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 02-SEP-2026, entry version 201. DE RecName: Full=Small ribosomal subunit protein eS6 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S6 {ECO:0000303|PubMed:29563586}; DE AltName: Full=Phosphoprotein NP33; 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 ADP-RIBOSYLATION AT GLU-35. RX PubMed=34314702; DOI=10.1016/j.cell.2021.07.005; RA Challa S., Khulpateea B.R., Nandu T., Camacho C.V., Ryu K.W., Chen H., RA Peng Y., Lea J.S., Kraus W.L.; RT "Ribosome ADP-ribosylation inhibits translation and maintains proteostasis RT in cancers."; RL Cell 184:4531-4546(2021). RN [27] RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. 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). RN [28] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). CC -!- FUNCTION: Component of the 40S small ribosomal subunit CC (PubMed:23636399, PubMed:8706699). Plays an important role in CC controlling cell growth and proliferation through the selective CC translation of particular classes of mRNA (PubMed:17220279). Part of CC the small subunit (SSU) processome, first precursor of the small CC eukaryotic ribosomal subunit. During the assembly of the SSU processome CC in the nucleolus, many ribosome biogenesis factors, an RNA chaperone CC and ribosomal proteins associate with the nascent pre-rRNA and work in CC concert to generate RNA folding, modifications, rearrangements and CC cleavage as well as targeted degradation of pre-ribosomal RNA by the CC RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:17220279, CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797, CC ECO:0000269|PubMed:8706699}. CC -!- SUBUNIT: Component of the small ribosomal subunit. Part of the small CC subunit (SSU) processome, composed of more than 70 proteins and the RNA CC chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}. 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 P62753; P0DTC9: N; Xeno; NbExp=6; IntAct=EBI-356625, EBI-25475856; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, CC nucleolus {ECO:0000269|PubMed:34516797}. 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 -!- PTM: Mono-ADP-ribosylation at Glu-35 by PARP16 inhibits polysome CC assembly and mRNA loading, thereby inhibiting protein translation. CC {ECO:0000269|PubMed:34314702}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001010.3. DR PDB; 22TU; EM; 3.00 A; SG=1-249. 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 PDB; 7QP6; EM; 4.70 A; S=1-249. DR PDB; 7QP7; EM; 3.70 A; S=1-249. DR PDB; 7QVP; EM; 3.00 A; RG/SG=1-249. DR PDB; 7R4X; EM; 2.15 A; G=1-249. DR PDB; 7TQL; EM; 3.40 A; G=1-226. DR PDB; 7WTS; EM; 3.20 A; G=1-249. DR PDB; 7WTT; EM; 3.10 A; G=1-249. DR PDB; 7WTU; EM; 3.00 A; G=1-249. DR PDB; 7WTV; EM; 3.50 A; G=1-249. DR PDB; 7WTW; EM; 3.20 A; G=1-249. DR PDB; 7WTX; EM; 3.10 A; G=1-249. DR PDB; 7WTZ; EM; 3.00 A; G=1-249. DR PDB; 7WU0; EM; 3.30 A; G=1-249. DR PDB; 7XNX; EM; 2.70 A; SG=1-249. DR PDB; 7XNY; EM; 2.50 