LSM11_HUMAN
ID LSM11_HUMAN Reviewed; 360 AA.
AC P83369; A0AVQ1; Q7Z7P0; Q8N975;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=U7 snRNA-associated Sm-like protein LSm11 {ECO:0000305};
GN Name=LSM11 {ECO:0000303|PubMed:12975319, ECO:0000312|HGNC:HGNC:30860};
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 PROTEIN SEQUENCE OF 115-130; 147-160; 217-224; 231-236; 242-260; 280-289;
RP 303-315 AND 333-360, INTERACTION WITH LSM10; SMN AND SNRPB, RNA-BINDING,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=12975319; DOI=10.1101/gad.274403;
RA Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U.,
RA Schuemperli D.;
RT "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN
RT complex and the role of a new component, Lsm11, in histone RNA
RT processing.";
RL Genes Dev. 17:2321-2333(2003).
RN [4]
RP IDENTIFICATION IN THE U7 SNRNP COMPLEX.
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 [5]
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).
RN [6]
RP INTERACTION WITH ZNF473.
RX PubMed=16714279; DOI=10.1261/rna.2606;
RA Wagner E.J., Ospina J.K., Hu Y., Dundr M., Matera A.G., Marzluff W.F.;
RT "Conserved zinc fingers mediate multiple functions of ZFP100, a U7snRNP
RT associated protein.";
RL RNA 12:1206-1218(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-21; SER-154 AND
RP SER-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [10]
RP VARIANT AGS8 SER-211, CHARACTERIZATION OF VARIANT AGS8 SER-211, AND
RP FUNCTION.
RX PubMed=33230297; DOI=10.1038/s41588-020-00737-3;
RA Uggenti C., Lepelley A., Depp M., Badrock A.P., Rodero M.P., El-Daher M.T.,
RA Rice G.I., Dhir S., Wheeler A.P., Dhir A., Albawardi W., Fremond M.L.,
RA Seabra L., Doig J., Blair N., Martin-Niclos M.J., Della Mina E.,
RA Rubio-Roldan A., Garcia-Perez J.L., Sproul D., Rehwinkel J., Hertzog J.,
RA Boland-Auge A., Olaso R., Deleuze J.F., Baruteau J., Brochard K.,
RA Buckley J., Cavallera V., Cereda C., De Waele L.M.H., Dobbie A.,
RA Doummar D., Elmslie F., Koch-Hogrebe M., Kumar R., Lamb K.,
RA Livingston J.H., Majumdar A., Lorenco C.M., Orcesi S., Peudenier S.,
RA Rostasy K., Salmon C.A., Scott C., Tonduti D., Touati G., Valente M.,
RA van der Linden H. Jr., Van Esch H., Vermelle M., Webb K., Jackson A.P.,
RA Reijns M.A.M., Gilbert N., Crow Y.J.;
RT "cGAS-mediated induction of type I interferon due to inborn errors of
RT histone pre-mRNA processing.";
RL Nat. Genet. 52:1364-1372(2020).
CC -!- FUNCTION: Component of the U7 snRNP complex that is involved in the
CC histone 3'-end pre-mRNA processing (PubMed:11574479, PubMed:16914750,
CC PubMed:33230297). Increases U7 snRNA levels but not histone 3'-end pre-
CC mRNA processing activity, when overexpressed (PubMed:11574479,
CC PubMed:16914750). Required for cell cycle progression from G1 to S
CC phases (By similarity). Binds specifically to the Sm-binding site of U7
CC snRNA (PubMed:11574479, PubMed:16914750).
CC {ECO:0000250|UniProtKB:Q8BUV6, ECO:0000269|PubMed:11574479,
CC ECO:0000269|PubMed:16914750, ECO:0000269|PubMed:33230297}.
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 (PubMed:12975319, PubMed:11574479).
CC Formation of the U7 snRNP is an ATP-dependent process mediated by a
CC specialized SMN complex containing at least the Sm protein core complex
CC and additionally, the U7-specific LSM10 and LSM11 proteins
CC (PubMed:11574479). Identified in a histone pre-mRNA complex, at least
CC composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By similarity).
CC Interacts (via the Sm domains) with CLNS1A (By similarity). Interacts
CC with SMN and ZNF473 (PubMed:12975319, PubMed:16714279). Interacts with
CC PRMT5 and WDR77 (By similarity). {ECO:0000250|UniProtKB:Q8BUV6,
CC ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:12975319,
CC ECO:0000269|PubMed:16714279}.
CC -!- INTERACTION:
CC P83369; A4D1S5: RAB19; NbExp=3; IntAct=EBI-2626024, EBI-4401710;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12975319}.
CC -!- DOMAIN: The C-terminal SM 1 domain is both necessary for the binding to
CC the Sm-binding site of U7 snRNA and U7 snRNP assembly (By similarity).
CC The N-terminal domain is essential for histone pre-mRNA cleavage (By
CC similarity). Amino acids 63-82 are sufficient to interact with ZNF473
CC (By similarity). {ECO:0000250|UniProtKB:Q8BUV6}.
CC -!- DISEASE: Aicardi-Goutieres syndrome 8 (AGS8) [MIM:619486]: A form of
CC Aicardi-Goutieres syndrome, a genetically heterogeneous disease
CC characterized by cerebral atrophy, leukoencephalopathy, intracranial
CC calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis,
CC increased CSF alpha-interferon, and negative serologic investigations
CC for common prenatal infection. Clinical features as thrombocytopenia,
CC hepatosplenomegaly and elevated hepatic transaminases along with
CC intermittent fever may erroneously suggest an infective process. Severe
CC neurological dysfunctions manifest in infancy as progressive
CC microcephaly, spasticity, dystonic posturing and profound psychomotor
CC retardation. Death often occurs in early childhood. AGS8 inheritance is
CC autosomal recessive. Note=The disease is caused by variants affecting
CC the gene represented in this entry. Impaired histone 3'-end pre-mRNA
CC processing caused by disease variants affects chromatin structure,
CC relieving CGAS inhibition by nucleosomes (PubMed:33230297). This
CC activates the cGAS-STING pathway, triggering type-I interferon
CC production and autoinflammation (PubMed:33230297).
