ID RS4X_HUMAN Reviewed; 263 AA. AC P62701; P12631; P12750; P27576; P55831; Q14727; Q6IPY4; DT 19-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 eS4, X isoform {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S4; DE AltName: Full=SCR10; DE AltName: Full=Single copy abundant mRNA protein; GN Name=RPS4X {ECO:0000312|HGNC:HGNC:10424}; Synonyms=CCG2, RPS4, SCAR; 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=2124517; DOI=10.1016/0092-8674(90)90416-c; RA Fisher E.M.C., Beer-Romero P., Brown L.G., Ridley A., McNeil J.A., RA Lawrence J.B., Willard H.F., Bieber F.R., Page D.C.; RT "Homologous ribosomal protein genes on the human X and Y chromosomes: RT escape from X inactivation and possible implications for Turner syndrome."; RL Cell 63:1205-1218(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1795030; DOI=10.1242/jcs.100.1.35; RA Watanabe M., Furuno N., Goebl M., Go M., Miyauchi K., Sekiguchi T., RA Basilico C., Nishimoto T.; RT "Molecular cloning of the human gene, CCG2, that complements the BHK- RT derived temperature-sensitive cell cycle mutant tsBN63: identity of CCG2 RT with the human X chromosomal SCAR/RPS4X gene."; RL J. Cell Sci. 100:35-43(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Zuo L., Baybayan P., Kuang W.-J., Brown L., Page D., Chen E.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Muscle; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-59. RC TISSUE=Brain; RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.; RT "Characterization of different mRNA types expressed in human brain."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP PROTEIN SEQUENCE OF 2-11. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 19-263. RX PubMed=2829364; DOI=10.1007/bf01535047; RA Wiles M.V., Alexander C.M., Goodfellow P.N.; RT "Isolation of an abundantly expressed sequence from the human X chromosome RT by differential screening."; RL Somat. Cell Mol. Genet. 14:31-39(1988). RN [9] 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 [10] 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 [11] 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 [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 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 [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-230, 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 [16] RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND RP 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 [17] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. 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. The ribosome is a CC large ribonucleoprotein complex responsible for the synthesis of CC proteins in the cell (PubMed:23636399). Part of the small subunit (SSU) CC processome, first precursor of the small eukaryotic ribosomal subunit. CC During the assembly of the SSU processome in the nucleolus, many CC ribosome biogenesis factors, an RNA chaperone and ribosomal proteins CC associate with the nascent pre-rRNA and work in concert to generate RNA CC folding, modifications, rearrangements and cleavage as well as targeted CC degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}. CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:23636399). CC Part of the small subunit (SSU) processome, composed of more than 70 CC proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 CC (PubMed:34516797). Identified in a IGF2BP1-dependent mRNP granule CC complex containing untranslated mRNAs (PubMed:17289661). CC {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:34516797}. CC -!