RS6_MOUSE
ID RS6_MOUSE Reviewed; 249 AA.
AC P62754; P08227; P10660;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=40S ribosomal protein S6;
DE AltName: Full=Phosphoprotein NP33;
GN Name=Rps6;
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 [MRNA].
RX PubMed=3601662; DOI=10.1093/nar/15.12.4990;
RA Lallanne J.-L., Lucero M., le Moullec J.-M.;
RT "Complete sequence of mouse S6 ribosomal protein.";
RL Nucleic Acids Res. 15:4990-4990(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=8917105; DOI=10.1016/0378-1119(96)00157-6;
RA Pata I., Metspalu A.;
RT "Structural characterization of the mouse ribosomal protein S6-encoding
RT gene.";
RL Gene 175:241-245(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary tumor;
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 [5]
RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-235; SER-236; SER-240
RP AND SER-244.
RX PubMed=1939282; DOI=10.1016/s0021-9258(18)54634-2;
RA Ferrari S., Bandi H.R., Hofsteenge J., Bussian B.M., Thomas G.;
RT "Mitogen-activated 70K S6 kinase. Identification of in vitro 40 S ribosomal
RT S6 phosphorylation sites.";
RL J. Biol. Chem. 266:22770-22775(1991).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-235; SER-240; SER-244
RP AND SER-247.
RX PubMed=8440735; DOI=10.1016/s0021-9258(18)53642-5;
RA Bandi H.R., Ferrari S., Krieg J., Meyer H.E., Thomas G.;
RT "Identification of 40 S ribosomal protein S6 phosphorylation sites in Swiss
RT mouse 3T3 fibroblasts stimulated with serum.";
RL J. Biol. Chem. 268:4530-4533(1993).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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).
CC -!- FUNCTION: Component of the 40S small ribosomal subunit (By similarity).
CC Plays an important role in controlling cell growth and proliferation
CC through the selective translation of particular classes of mRNA (By
CC similarity). {ECO:0000250|UniProtKB:P62753}.
CC -!- PTM: Ribosomal protein S6 is the major substrate of protein kinases in
CC eukaryote ribosomes. The phosphorylation is stimulated by growth
CC factors, tumor promoting agents, and mitogens. It is dephosphorylated
CC at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and
CC RPS6KA3; phosphorylation at these sites facilitates the assembly of the
CC pre-initiation complex. {ECO:0000269|PubMed:1939282,
CC ECO:0000269|PubMed:8440735}.
CC -!- PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of Arg-
CC 137 by KDM8. {ECO:0000250|UniProtKB:P62753}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family.
CC {ECO:0000305}.
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DR EMBL; Y00348; CAA68430.1; -; mRNA.
DR EMBL; Z54209; CAA90936.1; -; Genomic_DNA.
DR EMBL; AK012284; BAB28142.1; -; mRNA.
DR EMBL; AK012828; BAB28498.1; -; mRNA.
DR EMBL; AK013333; BAB28796.1; -; mRNA.
DR EMBL; AK050609; BAC34340.1; -; mRNA.
DR EMBL; BC010604; AAH10604.1; -; mRNA.
DR CCDS; CCDS18310.1; -.
DR PIR; S00660; R3MS6.
DR RefSeq; NP_033122.1; NM_009096.3.
DR RefSeq; XP_011238179.1; XM_011239877.1.
DR PDB; 7CPU; EM; 2.82 A; SG=1-249.
DR PDB; 7CPV; EM; 3.03 A; SG=1-249.
DR PDB; 7LS1; EM; 3.30 A; K3=1-249.
DR PDB; 7LS2; EM; 3.10 A; K3=1-249.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62754; -.
DR SMR; P62754; -.
DR BioGRID; 203013; 116.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR CORUM; P62754; -.
DR DIP; DIP-42772N; -.
DR IntAct; P62754; 12.
DR MINT; P62754; -.
DR STRING; 10090.ENSMUSP00000099878; -.
DR iPTMnet; P62754; -.
DR PhosphoSitePlus; P62754; -.
DR SwissPalm; P62754; -.
DR EPD; P62754; -.
DR jPOST; P62754; -.
DR PaxDb; P62754; -.
DR PeptideAtlas; P62754; -.
DR PRIDE; P62754; -.
DR ProteomicsDB; 257041; -.
DR Antibodypedia; 3412; 1327 antibodies from 47 providers.
DR DNASU; 20104; -.
DR Ensembl; ENSMUST00000102814; ENSMUSP00000099878; ENSMUSG00000028495.
DR GeneID; 105244208; -.
DR GeneID; 20104; -.
DR KEGG; mmu:20104; -.
DR UCSC; uc008tme.1; mouse.
DR CTD; 105244208; -.
DR CTD; 6194; -.
DR MGI; MGI:98159; Rps6.
DR VEuPathDB; HostDB:ENSMUSG00000028495; -.
DR eggNOG; KOG1646; Eukaryota.
DR GeneTree; ENSGT00390000009819; -.
DR HOGENOM; CLU_046346_0_1_1; -.
DR InParanoid; P62754; -.
DR OMA; FYEKRMS; -.
DR OrthoDB; 1326714at2759; -.
DR PhylomeDB; P62754; -.
DR TreeFam; TF300035; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
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; 20104; 16 hits in 41 CRISPR screens.
DR ChiTaRS; Rps6; mouse.
DR PRO; PR:P62754; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P62754; protein.
DR Bgee; ENSMUSG00000028495; Expressed in ectoplacental cone and 63 other tissues.
DR ExpressionAtlas; P62754; baseline and differential.
DR Genevisible; P62754; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
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:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005844; C:polysome; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0005840; C:ribosome; IDA:MGI.
DR GO; GO:0015935; C:small ribosomal subunit; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IMP:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
DR GO; GO:0022605; P:mammalian oogenesis stage; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:MGI.
DR GO; GO:0006364; P:rRNA processing; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0002309; P:T cell proliferation involved in immune response; IMP:MGI.
DR GO; GO:0031929; P:TOR signaling; ISO:MGI.
DR InterPro; IPR014401; Ribosomal_S6_euk.
DR InterPro; IPR001377; Ribosomal_S6e.
DR InterPro; IPR018282; Ribosomal_S6e_CS.
DR PANTHER; PTHR11502; PTHR11502; 1.
DR Pfam; PF01092; Ribosomal_S6e; 1.
DR PIRSF; PIRSF002129; Ribosom_S6_euk; 1.
DR SMART; SM01405; Ribosomal_S6e; 1.
DR PROSITE; PS00578; RIBOSOMAL_S6E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Hydroxylation;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..249
FT /note="40S ribosomal protein S6"
FT /id="PRO_0000137313"
FT REGION 217..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="(3R)-3-hydroxyarginine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 235
FT /note="Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 236
FT /note="Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1939282,
FT ECO:0000269|PubMed:8440735"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1939282,
FT ECO:0000269|PubMed:8440735, ECO:0007744|PubMed:21183079"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8440735"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62753"
SQ SEQUENCE 249 AA; 28681 MW; A61E435884E636AE CRC64;
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG
FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC IVDANLSVLN LVIVKKGEKD
IPGLTDTTVP RRLGPKRASR IRKLFNLSKE DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV
TPRVLQHKRR RIALKKQRTK KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS
TSKSESSQK
