ID   RS10_MOUSE              Reviewed;         165 AA.
AC   P63325; P09900; Q9DCR5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Small ribosomal subunit protein eS10 {ECO:0000305};
DE   AltName: Full=40S ribosomal protein S10;
GN   Name=Rps10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, Liver, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12 AND SER-146, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-153, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [8] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: Component of the 40S ribosomal subunit (PubMed:36517592). The
CC       ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592).
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:36517592).
CC       The methylated form interacts with NPM1 (By similarity).
CC       {ECO:0000250|UniProtKB:P46783, ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P46783}. Note=Localized in the
CC       granular component (GC) region of the nucleolus. Methylation is
CC       required for its localization in the GC region. Colocalizes with NPS1
CC       in the GC region of the nucleolus (By similarity).
CC       {ECO:0000250|UniProtKB:P46783}.
CC   -!- PTM: Methylated by PRMT5. Methylation is necessary for its interaction
CC       with NPS1, its localization in the granular component (GC) region of
CC       the nucleolus, for the proper assembly of ribosomes, protein synthesis
CC       and optimal cell proliferation. {ECO:0000250|UniProtKB:P46783}.
CC   -!- PTM: Monoubiquitinated by ZNF598 when a ribosome has stalled during
CC       translation of poly(A) sequences, leading to preclude synthesis of a
CC       long poly-lysine tail and initiate the ribosome quality control (RQC)
CC       pathway to degrade the potentially detrimental aberrant nascent
CC       polypeptide. Deubiquitinated by OTUD3 and USP21, antagonizing ZNF598
CC       activity. Deubiquitinated by OTUD1, antagonizing ZNF598 activity and
CC       stimulating formation of polysomes: deubiquitination by OTUD1 promotes
CC       stability and translation of a subset mRNAs with a high abundance of
CC       rare codons can limit the translation rate. Deubiquitinated by USP10.
CC       {ECO:0000250|UniProtKB:P46783}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK008797; BAB25901.1; -; mRNA.
DR   EMBL; AK011065; BAB27372.1; -; mRNA.
DR   EMBL; AK002558; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC003853; AAH03853.1; -; mRNA.
DR   EMBL; BC019725; AAH19725.1; -; mRNA.
DR   CCDS; CCDS37522.1; -.
DR   PIR; H59404; H59404.
DR   RefSeq; NP_080239.1; NM_025963.3.
DR   PDB; 7CPU; EM; 2.82 A; SK=1-165.
DR   PDB; 7CPV; EM; 3.03 A; SK=1-165.
DR   PDB; 7LS1; EM; 3.30 A; v2=1-165.
DR   PDB; 7LS2; EM; 3.10 A; v2=1-165.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P63325; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P63325; -.
DR   BioGRID; 211937; 78.
DR   ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR   IntAct; P63325; 1.
DR   STRING; 10090.ENSMUSP00000110532; -.
DR   GlyGen; P63325; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P63325; -.
DR   MetOSite; P63325; -.
DR   PhosphoSitePlus; P63325; -.
DR   SwissPalm; P63325; -.
DR   CPTAC; non-CPTAC-4058; -.
DR   EPD; P63325; -.
DR   jPOST; P63325; -.
DR   PaxDb; 10090-ENSMUSP00000110532; -.
DR   PeptideAtlas; P63325; -.
DR   ProteomicsDB; 262709; -.
DR   Pumba; P63325; -.
DR   TopDownProteomics; P63325; -.
DR   DNASU; 67097; -.
DR   Ensembl; ENSMUST00000114881.9; ENSMUSP00000110531.2; ENSMUSG00000052146.17.
DR   Ensembl; ENSMUST00000114882.9; ENSMUSP00000110532.2; ENSMUSG00000052146.17.
DR   Ensembl; ENSMUST00000178774.3; ENSMUSP00000136042.2; ENSMUSG00000052146.17.
DR   GeneID; 67097; -.
DR   KEGG; mmu:67097; -.
DR   UCSC; uc008bph.1; mouse.
DR   AGR; MGI:1914347; -.
DR   CTD; 6204; -.
DR   MGI; MGI:1914347; Rps10.
DR   VEuPathDB; HostDB:ENSMUSG00000052146; -.
DR   eggNOG; KOG3344; Eukaryota.
DR   GeneTree; ENSGT00440000034918; -.
DR   HOGENOM; CLU_089349_3_1_1; -.
DR   InParanoid; P63325; -.
DR   OMA; YRRRDQE; -.
DR   OrthoDB; 154729at2759; -.
DR   PhylomeDB; P63325; -.
DR   TreeFam; TF319100; -.
DR   Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-MMU-72649; Translation initiation complex formation.
DR   Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 67097; 23 hits in 76 CRISPR screens.
DR   ChiTaRS; Rps10; mouse.
DR   PRO; PR:P63325; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P63325; Protein.
DR   Bgee; ENSMUSG00000052146; Expressed in saccule of membranous labyrinth and 165 other cell types or tissues.
DR   ExpressionAtlas; P63325; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; NAS:SynGO.
DR   GO; GO:0098793; C:presynapse; NAS:SynGO.
DR   GO; GO:0005840; C:ribosome; NAS:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR   GO; GO:0140242; P:translation at postsynapse; NAS:SynGO.
DR   GO; GO:0140236; P:translation at presynapse; NAS:SynGO.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR005326; Plectin_eS10_N.
DR   InterPro; IPR037447; Ribosomal_eS10.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR12146; 40S RIBOSOMAL PROTEIN S10; 1.
DR   PANTHER; PTHR12146:SF10; 40S RIBOSOMAL PROTEIN S10; 1.
DR   Pfam; PF03501; S10_plectin; 1.
DR   Genevisible; P63325; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN           1..165
FT                   /note="Small ribosomal subunit protein eS10"
FT                   /id="PRO_0000116361"
FT   REGION          90..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         153
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         158
FT                   /note="Symmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
FT   MOD_RES         160
FT                   /note="Symmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
FT   CROSSLNK        138
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
FT   CROSSLNK        139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P46783"
SQ   SEQUENCE   165 AA;  18916 MW;  75B7005BA57AABA3 CRC64;
     MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE
     QFAWRHFYWY LTNEGIQYLR DYLHLPPEIV PATLRRSRPE TGRPRPKGPE GERPARFTRG
     EADRDTYRRS AVPPGADKKA EAGAGSATEF QFRGGFGRGR GQPPQ
//