RS6_HUMAN
ID RS6_HUMAN Reviewed; 249 AA.
AC P62753; P08227; P10660; Q4VBY7; Q8N6Z7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=40S ribosomal protein S6 {ECO:0000303|PubMed:29563586};
DE AltName: Full=Phosphoprotein NP33;
DE AltName: Full=Small ribosomal subunit protein eS6 {ECO:0000303|PubMed:24524803};
GN Name=RPS6 {ECO:0000303|PubMed:29563586, ECO:0000312|HGNC:HGNC:10429};
GN ORFNames=OK/SW-cl.2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2840355; DOI=10.1016/0378-1119(88)90414-3;
RA Lott J.B., Mackie G.A.;
RT "Isolation and characterization of cloned cDNAs that code for human
RT ribosomal protein S6.";
RL Gene 65:31-39(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3279029; DOI=10.1016/s0021-9258(18)68900-8;
RA Heinze H., Arnold H.H., Fischer D., Kruppa J.;
RT "The primary structure of the human ribosomal protein S6 derived from a
RT cloned cDNA.";
RL J. Biol. Chem. 263:4139-4144(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1301164; DOI=10.1093/hmg/1.8.565;
RA Antoine M., Fried M.;
RT "The organization of the intron-containing human S6 ribosomal protein
RT (rpS6) gene and determination of its location at chromosome 9p21.";
RL Hum. Mol. Genet. 1:565-570(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1446836; DOI=10.1016/0378-1119(92)90149-j;
RA Pata I., Hoth S., Kruppa J., Metspalu A.;
RT "The human ribosomal protein S6 gene: isolation, primary structure and
RT location in chromosome 9.";
RL Gene 121:387-392(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-221.
RC TISSUE=Colon, Muscle, Pancreas, Skin, and Testis;
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 [7]
RP PROTEIN SEQUENCE OF 1-15, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION AT SER-235 AND SER-236.
RX PubMed=17360704; DOI=10.1074/jbc.m700906200;
RA Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J.,
RA Sonenberg N., Blenis J.;
RT "RAS/ERK signaling promotes site-specific ribosomal protein S6
RT phosphorylation via RSK and stimulates cap-dependent translation.";
RL J. Biol. Chem. 282:14056-14064(2007).
RN [10]
RP FUNCTION.
RX PubMed=17220279; DOI=10.1128/mcb.01462-06;
RA Yamashita D., Sano Y., Adachi Y., Okamoto Y., Osada H., Takahashi T.,
RA Yamaguchi T., Osumi T., Hirose F.;
RT "hDREF regulates cell proliferation and expression of ribosomal protein
RT genes.";
RL Mol. Cell. Biol. 27:2003-2013(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-240;
RP SER-244 AND SER-247, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
RX PubMed=18974095; DOI=10.1074/jbc.m805165200;
RA Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O.,
RA Hupp T.;
RT "Peptide combinatorial libraries identify TSC2 as a death-associated
RT protein kinase (DAPK) death domain-binding protein and reveal a stimulatory
RT role for DAPK in mTORC1 signaling.";
RL J. Biol. Chem. 284:334-344(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION AT SER-235 AND SER-236, AND MUTAGENESIS OF 235-SER-SER-236.
RX PubMed=21418524; DOI=10.1111/j.1742-4658.2011.08100.x;
RA Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P., Wenger R.H.;
RT "Substrate preference and phosphatidylinositol monophosphate inhibition of
RT the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN.";
RL FEBS J. 278:1757-1768(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND SER-242, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-235; SER-236 AND
RP SER-240, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [25]
RP HYDROXYLATION AT ARG-137, AND MUTAGENESIS OF ARG-137.
RX PubMed=29563586; DOI=10.1038/s41467-018-03410-w;
RA Wilkins S.E., Islam S., Gannon J.M., Markolovic S., Hopkinson R.J., Ge W.,
RA Schofield C.J., Chowdhury R.;
RT "JMJD5 is a human L-arginyl C-3 hydroxylase.";
RL Nat. Commun. 9:1180-1180(2018).
RN [26]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Component of the 40S small ribosomal subunit
CC (PubMed:8706699). Plays an important role in controlling cell growth
CC and proliferation through the selective translation of particular
CC classes of mRNA (PubMed:17220279). {ECO:0000269|PubMed:17220279,
CC ECO:0000269|PubMed:8706699}.
CC -!- INTERACTION:
CC P62753; Q09161: NCBP1; NbExp=3; IntAct=EBI-356625, EBI-464743;
CC P62753; P06748: NPM1; NbExp=3; IntAct=EBI-356625, EBI-78579;
CC P62753; Q96RG2: PASK; NbExp=3; IntAct=EBI-356625, EBI-1042651;
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:17360704,
CC ECO:0000269|PubMed:18974095, ECO:0000269|PubMed:21418524}.
CC -!- PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of Arg-
CC 137 by KDM8. {ECO:0000269|PubMed:29563586}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family.
CC {ECO:0000305}.
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DR EMBL; M20020; AAA60288.1; -; mRNA.
DR EMBL; J03537; AAA60287.1; -; mRNA.
