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 02-SEP-2026, entry version 176. 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; DOI=10.1017/s1355838202021726; 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 a role in pre-mRNA splicing as component of the U4/U6- CC U5 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:26912367, PubMed:28781166). 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=12; IntAct=EBI-373310, EBI-724693; CC P62312; O15116: LSM1; NbExp=7; IntAct=EBI-373310, EBI-347619; CC P62312; Q9Y333: LSM2; NbExp=9; IntAct=EBI-373310, EBI-347416; CC P62312; P62310: LSM3; NbExp=17; IntAct=EBI-373310, EBI-348239; CC P62312; Q9Y4Y9: LSM5; NbExp=16; IntAct=EBI-373310, EBI-373007; CC P62312; Q9UK45: LSM7; NbExp=8; IntAct=EBI-373310, EBI-348372; CC P62312; O95777: LSM8; NbExp=5; IntAct=EBI-373310, EBI-347779; CC P62312; Q86TB9: PATL1; NbExp=6; IntAct=EBI-373310, EBI-2562092; CC P62312; O00560: SDCBP; NbExp=6; IntAct=EBI-373310, EBI-727004; CC P62312; P62316: SNRPD2; NbExp=6; IntAct=EBI-373310, EBI-297993; CC P62312; P62306: SNRPF; NbExp=3; IntAct=EBI-373310, EBI-356900; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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 CCDS; CCDS3767.1; -. DR RefSeq; NP_009011.1; NM_007080.3. DR RefSeq; XP_016863161.1; XM_017007672.2. DR RefSeq; XP_016863162.1; XM_017007673.2. DR RefSeq; XP_054204810.1; XM_054348835.1. DR RefSeq; XP_054204811.1; XM_054348836.1. 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 PDB; 8H6E; EM; 3.20 A; 6e=1-80. DR PDB; 8H6J; EM; 3.25 A; 6e=1-80. DR PDB; 8H6K; EM; 2.70 A; 6e=1-80. DR PDB; 8H6L; EM; 2.60 A; 6e=1-80. DR PDB; 8QO9; EM; 5.29 A; 66=1-80. DR PDB; 8QXD; EM; 9.60 A; 66=1-80. DR PDB; 8QZS; EM; 4.10 A; 66=1-80. DR PDB; 8R08; EM; 6.10 A; 66=1-80. DR PDB; 8R09; EM; 4.30 A; 66=1-80. DR PDB; 8R0A; EM; 5.80 A; 66=1-80. DR PDB; 8R0B; EM; 4.40 A; 66=1-80. DR PDB; 8RM5; EM; 6.90 A; 66=1-80. DR AlphaFoldDB; P62312; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-18529; -. DR EMDB; EMD-18718; -. DR EMDB; EMD-18781; -. DR EMDB; EMD-18786; -. DR EMDB; EMD-18787; -. DR EMDB; EMD-18788; -. DR EMDB; EMD-18789; -. DR EMDB; EMD-19349; -. DR EMDB; EMD-34500; -. DR EMDB; EMD-34505; -. DR EMDB; EMD-34507; -. DR EMDB; EMD-34508; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR SMR; P62312; -. DR BioGRID; 116328; 101. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26415; U6 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26435; Major Spliceosomal B complex. DR ComplexPortal; CPX-26499; U6atac small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26502; U4atac/U6atac.U5 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26553; LSM2-8 complex. DR ComplexPortal; CPX-26554; LSM1-7 complex. DR ComplexPortal; CPX-26558; LSM1-7, PATL1 complex. DR CORUM; P62312; -. DR DIP; DIP-31128N; -. DR FunCoup; P62312; 2144. DR IntAct; P62312; 60. DR MINT; P62312; -. DR NDEx; MUSIC2-C5191-LSM6; Osteosarcoma (U2OS) cell map - Actin filaments (48 proteins). DR STRING; 9606.ENSP00000296581; -. DR DrugBank; DB04272; Citric acid. DR DrugBank; DB02745; Uridine. DR DrugBank; DB03685; Uridine monophosphate. DR GlyGen; P62312; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62312; -. DR PhosphoSitePlus; P62312; -. DR SwissPalm; P62312; -. DR BioMuta; LSM6; -. DR DMDM; 61227727; -. DR jPOST; P62312; -. DR MassIVE; P62312; -. DR PaxDb; 9606-ENSP00000296581; -. DR PeptideAtlas; P62312; -. DR ProteomicsDB; 57390; -. DR Pumba; P62312; -. DR TopDownProteomics; P62312; -. DR Antibodypedia; 27518; 100 antibodies from 20 providers. DR DNASU; 11157; -. DR Ensembl; ENST00000296581.11; ENSP00000296581.5; ENSG00000164167.14. DR Ensembl; ENST00000502781.5; ENSP00000422392.1; ENSG00000164167.14. DR Ensembl; ENST00000504181.1; ENSP00000420929.1; ENSG00000164167.14. DR Ensembl; ENST00000515311.5; ENSP00000427036.1; ENSG00000164167.14. DR Ensembl; ENST00000649747.1; ENSP00000497311.1; ENSG00000164167.14. DR Ensembl; ENST00000850848.1; ENSP00000520937.1; ENSG00000164167.14. DR Ensembl; ENST00000871396.1; ENSP00000541455.1; ENSG00000164167.14. DR Ensembl; ENST00000871398.1; ENSP00000541457.1; ENSG00000164167.14. DR Ensembl; ENST00000871399.1; ENSP00000541458.1; ENSG00000164167.14. DR Ensembl; ENST00000871400.1; ENSP00000541459.1; ENSG00000164167.14. DR Ensembl; ENST00000871401.1; ENSP00000541460.1; ENSG00000164167.14. DR