CC {ECO:0000269|PubMed:33230297}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AK095592; BAC04581.1; -; mRNA.
DR EMBL; BC051353; AAH51353.1; -; mRNA.
DR EMBL; BC126449; AAI26450.1; -; mRNA.
DR CCDS; CCDS4342.1; -.
DR RefSeq; NP_775762.1; NM_173491.3.
DR PDB; 6V4X; EM; 3.20 A; D=1-360.
DR PDBsum; 6V4X; -.
DR AlphaFoldDB; P83369; -.
DR SMR; P83369; -.
DR BioGRID; 126394; 52.
DR CORUM; P83369; -.
DR IntAct; P83369; 28.
DR STRING; 9606.ENSP00000286307; -.
DR iPTMnet; P83369; -.
DR PhosphoSitePlus; P83369; -.
DR BioMuta; LSM11; -.
DR DMDM; 47117879; -.
DR EPD; P83369; -.
DR jPOST; P83369; -.
DR MassIVE; P83369; -.
DR MaxQB; P83369; -.
DR PaxDb; P83369; -.
DR PeptideAtlas; P83369; -.
DR PRIDE; P83369; -.
DR ProteomicsDB; 57735; -.
DR Antibodypedia; 48521; 147 antibodies from 22 providers.
DR DNASU; 134353; -.
DR Ensembl; ENST00000286307.6; ENSP00000286307.5; ENSG00000155858.6.
DR GeneID; 134353; -.
DR KEGG; hsa:134353; -.
DR MANE-Select; ENST00000286307.6; ENSP00000286307.5; NM_173491.4; NP_775762.1.
DR UCSC; uc003lxf.2; human.
DR CTD; 134353; -.
DR GeneCards; LSM11; -.
DR HGNC; HGNC:30860; LSM11.
DR HPA; ENSG00000155858; Low tissue specificity.
DR MIM; 617910; gene.
DR MIM; 619486; phenotype.
DR neXtProt; NX_P83369; -.
DR OpenTargets; ENSG00000155858; -.
DR PharmGKB; PA134983181; -.
DR VEuPathDB; HostDB:ENSG00000155858; -.
DR eggNOG; ENOG502QS1B; Eukaryota.
DR GeneTree; ENSGT00390000012944; -.
DR HOGENOM; CLU_065821_0_0_1; -.
DR InParanoid; P83369; -.
DR OMA; QETSECA; -.
DR OrthoDB; 1605022at2759; -.
DR PhylomeDB; P83369; -.
DR TreeFam; TF326954; -.
DR PathwayCommons; P83369; -.
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; P83369; -.
DR BioGRID-ORCS; 134353; 626 hits in 1096 CRISPR screens.
DR ChiTaRS; LSM11; human.
DR GenomeRNAi; 134353; -.
DR Pharos; P83369; Tbio.
DR PRO; PR:P83369; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P83369; protein.
DR Bgee; ENSG00000155858; Expressed in secondary oocyte and 175 other tissues.
DR Genevisible; P83369; HS.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL.
DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR GO; GO:0071209; F:U7 snRNA binding; IDA:UniProtKB.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IMP:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB.
DR CDD; cd01739; LSm11_M; 1.
DR InterPro; IPR039267; Lsm11.
DR InterPro; IPR034109; Lsm11_M.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR21415; PTHR21415; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aicardi-Goutieres syndrome; Direct protein sequencing;
KW Disease variant; Isopeptide bond; Methylation; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..360
FT /note="U7 snRNA-associated Sm-like protein LSm11"
FT /id="PRO_0000125587"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..204
FT /note="SM 1"
FT /evidence="ECO:0000303|PubMed:14702039"
FT REGION 268..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..356
FT /note="SM 2"
FT /evidence="ECO:0000303|PubMed:14702039"
FT COMPBIAS 99..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 41
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUV6"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 211
FT /note="G -> S (in AGS8; impaired histone 3'-end pre-mRNA
FT processing, leading to defects in chromatin structure;
FT promoting CGAS-dependent activation of the type I
FT interferon pathway)"
FT /evidence="ECO:0000269|PubMed:33230297"
FT /id="VAR_085527"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:6V4X"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:6V4X"
SQ SEQUENCE 360 AA; 39500 MW; 3C97710C28C0DCE1 CRC64;
MEERERGARS AGAGSPARPP SPRLDVSSDS FDPLLALYAP RLPPIPYPNA PCFNNVAEYE
SFLRTGVRGG GRGRGRARGA AAGSGVPAAP GPSGRTRRRP DAPAPDPERI QRLRRLMVAK
EEGDGAAGAG RRGPGRSRKA PRNVLTRMPL HEGSPLGELH RCIREGVKVN VHIRTFKGLR
GVCTGFLVAF DKFWNMALTD VDETYRKPVL GKAYERDSSL TLTRLFDRLK LQDSSKKEAD
SKSAVEDSTL SRYSQTSTWK LASVWGRADT GRGSHKRSRS VPSSLQASAR EESRSELSGR
TTRTDGSSVG GTFSRATTLS RGQSRKKKRK PKVDYQQVFT RHINQIFIRG ENVLLVHLAQ
