained by PCR amplification of a
HeLa cDNA library, they assembled full-length cDNA sequences for
LSM2-LSM8.
Salgado-Garrido et al. (1999) searched database sequence for Sm proteins
and identified 16 potential Sm-related genes in yeast as well as some
Sm-related genes in human and archaebacteria. Using a multiple sequence
alignment of Sm domains, they built a phylogenetic tree of yeast, human,
and archaeal Sm and Sm-like proteins.
GENE FUNCTION
Using electron-microscopy, Achsel et al. (1999) observed that purified
LSm proteins form a heteromer that is stable even in the absence of RNA
and exhibits a doughnut-shaped structure similar to the Sm core RNP
structure. They demonstrated that the purified LSm heteromer binds
specifically to the U6 snRNA at its 3-prime-terminal U-tract. They also
showed that the LSm proteins facilitate the formation of U4/U6 RNA
duplexes in vitro and concluded that the LSm proteins may play a role in
U4/U6 snRNP formation.
Using immunoprecipitation experiments, Salgado-Garrido et al. (1999)
concluded that there is a complex of 7 Sm-like proteins bound to RNA in
yeast. Lsm2-Lsm8 coprecipitate the U4, U5 and U6 snRNAs and directly
associate with the U6 snRNA present in the free U6 snRNP. Additionally,
the yeast Lsm2-Lsm7 proteins were found to be associated with the
pre-RNase P RNA but not the mature RNase RNA. Using immunoprecipitation
experiments from human cell extracts, Salgado-Garrido et al. (1999)
showed that the LSM3 and LSM4 proteins are specifically associated with
snRNP complexes containing the U6 snRNA. Salgado-Garrido et al. (1999)
concluded that Sm and Sm-like proteins assemble in at least 2
functionally conserved complexes of deep evolutionary origin.
By disrupting the Sm and Sm-like genes in yeast, Salgado-Garrido et al.
(1999) concluded that disruption of genes encoding Sm-like proteins
directly associated with the U6 snRNA (Lsm2-8) generated variable
phenotypes. Lsm2, Lsm3, Lsm4, and Lsm8 are essential for vegetative
growth. Lsm5, Lsm6, and Lsm7 are not essential for growth; however,
their disruptions lead to slow growth especially at elevated
temperature. The levels of the U6 snRNA were strongly reduced in the
strains harboring the Lsm5, Lsm6, and Lsm7 disruptions. Lsm1 and Lsm9
are dispensable for vegetative growth, but Lsm1 is required for optimal
vegetative growth at 30 degrees and is temperature sensitive.
Ingelfinger et al. (2002) determined that human LSM1 to LSM7, but not
LSM8, were expressed in HeLa cells within cytoplasmic foci. The foci
also contained a decapping enzyme (DCP1/2) and the exonuclease XRN1
(607994). Coexpression of wildtype and mutant LSM proteins, as well as
fluorescence resonance energy transfer, indicated that the LSM proteins
form a complex similar to one found in yeast. Ingelfinger et al. (2002)
concluded that the foci contain a partially or fully assembled machinery
for the degradation of mRNA.
Using a library of endoribonuclease-prepared short interfering RNAs
(esiRNAs), Kittler et al. (2004) identified 37 genes required for cell
division, one of which was LSM6. These 37 genes included several
splicing factors for which knockdown generates mitotic spindle defects.
In addition, a putative nuclear-export terminator was found to speed up
cell proliferation and mitotic progression after knockdown.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the LSM6
gene to chromosome 4 (TMAP stSG50602).
*FIELD* RF
1. Achsel, T.; Brahms, H.; Kastner, B.; Bachi, A.; Wilm, M.; Luhrmann,
R.: A doughnut-shaped heteromer of human Sm-like proteins binds to
the 3-prime end of U6 snRNA, thereby facilitating U4/U6 duplex formation
in vitro. EMBO J. 18: 5789-5802, 1999.
2. Ingelfinger, D.; Arndt-Jovin, D. J.; Luhrmann, R.; Achsel, T.:
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes
Dcp1/2 and Xrn1 in distinct cytoplasmic foci. RNA 8: 1489-1501,
2002.
3. Kittler, R.; Putz, G.; Pelletier, L.; Poser, I.; Heninger, A.-K.;
Drechsel, D.; Fischer, S.; Konstantinova, I.; Habermann, B.; Grabner,
H.; Yaspo, M.-L.; Himmelbauer, H.; Korn, B.; Neugebauer, K.; Pisabarro,
M. T.; Buchholz, F.: An endoribonuclease-prepared siRNA screen in
human cells identifies genes essential for cell division. Nature 432:
1036-1040, 2004.
4. Salgado-Garrido, J.; Bragado-Nilsson, E.; Kandels-Lewis, S.; Seraphin,
B.: Sm and Sm-like proteins assemble in two related complexes of
deep evolutionary origin. EMBO J. 18: 3451-3462, 1999.
*FIELD* CN
Ada Hamosh - updated: 03/08/2005
Patricia A. Hartz - updated: 7/29/2003
*FIELD* CD
Dawn Watkins-Chow: 10/9/2002
*FIELD* ED
alopez: 03/08/2005
mgross: 7/29/2003
carol: 10/9/2002
*RECORD*
*FIELD* NO
607286
*FIELD* TI
*607286 LSM6 PROTEIN; LSM6
*FIELD* TX
DESCRIPTION
Sm-like proteins were identified in a variety of organisms based on
read moresequence homology with the Sm protein family (see SNRPD2; 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.