- INTERACTION: CC P62701; P55212: CASP6; NbExp=3; IntAct=EBI-354303, EBI-718729; CC P62701; P06307: CCK; NbExp=3; IntAct=EBI-354303, EBI-6624398; CC P62701; G5E9A7: DMWD; NbExp=3; IntAct=EBI-354303, EBI-10976677; CC P62701; Q01658: DR1; NbExp=3; IntAct=EBI-354303, EBI-750300; CC P62701; P22607: FGFR3; NbExp=3; IntAct=EBI-354303, EBI-348399; CC P62701; Q14957: GRIN2C; NbExp=3; IntAct=EBI-354303, EBI-8285963; CC P62701; P06396: GSN; NbExp=3; IntAct=EBI-354303, EBI-351506; CC P62701; Q00403: GTF2B; NbExp=3; IntAct=EBI-354303, EBI-389564; CC P62701; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-354303, EBI-1054873; CC P62701; P02545: LMNA; NbExp=3; IntAct=EBI-354303, EBI-351935; CC P62701; P62826: RAN; NbExp=3; IntAct=EBI-354303, EBI-286642; CC P62701; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-354303, EBI-2623095; CC P62701; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-354303, EBI-5235340; CC P62701; Q9Y649; NbExp=3; IntAct=EBI-354303, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661, CC ECO:0000269|PubMed:23636399}. 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 eS4 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; M58458; AAA63255.1; -; mRNA. DR EMBL; AF041428; AAB96968.1; -; Genomic_DNA. DR EMBL; CR456735; CAG33016.1; -; mRNA. DR EMBL; BC000472; AAH00472.1; -; mRNA. DR EMBL; BC071662; AAH71662.1; -; mRNA. DR EMBL; BC100903; AAI00904.1; -; mRNA. DR EMBL; BC100904; AAI00905.1; -; mRNA. DR EMBL; Z70767; CAA94808.1; -; mRNA. DR EMBL; M22146; AAA36597.1; -; mRNA. DR CCDS; CCDS14418.1; -. DR PIR; B36338; R3HU4X. DR RefSeq; NP_000998.1; NM_001007.4. DR PDB; 4UG0; EM; -; SE=1-263. DR PDB; 4V6X; EM; 5.00 A; AE=1-263. DR PDB; 5A2Q; EM; 3.90 A; E=1-263. DR PDB; 5LKS; EM; 3.60 A; SE=1-263. DR PDB; 5OA3; EM; 4.30 A; E=1-263. DR PDB; 5T2C; EM; 3.60 A; Ar=1-263. DR PDB; 5VYC; X-ray; 6.00 A; E1/E2/E3/E4/E5/E6=1-263. DR PDB; 6FEC; EM; 6.30 A; I=1-263. DR PDB; 6G18; EM; 3.60 A; E=1-263. DR PDB; 6G4S; EM; 4.00 A; E=1-263. DR PDB; 6G4W; EM; 4.50 A; E=1-263. DR PDB; 6G51; EM; 4.10 A; E=1-263. DR PDB; 6G53; EM; 4.50 A; E=1-263. DR PDB; 6G5H; EM; 3.60 A; E=1-263. DR PDB; 6G5I; EM; 3.50 A; E=1-263. DR PDB; 6IP5; EM; 3.90 A; 2q=1-263. DR PDB; 6IP6; EM; 4.50 A; 2q=1-263. DR PDB; 6IP8; EM; 3.90 A; 2q=1-263. DR PDB; 6OLE; EM; 3.10 A; SE=2-260. DR PDB; 6OLF; EM; 3.90 A; SE=2-260. DR PDB; 6OLI; EM; 3.50 A; SE=2-260. DR PDB; 6OM0; EM; 3.10 A; SE=2-260. DR PDB; 6OM7; EM; 3.70 A; SE=2-260. DR PDB; 6QZP; EM; 2.90 A; SE=2-263. DR PDB; 6XA1; EM; 2.80 A; SE=2-259. DR PDB; 6Y0G; EM; 3.20 A; SE=1-263. DR PDB; 6Y2L; EM; 3.00 A; SE=1-263. DR PDB; 6Y57; EM; 3.50 A; SE=1-263. DR PDB; 6YBW; EM; 3.10 A; C=1-263. DR PDB; 6Z6L; EM; 3.00 A; SE=1-263. DR PDB; 6Z6M; EM; 3.10 A; SE=1-263. DR PDB; 6Z6N; EM; 2.90 A; SE=1-263. DR PDB; 6ZLW; EM; 2.60 A; E=1-263. DR PDB; 6ZM7; EM; 2.70 A; SE=1-263. DR PDB; 6ZME; EM; 3.00 A; SE=1-263. DR PDB; 6ZMI; EM; 2.60 A; SE=1-263. DR PDB; 6ZMO; EM; 3.10 A; SE=1-263. DR PDB; 6ZMT; EM; 3.00 A; E=1-263. DR PDB; 6ZMW; EM; 3.70 A; C=1-263. DR PDB; 6ZN5; EM; 3.20 A; E=2-263. DR PDB; 6ZOJ; EM; 2.80 A; E=1-263. DR PDB; 6ZOK; EM; 2.80 A; E=1-263. DR PDB; 6ZON; EM; 3.00 A; q=1-263. DR PDB; 6ZP4; EM; 2.90 A; q=1-263. DR PDB; 6ZUO; EM; 3.10 A; E=1-263. DR PDB; 6ZV6; EM; 2.90 A; E=1-263. DR PDB; 6ZVH; EM; 2.90 A; E=2-263. DR PDB; 6ZVJ; EM; 3.80 A; q=2-256. DR PDB; 6ZXD; EM; 3.20 A; E=1-263. DR PDB; 6ZXE; EM; 3.00 A; E=1-263. DR PDB; 6ZXF; EM; 3.70 A; E=1-263. DR PDB; 6ZXG; EM; 2.60 A; E=1-263. DR PDB; 6ZXH; EM; 2.70 A; E=1-263. DR PDB; 7A09; EM; 3.50 A; q=1-263. DR PDB; 7K5I; EM; 2.90 A; E=1-263. DR PDB; 7MQ8; EM; 3.60 A; L4=1-263. DR PDB; 7MQA; EM; 2.70 A; L4=1-263. DR PDB; 7QP6; EM; 4.70 A; C=1-263. DR PDB; 7QP7; EM; 3.70 A; C=1-263. DR PDB; 7QVP; EM; 3.00 A; RE/SE=1-263. DR PDB; 7R4X; EM; 2.15 A; E=1-263. DR PDB; 7TQL; EM; 3.40 A; E=2-259. DR PDB; 7WTS; EM; 3.20 A; E=1-263. DR PDB; 7WTT; EM; 3.10 A; E=1-263. DR PDB; 7WTU; EM; 3.00 A; E=1-263. DR PDB; 7WTV; EM; 3.50 A; E=1-263. DR PDB; 7WTW; EM; 3.20 A; E=1-263. DR PDB; 7WTX; EM; 3.10 A; E=1-263. DR PDB; 7WTZ; EM; 3.00 A; E=1-263. DR PDB; 7WU0; EM; 3.30 A; E=1-263. DR PDB; 7XNX; EM; 2.70 A; SE=1-263. DR PDB; 7XNY; EM; 2.50 A; SE=1-263. DR PDB; 8G5Y; EM; 2.29 A; SE=1-263. DR PDB; 8G60; EM; 2.54 A; SE=1-263. DR PDB; 8G61; EM; 2.94 A; SE=1-263. DR PDB; 8G6J; EM; 2.80 A; SE=1-263. DR PDB; 8GLP; EM; 1.67 A; SE=1-263. DR PDB; 8JDJ; EM; 2.50 A; 1=1-263. DR PDB; 8JDK; EM; 2.26 A; 1=1-263. DR PDB; 8JDL; EM; 2.42 A; 1=1-263. DR PDB; 8JDM; EM; 2.67 A; 1=1-263. DR PDB; 8PPK; EM; 2.98 A; E=1-263. DR PDB; 8PPL; EM; 2.65 A; AE=1-263. DR PDB; 8T4S; EM; 2.60 A; E=1-263. DR PDBsum; 4UG0; -. DR PDBsum; 4V6X; -. DR PDBsum; 5A2Q; -. 