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   03-NOV-2009, entry version 94.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm2;
DE   AltName: Full=snRNP core Sm-like protein Sm-x5;
DE   AltName: Full=Small nuclear ribonuclear protein D homolog;
DE   AltName: Full=Protein G7b;
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   SPICEOSOMAL 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.
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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
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, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. LSm
CC       subunits form a heteromer with a donut shape.
CC   -!- INTERACTION:
CC       P31689:DNAJA1; NbExp=2; IntAct=EBI-347416, EBI-347834;
CC       Q01780:EXOSC10; NbExp=1; IntAct=EBI-347416, EBI-358236;
CC       O15116:LSM1; NbExp=2; IntAct=EBI-347416, EBI-347619;
CC       P62310:LSM3; NbExp=5; IntAct=EBI-347416, EBI-348239;
CC       Q9UK45:LSM7; NbExp=3; IntAct=EBI-347416, EBI-348372;
CC       O95777:LSM8; NbExp=3; IntAct=EBI-347416, EBI-347779;
CC       P62316:SNRPD2; NbExp=2; IntAct=EBI-347416, EBI-297993;
CC       P62304:SNRPE; NbExp=2; IntAct=EBI-347416, EBI-348082;
CC       Q9H9D4:ZNF408; NbExp=3; 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.
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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; BC009192; AAH09192.1; -; mRNA.
DR   IPI; IPI00032460; -.
DR   RefSeq; NP_067000.1; -.
DR   UniGene; Hs.103106; -.
DR   HSSP; P13641; 1B34.
DR   IntAct; Q9Y333; 15.
DR   STRING; Q9Y333; -.
DR   PhosphoSite; Q9Y333; -.
DR   PeptideAtlas; Q9Y333; -.
DR   PRIDE; Q9Y333; -.
DR   Ensembl; ENST00000375661; ENSP00000364813; ENSG00000204392; Homo sapiens.
DR   Ensembl; ENST00000383391; ENSP00000372883; ENSG00000172850; Homo sapiens.
DR   Ensembl; ENST00000424975; ENSP00000403345; ENSG00000231502; Homo sapiens.
DR   Ensembl; ENST00000432122; ENSP00000414006; ENSG00000224979; Homo sapiens.
DR   Ensembl; ENST00000434125; ENSP00000406280; ENSG00000225998; Homo sapiens.
DR   Ensembl; ENST00000455705; ENSP00000414634; ENSG00000236826; Homo sapiens.
DR   GeneID; 57819; -.
DR   KEGG; hsa:57819; -.
DR   UCSC; uc003nxg.1; human.
DR   CTD; 57819; -.
DR   GeneCards; GC06M031873; -.
DR   H-InvDB; HIX0005732; -.
DR   H-InvDB; HIX0057905; -.
DR   H-InvDB; HIX0058082; -.
DR   HGNC; HGNC:13940; LSM2.
DR   MIM; 607282; gene.
DR   PharmGKB; PA25929; -.
DR   HOGENOM; Q9Y333; -.
DR   HOVERGEN; Q9Y333; -.
DR   OMA; FIRGSTV; -.
DR   Reactome; REACT_125; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; REACT_71; Gene Expression.
DR   NextBio; 64772; -.
DR   ArrayExpress; Q9Y333; -.
DR   CleanEx; HS_LSM2; -.
DR   Genevestigator; Q9Y333; -.
DR   GermOnline; ENSG00000204392; Homo sapiens.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0017070; F:U6 snRNA binding; NAS:UniProtKB.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; NAS:UniProtKB.
DR   InterPro; IPR006649; Like-Sm_rNuclprot_core_euk/arc.
DR   InterPro; IPR001163; LSM_snRNP_core.
DR   InterPro; IPR016654; U6_snRNA_Lsm2.
DR   Pfam; PF01423; LSM; 1.
DR   PIRSF; PIRSF016394; U6_snRNA_Lsm2; 1.
DR   SMART; SM00651; Sm; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Ribonucleoprotein;
KW   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
//