CLONING
In a search for human Sm-like proteins, Achsel et al. (1999)
fractionated proteins present in purified (U4/U6.U5) tri-snRNPs and
isolated 7 Sm-like proteins, which they named LSm2-LSm8. Using partial
peptide sequence for database searches, they identified and sequenced
EST clones. Using additional sequence obtained by PCR amplification of a
HeLa cDNA library, they assembled full-length cDNA sequences for
LSM2-LSM8.
Salgado-Garrido et al. (1999) searched database sequence for Sm proteins
and identified 16 potential Sm-related genes in yeast as well as some
Sm-related genes in human and archaebacteria. Using a multiple sequence
alignment of Sm domains, they built a phylogenetic tree of yeast, human,
and archaeal Sm and Sm-like proteins.
GENE FUNCTION
Using electron-microscopy, Achsel et al. (1999) observed that purified
LSm proteins form a heteromer that is stable even in the absence of RNA
and exhibits a doughnut-shaped structure similar to the Sm core RNP
structure. They demonstrated that the purified LSm heteromer binds
specifically to the U6 snRNA at its 3-prime-terminal U-tract. They also
showed that the LSm proteins facilitate the formation of U4/U6 RNA
duplexes in vitro and concluded that the LSm proteins may play a role in
U4/U6 snRNP formation.
Using immunoprecipitation experiments, Salgado-Garrido et al. (1999)
concluded that there is a complex of 7 Sm-like proteins bound to RNA in
yeast. Lsm2-Lsm8 coprecipitate the U4, U5 and U6 snRNAs and directly
associate with the U6 snRNA present in the free U6 snRNP. Additionally,
the yeast Lsm2-Lsm7 proteins were found to be associated with the
pre-RNase P RNA but not the mature RNase RNA. Using immunoprecipitation
experiments from human cell extracts, Salgado-Garrido et al. (1999)
showed that the LSM3 and LSM4 proteins are specifically associated with
snRNP complexes containing the U6 snRNA. Salgado-Garrido et al. (1999)
concluded that Sm and Sm-like proteins assemble in at least 2
functionally conserved complexes of deep evolutionary origin.
By disrupting the Sm and Sm-like genes in yeast, Salgado-Garrido et al.
(1999) concluded that disruption of genes encoding Sm-like proteins
directly associated with the U6 snRNA (Lsm2-8) generated variable
phenotypes. Lsm2, Lsm3, Lsm4, and Lsm8 are essential for vegetative
growth. Lsm5, Lsm6, and Lsm7 are not essential for growth; however,
their disruptions lead to slow growth especially at elevated
temperature. The levels of the U6 snRNA were strongly reduced in the
strains harboring the Lsm5, Lsm6, and Lsm7 disruptions. Lsm1 and Lsm9
are dispensable for vegetative growth, but Lsm1 is required for optimal
vegetative growth at 30 degrees and is temperature sensitive.
Ingelfinger et al. (2002) determined that human LSM1 to LSM7, but not
LSM8, were expressed in HeLa cells within cytoplasmic foci. The foci
also contained a decapping enzyme (DCP1/2) and the exonuclease XRN1
(607994). Coexpression of wildtype and mutant LSM proteins, as well as
fluorescence resonance energy transfer, indicated that the LSM proteins
form a complex similar to one found in yeast. Ingelfinger et al. (2002)
concluded that the foci contain a partially or fully assembled machinery
for the degradation of mRNA.
Using a library of endoribonuclease-prepared short interfering RNAs
(esiRNAs), Kittler et al. (2004) identified 37 genes required for cell
division, one of which was LSM6. These 37 genes included several
splicing factors for which knockdown generates mitotic spindle defects.
In addition, a putative nuclear-export terminator was found to speed up
cell proliferation and mitotic progression after knockdown.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the LSM6
gene to chromosome 4 (TMAP stSG50602).
*FIELD* RF
1. Achsel, T.; Brahms, H.; Kastner, B.; Bachi, A.; Wilm, M.; Luhrmann,
R.: A doughnut-shaped heteromer of human Sm-like proteins binds to
the 3-prime end of U6 snRNA, thereby facilitating U4/U6 duplex formation
in vitro. EMBO J. 18: 5789-5802, 1999.
2. Ingelfinger, D.; Arndt-Jovin, D. J.; Luhrmann, R.; Achsel, T.:
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes
Dcp1/2 and Xrn1 in distinct cytoplasmic foci. RNA 8: 1489-1501,
2002.
3. Kittler, R.; Putz, G.; Pelletier, L.; Poser, I.; Heninger, A.-K.;
Drechsel, D.; Fischer, S.; Konstantinova, I.; Habermann, B.; Grabner,
H.; Yaspo, M.-L.; Himmelbauer, H.; Korn, B.; Neugebauer, K.; Pisabarro,
M. T.; Buchholz, F.: An endoribonuclease-prepared siRNA screen in
human cells identifies genes essential for cell division. Nature 432:
1036-1040, 2004.
4. Salgado-Garrido, J.; Bragado-Nilsson, E.; Kandels-Lewis, S.; Seraphin,
B.: Sm and Sm-like proteins assemble in two related complexes of
deep evolutionary origin. EMBO J. 18: 3451-3462, 1999.
*FIELD* CN
Ada Hamosh - updated: 03/08/2005
Patricia A. Hartz - updated: 7/29/2003
*FIELD* CD
Dawn Watkins-Chow: 10/9/2002
*FIELD* ED
alopez: 03/08/2005
mgross: 7/29/2003
carol: 10/9/2002