LSM10_HUMAN
ID LSM10_HUMAN Reviewed; 123 AA.
AC Q969L4;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=U7 snRNA-associated Sm-like protein LSm10;
GN Name=LSM10;
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], IDENTIFICATION IN THE U7 SNRNP COMPLEX,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11574479; DOI=10.1093/emboj/20.19.5470;
RA Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.;
RT "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new
RT 14 kDa Sm D1-like protein.";
RL EMBO J. 20:5470-5479(2001).
RN [2]
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 [3]
RP INTERACTION WITH CLNS1A AND SMN, AND LACK OF METHYLATION.
RX PubMed=16087681; DOI=10.1074/jbc.m505077200;
RA Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
RA Fischer U., Schuemperli D.;
RT "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm
RT proteins with PRMT5 and SMN complexes.";
RL J. Biol. Chem. 280:34435-34440(2005).
RN [4]
RP FUNCTION.
RX PubMed=16914750; DOI=10.1128/mcb.00391-06;
RA Wagner E.J., Marzluff W.F.;
RT "ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA
RT processing, is required for entry into S phase.";
RL Mol. Cell. Biol. 26:6702-6712(2006).
CC -!- FUNCTION: Appears to function in the U7 snRNP complex that is involved
CC in histone 3'-end processing. Increases U7 snRNA levels but not histone
CC 3'-end pre-mRNA processing activity, when overexpressed. Required for
CC cell cycle progression from G1 to S phases. Binds specifically to U7
CC snRNA. Binds to the downstream cleavage product (DCP) of histone pre-
CC mRNA in a U7 snRNP dependent manner. {ECO:0000269|PubMed:16914750}.
CC -!- SUBUNIT: Component of the heptameric ring U7 snRNP complex, or U7 Sm
CC protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3,
CC SNRPE, SNRPF, SNRPG and U7 snRNA. Formation of the U7 snRNP is an ATP-
CC dependent process mediated by a specialized SMN complex containing at
CC least the Sm protein core complex and additionally, the U7-specific
CC LSM10 and LSM11 proteins. Interacts with CLNS1A and SMN.
CC {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:16087681}.
CC -!- INTERACTION:
CC Q969L4; P62310: LSM3; NbExp=4; IntAct=EBI-373268, EBI-348239;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11574479}.
CC -!- PTM: Not methylated. Methylation is not necessary for interaction with
CC SMN.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AF394685; AAL07689.1; -; mRNA.
DR EMBL; BC007623; AAH07623.1; -; mRNA.
DR CCDS; CCDS408.1; -.
DR RefSeq; NP_116270.1; NM_032881.2.
DR PDB; 6V4X; EM; 3.20 A; C=1-123.
DR PDBsum; 6V4X; -.
DR AlphaFoldDB; Q969L4; -.
DR SMR; Q969L4; -.
DR BioGRID; 124397; 19.
DR CORUM; Q969L4; -.
DR IntAct; Q969L4; 7.
DR STRING; 9606.ENSP00000319341; -.
DR PhosphoSitePlus; Q969L4; -.
DR BioMuta; LSM10; -.
DR DMDM; 20177959; -.
DR EPD; Q969L4; -.
DR jPOST; Q969L4; -.
DR MassIVE; Q969L4; -.
DR MaxQB; Q969L4; -.
DR PaxDb; Q969L4; -.
DR PeptideAtlas; Q969L4; -.
DR PRIDE; Q969L4; -.
DR ProteomicsDB; 75789; -.
DR Antibodypedia; 17475; 70 antibodies from 16 providers.
DR DNASU; 84967; -.
DR Ensembl; ENST00000315732.3; ENSP00000319341.2; ENSG00000181817.6.
DR GeneID; 84967; -.
DR KEGG; hsa:84967; -.
DR MANE-Select; ENST00000315732.3; ENSP00000319341.2; NM_032881.3; NP_116270.1.
DR UCSC; uc001cao.1; human.
DR CTD; 84967; -.
DR GeneCards; LSM10; -.
DR HGNC; HGNC:17562; LSM10.
DR HPA; ENSG00000181817; Low tissue specificity.
DR MIM; 617909; gene.
DR neXtProt; NX_Q969L4; -.
DR OpenTargets; ENSG00000181817; -.
DR PharmGKB; PA134977215; -.
DR VEuPathDB; HostDB:ENSG00000181817; -.
DR eggNOG; KOG3428; Eukaryota.
DR GeneTree; ENSGT00510000048364; -.
DR HOGENOM; CLU_141832_1_0_1; -.
DR InParanoid; Q969L4; -.
DR OMA; IADGHMT; -.
DR OrthoDB; 1571169at2759; -.
DR PhylomeDB; Q969L4; -.
DR TreeFam; TF332356; -.
DR PathwayCommons; Q969L4; -.
DR Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR SignaLink; Q969L4; -.
DR BioGRID-ORCS; 84967; 376 hits in 1083 CRISPR screens.
DR ChiTaRS; LSM10; human.
DR GeneWiki; LSM10; -.
DR GenomeRNAi; 84967; -.
DR Pharos; Q969L4; Tbio.
DR PRO; PR:Q969L4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q969L4; protein.
DR Bgee; ENSG00000181817; Expressed in hindlimb stylopod muscle and 171 other tissues.
DR Genevisible; Q969L4; HS.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0071254; C:cytoplasmic U snRNP body; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR GO; GO:0071208; F:histone pre-mRNA DCP binding; ISS:UniProtKB.
DR GO; GO:0071209; F:U7 snRNA binding; IPI:BHF-UCL.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1..123
FT /note="U7 snRNA-associated Sm-like protein LSm10"
FT /id="PRO_0000125585"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:6V4X"
FT TURN 22..26
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 90..105
FT /evidence="ECO:0007829|PDB:6V4X"
SQ SEQUENCE 123 AA; 14080 MW; B994B1DC6776BB02 CRC64;
MAVSHSVKER TISENSLIIL LQGLQGRVTT VDLRDESVAH GRIDNVDAFM NIRLAKVTYT
DRWGHQVKLD DLFVTGRNVR YVHIPDDVNI TSTIEQQLQI IHRVRNFGGK GQGRWEFPPK
NCK
