LSM6_HUMAN
ID LSM6_HUMAN Reviewed; 80 AA.
AC P62312; Q4W5J5; Q9Y4Y8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN Name=LSM6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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, IDENTIFICATION IN THE
RP LSM2-LSM8 COMPLEX, SUBUNIT, FUNCTION, AND SUBCELLULAR LOCATION.
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 3'-end
RT of U6 snRNA, thereby facilitating U4/U6 duplex formation in 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROBABLE FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION, AND
RP 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26912367; DOI=10.1126/science.aad2085;
RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA Luhrmann R., Stark H.;
RT "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL Science 351:1416-1420(2016).
RN [11] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5
CC tri-snRNP complex that is involved in spliceosome assembly, and as
CC component of the precatalytic spliceosome (spliceosome B complex)
CC (PubMed:28781166). The heptameric LSM2-8 complex binds specifically to
CC the 3'-terminal U-tract of U6 snRNA (PubMed:10523320). Component of LSm
CC protein complexes, which are involved in RNA processing and may
CC function in a chaperone-like manner, facilitating the efficient
CC association of RNA processing factors with their substrates. Component
CC of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved
CC in mRNA degradation by activating the decapping step in the 5'-to-3'
CC mRNA decay pathway (Probable). {ECO:0000269|PubMed:10523320,
CC ECO:0000269|PubMed:28781166, ECO:0000305|PubMed:12515382}.
CC -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC complex) (PubMed:28781166). Component of the U4/U6-U5 tri-snRNP
CC complex, a building block of the precatalytic spliceosome (spliceosome
CC B complex) (PubMed:10523320, PubMed:28781166, PubMed:26912367). The
CC U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and
CC at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2,
CC PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5,
CC LSM6, LSM7 and LSM8 (PubMed:26912367). LSM2, LSM3, LSM4, LSM5, LSM6,
CC LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8
CC complex) that is part of the U4/U6-U5 tri-snRNP complex and the
CC precatalytic spliceosome (PubMed:10523320, PubMed:26912367,
CC PubMed:28781166). Component of the heptameric LSM1-LSM7 complex, which
CC consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7
CC (PubMed:12515382). {ECO:0000269|PubMed:10523320,
CC ECO:0000269|PubMed:12515382, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC P62312; P54105: CLNS1A; NbExp=8; IntAct=EBI-373310, EBI-724693;
CC P62312; O15116: LSM1; NbExp=4; IntAct=EBI-373310, EBI-347619;
CC P62312; Q9Y333: LSM2; NbExp=7; IntAct=EBI-373310, EBI-347416;
CC P62312; P62310: LSM3; NbExp=15; IntAct=EBI-373310, EBI-348239;
CC P62312; Q9Y4Y9: LSM5; NbExp=13; IntAct=EBI-373310, EBI-373007;
CC P62312; Q9UK45: LSM7; NbExp=5; IntAct=EBI-373310, EBI-348372;
CC P62312; O95777: LSM8; NbExp=3; IntAct=EBI-373310, EBI-347779;
CC P62312; Q86TB9: PATL1; NbExp=3; IntAct=EBI-373310, EBI-2562092;
CC P62312; O00560: SDCBP; NbExp=6; IntAct=EBI-373310, EBI-727004;
CC P62312; P62316: SNRPD2; NbExp=3; IntAct=EBI-373310, EBI-297993;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12515382}. Nucleus
CC {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily. {ECO:0000305}.
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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 CCDS; CCDS3767.1; -.
DR RefSeq; NP_009011.1; NM_007080.2.
DR RefSeq; XP_016863161.1; XM_017007672.1.
DR RefSeq; XP_016863162.1; XM_017007673.1.
DR PDB; 3JCR; EM; 7.00 A; 6=1-80.
DR PDB; 5O9Z; EM; 4.50 A; s=1-80.
DR PDB; 6AH0; EM; 5.70 A; x=1-80.
DR PDB; 6AHD; EM; 3.80 A; x=1-80.