A; SG=1-249. DR PDB; 7ZJW; EM; 2.80 A; SR=1-249. DR PDB; 7ZJX; EM; 3.10 A; SR=1-249. DR PDB; 8G5Y; EM; 2.29 A; SG=1-249. DR PDB; 8G5Z; EM; 2.64 A; SG=1-237. DR PDB; 8G60; EM; 2.54 A; SG=1-249. DR PDB; 8G61; EM; 2.94 A; SG=1-249. DR PDB; 8G6J; EM; 2.80 A; SG=1-249. DR PDB; 8GLP; EM; 1.67 A; SG=1-249. DR PDB; 8IFD; EM; 2.59 A; 3H=1-249. DR PDB; 8IFE; EM; 2.57 A; 3H=1-249. DR PDB; 8JDJ; EM; 2.50 A; 3=1-249. DR PDB; 8JDK; EM; 2.26 A; 3=1-249. DR PDB; 8JDL; EM; 2.42 A; 3=1-249. DR PDB; 8JDM; EM; 2.67 A; 3=1-249. DR PDB; 8K2C; EM; 2.40 A; SG=1-249. DR PDB; 8OZ0; EM; 3.50 A; S=1-249. DR PDB; 8PJ1; EM; 3.40 A; S=1-249. DR PDB; 8PJ2; EM; 3.40 A; S=1-249. DR PDB; 8PJ3; EM; 3.70 A; S=1-249. DR PDB; 8PJ4; EM; 3.20 A; S=1-249. DR PDB; 8PJ5; EM; 2.90 A; S=1-249. DR PDB; 8PJ6; EM; 2.90 A; S=1-249. DR PDB; 8PPK; EM; 2.98 A; G=1-249. DR PDB; 8PPL; EM; 2.65 A; AG=1-249. DR PDB; 8QOI; EM; 1.90 A; SG=1-249. DR PDB; 8T4S; EM; 2.60 A; G=1-249. DR PDB; 8UKB; EM; 3.05 A; SG=1-237. DR PDB; 8XP2; EM; 3.20 A; SG=1-249. DR PDB; 8XP3; EM; 3.40 A; SG=1-249. DR PDB; 8XSX; EM; 2.40 A; SG=1-249. DR PDB; 8XSY; EM; 3.00 A; SG=1-249. DR PDB; 8XSZ; EM; 3.20 A; SG=1-249. DR PDB; 8XXL; EM; 2.90 A; SG=1-249. DR PDB; 8XXM; EM; 3.20 A; SG=1-249. DR PDB; 8XXN; EM; 3.60 A; SG=1-249. DR PDB; 8Y0W; EM; 3.40 A; SG=1-249. DR PDB; 8Y0X; EM; 3.30 A; SG=1-249. DR PDB; 8YOO; EM; 2.00 A; SG=1-249. DR PDB; 8YOP; EM; 2.20 A; SG=1-249. DR PDB; 8ZDB; EM; 3.60 A; G=1-249. DR PDB; 8ZDC; EM; 3.80 A; G=1-249. DR PDB; 8ZDD; EM; 3.70 A; G=1-249. DR PDB; 9B0P; EM; 2.82 A; SG=1-237. DR PDB; 9B0Q; EM; 3.20 A; SG/sG=1-237. DR PDB; 9B0S; EM; 3.80 A; SG/sG=1-237. DR PDB; 9BKD; EM; 2.60 A; S=1-249. DR PDB; 9BLN; EM; 3.90 A; S=1-249. DR PDB; 9C3H; EM; 2.00 A; SG=1-249. DR PDB; 9ED0; EM; 2.80 A; G=1-249. DR PDB; 9FQZ; EM; 2.85 A; SG=1-249. DR PDB; 9G8M; EM; 3.30 A; SG=1-249. DR PDB; 9G8O; EM; 3.40 A; SG=1-249. DR PDB; 9I14; EM; 3.34 A; SG=1-249. DR PDB; 9I2D; EM; 2.19 A; SG=1-249. DR PDB; 9I2E; EM; 2.95 A; SG=1-249. DR PDB; 9KKF; EM; 3.30 A; SG=1-249. DR PDB; 9KMT; EM; 2.81 A; G=1-249. DR PDB; 9KMU; EM; 2.87 A; G=1-249. DR PDB; 9KMV; EM; 2.65 A; G=1-249. DR PDB; 9KMW; EM; 2.73 A; G=1-249. DR PDB; 9KMX; EM; 2.89 A; G=1-249. DR PDB; 9KMY; EM; 2.70 A; G=1-249. DR PDB; 9KMZ; EM; 2.78 A; G=1-249. DR PDB; 9KN0; EM; 2.65 A; G=1-249. DR PDB; 9KN5; EM; 3.20 A; SG=1-249. DR PDB; 9KN6; EM; 3.30 A; SG=1-249. DR PDB; 9KRP; EM; 3.20 A; SG=1-249. DR PDB; 9KZU; EM; 3.00 A; SG=1-249. DR PDB; 9KZX; EM; 3.30 A; SG=1-249. DR PDB; 9M0P; EM; 2.78 A; SG=1-249. DR PDB; 9O3W; EM; 1.90 A; SG=1-249. DR PDB; 9O3Y; EM; 2.20 A; SG=1-249. DR PDB; 9P6Z; EM; 2.97 A; SG=1-237. DR PDB; 9P72; EM; 2.80 A; SG=1-237. DR PDB; 9P73; EM; 2.66 A; SG=1-237. DR PDB; 9P76; EM; 2.83 A; SG=1-237. DR PDB; 9P78; EM; 2.90 A; SG=1-237. DR PDB; 9P79; EM; 3.10 A; SG=1-237. DR PDB; 9P7A; EM; 2.81 A; SG=1-237. DR PDB; 9P7C; EM; 2.78 A; SG=1-237. DR PDB; 9P7D; EM; 2.57 A; SG=1-237. DR PDB; 9P7E; EM; 2.59 A; SG=1-237. DR PDB; 9P7F; EM; 3.56 A; SG=1-237. DR PDB; 9P7G; EM; 3.54 