ID RS8_HUMAN Reviewed; 208 AA. AC P62241; P09058; Q6IRL7; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 184. DE RecName: Full=Small ribosomal subunit protein eS8 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S8; GN Name=RPS8 {ECO:0000312|HGNC:HGNC:10441}; ORFNames=OK/SW-cl.83; 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 [GENOMIC DNA]. RX PubMed=8432552; DOI=10.1006/geno.1993.1011; RA Davies B., Fried M.; RT "The structure of the human intron-containing S8 ribosomal protein gene and RT determination of its chromosomal location at 1p32-p34.1."; RL Genomics 15:68-75(1993). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 [4] RP PROTEIN SEQUENCE OF 2-17, AND CLEAVAGE OF INITIATOR METHIONINE. 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [6] RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS RP SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200; RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., RA Johnsen A.H., Christiansen J., Nielsen F.C.; RT "Molecular composition of IMP1 ribonucleoprotein granules."; RL Mol. Cell. Proteomics 6:798-811(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130 AND SER-160, AND RP 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 [12] 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 [13] 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 [14] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25255805; DOI=10.1038/ncomms5919; RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.; RT "Global profiling of co- and post-translationally N-myristoylated proteomes RT in human cells."; RL Nat. Commun. 5:4919-4919(2014). RN [15] 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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-170 AND LYS-193, AND RP IDENTIFICATION BY MASS 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 [17] 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 [18] {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 small ribosomal subunit (PubMed:23636399). CC The ribosome is a large ribonucleoprotein complex responsible for the CC synthesis of proteins in the cell (PubMed:23636399). Part of the small CC subunit (SSU) processome, first precursor of the small eukaryotic CC ribosomal subunit. During the assembly of the SSU processome in the CC nucleolus, many ribosome biogenesis factors, an RNA chaperone and CC 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:23636399, CC ECO:0000269|PubMed:34516797}. CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:23636399). CC Identified in a IGF2BP1-dependent mRNP granule complex containing CC untranslated mRNAs (PubMed:17289661). Part of the small subunit (SSU) CC processome, composed of more than 70 proteins and the RNA chaperone CC small nucleolar RNA (snoRNA) U3 (PubMed:34516797). CC {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:34516797}. CC -!- INTERACTION: CC P62241; Q15700: DLG2; NbExp=3; IntAct=EBI-351811, EBI-80426; CC P62241; Q92796: DLG3; NbExp=3; IntAct=EBI-351811, EBI-80440; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661, CC ECO:0000269|PubMed:23636399}. Membrane {ECO:0000305|PubMed:17289661}; CC Lipid-anchor {ECO:0000305|PubMed:17289661}. Nucleus, nucleolus CC {ECO:0000269|PubMed:34516797}. Note=Localized in cytoplasmic mRNP CC granules containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 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; X67247; CAA47670.1; -; Genomic_DNA. DR EMBL; AB062401; BAB93488.1; -; mRNA. DR EMBL; BC070875; AAH70875.1; -; mRNA. DR CCDS; CCDS513.1; -. DR PIR; S25022; S25022. DR RefSeq; NP_001003.1; NM_001012.1. DR PDB; 4UG0; EM; -; SI=1-208. DR PDB; 4V6X; EM; 5.00 A; AI=1-208. DR PDB; 5A2Q; EM; 3.90 A; I=1-208. DR PDB; 5AJ0; EM; 3.50 A; BI=1-208. DR PDB; 5FLX; EM; 3.90 A; I=1-208. DR PDB; 5LKS; EM; 3.60 A; SI=1-208. DR PDB; 5OA3; EM; 4.30 A; I=1-208. DR PDB; 5T2C; EM; 3.60 A; Au=1-208. DR PDB; 5VYC; X-ray; 6.00 A; I1/I2/I3/I4/I5/I6=1-208. DR PDB; 6FEC; EM; 6.30 A; o=2-207. DR PDB; 6G18; EM; 3.60 A; I=1-208. DR PDB; 6G4S; EM; 4.00 A; I=1-208. DR PDB; 6G4W; EM; 