LSM7_HUMAN
ID LSM7_HUMAN Reviewed; 103 AA.
AC Q9UK45;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm7;
GN Name=LSM7;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 INTERACTION WITH TACC1.
RX PubMed=12165861; DOI=10.1038/sj.onc.1205658;
RA Conte N., Charafe-Jauffret E., Delaval B., Adelaide J., Ginestier C.,
RA Geneix J., Isnardon D., Jacquemier J., Birnbaum D.;
RT "Carcinogenesis and translational controls: TACC1 is down-regulated in
RT human cancers and associates with mRNA regulators.";
RL Oncogene 21:5619-5630(2002).
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 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 [7]
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 [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). Interacts with TACC1 (PubMed:12165861).
CC {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:12165861,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC Q9UK45; Q96D03: DDIT4L; NbExp=10; IntAct=EBI-348372, EBI-742054;
CC Q9UK45; Q9Y333: LSM2; NbExp=13; IntAct=EBI-348372, EBI-347416;
CC Q9UK45; P62310: LSM3; NbExp=9; IntAct=EBI-348372, EBI-348239;
CC Q9UK45; Q9Y4Z0: LSM4; NbExp=11; IntAct=EBI-348372, EBI-372521;
CC Q9UK45; Q9Y4Y9: LSM5; NbExp=18; IntAct=EBI-348372, EBI-373007;
CC Q9UK45; P62312: LSM6; NbExp=5; IntAct=EBI-348372, EBI-373310;
CC Q9UK45; P62318: SNRPD3; NbExp=3; IntAct=EBI-348372, EBI-372789;
CC Q9UK45; P62306: SNRPF; NbExp=6; IntAct=EBI-348372, EBI-356900;
CC Q9UK45; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-348372, EBI-745392;
CC Q9UK45; O75410-1: TACC1; NbExp=4; IntAct=EBI-348372, EBI-624252;
CC Q9UK45; O75410-6: TACC1; NbExp=2; IntAct=EBI-348372, EBI-624278;
CC Q9UK45; O95988: TCL1B; NbExp=3; IntAct=EBI-348372, EBI-727338;
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}.
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; AF182293; AAD56231.1; -; mRNA.
DR EMBL; AC005258; AAG45442.1; -; Genomic_DNA.
DR EMBL; BC018621; AAH18621.1; -; mRNA.
DR CCDS; CCDS45907.1; -.
DR RefSeq; NP_057283.1; NM_016199.2.
DR PDB; 3JCR; EM; 7.00 A; 7=1-103.
DR PDB; 5O9Z; EM; 4.50 A; t=1-103.
DR PDB; 6AH0; EM; 5.70 A; y=1-103.
DR PDB; 6AHD; EM; 3.80 A; y=1-103.
DR PDB; 6QW6; EM; 2.92 A; 67=1-103.
DR PDB; 6QX9; EM; 3.28 A; 67=1-103.
DR PDB; 7ABG; EM; 7.80 A; A2=1-103.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; Q9UK45; -.
DR SMR; Q9UK45; -.
DR BioGRID; 119678; 92.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q9UK45; -.
DR DIP; DIP-31129N; -.
DR IntAct; Q9UK45; 27.
DR MINT; Q9UK45; -.
DR STRING; 9606.ENSP00000252622; -.
DR iPTMnet; Q9UK45; -.
DR MetOSite; Q9UK45; -.
DR PhosphoSitePlus; Q9UK45; -.
DR SwissPalm; Q9UK45; -.
DR BioMuta; LSM7; -.
DR DMDM; 10720075; -.
DR EPD; Q9UK45; -.
DR jPOST; Q9UK45; -.
DR MassIVE; Q9UK45; -.
DR MaxQB; Q9UK45; -.
DR PaxDb; Q9UK45; -.
DR PeptideAtlas; Q9UK45; -.
DR PRIDE; Q9UK45; -.
DR ProteomicsDB; 84717; -.
DR TopDownProteomics; Q9UK45; -.
DR Antibodypedia; 42295; 150 antibodies from 24 providers.
DR DNASU; 51690; -.
DR Ensembl; ENST00000252622.15; ENSP00000252622.8; ENSG00000130332.15.
DR GeneID; 51690; -.
DR KEGG; hsa:51690; -.
DR MANE-Select; ENST00000252622.15; ENSP00000252622.8; NM_016199.3; NP_057283.1.
DR UCSC; uc002lvp.5; human.
DR CTD; 51690; -.
DR DisGeNET; 51690; -.
DR GeneCards; LSM7; -.
DR HGNC; HGNC:20470; LSM7.
DR HPA; ENSG00000130332; Low tissue specificity.
DR MIM; 607287; gene.
DR neXtProt; NX_Q9UK45; -.
DR OpenTargets; ENSG00000130332; -.
DR PharmGKB; PA134888612; -.
DR VEuPathDB; HostDB:ENSG00000130332; -.
DR eggNOG; KOG1781; Eukaryota.
DR GeneTree; ENSGT00510000047872; -.
DR HOGENOM; CLU_076902_3_1_1; -.
DR InParanoid; Q9UK45; -.
DR OMA; ICPADGM; -.
DR OrthoDB; 1593201at2759; -.
DR PhylomeDB; Q9UK45; -.
DR TreeFam; TF314385; -.
DR PathwayCommons; Q9UK45; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9UK45; -.
DR BioGRID-ORCS; 51690; 805 hits in 1079 CRISPR screens.
DR ChiTaRS; LSM7; human.
DR GeneWiki; LSM7; -.
DR GenomeRNAi; 51690; -.
DR Pharos; Q9UK45; Tbio.
DR PRO; PR:Q9UK45; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UK45; protein.
DR Bgee; ENSG00000130332; Expressed in mucosa of transverse colon and 201 other tissues.
DR ExpressionAtlas; Q9UK45; baseline and differential.
DR Genevisible; Q9UK45; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
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:0017070; F:U6 snRNA binding; NAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
DR CDD; cd01729; LSm7; 1.
DR InterPro; IPR017132; Lsm7.
DR InterPro; IPR044641; Lsm7/SmG-like.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR10553; PTHR10553; 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:22814378"
FT CHAIN 2..103
FT /note="U6 snRNA-associated Sm-like protein LSm7"
FT /id="PRO_0000125579"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 103 AA; 11602 MW; 7429DC0FB365C9C8 CRC64;
MADKEKKKKE SILDLSKYID KTIRVKFQGG REASGILKGF DPLLNLVLDG TIEYMRDPDD
QYKLTEDTRQ LGLVVCRGTS VVLICPQDGM EAIPNPFIQQ QDA
