LSM2_HUMAN
ID LSM2_HUMAN Reviewed; 95 AA.
AC Q9Y333; Q6FGG1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm2;
DE AltName: Full=Protein G7b;
DE AltName: Full=Small nuclear ribonuclear protein D homolog;
DE AltName: Full=snRNP core Sm-like protein Sm-x5;
GN Name=LSM2; Synonyms=C6orf28, G7B;
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 [MRNA].
RA Olavesen M.G., Campbell R.D.;
RT "Characterisation of the novel gene G7b located in the class III region of
RT the human major histocompatibility complex.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schmarda A., Fresser F., Paulmichl M.;
RT "Human SMX5 homolog.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL
RP COMPLEX, SUBCELLULAR LOCATION, AND SUBUNIT.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
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 [14] {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 [15] {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 Q9Y333; Q8N9N5: BANP; NbExp=3; IntAct=EBI-347416, EBI-744695;
CC Q9Y333; Q9HC52: CBX8; NbExp=3; IntAct=EBI-347416, EBI-712912;
CC Q9Y333; P54105: CLNS1A; NbExp=7; IntAct=EBI-347416, EBI-724693;
CC Q9Y333; Q86X45: DNAAF11; NbExp=3; IntAct=EBI-347416, EBI-9379658;
CC Q9Y333; A1A4E9: KRT13; NbExp=3; IntAct=EBI-347416, EBI-10171552;
CC Q9Y333; P47929: LGALS7B; NbExp=3; IntAct=EBI-347416, EBI-357504;
CC Q9Y333; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-347416, EBI-739832;
CC Q9Y333; O15116: LSM1; NbExp=11; IntAct=EBI-347416, EBI-347619;
CC Q9Y333; Q3MHD2: LSM12; NbExp=3; IntAct=EBI-347416, EBI-725133;
CC Q9Y333; P62310: LSM3; NbExp=55; IntAct=EBI-347416, EBI-348239;
CC Q9Y333; P62312: LSM6; NbExp=7; IntAct=EBI-347416, EBI-373310;
CC Q9Y333; Q9UK45: LSM7; NbExp=13; IntAct=EBI-347416, EBI-348372;
CC Q9Y333; O95777: LSM8; NbExp=8; IntAct=EBI-347416, EBI-347779;
CC Q9Y333; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-347416, EBI-1216080;
CC Q9Y333; P43357: MAGEA3; NbExp=3; IntAct=EBI-347416, EBI-5651459;
CC Q9Y333; P43360: MAGEA6; NbExp=6; IntAct=EBI-347416, EBI-1045155;
CC Q9Y333; P50222: MEOX2; NbExp=3; IntAct=EBI-347416, EBI-748397;
CC Q9Y333; Q86TB9: PATL1; NbExp=3; IntAct=EBI-347416, EBI-2562092;
CC Q9Y333; Q04864: REL; NbExp=3; IntAct=EBI-347416, EBI-307352;
CC Q9Y333; P14678-2: SNRPB; NbExp=6; IntAct=EBI-347416, EBI-372475;
CC Q9Y333; P62316: SNRPD2; NbExp=3; IntAct=EBI-347416, EBI-297993;
CC Q9Y333; P62304: SNRPE; NbExp=3; IntAct=EBI-347416, EBI-348082;
CC Q9Y333; Q08117: TLE5; NbExp=3; IntAct=EBI-347416, EBI-717810;
CC Q9Y333; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-347416, EBI-2130429;
CC Q9Y333; Q9H9D4: ZNF408; NbExp=4; IntAct=EBI-347416, EBI-347633;
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; AF182288; AAD56226.1; -; mRNA.
DR EMBL; AJ245416; CAB52190.1; -; mRNA.
DR EMBL; AF196468; AAG33023.1; -; mRNA.
DR EMBL; AF134726; AAD21818.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63302.1; -; Genomic_DNA.
DR EMBL; AF136977; AAG49438.1; -; mRNA.
DR EMBL; CR542146; CAG46943.1; -; mRNA.
DR EMBL; CR542157; CAG46954.1; -; mRNA.
DR EMBL; AL929592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR925765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03525.1; -; Genomic_DNA.
DR EMBL; BC009192; AAH09192.1; -; mRNA.
DR CCDS; CCDS4722.1; -.
DR RefSeq; NP_067000.1; NM_021177.4.
DR PDB; 3JCR; EM; 7.00 A; 2=1-95.
DR PDB; 5O9Z; EM; 4.50 A; o=1-95.
