LSM5_HUMAN
ID LSM5_HUMAN Reviewed; 91 AA.
AC Q9Y4Y9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm5;
GN Name=LSM5;
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] (ISOFORM 1).
RC TISSUE=Placenta;
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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, SUBUNIT,
RP 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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, and Brain;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 ALA-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] {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 [9] {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 Q9Y4Y9; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-373007, EBI-742054;
CC Q9Y4Y9; P62310: LSM3; NbExp=6; IntAct=EBI-373007, EBI-348239;
CC Q9Y4Y9; P62312: LSM6; NbExp=13; IntAct=EBI-373007, EBI-373310;
CC Q9Y4Y9; Q9UK45: LSM7; NbExp=18; IntAct=EBI-373007, EBI-348372;
CC Q9Y4Y9; Q9H4B4: PLK3; NbExp=3; IntAct=EBI-373007, EBI-751877;
CC Q9Y4Y9; P62304: SNRPE; NbExp=4; IntAct=EBI-373007, EBI-348082;
CC Q9Y4Y9; P62306: SNRPF; NbExp=11; IntAct=EBI-373007, EBI-356900;
CC Q9Y4Y9; P62380: TBPL1; NbExp=3; IntAct=EBI-373007, EBI-716225;
CC Q9Y4Y9; O95988: TCL1B; NbExp=3; IntAct=EBI-373007, EBI-727338;
CC Q9Y4Y9; Q6ZNM6: TEX43; NbExp=3; IntAct=EBI-373007, EBI-18115728;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10523320,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y4Y9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4Y9-2; Sequence=VSP_040991;
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AJ238097; CAB45868.1; -; mRNA.
DR EMBL; AF182291; AAD56229.1; -; mRNA.
DR EMBL; AC018641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005938; AAH05938.1; -; mRNA.
DR EMBL; BF701546; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47571.1; -. [Q9Y4Y9-2]
DR CCDS; CCDS5438.1; -. [Q9Y4Y9-1]
DR RefSeq; NP_001124182.1; NM_001130710.1. [Q9Y4Y9-2]
DR RefSeq; NP_001132971.1; NM_001139499.1. [Q9Y4Y9-2]
DR RefSeq; NP_036454.1; NM_012322.2. [Q9Y4Y9-1]
DR PDB; 3JCR; EM; 7.00 A; 5=1-91.
DR PDB; 5O9Z; EM; 4.50 A; r=1-91.
DR PDB; 6AH0; EM; 5.70 A; t=1-91.
DR PDB; 6AHD; EM; 3.80 A; t=1-91.
DR PDB; 6QW6; EM; 2.92 A; 65=1-91.
DR PDB; 6QX9; EM; 3.28 A; 65=1-91.
DR PDB; 7ABG; EM; 7.80 A; H=1-91.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; Q9Y4Y9; -.
DR SMR; Q9Y4Y9; -.
DR BioGRID; 117180; 73.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q9Y4Y9; -.
DR DIP; DIP-31162N; -.
DR IntAct; Q9Y4Y9; 43.
DR MINT; Q9Y4Y9; -.
DR STRING; 9606.ENSP00000410758; -.
DR iPTMnet; Q9Y4Y9; -.
DR PhosphoSitePlus; Q9Y4Y9; -.
DR SwissPalm; Q9Y4Y9; -.
DR BioMuta; LSM5; -.
DR DMDM; 10720081; -.
DR EPD; Q9Y4Y9; -.
DR jPOST; Q9Y4Y9; -.
DR MassIVE; Q9Y4Y9; -.
DR MaxQB; Q9Y4Y9; -.
DR PaxDb; Q9Y4Y9; -.
DR PeptideAtlas; Q9Y4Y9; -.
DR PRIDE; Q9Y4Y9; -.
DR ProteomicsDB; 86265; -. [Q9Y4Y9-1]
DR ProteomicsDB; 86266; -. [Q9Y4Y9-2]
DR TopDownProteomics; Q9Y4Y9-1; -. [Q9Y4Y9-1]
DR TopDownProteomics; Q9Y4Y9-2; -. [Q9Y4Y9-2]
DR Antibodypedia; 44303; 76 antibodies from 25 providers.
DR DNASU; 23658; -.
DR Ensembl; ENST00000409292.5; ENSP00000386814.1; ENSG00000106355.10. [Q9Y4Y9-2]
DR Ensembl; ENST00000409782.5; ENSP00000387109.1; ENSG00000106355.10. [Q9Y4Y9-2]
DR Ensembl; ENST00000409909.7; ENSP00000386363.3; ENSG00000106355.10. [Q9Y4Y9-2]
DR Ensembl; ENST00000409952.3; ENSP00000387126.3; ENSG00000106355.10. [Q9Y4Y9-2]
DR Ensembl; ENST00000410044.5; ENSP00000386707.1; ENSG00000106355.10. [Q9Y4Y9-2]
DR Ensembl; ENST00000450169.7; ENSP00000410758.2; ENSG00000106355.10. [Q9Y4Y9-1]
DR GeneID; 23658; -.
DR KEGG; hsa:23658; -.
DR MANE-Select; ENST00000450169.7; ENSP00000410758.2; NM_012322.3; NP_036454.1.
DR UCSC; uc003tct.3; human. [Q9Y4Y9-1]
DR CTD; 23658; -.
DR DisGeNET; 23658; -.
DR GeneCards; LSM5; -.
DR HGNC; HGNC:17162; LSM5.
DR HPA; ENSG00000106355; Low tissue specificity.
DR MIM; 607285; gene.
DR neXtProt; NX_Q9Y4Y9; -.
DR OpenTargets; ENSG00000106355; -.
DR PharmGKB; PA134881171; -.
DR VEuPathDB; HostDB:ENSG00000106355; -.
DR eggNOG; KOG1775; Eukaryota.
DR GeneTree; ENSGT00390000001455; -.
DR HOGENOM; CLU_076902_6_1_1; -.
DR InParanoid; Q9Y4Y9; -.
DR OMA; YETTPQG; -.
DR PhylomeDB; Q9Y4Y9; -.
DR TreeFam; TF313575; -.
DR PathwayCommons; Q9Y4Y9; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9Y4Y9; -.
DR BioGRID-ORCS; 23658; 651 hits in 1047 CRISPR screens.
DR ChiTaRS; LSM5; human.
DR GeneWiki; LSM5; -.
DR GenomeRNAi; 23658; -.
DR Pharos; Q9Y4Y9; Tbio.
DR PRO; PR:Q9Y4Y9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y4Y9; protein.
DR Bgee; ENSG00000106355; Expressed in ventricular zone and 212 other tissues.
DR ExpressionAtlas; Q9Y4Y9; baseline and differential.
DR Genevisible; Q9Y4Y9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
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: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; TAS:ProtInc.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd01732; LSm5; 1.
DR InterPro; IPR033871; LSm5.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR20971; PTHR20971; 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; Alternative splicing; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..91
FT /note="U6 snRNA-associated Sm-like protein LSm5"
FT /id="PRO_0000125572"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040991"
SQ SEQUENCE 91 AA; 9937 MW; 82B5C8830E64C992 CRC64;
MAANATTNPS QLLPLELVDK CIGSRIHIVM KSDKEIVGTL LGFDDFVNMV LEDVTEFEIT
PEGRRITKLD QILLNGNNIT MLVPGGEGPE V