A; SG=1-237. DR PDB; 9P7H; EM; 3.68 A; SG=1-237. DR PDB; 9P7I; EM; 3.69 A; SG=1-237. DR PDB; 9P7J; EM; 3.91 A; SG=1-237. DR PDB; 9P7K; EM; 2.80 A; SG=1-237. DR PDB; 9P7L; EM; 2.92 A; SG=1-237. DR PDB; 9P7N; EM; 2.83 A; SG=1-237. DR PDB; 9P7O; EM; 2.65 A; SG=1-237. DR PDB; 9P7W; EM; 2.93 A; SG=1-237. DR PDB; 9P7X; EM; 2.83 A; SG=1-237. DR PDB; 9P7Y; EM; 2.75 A; SG=1-237. DR PDB; 9P8B; EM; 2.48 A; SG=1-237. DR PDB; 9P8C; EM; 3.11 A; SG=1-237. DR PDB; 9P8H; EM; 2.98 A; SG=1-237. DR PDB; 9P8I; EM; 3.89 A; SG=1-237. DR PDB; 9P9H; EM; 2.84 A; SG=1-237. DR PDB; 9P9I; EM; 2.77 A; SG=1-237. DR PDB; 9PA7; EM; 2.67 A; SG=1-237. DR PDB; 9PBE; EM; 2.19 A; SG=1-237. DR PDB; 9PKG; EM; 3.26 A; SG=1-237. DR PDB; 9QLO; EM; 2.47 A; SG=1-249. DR PDB; 9QLP; EM; 2.75 A; SG=1-249. DR PDB; 9QLQ; EM; 2.57 A; SG=1-249. DR PDB; 9RPV; EM; 2.35 A; RG/SG=1-249. DR PDB; 9S3B; EM; 2.38 A; SG=1-249. DR PDB; 9S3C; EM; 2.42 A; SG=1-249. DR PDB; 9S3D; EM; 2.32 A; SG=1-249. DR PDB; 9SPF; EM; 2.40 A; SG=1-249. DR PDB; 9SPI; EM; 2.40 A; SG=1-249. DR PDB; 9SYR; EM; 3.55 A; Sy=1-249. DR AlphaFoldDB; P62753; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10775; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11276; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-11301; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11310; -. DR EMDB; EMD-11320; -. DR EMDB; EMD-11321; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11440; -. DR EMDB; EMD-11441; -. DR EMDB; EMD-11456; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11517; -. DR EMDB; EMD-11518; -. DR EMDB; EMD-11519; -. DR EMDB; EMD-11520; -. DR EMDB; EMD-11521; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-14181; -. DR EMDB; EMD-14317; -. DR EMDB; EMD-14751; -. DR EMDB; EMD-14752; -. DR EMDB; EMD-17297; -. DR EMDB; EMD-17696; -. DR EMDB; EMD-17697; -. DR EMDB; EMD-17698; -. DR EMDB; EMD-17699; -. DR EMDB; EMD-17700; -. DR EMDB; EMD-17701; -. DR EMDB; EMD-17804; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-18539; -. DR EMDB; EMD-22681; -. DR EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR EMDB; EMD-23938; -. DR EMDB; EMD-26067; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-32799; -. DR EMDB; EMD-32800; -. DR EMDB; EMD-32801; -. DR EMDB; EMD-32802; -. DR EMDB; EMD-32803; -. DR EMDB; EMD-32804; -. DR EMDB; EMD-32806; -. DR EMDB; EMD-32807; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-35413; -. DR EMDB; EMD-35414; -. DR EMDB; EMD-36178; -. DR EMDB; EMD-36179; -. DR EMDB; EMD-36180; -. DR EMDB; EMD-36181; -. DR EMDB; EMD-36838; -. DR EMDB; EMD-3770; -. DR EMDB; EMD-38548; -. DR EMDB; EMD-38549; -. DR EMDB; EMD-38629; -. DR EMDB; EMD-38630; -. DR EMDB; EMD-38631; -. DR EMDB; EMD-38752; -. DR EMDB; EMD-38753; -. DR EMDB; EMD-38754; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-39455; -. DR EMDB; EMD-39456; -. DR EMDB; EMD-39956; -. DR EMDB; EMD-39957; -. DR EMDB; EMD-39958; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. DR EMDB; EMD-42297; -. DR EMDB; EMD-42351; -. DR