DR EMBL; X67309; CAA47719.1; -; Genomic_DNA.
DR EMBL; M77232; AAA60289.1; -; Genomic_DNA.
DR EMBL; AB062123; BAB93455.1; -; mRNA.
DR EMBL; BC000524; AAH00524.1; -; mRNA.
DR EMBL; BC009427; AAH09427.2; -; mRNA.
DR EMBL; BC027620; AAH27620.1; -; mRNA.
DR EMBL; BC071907; AAH71907.1; -; mRNA.
DR EMBL; BC071908; AAH71908.1; -; mRNA.
DR EMBL; BC094826; AAH94826.1; -; mRNA.
DR CCDS; CCDS6492.1; -.
DR PIR; JC1394; R3HU6.
DR RefSeq; NP_001001.2; NM_001010.2.
DR PDB; 4UG0; EM; -; SG=1-249.
DR PDB; 4V6X; EM; 5.00 A; AG=1-249.
DR PDB; 5A2Q; EM; 3.90 A; G=1-249.
DR PDB; 5AJ0; EM; 3.50 A; BG=1-249.
DR PDB; 5FLX; EM; 3.90 A; G=1-249.
DR PDB; 5LKS; EM; 3.60 A; SG=1-249.
DR PDB; 5OA3; EM; 4.30 A; G=1-249.
DR PDB; 5T2C; EM; 3.60 A; AK=1-249.
DR PDB; 5VYC; X-ray; 6.00 A; G1/G2/G3/G4/G5/G6=1-249.
DR PDB; 6F4P; X-ray; 1.45 A; B=129-144.
DR PDB; 6F4Q; X-ray; 1.12 A; B=129-144.
DR PDB; 6FEC; EM; 6.30 A; q=1-237.
DR PDB; 6G18; EM; 3.60 A; G=1-249.
DR PDB; 6G4S; EM; 4.00 A; G=1-249.
DR PDB; 6G4W; EM; 4.50 A; G=1-249.
DR PDB; 6G51; EM; 4.10 A; G=1-249.
DR PDB; 6G53; EM; 4.50 A; G=1-249.
DR PDB; 6G5H; EM; 3.60 A; G=1-249.
DR PDB; 6G5I; EM; 3.50 A; G=1-249.
DR PDB; 6IP5; EM; 3.90 A; 3H=1-249.
DR PDB; 6IP6; EM; 4.50 A; 3H=1-249.
DR PDB; 6IP8; EM; 3.90 A; 3H=1-249.
DR PDB; 6OLE; EM; 3.10 A; SG=1-237.
DR PDB; 6OLF; EM; 3.90 A; SG=1-237.
DR PDB; 6OLG; EM; 3.40 A; BG=1-232.
DR PDB; 6OLI; EM; 3.50 A; SG=1-237.
DR PDB; 6OLZ; EM; 3.90 A; BG=1-232.
DR PDB; 6OM0; EM; 3.10 A; SG=1-237.
DR PDB; 6OM7; EM; 3.70 A; SG=1-237.
DR PDB; 6QZP; EM; 2.90 A; SG=1-237.
DR PDB; 6XA1; EM; 2.80 A; SG=1-228.
DR PDB; 6Y0G; EM; 3.20 A; SG=1-249.
DR PDB; 6Y2L; EM; 3.00 A; SG=1-249.
DR PDB; 6Y57; EM; 3.50 A; SG=1-249.
DR PDB; 6YBW; EM; 3.10 A; S=1-249.
DR PDB; 6Z6L; EM; 3.00 A; SG=1-249.
DR PDB; 6Z6M; EM; 3.10 A; SG=1-249.
DR PDB; 6Z6N; EM; 2.90 A; SG=1-249.
DR PDB; 6ZLW; EM; 2.60 A; G=1-249.
DR PDB; 6ZM7; EM; 2.70 A; SG=1-249.
DR PDB; 6ZME; EM; 3.00 A; SG=1-249.
DR PDB; 6ZMI; EM; 2.60 A; SG=1-249.
DR PDB; 6ZMO; EM; 3.10 A; SG=1-249.
DR PDB; 6ZMT; EM; 3.00 A; G=1-249.
DR PDB; 6ZMW; EM; 3.70 A; S=1-249.
DR PDB; 6ZN5; EM; 3.20 A; G=1-230.
DR PDB; 6ZOJ; EM; 2.80 A; G=1-249.
DR PDB; 6ZOK; EM; 2.80 A; G=1-249.
DR PDB; 6ZON; EM; 3.00 A; r=1-249.
DR PDB; 6ZP4; EM; 2.90 A; r=1-249.
DR PDB; 6ZUO; EM; 3.10 A; G=1-249.
DR PDB; 6ZV6; EM; 2.90 A; G=1-249.
DR PDB; 6ZVH; EM; 2.90 A; G=1-237.
DR PDB; 6ZVJ; EM; 3.80 A; r=2-223.
DR PDB; 6ZXD; EM; 3.20 A; G=1-249.
DR PDB; 6ZXE; EM; 3.00 A; G=1-249.
