ID   LSM1_HUMAN              Reviewed;         133 AA.
AC   O15116; B2R5E6;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1;
DE   AltName: Full=Cancer-associated Sm-like;
DE   AltName: Full=Small nuclear ribonuclear CaSm;
GN   Name=LSM1; Synonyms=CASM;
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].
RX   PubMed=9230209;
RA   Schweinfest C.W., Graber M.W., Chapman J.M., Papas T.S., Baron P.L.,
RA   Watson D.K.;
RT   "CaSm: an Sm-like protein that contributes to the transformed state in
RT   cancer cells.";
RL   Cancer Res. 57:2961-2965(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymph node;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Substantia nigra;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [6]
RP   FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY, INTERACTION WITH SLBP, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=18172165; DOI=10.1101/gad.1622708;
RA   Mullen T.E., Marzluff W.F.;
RT   "Degradation of histone mRNA requires oligouridylation followed by
RT   decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT   5'.";
RL   Genes Dev. 22:50-65(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND THR-129, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Plays a role in the degradation of histone mRNAs, the only
CC       eukaryotic mRNAs that are not polyadenylated (PubMed:18172165).
CC       Probably also part of an LSm subunits-containing complex involved in
CC       the general process of mRNA degradation (By similarity).
CC       {ECO:0000250|UniProtKB:P47017, ECO:0000269|PubMed:18172165}.
CC   -!- SUBUNIT: Interacts with SLBP; interaction with SLBP occurs when histone
CC       mRNA is being rapidly degraded during the S phase (PubMed:18172165).
CC       LSm subunits form a heteromer with a donut shape (By similarity).
CC       {ECO:0000250|UniProtKB:P47017, ECO:0000269|PubMed:18172165}.
CC   -!- INTERACTION:
CC       O15116; O95994: AGR2; NbExp=3; IntAct=EBI-347619, EBI-712648;
CC       O15116; Q8TD06: AGR3; NbExp=3; IntAct=EBI-347619, EBI-3925742;
CC       O15116; O00213-2: APBB1; NbExp=3; IntAct=EBI-347619, EBI-13307975;
CC       O15116; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-347619, EBI-10243741;
CC       O15116; O00299: CLIC1; NbExp=4; IntAct=EBI-347619, EBI-347404;
CC       O15116; P21964-2: COMT; NbExp=3; IntAct=EBI-347619, EBI-10200977;
CC       O15116; A0PJW8: DAPL1; NbExp=3; IntAct=EBI-347619, EBI-12840152;
CC       O15116; O15217: GSTA4; NbExp=3; IntAct=EBI-347619, EBI-752440;
CC       O15116; Q9Y333: LSM2; NbExp=11; IntAct=EBI-347619, EBI-347416;
CC       O15116; P62310: LSM3; NbExp=16; IntAct=EBI-347619, EBI-348239;
CC       O15116; Q9Y4Z0: LSM4; NbExp=4; IntAct=EBI-347619, EBI-372521;
CC       O15116; P62312: LSM6; NbExp=4; IntAct=EBI-347619, EBI-373310;
CC       O15116; P59942: MCCD1; NbExp=3; IntAct=EBI-347619, EBI-11987923;
CC       O15116; Q86TB9: PATL1; NbExp=17; IntAct=EBI-347619, EBI-2562092;
CC       O15116; P28074: PSMB5; NbExp=4; IntAct=EBI-347619, EBI-357828;
CC       O15116; P28062-2: PSMB8; NbExp=3; IntAct=EBI-347619, EBI-372312;
CC       O15116; O95988: TCL1B; NbExp=3; IntAct=EBI-347619, EBI-727338;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:18172165}.
CC       Cytoplasm, P-body {ECO:0000305|PubMed:18172165}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR   EMBL; AF000177; AAB62189.1; -; mRNA.
DR   EMBL; AJ238094; CAB45865.1; -; mRNA.
DR   EMBL; AK312159; BAG35093.1; -; mRNA.
DR   EMBL; CH471080; EAW63332.1; -; Genomic_DNA.
DR   EMBL; BC001767; AAH01767.1; -; mRNA.