EMDB; EMD-4242; -. DR EMDB; EMD-4337; -. DR EMDB; EMD-4348; -. DR EMDB; EMD-4349; -. DR EMDB; EMD-4350; -. DR EMDB; EMD-4351; -. DR EMDB; EMD-4352; -. DR EMDB; EMD-4353; -. DR EMDB; EMD-44014; -. DR EMDB; EMD-44049; -. DR EMDB; EMD-44050; -. DR EMDB; EMD-44052; -. DR EMDB; EMD-44641; -. DR EMDB; EMD-44671; -. DR EMDB; EMD-45170; -. DR EMDB; EMD-47929; -. DR EMDB; EMD-50673; -. DR EMDB; EMD-51132; -. DR EMDB; EMD-51134; -. DR EMDB; EMD-52565; -. DR EMDB; EMD-52581; -. DR EMDB; EMD-52582; -. DR EMDB; EMD-53230; -. DR EMDB; EMD-53231; -. DR EMDB; EMD-53232; -. DR EMDB; EMD-54172; -. DR EMDB; EMD-54528; -. DR EMDB; EMD-54529; -. DR EMDB; EMD-54530; -. DR EMDB; EMD-55083; -. DR EMDB; EMD-55091; -. DR EMDB; EMD-55351; -. DR EMDB; EMD-62386; -. DR EMDB; EMD-62444; -. DR EMDB; EMD-62445; -. DR EMDB; EMD-62446; -. DR EMDB; EMD-62447; -. DR EMDB; EMD-62448; -. DR EMDB; EMD-62449; -. DR EMDB; EMD-62450; -. DR EMDB; EMD-62451; -. DR EMDB; EMD-62453; -. DR EMDB; EMD-62454; -. DR EMDB; EMD-62535; -. DR EMDB; EMD-62671; -. DR EMDB; EMD-62679; -. DR EMDB; EMD-63560; -. DR EMDB; EMD-68666; -. DR EMDB; EMD-70083; -. DR EMDB; EMD-70084; -. DR EMDB; EMD-70086; -. DR EMDB; EMD-71329; -. DR EMDB; EMD-71331; -. DR EMDB; EMD-71332; -. DR EMDB; EMD-71333; -. DR EMDB; EMD-71334; -. DR EMDB; EMD-71335; -. DR EMDB; EMD-71336; -. DR EMDB; EMD-71337; -. DR EMDB; EMD-71338; -. DR EMDB; EMD-71339; -. DR EMDB; EMD-71340; -. DR EMDB; EMD-71341; -. DR EMDB; EMD-71342; -. DR EMDB; EMD-71343; -. DR EMDB; EMD-71344; -. DR EMDB; EMD-71345; -. DR EMDB; EMD-71346; -. DR EMDB; EMD-71348; -. DR EMDB; EMD-71349; -. DR EMDB; EMD-71355; -. DR EMDB; EMD-71356; -. DR EMDB; EMD-71357; -. DR EMDB; EMD-71371; -. DR EMDB; EMD-71372; -. DR EMDB; EMD-71377; -. DR EMDB; EMD-71378; -. DR EMDB; EMD-71411; -. DR EMDB; EMD-71412; -. DR EMDB; EMD-71435; -. DR EMDB; EMD-71477; -. DR EMDB; EMD-71696; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P62753; -. DR BioGRID; 112108; 922. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P62753; -. DR DIP; DIP-31507N; -. DR FunCoup; P62753; 2834. DR IntAct; P62753; 525. DR MINT; P62753; -. DR NDEx; IQUERY-CP-RPS6; 42 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000369757; -. DR BindingDB; P62753; -. DR ChEMBL; CHEMBL3351215; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P62753; 2 sites, 1 N-linked glycan (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 jPOST; P62753; -. DR MassIVE; P62753; -. DR PaxDb; 9606-ENSP00000369757; -. DR PeptideAtlas; P62753; -. DR ProteomicsDB; 57422; -. DR Pumba; P62753; -. DR TopDownProteomics; P62753; -. DR Antibodypedia; 3412; 1360 antibodies from 50 providers. DR DNASU; 6194; -. DR Ensembl; ENST00000380394.9; ENSP00000369757.4; ENSG00000137154.14. 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 AGR; HGNC:10429; -. DR CIViC; 6194; 1 evidence item across 1 molecular profile. DR ClinPGx; PA34844; -. 