LSM8_HUMAN
ID LSM8_HUMAN Reviewed; 96 AA.
AC O95777;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm8;
GN Name=LSM8;
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], PARTIAL PROTEIN SEQUENCE, SUBUNIT, FUNCTION,
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 [4]
RP PROTEIN SEQUENCE OF 2-11; 29-44 AND 88-96, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9] {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 [10] {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).
CC {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:28781166}.
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). {ECO:0000269|PubMed:10523320,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC O95777; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-347779, EBI-25840379;
CC O95777; P42858: HTT; NbExp=15; IntAct=EBI-347779, EBI-466029;
CC O95777; Q9Y333: LSM2; NbExp=8; IntAct=EBI-347779, EBI-347416;
CC O95777; P62310: LSM3; NbExp=6; IntAct=EBI-347779, EBI-348239;
CC O95777; Q9Y4Z0: LSM4; NbExp=4; IntAct=EBI-347779, EBI-372521;
CC O95777; P62312: LSM6; NbExp=3; IntAct=EBI-347779, EBI-373310;
CC O95777; D3DTS7: PMP22; NbExp=3; IntAct=EBI-347779, EBI-25882629;
CC O95777; O60260-5: PRKN; NbExp=6; IntAct=EBI-347779, EBI-21251460;
CC O95777; P37840: SNCA; NbExp=3; IntAct=EBI-347779, EBI-985879;
CC O95777; P00441: SOD1; NbExp=3; IntAct=EBI-347779, EBI-990792;
CC O95777; Q13148: TARDBP; NbExp=6; IntAct=EBI-347779, EBI-372899;
CC O95777; P09936: UCHL1; NbExp=3; IntAct=EBI-347779, EBI-714860;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10523320,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AF182294; AAD56232.1; -; mRNA.
DR EMBL; AC006389; AAD15542.1; -; Genomic_DNA.
DR EMBL; BC002742; AAH02742.1; -; mRNA.
DR EMBL; BC022440; AAH22440.1; -; mRNA.
DR CCDS; CCDS5775.1; -.
DR RefSeq; NP_057284.1; NM_016200.4.
DR PDB; 3JCR; EM; 7.00 A; 8=1-96.
DR PDB; 5O9Z; EM; 4.50 A; u=1-96.
DR PDB; 6AH0; EM; 5.70 A; z=1-96.
DR PDB; 6AHD; EM; 3.80 A; z=1-96.
DR PDB; 6QW6; EM; 2.92 A; 68=1-96.
DR PDB; 6QX9; EM; 3.28 A; 68=1-96.
DR PDB; 7ABG; EM; 7.80 A; A3=1-96.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; O95777; -.
DR SMR; O95777; -.
DR BioGRID; 119679; 87.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; O95777; -.
DR DIP; DIP-31195N; -.
DR IntAct; O95777; 66.
DR MINT; O95777; -.
DR STRING; 9606.ENSP00000249299; -.
DR GlyGen; O95777; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95777; -.
DR PhosphoSitePlus; O95777; -.
DR BioMuta; LSM8; -.
DR EPD; O95777; -.
DR jPOST; O95777; -.
DR MassIVE; O95777; -.
DR MaxQB; O95777; -.
DR PaxDb; O95777; -.
DR PeptideAtlas; O95777; -.
DR PRIDE; O95777; -.
DR ProteomicsDB; 51040; -.
DR TopDownProteomics; O95777; -.
DR Antibodypedia; 17509; 66 antibodies from 22 providers.
DR DNASU; 51691; -.
DR Ensembl; ENST00000249299.7; ENSP00000249299.2; ENSG00000128534.8.
DR GeneID; 51691; -.
DR KEGG; hsa:51691; -.
DR MANE-Select; ENST00000249299.7; ENSP00000249299.2; NM_016200.5; NP_057284.1.
DR UCSC; uc003vjg.4; human.
DR CTD; 51691; -.
DR GeneCards; LSM8; -.
DR HGNC; HGNC:20471; LSM8.
DR HPA; ENSG00000128534; Low tissue specificity.
DR MIM; 607288; gene.
DR neXtProt; NX_O95777; -.
DR OpenTargets; ENSG00000128534; -.
DR PharmGKB; PA165618166; -.
DR VEuPathDB; HostDB:ENSG00000128534; -.
DR eggNOG; KOG1784; Eukaryota.
DR GeneTree; ENSGT00730000111212; -.
DR InParanoid; O95777; -.
DR OMA; CDGSMNL; -.
DR OrthoDB; 1545004at2759; -.
DR PhylomeDB; O95777; -.
DR TreeFam; TF314555; -.
DR PathwayCommons; O95777; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O95777; -.
DR BioGRID-ORCS; 51691; 384 hits in 501 CRISPR screens.
DR ChiTaRS; LSM8; human.
DR GeneWiki; LSM8; -.
DR GenomeRNAi; 51691; -.
DR Pharos; O95777; Tbio.
DR PRO; PR:O95777; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O95777; protein.
DR Bgee; ENSG00000128534; Expressed in calcaneal tendon and 199 other tissues.
DR ExpressionAtlas; O95777; baseline and differential.
DR Genevisible; O95777; HS.
DR GO; GO:0120115; C:Lsm2-8 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; 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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; NAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0016070; P:RNA metabolic process; IBA:GO_Central.
DR CDD; cd01727; LSm8; 1.
DR InterPro; IPR034103; Lsm8.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR044642; PTHR15588.
DR PANTHER; PTHR15588; PTHR15588; 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; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..96
FT /note="U6 snRNA-associated Sm-like protein LSm8"
FT /id="PRO_0000125582"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
SQ SEQUENCE 96 AA; 10403 MW; 15D26E6B75AA2EE1 CRC64;
MTSALENYIN RTVAVITSDG RMIVGTLKGF DQTINLILDE SHERVFSSSQ GVEQVVLGLY
IVRGDNVAVI GEIDEETDSA LDLGNIRAEP LNSVAH