DR PDB; 6AH0; EM; 5.70 A; q=1-95.
DR PDB; 6AHD; EM; 3.80 A; q=1-95.
DR PDB; 6QW6; EM; 2.92 A; 62=1-95.
DR PDB; 6QX9; EM; 3.28 A; 62=1-95.
DR PDB; 7ABG; EM; 7.80 A; V=1-95.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; Q9Y333; -.
DR SMR; Q9Y333; -.
DR BioGRID; 121778; 140.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q9Y333; -.
DR DIP; DIP-31139N; -.
DR IntAct; Q9Y333; 52.
DR MINT; Q9Y333; -.
DR STRING; 9606.ENSP00000364813; -.
DR GlyGen; Q9Y333; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y333; -.
DR PhosphoSitePlus; Q9Y333; -.
DR SwissPalm; Q9Y333; -.
DR BioMuta; LSM2; -.
DR DMDM; 10720079; -.
DR EPD; Q9Y333; -.
DR jPOST; Q9Y333; -.
DR MassIVE; Q9Y333; -.
DR MaxQB; Q9Y333; -.
DR PaxDb; Q9Y333; -.
DR PeptideAtlas; Q9Y333; -.
DR PRIDE; Q9Y333; -.
DR ProteomicsDB; 85967; -.
DR TopDownProteomics; Q9Y333; -.
DR Antibodypedia; 27800; 201 antibodies from 34 providers.
DR DNASU; 57819; -.
DR Ensembl; ENST00000375661.6; ENSP00000364813.5; ENSG00000204392.11.
DR Ensembl; ENST00000383391.4; ENSP00000372883.4; ENSG00000172850.11.
DR Ensembl; ENST00000424975.2; ENSP00000403345.2; ENSG00000231502.6.
DR Ensembl; ENST00000432122.2; ENSP00000414006.2; ENSG00000224979.6.
DR Ensembl; ENST00000434125.2; ENSP00000406280.2; ENSG00000225998.6.
DR Ensembl; ENST00000455705.2; ENSP00000414634.2; ENSG00000236826.7.
DR GeneID; 57819; -.
DR KEGG; hsa:57819; -.
DR MANE-Select; ENST00000375661.6; ENSP00000364813.5; NM_021177.5; NP_067000.1.
DR UCSC; uc003nxg.4; human.
DR CTD; 57819; -.
DR DisGeNET; 57819; -.
DR GeneCards; LSM2; -.
DR HGNC; HGNC:13940; LSM2.
DR HPA; ENSG00000204392; Low tissue specificity.
DR MIM; 607282; gene.
DR neXtProt; NX_Q9Y333; -.
DR OpenTargets; ENSG00000204392; -.
DR PharmGKB; PA25929; -.
DR VEuPathDB; HostDB:ENSG00000204392; -.
DR eggNOG; KOG3448; Eukaryota.
DR GeneTree; ENSGT00390000016597; -.
DR HOGENOM; CLU_130474_3_0_1; -.
DR InParanoid; Q9Y333; -.
DR OMA; EERYPHM; -.
DR OrthoDB; 1571169at2759; -.
DR PhylomeDB; Q9Y333; -.
DR TreeFam; TF314960; -.
DR PathwayCommons; Q9Y333; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q9Y333; -.
DR BioGRID-ORCS; 57819; 787 hits in 1049 CRISPR screens.
DR ChiTaRS; LSM2; human.
DR GeneWiki; LSM2; -.
DR GenomeRNAi; 57819; -.
DR Pharos; Q9Y333; Tbio.
DR PRO; PR:Q9Y333; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y333; protein.
DR Bgee; ENSG00000204392; Expressed in ventricular zone and 95 other tissues.
DR Genevisible; Q9Y333; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
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; IDA:HPA.
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:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; NAS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:MGI.
DR CDD; cd01725; LSm2; 1.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR016654; U6_snRNA_Lsm2.
DR PANTHER; PTHR13829; PTHR13829; 1.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF016394; U6_snRNA_Lsm2; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Spliceosome.
FT CHAIN 1..95
FT /note="U6 snRNA-associated Sm-like protein LSm2"
FT /id="PRO_0000125556"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
SQ SEQUENCE 95 AA; 10835 MW; 623591A09A6ABACE CRC64;
MLFYSFFKSL VGKDVVVELK NDLSICGTLH SVDQYLNIKL TDISVTDPEK YPHMLSVKNC
FIRGSVVRYV QLPADEVDTQ LLQDAARKEA LQQKQ