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 OpenTargets; ENSG00000137154; -. DR VEuPathDB; HostDB:ENSG00000137154; -. DR eggNOG; KOG1646; Eukaryota. DR GeneTree; ENSGT00390000009819; -. DR HOGENOM; CLU_046346_0_1_1; -. DR InParanoid; P62753; -. DR OMA; KPRYKAP; -. DR OrthoDB; 9530936at2759; -. DR PAN-GO; P62753; 0 GO annotations based on evolutionary models. DR PhylomeDB; P62753; -. 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-9629569; Protein hydroxylation. 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-9735869; SARS-CoV-1 modulates host translation machinery. 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 Reactome; R-HSA-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA. DR Reactome; R-HSA-9954716; ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA. DR SABIO-RK; P62753; -. DR SignaLink; P62753; -. DR SIGNOR; P62753; -. DR Agora; ENSG00000137154; -. DR BioGRID-ORCS; 6194; 788 hits in 1134 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. 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 213 other cell types or tissues. DR ExpressionAtlas; P62753; baseline and differential. DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. 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:1990904; C:ribonucleoprotein complex; IDA:MGI. DR GO; GO:0015935; C:small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0032040; C:small-subunit processome; 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:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB. DR GO; GO:0031929; P:TOR signaling; IDA:UniProtKB. DR GO; GO:0006412; P:translation; IC:UniProtKB. DR FunFam; 1.20.5.2650:FF:000001; 40S ribosomal protein S6; 1. DR Gene3D; 1.20.5.2650; -; 1. DR InterPro; IPR001377; Ribosomal_eS6. DR InterPro; IPR014401; Ribosomal_eS6-like. DR InterPro; IPR018282; Ribosomal_eS6_CS. DR PANTHER; PTHR11502; 40S RIBOSOMAL PROTEIN S6; 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. DR PDBsum; 22TU; -. 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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 7QVP; -. DR PDBsum; 7R4X; -. DR PDBsum; 7TQL; -. DR PDBsum; 7WTS; -. DR PDBsum; 7WTT; -. DR PDBsum; 7WTU; -. DR PDBsum; 7WTV; -. DR PDBsum; 7WTW; -. DR PDBsum; 7WTX; -. DR PDBsum; 7WTZ; -. DR PDBsum; 7WU0; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 7ZJW; -. DR PDBsum; 7ZJX; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8IFD; -. DR PDBsum; 8IFE; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8K2C; -. DR PDBsum; 8OZ0; -. DR PDBsum; 8PJ1; -. DR PDBsum; 8PJ2; -. DR PDBsum; 8PJ3; -. DR PDBsum; 8PJ4; -. DR PDBsum; 8PJ5; -. DR PDBsum; 8PJ6; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8QOI; -. DR PDBsum; 8T4S; -. DR PDBsum; 8UKB; -. DR PDBsum; 8XP2; -. DR PDBsum; 8XP3; -. DR PDBsum; 8XSX; -. DR PDBsum; 8XSY; -. DR PDBsum; 8XSZ; -. DR PDBsum; 8XXL; -. DR PDBsum; 8XXM; -. DR PDBsum; 8XXN; -. DR PDBsum; 8Y0W; -. DR PDBsum; 8Y0X; -. DR PDBsum; 8YOO; -. DR PDBsum; 8YOP; -. DR PDBsum; 8ZDB; -. DR PDBsum; 8ZDC; -. DR PDBsum; 8ZDD; -. DR PDBsum; 9B0P; -. DR PDBsum; 9B0Q; -. DR PDBsum; 9B0S; -. DR PDBsum; 