ID LSM2_HUMAN Reviewed; 95 AA. AC Q9Y333; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 25-JAN-2012, entry version 117. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=99452783; 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 RT 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in RT 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 RT region of 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., RA Campbell R.D., 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 MEDLINE=20402571; 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., RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal RT axis 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]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RP SPLICEOSOMAL C 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND MASS RP SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., 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 [11] 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., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 CC snRNA. May be involved in pre-mRNA splicing. CC -!- SUBUNIT: Identified in the spliceosome C complex. LSm subunits CC form a heteromer with a donut shape. CC -!- INTERACTION: CC O15116:LSM1; NbExp=3; IntAct=EBI-347416, EBI-347619; CC P62310:LSM3; NbExp=8; IntAct=EBI-347416, EBI-348239; CC Q9UK45:LSM7; NbExp=4; IntAct=EBI-347416, EBI-348372; CC O95777:NAA38; NbExp=5; IntAct=EBI-347416, EBI-347779; CC Q9H9D4:ZNF408; NbExp=4; IntAct=EBI-347416, EBI-347633; CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; BC009192; AAH09192.1; -; mRNA. DR IPI; IPI00032460; -. DR RefSeq; NP_067000.1; NM_021177.4. DR UniGene; Hs.103106; -. DR ProteinModelPortal; Q9Y333; -. DR SMR; Q9Y333; 1-71. DR DIP; DIP-31139N; -. DR IntAct; Q9Y333; 20. DR MINT; MINT-1032572; -. DR STRING; Q9Y333; -. DR PhosphoSite; Q9Y333; -. DR DMDM; 10720079; -. DR PeptideAtlas; Q9Y333; -. DR PRIDE; Q9Y333; -. DR Ensembl; ENST00000375661; ENSP00000364813; ENSG00000204392. DR Ensembl; ENST00000383391; ENSP00000372883; ENSG00000172850. DR Ensembl; ENST00000424975; ENSP00000403345; ENSG00000231502. DR Ensembl; ENST00000432122; ENSP00000414006; ENSG00000224979. DR Ensembl; ENST00000434125; ENSP00000406280; ENSG00000225998. DR Ensembl; ENST00000455705; ENSP00000414634; ENSG00000236826. DR GeneID; 57819; -. DR KEGG; hsa:57819; -. DR UCSC; uc003nxg.1; human. DR CTD; 57819; -. DR GeneCards; GC06M031765; -. DR HGNC; HGNC:13940; LSM2. DR MIM; 607282; gene. DR neXtProt; NX_Q9Y333; -. DR GeneTree; ENSGT00390000016597; -. DR HOGENOM; HBG749684; -. DR HOVERGEN; HBG000486; -. DR InParanoid; Q9Y333; -. DR OMA; FIRGSTV; -. DR OrthoDB; EOG4Z36G9; -. DR PhylomeDB; Q9Y333; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_1675; mRNA Processing. DR Reactome; REACT_71; Gene Expression. DR NextBio; 64772; -. DR CleanEx; HS_LSM2; -. DR Genevestigator; Q9Y333; -. DR GermOnline; ENSG00000204392; Homo sapiens. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0017070; F:U6 snRNA binding; NAS:UniProtKB. DR GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; NAS:UniProtKB. DR InterPro; IPR010920; LSM-related_domain. DR InterPro; IPR001163; LSM_domain. DR InterPro; IPR006649; LSM_domain_euk/arc. DR InterPro; IPR016654; U6_snRNA_Lsm2. DR KO; K12621; -. 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; Sm_like_riboprot; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; RNA-binding; Spliceosome. FT CHAIN 1 95 U6 snRNA-associated Sm-like protein LSm2. FT /FTId=PRO_0000125556. FT MOD_RES 35 35 Phosphotyrosine. FT MOD_RES 79 79 Phosphothreonine. SQ SEQUENCE 95 AA; 10835 MW; 623591A09A6ABACE CRC64; MLFYSFFKSL VGKDVVVELK NDLSICGTLH SVDQYLNIKL TDISVTDPEK YPHMLSVKNC FIRGSVVRYV QLPADEVDTQ LLQDAARKEA LQQKQ //