ID   RS16_MOUSE              Reviewed;         146 AA.
AC   P14131; Q3THM9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Small ribosomal subunit protein uS9 {ECO:0000305};
DE   AltName: Full=40S ribosomal protein S16;
GN   Name=Rps16;
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.
RX   PubMed=3915781; DOI=10.1128/mcb.5.12.3560-3576.1985;
RA   Wagner M., Perry R.P.;
RT   "Characterization of the multigene family encoding the mouse S16 ribosomal
RT   protein: strategy for distinguishing an expressed gene from its processed
RT   pseudogene counterparts by an analysis of total genomic DNA.";
RL   Mol. Cell. Biol. 5:3560-3576(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Head, Kidney, Liver, Spinal ganglion, and Thymus;
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   [3]
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   [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. The ribosome is a
CC       large ribonucleoprotein complex responsible for the synthesis of
CC       proteins in the cell (PubMed:36517592). Part of the small subunit (SSU)
CC       processome, first precursor of the small eukaryotic ribosomal subunit.
CC       During the assembly of the SSU processome in the nucleolus, many
CC       ribosome biogenesis factors, an RNA chaperone and ribosomal proteins
CC       associate with the nascent pre-rRNA and work in concert to generate RNA
CC       folding, modifications, rearrangements and cleavage as well as targeted
CC       degradation of pre-ribosomal RNA by the RNA exosome (By similarity).
CC       {ECO:0000250|UniProtKB:P62249, ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:36517592).
CC       Part of the small subunit (SSU) processome, composed of more than 70
CC       proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (By
CC       similarity). {ECO:0000250|UniProtKB:P62249,
CC       ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P62249}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC       {ECO:0000305}.
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DR   EMBL; M11408; AAA03646.1; -; Unassigned_DNA.
DR   EMBL; AK010613; BAB27062.1; -; mRNA.
DR   EMBL; AK010641; BAB27083.1; -; mRNA.
DR   EMBL; AK011060; BAB27368.1; -; mRNA.
DR   EMBL; AK019400; BAB31702.1; -; mRNA.
DR   EMBL; AK083946; BAC39077.1; -; mRNA.
DR   EMBL; AK088413; BAC40341.1; -; mRNA.
DR   EMBL; AK088716; BAC40524.1; -; mRNA.
DR   EMBL; AK150808; BAE29871.1; -; mRNA.
DR   EMBL; AK168207; BAE40167.1; -; mRNA.
DR   EMBL; AK169328; BAE41081.1; -; mRNA.
DR   CCDS; CCDS39858.1; -.
DR   PIR; S11623; R3MS16.
DR   RefSeq; NP_038675.2; NM_013647.2.
DR   PDB; 7CPU; EM; 2.82 A; SQ=1-146.
DR   PDB; 7CPV; EM; 3.03 A; SQ=1-146.
DR   PDB; 7LS1; EM; 3.30 A; y2=1-146.
DR   PDB; 7LS2; EM; 3.10 A; y2=1-146.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P14131; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P14131; -.
DR   BioGRID; 203004; 105.
DR   ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR   IntAct; P14131; 7.
DR   MINT; P14131; -.
DR   STRING; 10090.ENSMUSP00000103940; -.
DR   GlyGen; P14131; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P14131; -.
DR   PhosphoSitePlus; P14131; -.
DR   SwissPalm; P14131; -.
DR   EPD; P14131; -.
DR   jPOST; P14131; -.
DR   MaxQB; P14131; -.
DR   PaxDb; 10090-ENSMUSP00000103940; -.
DR   ProteomicsDB; 299938; -.
DR   Pumba; P14131; -.
DR   Antibodypedia; 30342; 227 antibodies from 25 providers.
DR   DNASU; 20055; -.
DR   Ensembl; ENSMUST00000082134.6; ENSMUSP00000103940.2; ENSMUSG00000037563.16.
DR   GeneID; 20055; -.
DR   KEGG; mmu:20055; -.
DR   UCSC; uc012fgr.1; mouse.
DR   AGR; MGI:98118; -.
DR   CTD; 6217; -.
DR   MGI; MGI:98118; Rps16.
DR   VEuPathDB; HostDB:ENSMUSG00000037563; -.
DR   eggNOG; KOG1753; Eukaryota.
DR   GeneTree; ENSGT00390000013067; -.
DR   HOGENOM; CLU_046483_4_0_1; -.
DR   InParanoid; P14131; -.
DR   OMA; WPIEMAR; -.
DR   OrthoDB; 22228at2759; -.
DR   PhylomeDB; P14131; -.
DR   TreeFam; TF300088; -.
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; 20055; 25 hits in 75 CRISPR screens.
DR   ChiTaRS; Rps16; mouse.
DR   PRO; PR:P14131; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P14131; Protein.
DR   Bgee; ENSMUSG00000037563; Expressed in yolk sac and 66 other cell types or tissues.
DR   ExpressionAtlas; P14131; 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; IEA:UniProtKB-SubCell.
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:0015935; C:small ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0003723; F:RNA binding; ISO:MGI.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR   GO; GO:0140242; P:translation at postsynapse; NAS:SynGO.
DR   GO; GO:0140236; P:translation at presynapse; NAS:SynGO.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR000754; Ribosomal_uS9.
DR   InterPro; IPR020574; Ribosomal_uS9_CS.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR21569:SF16; 40S RIBOSOMAL PROTEIN S16; 1.
DR   PANTHER; PTHR21569; RIBOSOMAL PROTEIN S9; 1.
DR   Pfam; PF00380; Ribosomal_S9; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00360; RIBOSOMAL_S9; 1.
DR   Genevisible; P14131; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..146
FT                   /note="Small ribosomal subunit protein uS9"
FT                   /id="PRO_0000111480"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62249"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62249"
FT   CONFLICT        19..20
FT                   /note="AT -> L (in Ref. 1; AAA03646)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="T -> A (in Ref. 1; AAA03646)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   146 AA;  16445 MW;  519BCFB91BB68A15 CRC64;
     MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK LLEPVLLLGK
     ERFAGVDIRV RVKGGGHVAQ IYAIRQSISK ALVAYYQKYV DEASKKEIKD ILIQYDRTLL
     VADPRRCESK KFGGPGARAR YQKSYR
//