9BKD; -. DR PDBsum; 9BLN; -. DR PDBsum; 9C3H; -. DR PDBsum; 9ED0; -. DR PDBsum; 9FQZ; -. DR PDBsum; 9G8M; -. DR PDBsum; 9G8O; -. DR PDBsum; 9I14; -. DR PDBsum; 9I2D; -. DR PDBsum; 9I2E; -. DR PDBsum; 9KKF; -. DR PDBsum; 9KMT; -. DR PDBsum; 9KMU; -. DR PDBsum; 9KMV; -. DR PDBsum; 9KMW; -. DR PDBsum; 9KMX; -. DR PDBsum; 9KMY; -. DR PDBsum; 9KMZ; -. DR PDBsum; 9KN0; -. DR PDBsum; 9KN5; -. DR PDBsum; 9KN6; -. DR PDBsum; 9KRP; -. DR PDBsum; 9KZU; -. DR PDBsum; 9KZX; -. DR PDBsum; 9M0P; -. DR PDBsum; 9O3W; -. DR PDBsum; 9O3Y; -. DR PDBsum; 9P6Z; -. DR PDBsum; 9P72; -. DR PDBsum; 9P73; -. DR PDBsum; 9P76; -. DR PDBsum; 9P78; -. DR PDBsum; 9P79; -. DR PDBsum; 9P7A; -. DR PDBsum; 9P7C; -. DR PDBsum; 9P7D; -. DR PDBsum; 9P7E; -. DR PDBsum; 9P7F; -. DR PDBsum; 9P7G; -. DR PDBsum; 9P7H; -. DR PDBsum; 9P7I; -. DR PDBsum; 9P7J; -. DR PDBsum; 9P7K; -. DR PDBsum; 9P7L; -. DR PDBsum; 9P7N; -. DR PDBsum; 9P7O; -. DR PDBsum; 9P7W; -. DR PDBsum; 9P7X; -. DR PDBsum; 9P7Y; -. DR PDBsum; 9P8B; -. DR PDBsum; 9P8C; -. DR PDBsum; 9P8H; -. DR PDBsum; 9P8I; -. DR PDBsum; 9P9H; -. DR PDBsum; 9P9I; -. DR PDBsum; 9PA7; -. DR PDBsum; 9PBE; -. DR PDBsum; 9PKG; -. DR PDBsum; 9QLO; -. DR PDBsum; 9QLP; -. DR PDBsum; 9QLQ; -. DR PDBsum; 9RPV; -. DR PDBsum; 9S3B; -. DR PDBsum; 9S3C; -. DR PDBsum; 9S3D; -. DR PDBsum; 9SPF; -. DR PDBsum; 9SPI; -. DR PDBsum; 9SYR; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Cytoplasm; KW Direct protein sequencing; Hydroxylation; Isopeptide bond; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT CHAIN 1..249 FT /note="Small ribosomal subunit protein eS6" FT /id="PRO_0000137312" FT REGION 217..249 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 217..229 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 236..249 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 35 FT /note="ADP-ribosyl glutamic acid" FT /evidence="ECO:0000269|PubMed:34314702" 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..7 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 8..11 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 25..29 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:6Z6M" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 42..47 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:6Z6N" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:6Z6N" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:7MQA" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:6YBW" FT STRAND 93..98 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:8JDK" FT STRAND 106..115 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 122..125 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 138..144 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:8YOO" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:6ZLW" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:8YOO" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:8UKB" FT HELIX 182..236 FT /evidence="ECO:0007829|PDB:8GLP" 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 //