DR PDB; 6ZXF; EM; 3.70 A; G=1-249.
DR PDB; 6ZXG; EM; 2.60 A; G=1-249.
DR PDB; 6ZXH; EM; 2.70 A; G=1-249.
DR PDB; 7A09; EM; 3.50 A; r=1-249.
DR PDB; 7K5I; EM; 2.90 A; G=1-249.
DR PDB; 7MQ8; EM; 3.60 A; L6=1-249.
DR PDB; 7MQ9; EM; 3.87 A; L6=1-249.
DR PDB; 7MQA; EM; 2.70 A; L6=1-249.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6F4P; -.
DR PDBsum; 6F4Q; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P62753; -.
DR SMR; P62753; -.
DR BioGRID; 112108; 740.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62753; -.
DR DIP; DIP-31507N; -.
DR IntAct; P62753; 349.
DR MINT; P62753; -.
DR STRING; 9606.ENSP00000369757; -.
DR ChEMBL; CHEMBL3351215; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; P62753; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62753; -.
DR MetOSite; P62753; -.
DR PhosphoSitePlus; P62753; -.
DR SwissPalm; P62753; -.
DR BioMuta; RPS6; -.
DR DMDM; 51338632; -.
DR CPTAC; CPTAC-1331; -.
DR CPTAC; CPTAC-1332; -.
DR CPTAC; CPTAC-1333; -.
DR EPD; P62753; -.
DR jPOST; P62753; -.
DR MassIVE; P62753; -.
DR MaxQB; P62753; -.
DR PaxDb; P62753; -.
DR PeptideAtlas; P62753; -.
DR PRIDE; P62753; -.
DR ProteomicsDB; 57422; -.
DR TopDownProteomics; P62753; -.
DR Antibodypedia; 3412; 1327 antibodies from 47 providers.
DR DNASU; 6194; -.
DR Ensembl; ENST00000380394.9; ENSP00000369757.4; ENSG00000137154.13.
DR GeneID; 6194; -.
DR KEGG; hsa:6194; -.
DR MANE-Select; ENST00000380394.9; ENSP00000369757.4; NM_001010.3; NP_001001.2.
DR UCSC; uc003znv.2; human.
DR CTD; 6194; -.
DR DisGeNET; 6194; -.
DR GeneCards; RPS6; -.
DR HGNC; HGNC:10429; RPS6.
DR HPA; ENSG00000137154; Low tissue specificity.
DR MIM; 180460; gene.
DR neXtProt; NX_P62753; -.
DR OpenTargets; ENSG00000137154; -.
DR PharmGKB; PA34844; -.
DR VEuPathDB; HostDB:ENSG00000137154; -.
DR eggNOG; KOG1646; Eukaryota.
DR GeneTree; ENSGT00390000009819; -.
DR HOGENOM; CLU_046346_0_1_1; -.
DR InParanoid; P62753; -.
DR OMA; FYEKRMS; -.
DR OrthoDB; 1326714at2759; -.
DR PhylomeDB; P62753; -.
DR TreeFam; TF300035; -.
DR PathwayCommons; P62753; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62753; -.
DR SIGNOR; P62753; -.
DR BioGRID-ORCS; 6194; 771 hits in 1052 CRISPR screens.
DR ChiTaRS; RPS6; human.
DR GenomeRNAi; 6194; -.
DR Pharos; P62753; Tbio.
DR PRO; PR:P62753; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P62753; protein.
DR Bgee; ENSG00000137154; Expressed in skin of hip and 211 other tissues.
DR ExpressionAtlas; P62753; baseline and differential.
DR Genevisible; P62753; HS.
DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005844; C:polysome; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0015935; C:small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0022605; P:mammalian oogenesis stage; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0002309; P:T cell proliferation involved in immune response; IEA:Ensembl.
DR GO; GO:0031929; P:TOR signaling; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
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_0000137312"
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:0000269|PubMed:29563586"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 235
FT /note="Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK"
FT /evidence="ECO:0000269|PubMed:17360704,
FT ECO:0000269|PubMed:18974095, ECO:0000269|PubMed:21418524,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 236
FT /note="Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK"
FT /evidence="ECO:0000269|PubMed:17360704,
FT ECO:0000269|PubMed:18974095, ECO:0000269|PubMed:21418524,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 221
FT /note="K -> R (in dbSNP:rs17852447)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025314"
FT MUTAGEN 137
FT /note="R->X: Abolishes hydroxylation by KDM8."
FT /evidence="ECO:0000269|PubMed:29563586"
FT MUTAGEN 235..236
FT /note="SS->AA: Abolishes phosphorylation by PASK."
FT /evidence="ECO:0000269|PubMed:21418524"
FT CONFLICT 23
FT /note="K -> T (in Ref. 1; AAA60288)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> R (in Ref. 1; AAA60288)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="QY -> EC (in Ref. 2; AAA60287)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="K -> R (in Ref. 2; AAA60287)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="K -> Q (in Ref. 1; AAA60288)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="E -> Q (in Ref. 2; AAA60287)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6ZV6"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6ZUO"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 193..216
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:6ZLW"
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
