RS6_RAT
ID RS6_RAT Reviewed; 249 AA.
AC P62755; P08227; P10660;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=40S ribosomal protein S6;
GN Name=Rps6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3277962; DOI=10.1016/s0021-9258(18)69152-5;
RA Chan Y.-L., Wool I.G.;
RT "The primary structure of rat ribosomal protein S6.";
RL J. Biol. Chem. 263:2891-2896(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=398910; DOI=10.1002/jss.400120403;
RA Wittmann-Liebold B., Geissler A.W., Lin A., Wool I.G.;
RT "Sequence of the amino-terminal region of rat liver ribosomal proteins S4,
RT S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and L39.";
RL J. Supramol. Struct. 12:425-433(1979).
RN [4]
RP PHOSPHORYLATION, AND PROTEIN SEQUENCE OF 1-23.
RX PubMed=2106518; DOI=10.1016/s0021-9258(19)39566-3;
RA Franco R., Rosenfeld M.G.;
RT "Hormonally inducible phosphorylation of a nuclear pool of ribosomal
RT protein S6.";
RL J. Biol. Chem. 265:4321-4325(1990).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:P62753}.
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; M29358; AAA42079.1; -; mRNA.
DR EMBL; BC058149; AAH58149.1; -; mRNA.
DR PIR; A29929; R3RTS6.
DR RefSeq; NP_058856.1; NM_017160.1.
DR RefSeq; XP_003750019.1; XM_003749971.3.
DR AlphaFoldDB; P62755; -.
DR SMR; P62755; -.
DR BioGRID; 247970; 5.
DR IntAct; P62755; 7.
DR MINT; P62755; -.
DR STRING; 10116.ENSRNOP00000010383; -.
DR iPTMnet; P62755; -.
DR PhosphoSitePlus; P62755; -.
DR jPOST; P62755; -.
DR PaxDb; P62755; -.
DR PRIDE; P62755; -.
DR Ensembl; ENSRNOT00000073270; ENSRNOP00000067572; ENSRNOG00000007663.
DR GeneID; 29304; -.
DR KEGG; rno:29304; -.
DR UCSC; RGD:3602; rat.
DR CTD; 6194; -.
DR RGD; 3602; Rps6.
DR eggNOG; KOG1646; Eukaryota.
DR GeneTree; ENSGT00390000009819; -.
DR HOGENOM; CLU_046346_0_1_1; -.
DR InParanoid; P62755; -.
DR OrthoDB; 1326714at2759; -.
DR PhylomeDB; P62755; -.
DR TreeFam; TF300035; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-166208; mTORC1-mediated signalling.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P62755; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Genevisible; P62755; RN.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005844; C:polysome; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0005840; C:ribosome; ISO:RGD.
DR GO; GO:0015935; C:small ribosomal subunit; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IMP:RGD.
DR GO; GO:0006924; P:activation-induced cell death of T cells; ISO:RGD.
DR GO; GO:0071361; P:cellular response to ethanol; IDA:RGD.
DR GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0007369; P:gastrulation; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0022605; P:mammalian oogenesis stage; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IDA:RGD.
DR GO; GO:0001890; P:placenta development; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IDA:RGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:RGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0002309; P:T cell proliferation involved in immune response; ISO:RGD.
DR GO; GO:0031929; P:TOR signaling; ISO:RGD.
DR GO; GO:0006412; P:translation; IEA:InterPro.
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 Acetylation; Direct protein sequencing; Hydroxylation; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..249
FT /note="40S ribosomal protein S6"
FT /id="PRO_0000137314"
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:0000250|UniProtKB:P62753"
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"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
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