DR PDB; 6QW6; EM; 2.92 A; 66=1-80.
DR PDB; 6QX9; EM; 3.28 A; 66=1-80.
DR PDB; 7ABG; EM; 7.80 A; J=1-80.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; P62312; -.
DR SMR; P62312; -.
DR BioGRID; 116328; 73.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; P62312; -.
DR DIP; DIP-31128N; -.
DR IntAct; P62312; 36.
DR MINT; P62312; -.
DR STRING; 9606.ENSP00000422392; -.
DR DrugBank; DB04272; Citric acid.
DR DrugBank; DB02745; Uridine.
DR DrugBank; DB03685; Uridine monophosphate.
DR iPTMnet; P62312; -.
DR PhosphoSitePlus; P62312; -.
DR SwissPalm; P62312; -.
DR BioMuta; LSM6; -.
DR DMDM; 61227727; -.
DR EPD; P62312; -.
DR jPOST; P62312; -.
DR MassIVE; P62312; -.
DR PaxDb; P62312; -.
DR PeptideAtlas; P62312; -.
DR PRIDE; P62312; -.
DR ProteomicsDB; 57390; -.
DR TopDownProteomics; P62312; -.
DR Antibodypedia; 27518; 107 antibodies from 21 providers.
DR DNASU; 11157; -.
DR Ensembl; ENST00000296581.11; ENSP00000296581.5; ENSG00000164167.12.
DR Ensembl; ENST00000502781.5; ENSP00000422392.1; ENSG00000164167.12.
DR Ensembl; ENST00000504181.1; ENSP00000420929.1; ENSG00000164167.12.
DR Ensembl; ENST00000515311.5; ENSP00000427036.1; ENSG00000164167.12.
DR Ensembl; ENST00000649747.1; ENSP00000497311.1; ENSG00000164167.12.
DR GeneID; 11157; -.
DR KEGG; hsa:11157; -.
DR MANE-Select; ENST00000296581.11; ENSP00000296581.5; NM_007080.3; NP_009011.1.
DR UCSC; uc003ikq.5; human.
DR CTD; 11157; -.
DR GeneCards; LSM6; -.
DR HGNC; HGNC:17017; LSM6.
DR HPA; ENSG00000164167; Low tissue specificity.
DR MIM; 607286; gene.
DR neXtProt; NX_P62312; -.
DR OpenTargets; ENSG00000164167; -.
DR PharmGKB; PA128394584; -.
DR VEuPathDB; HostDB:ENSG00000164167; -.
DR eggNOG; KOG1783; Eukaryota.
DR GeneTree; ENSGT00940000154978; -.
DR HOGENOM; CLU_076902_7_4_1; -.
DR InParanoid; P62312; -.
DR OMA; KMRRSYG; -.
DR OrthoDB; 1627235at2759; -.
DR PhylomeDB; P62312; -.
DR TreeFam; TF313751; -.
DR PathwayCommons; P62312; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P62312; -.
DR BioGRID-ORCS; 11157; 666 hits in 1013 CRISPR screens.
DR ChiTaRS; LSM6; human.
DR GeneWiki; LSM6; -.
DR GenomeRNAi; 11157; -.
DR Pharos; P62312; Tbio.
DR PRO; PR:P62312; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P62312; protein.
DR Bgee; ENSG00000164167; Expressed in monocyte and 205 other tissues.
DR Genevisible; P62312; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0120115; C:Lsm2-8 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:UniProtKB.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB.
DR GO; GO:0005688; C:U6 snRNP; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR016487; Lsm6/sSmF.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR11021; PTHR11021; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; 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
FT /note="U6 snRNA-associated Sm-like protein LSm6"
FT /id="PRO_0000125575"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 80 AA; 9128 MW; 21167891FDE804F1 CRC64;
MSLRKQTPSD FLKQIIGRPV VVKLNSGVDY RGVLACLDGY MNIALEQTEE YVNGQLKNKY
GDAFIRGNNV LYISTQKRRM