DR   CCDS; CCDS6103.1; -.
DR   RefSeq; NP_055277.1; NM_014462.2.
DR   AlphaFoldDB; O15116; -.
DR   SMR; O15116; -.
DR   BioGRID; 118104; 97.
DR   CORUM; O15116; -.
DR   DIP; DIP-31130N; -.
DR   IntAct; O15116; 42.
DR   MINT; O15116; -.
DR   STRING; 9606.ENSP00000310596; -.
DR   GlyGen; O15116; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O15116; -.
DR   PhosphoSitePlus; O15116; -.
DR   BioMuta; LSM1; -.
DR   EPD; O15116; -.
DR   jPOST; O15116; -.
DR   MassIVE; O15116; -.
DR   MaxQB; O15116; -.
DR   PaxDb; 9606-ENSP00000310596; -.
DR   PeptideAtlas; O15116; -.
DR   ProteomicsDB; 48450; -.
DR   Pumba; O15116; -.
DR   TopDownProteomics; O15116; -.
DR   Antibodypedia; 10914; 361 antibodies from 29 providers.
DR   DNASU; 27257; -.
DR   Ensembl; ENST00000311351.9; ENSP00000310596.4; ENSG00000175324.10.
DR   GeneID; 27257; -.
DR   KEGG; hsa:27257; -.
DR   MANE-Select; ENST00000311351.9; ENSP00000310596.4; NM_014462.3; NP_055277.1.
DR   UCSC; uc003xkw.4; human.
DR   AGR; HGNC:20472; -.
DR   CTD; 27257; -.
DR   DisGeNET; 27257; -.
DR   GeneCards; LSM1; -.
DR   HGNC; HGNC:20472; LSM1.
DR   HPA; ENSG00000175324; Low tissue specificity.
DR   MIM; 607281; gene.
DR   neXtProt; NX_O15116; -.
DR   OpenTargets; ENSG00000175324; -.
DR   PharmGKB; PA134864226; -.
DR   VEuPathDB; HostDB:ENSG00000175324; -.
DR   eggNOG; KOG1782; Eukaryota.
DR   GeneTree; ENSGT00730000111133; -.
DR   HOGENOM; CLU_076902_0_1_1; -.
DR   InParanoid; O15116; -.
DR   OMA; IHVGREY; -.
DR   OrthoDB; 1113423at2759; -.
DR   PhylomeDB; O15116; -.
DR   TreeFam; TF105846; -.
DR   PathwayCommons; O15116; -.
DR   Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR   SignaLink; O15116; -.
DR   BioGRID-ORCS; 27257; 19 hits in 1132 CRISPR screens.
DR   ChiTaRS; LSM1; human.
DR   GeneWiki; LSM1; -.
DR   GenomeRNAi; 27257; -.
DR   Pharos; O15116; Tbio.
DR   PRO; PR:O15116; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; O15116; Protein.
DR   Bgee; ENSG00000175324; Expressed in parotid gland and 211 other cell types or tissues.
DR   ExpressionAtlas; O15116; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
DR   GO; GO:1990124; C:messenger ribonucleoprotein complex; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR   GO; GO:0036002; F:pre-mRNA binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR   GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR   GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR   GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR   CDD; cd01728; LSm1; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR034104; Lsm1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR044642; PTHR15588.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR15588; LSM1; 1.
DR   PANTHER; PTHR15588:SF8; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM1; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
DR   Genevisible; O15116; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; RNA-binding.
FT   CHAIN           1..133
FT                   /note="U6 snRNA-associated Sm-like protein LSm1"
FT                   /id="PRO_0000125554"
FT   DOMAIN          5..80
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         129
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
SQ   SEQUENCE   133 AA;  15179 MW;  FF798CDA9447037A CRC64;
     MNYMPGTASL IEDIDKKHLV LLRDGRTLIG FLRSIDQFAN LVLHQTVERI HVGKKYGDIP
     RGIFVVRGEN VVLLGEIDLE KESDTPLQQV SIEEILEEQR VEQQTKLEAE KLKVQALKDR
     GLSIPRADTL DEY
//