LSM1_HUMAN
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 03-AUG-2022, entry version 174.
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; 85.
DR CORUM; O15116; -.
DR DIP; DIP-31130N; -.
DR IntAct; O15116; 42.
DR MINT; O15116; -.
DR STRING; 9606.ENSP00000310596; -.
DR iPTMnet; O15116; -.
DR PhosphoSitePlus; O15116; -.
DR BioMuta; LSM1; -.
DR EPD; O15116; -.
DR jPOST; O15116; -.
DR MassIVE; O15116; -.
DR MaxQB; O15116; -.
DR PaxDb; O15116; -.
DR PeptideAtlas; O15116; -.
DR PRIDE; O15116; -.
DR ProteomicsDB; 48450; -.
DR TopDownProteomics; O15116; -.
DR Antibodypedia; 10914; 328 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 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; FMVRGEN; -.
DR OrthoDB; 1508864at2759; -.
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; 17 hits in 1053 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 209 other tissues.
DR ExpressionAtlas; O15116; baseline and differential.
DR Genevisible; O15116; HS.
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:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
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:0016070; P:RNA metabolic process; IBA:GO_Central.
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 InterPro; IPR034104; Lsm1.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR044642; PTHR15588.
DR PANTHER; PTHR15588; PTHR15588; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
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 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
