ID   RS13_MOUSE              Reviewed;         151 AA.
AC   P62301;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Small ribosomal subunit protein uS15 {ECO:0000305};
DE   AltName: Full=40S ribosomal protein S13;
GN   Name=Rps13;
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;
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   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   [3]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-34, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [4] {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 small ribosomal subunit (PubMed:36517592).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592). Part of the small
CC       subunit (SSU) processome, first precursor of the small eukaryotic
CC       ribosomal subunit. During the assembly of the SSU processome in the
CC       nucleolus, many ribosome biogenesis factors, an RNA chaperone and
CC       ribosomal proteins associate with the nascent pre-rRNA and work in
CC       concert to generate RNA folding, modifications, rearrangements and
CC       cleavage as well as targeted degradation of pre-ribosomal RNA by the
CC       RNA exosome (By similarity). {ECO:0000250|UniProtKB:P62277,
CC       ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Part of the small
CC       subunit (SSU) processome, composed of more than 70 proteins and the RNA
CC       chaperone small nucleolar RNA (snoRNA) U3 (By similarity).
CC       {ECO:0000250|UniProtKB:P62277, ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P62277}.
CC   -!- PTM: Ubiquitinated at Lys-27 by RNF14 and RNF25 in response to ribosome
CC       collisions (ribosome stalling). {ECO:0000250|UniProtKB:P62277}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 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; AK012479; BAB28268.1; -; mRNA.
DR   EMBL; AK018703; BAB31354.1; -; mRNA.
DR   EMBL; AK076060; BAC36154.1; -; mRNA.
DR   CCDS; CCDS52370.1; -.
DR   RefSeq; NP_080809.1; NM_026533.3.
DR   PDB; 7CPU; EM; 2.82 A; SN=1-151.
DR   PDB; 7CPV; EM; 3.03 A; SN=1-151.
DR   PDB; 7LS1; EM; 3.30 A; N3=1-151.
DR   PDB; 7LS2; EM; 3.10 A; N3=1-151.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P62301; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P62301; -.
DR   BioGRID; 212630; 102.
DR   ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR   DIP; DIP-59976N; -.
DR   IntAct; P62301; 3.
DR   STRING; 10090.ENSMUSP00000126294; -.
DR   GlyGen; P62301; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62301; -.
DR   PhosphoSitePlus; P62301; -.
DR   SwissPalm; P62301; -.
DR   EPD; P62301; -.
DR   jPOST; P62301; -.
DR   PaxDb; 10090-ENSMUSP00000126294; -.
DR   PeptideAtlas; P62301; -.
DR   ProteomicsDB; 299936; -.
DR   Pumba; P62301; -.
DR   Antibodypedia; 42458; 262 antibodies from 28 providers.
DR   DNASU; 68052; -.
DR   Ensembl; ENSMUST00000170953.3; ENSMUSP00000126294.2; ENSMUSG00000090862.4.
DR   GeneID; 68052; -.
DR   KEGG; mmu:68052; -.
DR   UCSC; uc009jje.2; mouse.
DR   AGR; MGI:1915302; -.
DR   CTD; 6207; -.
DR   MGI; MGI:1915302; Rps13.
DR   VEuPathDB; HostDB:ENSMUSG00000090862; -.
DR   eggNOG; KOG0400; Eukaryota.
DR   GeneTree; ENSGT00390000017491; -.
DR   HOGENOM; CLU_090139_1_0_1; -.
DR   InParanoid; P62301; -.
DR   OMA; EEHPKDM; -.
DR   OrthoDB; 5188951at2759; -.
DR   PhylomeDB; P62301; -.
DR   TreeFam; TF300190; -.
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; 68052; 27 hits in 72 CRISPR screens.
DR   ChiTaRS; Rps13; mouse.
DR   PRO; PR:P62301; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P62301; Protein.
DR   Bgee; ENSMUSG00000090862; Expressed in epiblast (generic) and 66 other cell types or tissues.
DR   ExpressionAtlas; P62301; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:1990932; F:5.8S rRNA binding; ISO:MGI.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR   GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR   GO; GO:0033119; P:negative regulation of RNA splicing; ISO:MGI.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR   CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR   Gene3D; 4.10.860.130; -; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   HAMAP; MF_01343_A; Ribosomal_uS15_A; 1.
DR   InterPro; IPR000589; Ribosomal_uS15.
DR   InterPro; IPR023029; Ribosomal_uS15_arc_euk.
DR   InterPro; IPR012606; Ribosomal_uS15_N.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   PANTHER; PTHR11885:SF20; 40S RIBOSOMAL PROTEIN S13; 1.
DR   PANTHER; PTHR11885; RIBOSOMAL PROTEIN S15P/S13E; 1.
DR   Pfam; PF08069; Ribosomal_S13_N; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01386; Ribosomal_S13_N; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR   PROSITE; PS00362; RIBOSOMAL_S15; 1.
DR   Genevisible; P62301; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN           1..151
FT                   /note="Small ribosomal subunit protein uS15"
FT                   /id="PRO_0000115662"
FT   MOD_RES         27
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62277"
FT   MOD_RES         27
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62277"
FT   MOD_RES         34
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         38
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62277"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62277"
FT   CROSSLNK        43
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62277"
SQ   SEQUENCE   151 AA;  17222 MW;  23F94D38F87B8D53 CRC64;
     MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV
     AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES
     RIHRLARYYK TKRVLPPNWK YESSTASALV A
//