Ensembl; ENST00000871402.1; ENSP00000541461.1; ENSG00000164167.14. DR Ensembl; ENST00000871404.1; ENSP00000541463.1; ENSG00000164167.14. DR Ensembl; ENST00000871405.1; ENSP00000541464.1; ENSG00000164167.14. DR Ensembl; ENST00000937837.1; ENSP00000607896.1; ENSG00000164167.14. DR Ensembl; ENST00000937838.1; ENSP00000607897.1; ENSG00000164167.14. DR Ensembl; ENST00000937839.1; ENSP00000607898.1; ENSG00000164167.14. DR Ensembl; ENST00000937840.1; ENSP00000607899.1; ENSG00000164167.14. DR Ensembl; ENST00000946380.1; ENSP00000616439.1; ENSG00000164167.14. DR Ensembl; ENST00000946381.1; ENSP00000616440.1; ENSG00000164167.14. 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 AGR; HGNC:17017; -. DR ClinPGx; PA128394584; -. DR CTD; 11157; -. DR GeneCards; LSM6; -. DR HGNC; HGNC:17017; LSM6. DR HPA; ENSG00000164167; Low tissue specificity. DR MIM; 607286; gene. DR OpenTargets; ENSG00000164167; -. DR VEuPathDB; HostDB:ENSG00000164167; -. DR eggNOG; KOG1783; Eukaryota. DR GeneTree; ENSGT00940000154978; -. DR HOGENOM; CLU_076902_7_4_1; -. DR InParanoid; P62312; -. DR OMA; EQTVEYV; -. DR OrthoDB; 268799at2759; -. DR PAN-GO; P62312; 8 GO annotations based on evolutionary models. DR PhylomeDB; P62312; -. 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 SIGNOR; P62312; -. DR Agora; ENSG00000164167; -. DR BioGRID-ORCS; 11157; 696 hits in 1090 CRISPR screens. DR CD-CODE; 232F8A39; P-body. 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 207 other cell types or tissues. 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:0071011; C:precatalytic spliceosome; IPI:ComplexPortal. 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:0005681; C:spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0071001; C:U4/U6 snRNP; NAS:ComplexPortal. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB. DR GO; GO:0071002; C:U4atac/U6atac snRNP; NAS:ComplexPortal. DR GO; GO:0071009; C:U4atac/U6atac x U5 tri-snRNP complex; NAS:ComplexPortal. DR GO; GO:0005688; C:U6 snRNP; IBA:GO_Central. DR GO; GO:0005691; C:U6atac snRNP; NAS:ComplexPortal. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; NAS:ComplexPortal. 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:0000387; P:spliceosomal snRNP assembly; NAS:ComplexPortal. DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; NAS:ComplexPortal. DR CDD; cd01726; LSm6; 1. DR FunFam; 2.30.30.100:FF:000010; U6 snRNA-associated Sm-like protein LSm6; 1. DR Gene3D; 2.30.30.100; -; 1. DR InterPro; IPR016487; Lsm6/sSmF. DR InterPro; IPR010920; LSM_dom_sf. DR InterPro; IPR047575; Sm. DR InterPro; IPR001163; Sm_dom_euk/arc. DR PANTHER; PTHR11021; SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F; 1. DR PANTHER; PTHR11021:SF1; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM6; 1. DR Pfam; PF01423; LSM; 1. DR PIRSF; PIRSF006609; snRNP_SmF; 1. DR SMART; SM00651; Sm; 1. DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1. DR PROSITE; PS52002; SM; 1. DR PDBsum; 3JCR; -. DR PDBsum; 5O9Z; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6QW6; -. DR PDBsum; 6QX9; -. DR PDBsum; 7ABG; -. DR PDBsum; 8H6E; -. DR PDBsum; 8H6J; -. DR PDBsum; 8H6K; -. DR PDBsum; 8H6L; -. DR PDBsum; 8QO9; -. DR PDBsum; 8QXD; -. DR PDBsum; 8QZS; -. DR PDBsum; 8R08; -. DR PDBsum; 8R09; -. DR PDBsum; 8R0A; -. DR PDBsum; 8R0B; -. DR PDBsum; 8RM5; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW mRNA processing; mRNA splicing; Nucleus; Proteomics identification; KW Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing; KW Spliceosome; tRNA processing. FT CHAIN 1..80 FT /note="U6 snRNA-associated Sm-like protein LSm6" FT /id="PRO_0000125575" FT DOMAIN 7..79 FT /note="Sm" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346" FT MOD_RES 59 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT HELIX 8..14 FT /evidence="ECO:0007829|PDB:8H6L" FT STRAND 18..24 FT /evidence="ECO:0007829|PDB:8H6L" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:8H6L" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:8H6L" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:6QW6" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:8H6L" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:8H6L" SQ SEQUENCE 80 AA; 9128 MW; 21167891FDE804F1 CRC64; MSLRKQTPSD FLKQIIGRPV VVKLNSGVDY RGVLACLDGY MNIALEQTEE YVNGQLKNKY GDAFIRGNNV LYISTQKRRM //