4.50 A; I=1-208. DR PDB; 6G51; EM; 4.10 A; I=1-208. DR PDB; 6G53; EM; 4.50 A; I=1-208. DR PDB; 6G5H; EM; 3.60 A; I=1-208. DR PDB; 6G5I; EM; 3.50 A; I=1-208. DR PDB; 6IP5; EM; 3.90 A; 2t=1-208. DR PDB; 6IP6; EM; 4.50 A; 2t=1-208. DR PDB; 6IP8; EM; 3.90 A; 2t=1-208. DR PDB; 6OLE; EM; 3.10 A; SI=2-205. DR PDB; 6OLF; EM; 3.90 A; SI=2-205. DR PDB; 6OLG; EM; 3.40 A; BI=2-208. DR PDB; 6OLI; EM; 3.50 A; SI=2-205. DR PDB; 6OLZ; EM; 3.90 A; BI=2-208. DR PDB; 6OM0; EM; 3.10 A; SI=2-205. DR PDB; 6OM7; EM; 3.70 A; SI=2-205. DR PDB; 6QZP; EM; 2.90 A; SI=2-207. DR PDB; 6XA1; EM; 2.80 A; SI=2-206. DR PDB; 6Y0G; EM; 3.20 A; SI=1-208. DR PDB; 6Y2L; EM; 3.00 A; SI=1-208. DR PDB; 6Y57; EM; 3.50 A; SI=1-208. DR PDB; 6YBW; EM; 3.10 A; R=1-208. DR PDB; 6Z6L; EM; 3.00 A; SI=1-208. DR PDB; 6Z6M; EM; 3.10 A; SI=1-208. DR PDB; 6Z6N; EM; 2.90 A; SI=1-208. DR PDB; 6ZLW; EM; 2.60 A; I=1-208. DR PDB; 6ZM7; EM; 2.70 A; SI=1-208. DR PDB; 6ZME; EM; 3.00 A; SI=1-208. DR PDB; 6ZMI; EM; 2.60 A; SI=1-208. DR PDB; 6ZMO; EM; 3.10 A; SI=1-208. DR PDB; 6ZMT; EM; 3.00 A; I=1-208. DR PDB; 6ZMW; EM; 3.70 A; R=1-208. DR PDB; 6ZN5; EM; 3.20 A; I=2-206. DR PDB; 6ZOJ; EM; 2.80 A; I=1-208. DR PDB; 6ZOK; EM; 2.80 A; I=1-208. DR PDB; 6ZON; EM; 3.00 A; t=1-208. DR PDB; 6ZP4; EM; 2.90 A; t=1-208. DR PDB; 6ZUO; EM; 3.10 A; I=1-208. DR PDB; 6ZV6; EM; 2.90 A; I=1-208. DR PDB; 6ZVH; EM; 2.90 A; I=2-207. DR PDB; 6ZVJ; EM; 3.80 A; t=2-206. DR PDB; 6ZXD; EM; 3.20 A; I=1-208. DR PDB; 6ZXE; EM; 3.00 A; I=1-208. DR PDB; 6ZXF; EM; 3.70 A; I=1-208. DR PDB; 6ZXG; EM; 2.60 A; I=1-208. DR PDB; 6ZXH; EM; 2.70 A; I=1-208. DR PDB; 7A09; EM; 3.50 A; t=1-208. DR PDB; 7K5I; EM; 2.90 A; I=1-208. DR PDB; 7MQ8; EM; 3.60 A; L8=1-208. DR PDB; 7MQ9; EM; 3.87 A; L8=1-208. DR PDB; 7MQA; EM; 2.70 A; L8=1-208. DR PDB; 7QP6; EM; 4.70 A; R=1-208. DR PDB; 7QP7; EM; 3.70 A; R=1-208. DR PDB; 7QVP; EM; 3.00 A; RI/SI=1-208. DR PDB; 7R4X; EM; 2.15 A; I=1-208. DR PDB; 7TQL; EM; 3.40 A; I=2-206. DR PDB; 7WTS; EM; 3.20 A; I=1-208. DR PDB; 7WTT; EM; 3.10 A; I=1-208. DR PDB; 7WTU; EM; 3.00 A; I=1-208. DR PDB; 7WTV; EM; 3.50 A; I=1-208. DR PDB; 7WTW; EM; 3.20 A; I=1-208. DR PDB; 7WTX; EM; 3.10 A; I=1-208. DR PDB; 7WTZ; EM; 3.00 A; I=1-208. DR PDB; 7WU0; EM; 3.30 A; I=1-208. DR PDB; 7XNX; EM; 2.70 A; SI=1-208. DR PDB; 7XNY; EM; 2.50 A; SI=1-208. DR PDB; 8G5Y; EM; 2.29 A; SI=1-208. DR PDB; 8G5Z; EM; 2.64 A; SI=2-207. DR PDB; 8G60; EM; 2.54 A; SI=1-208. DR PDB; 8G61; EM; 2.94 A; SI=1-208. DR PDB; 8G6J; EM; 2.80 A; SI=1-208. DR PDB; 8GLP; EM; 1.67 A; SI=1-208. DR PDB; 8JDJ; EM; 2.50 A; 5=1-208. DR PDB; 8JDK; EM; 2.26 A; 5=1-208. DR PDB; 8JDL; EM; 2.42 A; 5=1-208. DR PDB; 8JDM; EM; 2.67 A; 5=1-208. DR PDB; 8PPK; EM; 2.98 A; I=1-208. DR PDB; 8PPL; EM; 2.65 A; AI=1-208. DR PDB; 8T4S; EM; 2.60 A; I=1-208. 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; 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; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8T4S; -. DR AlphaFoldDB; P62241; -. 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-17804; -. DR EMDB; EMD-17805; -. 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-3770; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. 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-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P62241; -. DR BioGRID; 112116; 636. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P62241; -. DR IntAct; P62241; 177. DR MINT; P62241; -. DR STRING; 9606.ENSP00000379888; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P62241; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62241; -. DR PhosphoSitePlus; P62241; -. DR SwissPalm; P62241; -. DR BioMuta; RPS8; -. DR DMDM; 50403622; -. DR CPTAC; CPTAC-581; -. DR EPD; P62241; -. DR jPOST; P62241; -. DR MassIVE; P62241; -. DR PaxDb; 9606-ENSP00000379888; -. DR PeptideAtlas; P62241; -. DR ProteomicsDB; 57372; -. DR Pumba; P62241; -. DR TopDownProteomics; P62241; -. DR Antibodypedia; 32545; 205 antibodies from 26 providers. DR DNASU; 6202; -. DR Ensembl; ENST00000396651.8; ENSP00000379888.3; ENSG00000142937.12. DR GeneID; 6202; -. DR KEGG; hsa:6202; -. DR