RS16_MOUSE
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 03-AUG-2022, entry version 169.
DE RecName: 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, Pancreas,
RC 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).
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 SMR; P14131; -.
DR BioGRID; 203004; 104.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; P14131; 7.
DR MINT; P14131; -.
DR STRING; 10090.ENSMUSP00000103940; -.
DR iPTMnet; P14131; -.
DR PhosphoSitePlus; P14131; -.
DR SwissPalm; P14131; -.
DR EPD; P14131; -.
DR jPOST; P14131; -.
DR MaxQB; P14131; -.
DR PaxDb; P14131; -.
DR PRIDE; P14131; -.
DR ProteomicsDB; 299938; -.
DR Antibodypedia; 30342; 207 antibodies from 25 providers.
DR DNASU; 20055; -.
DR Ensembl; ENSMUST00000082134; ENSMUSP00000103940; ENSMUSG00000037563.
DR GeneID; 20055; -.
DR KEGG; mmu:20055; -.
DR UCSC; uc012fgr.1; mouse.
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; FMGQAEA; -.
DR OrthoDB; 1347615at2759; -.
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 72 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 63 other tissues.
DR ExpressionAtlas; P14131; baseline and differential.
DR Genevisible; P14131; MM.
DR GO; GO:0005737; C:cytoplasm; IC: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; ISO:MGI.
DR GO; GO:0015935; C:small ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC: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; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..146
FT /note="40S ribosomal protein S16"
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
