LSM3_HUMAN
ID LSM3_HUMAN Reviewed; 102 AA.
AC P62310; Q6IAH0; Q9Y4Z1;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm3;
GN Name=LSM3; ORFNames=MDS017;
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].
RC TISSUE=Fetal liver, and Spleen;
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, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [8]
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 [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]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12] {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 [13] {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:11991638, PubMed:28781166). Component of the U4/U6-U5
CC tri-snRNP complex, a building block of the precatalytic spliceosome
CC (spliceosome B complex) (PubMed:10523320, PubMed:28781166,
CC PubMed:26912367). The U4/U6-U5 tri-snRNP complex is composed of the U4,
CC U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31,
CC SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF,
CC SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2,
CC LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 (PubMed:26912367). LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped
CC subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP
CC complex and the precatalytic spliceosome (PubMed:10523320,
CC PubMed:26912367, PubMed:28781166). {ECO:0000269|PubMed:10523320,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC P62310; P54105: CLNS1A; NbExp=7; IntAct=EBI-348239, EBI-724693;
CC P62310; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-348239, EBI-742054;
CC P62310; Q0VD86: INCA1; NbExp=3; IntAct=EBI-348239, EBI-6509505;
CC P62310; Q14145: KEAP1; NbExp=6; IntAct=EBI-348239, EBI-751001;
CC P62310; O15116: LSM1; NbExp=16; IntAct=EBI-348239, EBI-347619;
CC P62310; Q969L4: LSM10; NbExp=4; IntAct=EBI-348239, EBI-373268;
CC P62310; Q3MHD2: LSM12; NbExp=3; IntAct=EBI-348239, EBI-725133;
CC P62310; Q9Y333: LSM2; NbExp=55; IntAct=EBI-348239, EBI-347416;
CC P62310; Q9Y4Y9: LSM5; NbExp=6; IntAct=EBI-348239, EBI-373007;
CC P62310; P62312: LSM6; NbExp=15; IntAct=EBI-348239, EBI-373310;
CC P62310; Q9UK45: LSM7; NbExp=9; IntAct=EBI-348239, EBI-348372;
CC P62310; O95777: LSM8; NbExp=6; IntAct=EBI-348239, EBI-347779;
CC P62310; Q96RE7: NACC1; NbExp=3; IntAct=EBI-348239, EBI-7950997;
CC P62310; P62318: SNRPD3; NbExp=5; IntAct=EBI-348239, EBI-372789;
CC P62310; P62306: SNRPF; NbExp=3; IntAct=EBI-348239, EBI-356900;
CC P62310; P56279: TCL1A; NbExp=6; IntAct=EBI-348239, EBI-749995;
CC P62310; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-348239, EBI-11139477;
CC P62310; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-348239, EBI-11961968;
CC P62310; P67809: YBX1; NbExp=2; IntAct=EBI-348239, EBI-354065;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10523320,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AJ238095; CAB45866.1; -; mRNA.
DR EMBL; AF182289; AAD56227.1; -; mRNA.
DR EMBL; AF182418; AAG14954.1; -; mRNA.
DR EMBL; CR457185; CAG33466.1; -; mRNA.
DR EMBL; CH471055; EAW64190.1; -; Genomic_DNA.
DR EMBL; BC007055; AAH07055.1; -; mRNA.
DR CCDS; CCDS2619.1; -.
DR RefSeq; NP_055278.1; NM_014463.2.
DR PDB; 3JCR; EM; 7.00 A; 3=1-102.
DR PDB; 5O9Z; EM; 4.50 A; p=1-102.
DR PDB; 6AH0; EM; 5.70 A; r=1-102.
DR PDB; 6AHD; EM; 3.80 A; r=1-102.
DR PDB; 6QW6; EM; 2.92 A; 63=1-102.
DR PDB; 6QX9; EM; 3.28 A; 63=1-102.
DR PDB; 7ABG; EM; 7.80 A; 9=1-102.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; P62310; -.
DR SMR; P62310; -.
DR BioGRID; 118105; 110.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; P62310; -.
DR DIP; DIP-31218N; -.
DR IntAct; P62310; 51.
DR MINT; P62310; -.
DR STRING; 9606.ENSP00000302160; -.
DR MoonDB; P62310; Predicted.
DR iPTMnet; P62310; -.
DR PhosphoSitePlus; P62310; -.
DR BioMuta; LSM3; -.
DR DMDM; 61227725; -.
DR EPD; P62310; -.
DR jPOST; P62310; -.
DR MassIVE; P62310; -.
DR MaxQB; P62310; -.
DR PaxDb; P62310; -.
DR PeptideAtlas; P62310; -.
DR PRIDE; P62310; -.
DR ProteomicsDB; 57389; -.
DR TopDownProteomics; P62310; -.
DR Antibodypedia; 26522; 101 antibodies from 21 providers.
DR DNASU; 27258; -.
DR Ensembl; ENST00000306024.4; ENSP00000302160.3; ENSG00000170860.4.
DR GeneID; 27258; -.
DR KEGG; hsa:27258; -.
DR MANE-Select; ENST00000306024.4; ENSP00000302160.3; NM_014463.3; NP_055278.1.
DR UCSC; uc003byo.2; human.
DR CTD; 27258; -.
DR DisGeNET; 27258; -.
DR GeneCards; LSM3; -.
DR HGNC; HGNC:17874; LSM3.
DR HPA; ENSG00000170860; Low tissue specificity.
DR MIM; 607283; gene.
DR neXtProt; NX_P62310; -.
DR OpenTargets; ENSG00000170860; -.
DR PharmGKB; PA134881991; -.
DR VEuPathDB; HostDB:ENSG00000170860; -.
DR eggNOG; KOG3460; Eukaryota.
DR GeneTree; ENSGT00390000013951; -.
DR HOGENOM; CLU_076902_5_1_1; -.
DR InParanoid; P62310; -.
DR OMA; SEMIFVR; -.
DR OrthoDB; 1633672at2759; -.
DR PhylomeDB; P62310; -.
DR TreeFam; TF312907; -.
DR PathwayCommons; P62310; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P62310; -.
DR BioGRID-ORCS; 27258; 759 hits in 1046 CRISPR screens.
DR ChiTaRS; LSM3; human.
DR GeneWiki; LSM3; -.
DR GenomeRNAi; 27258; -.
DR Pharos; P62310; Tbio.
DR PRO; PR:P62310; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P62310; protein.
DR Bgee; ENSG00000170860; Expressed in biceps brachii and 219 other tissues.
DR Genevisible; P62310; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
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:0000932; C:P-body; IBA:GO_Central.
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:0030629; F:U6 snRNA 3'-end binding; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; TAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR CDD; cd01730; LSm3; 1.
DR InterPro; IPR034105; Lsm3.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR040002; Sm-like_LSM3.
DR PANTHER; PTHR13110; PTHR13110; 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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..102
FT /note="U6 snRNA-associated Sm-like protein LSm3"
FT /id="PRO_0000125560"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
SQ SEQUENCE 102 AA; 11845 MW; 206B0DF0D95CD4D2 CRC64;
MADDVDQQQT TNTVEEPLDL IRLSLDERIY VKMRNDRELR GRLHAYDQHL NMILGDVEET
VTTIEIDEET YEEIYKSTKR NIPMLFVRGD GVVLVAPPLR VG