MANE-Select; ENST00000396651.8; ENSP00000379888.3; NM_001012.2; NP_001003.1. DR AGR; HGNC:10441; -. DR CTD; 6202; -. DR DisGeNET; 6202; -. DR GeneCards; RPS8; -. DR HGNC; HGNC:10441; RPS8. DR HPA; ENSG00000142937; Low tissue specificity. DR MIM; 600357; gene. DR neXtProt; NX_P62241; -. DR OpenTargets; ENSG00000142937; -. DR PharmGKB; PA34856; -. DR VEuPathDB; HostDB:ENSG00000142937; -. DR eggNOG; KOG3283; Eukaryota. DR GeneTree; ENSGT00390000012433; -. DR HOGENOM; CLU_080597_1_1_1; -. DR InParanoid; P62241; -. DR OMA; QRPHYRK; -. DR OrthoDB; 1118725at2759; -. DR PhylomeDB; P62241; -. DR TreeFam; TF300041; -. DR PathwayCommons; P62241; -. DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-HSA-156902; Peptide chain elongation. 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-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-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 SignaLink; P62241; -. DR SIGNOR; P62241; -. DR BioGRID-ORCS; 6202; 840 hits in 1143 CRISPR screens. DR ChiTaRS; RPS8; human. DR GeneWiki; RPS8; -. DR GenomeRNAi; 6202; -. DR Pharos; P62241; Tbio. DR PRO; PR:P62241; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P62241; Protein. DR Bgee; ENSG00000142937; Expressed in left ovary and 101 other cell types or tissues. DR ExpressionAtlas; P62241; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal. 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:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:0002181; P:cytoplasmic translation; NAS: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; IDA:UniProtKB. DR GO; GO:0006412; P:translation; NAS:UniProtKB. DR CDD; cd11380; Ribosomal_S8e_like; 1. DR Gene3D; 3.10.290.70; -; 1. DR Gene3D; 1.10.168.20; Ribosomal protein S8e, subdomain; 1. DR InterPro; IPR001047; Ribosomal_eS8. DR InterPro; IPR018283; Ribosomal_eS8_CS. DR InterPro; IPR042563; Ribosomal_protein_eS8_euk. DR InterPro; IPR022309; Ribosomal_Se8/biogenesis_NSA2. DR NCBIfam; TIGR00307; eS8; 1. DR PANTHER; PTHR10394; 40S RIBOSOMAL PROTEIN S8; 1. DR PANTHER; PTHR10394:SF3; 40S RIBOSOMAL PROTEIN S8; 1. DR Pfam; PF01201; Ribosomal_S8e; 1. DR PROSITE; PS01193; RIBOSOMAL_S8E; 1. DR Genevisible; P62241; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Lipoprotein; Membrane; Myristate; Nucleus; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:8706699" FT CHAIN 2..208 FT /note="Small ribosomal subunit protein eS8" FT /id="PRO_0000122240" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..26 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 37 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62242" FT MOD_RES 128 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62242" FT MOD_RES 130 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:25255805" FT CROSSLNK 170 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 193 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 110 FT /note="R -> G (in dbSNP:rs11537870)" FT /id="VAR_051861" FT STRAND 7..10 FT /evidence="ECO:0007829|PDB:6ZXG" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:6ZMT" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 36..40 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 53..60 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 73..83 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 89..92 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 107..117 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 131..137 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 143..152 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 160..168 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 170..175 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 179..182 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 192..205 FT /evidence="ECO:0007829|PDB:7R4X" SQ SEQUENCE 208 AA; 24205 MW; 407FDF59171F7422 CRC64; MGISRDNWHK RRKTGGKRKP YHKKRKYELG RPAANTKIGP RRIHTVRVRG GNKKYRALRL DVGNFSWGSE CCTRKTRIID VVYNASNNEL VRTKTLVKNC IVLIDSTPYR QWYESHYALP LGRKKGAKLT PEEEEILNKK RSKKIQKKYD ERKKNAKISS LLEEQFQQGK LLACIASRPG QCGRADGYVL EGKELEFYLR KIKARKGK //