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; 6OLI; -. 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; 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; 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; P62701; -. 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; P62701; -. DR BioGRID; 112105; 470. DR CORUM; P62701; -. DR IntAct; P62701; 117. DR MINT; P62701; -. DR STRING; 9606.ENSP00000362744; -. DR GlyGen; P62701; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62701; -. DR MetOSite; P62701; -. DR PhosphoSitePlus; P62701; -. DR SwissPalm; P62701; -. DR BioMuta; RPS4X; -. DR DMDM; 50403628; -. DR EPD; P62701; -. DR jPOST; P62701; -. DR MassIVE; P62701; -. DR MaxQB; P62701; -. DR PaxDb; 9606-ENSP00000362744; -. DR PeptideAtlas; P62701; -. DR ProteomicsDB; 57417; -. DR Pumba; P62701; -. DR TopDownProteomics; P62701; -. DR Antibodypedia; 27877; 212 antibodies from 30 providers. DR DNASU; 6191; -. DR Ensembl; ENST00000316084.10; ENSP00000362744.4; ENSG00000198034.11. DR GeneID; 6191; -. DR KEGG; hsa:6191; -. DR MANE-Select; ENST00000316084.10; ENSP00000362744.4; NM_001007.5; NP_000998.1. DR UCSC; uc004ear.4; human. DR AGR; HGNC:10424; -. DR CTD; 6191; -. DR DisGeNET; 6191; -. DR GeneCards; RPS4X; -. DR HGNC; HGNC:10424; RPS4X. DR HPA; ENSG00000198034; Low tissue specificity. DR MIM; 312760; gene. DR neXtProt; NX_P62701; -. DR OpenTargets; ENSG00000198034; -. DR PharmGKB; PA34839; -. DR VEuPathDB; HostDB:ENSG00000198034; -. DR eggNOG; KOG0378; Eukaryota. DR GeneTree; ENSGT00390000005569; -. DR HOGENOM; CLU_060400_1_0_1; -. DR InParanoid; P62701; -. DR OMA; RKDYKFP; -. DR OrthoDB; 5471107at2759; -. DR PhylomeDB; P62701; -. DR TreeFam; TF300612; -. DR PathwayCommons; P62701; -. 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; P62701; -. DR SIGNOR; P62701; -. DR BioGRID-ORCS; 6191; 472 hits in 749 CRISPR screens. DR ChiTaRS; RPS4X; human. DR GeneWiki; RPS4X; -. DR GenomeRNAi; 6191; -. DR Pharos; P62701; Tbio. DR PRO; PR:P62701; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P62701; Protein. DR Bgee; ENSG00000198034; Expressed in germinal epithelium of ovary and 217 other cell types or tissues. DR ExpressionAtlas; P62701; baseline and differential. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB. 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:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IDA:UniProtKB. DR GO; GO:0015935; C:small ribosomal subunit; IDA:MGI. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0006412; P:translation; IMP:UniProtKB. DR CDD; cd06087; KOW_RPS4; 1. DR CDD; cd00165; S4; 1. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.740; -; 1. DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1. DR HAMAP; MF_00485; Ribosomal_eS4; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR000876; Ribosomal_eS4. DR InterPro; IPR032277; Ribosomal_eS4_C. DR InterPro; IPR013845; Ribosomal_eS4_central_region. DR InterPro; IPR038237; Ribosomal_eS4_central_sf. DR InterPro; IPR041982; Ribosomal_eS4_KOW. DR InterPro; IPR013843; Ribosomal_eS4_N. DR InterPro; IPR018199; Ribosomal_eS4_N_CS. DR InterPro; IPR002942; S4_RNA-bd. DR InterPro; IPR036986; S4_RNA-bd_sf. DR PANTHER; PTHR11581; 30S/40S RIBOSOMAL PROTEIN S4; 1. DR PANTHER; PTHR11581:SF47; 40S RIBOSOMAL PROTEIN S4, X ISOFORM; 1. DR Pfam; PF16121; 40S_S4_C; 1. DR Pfam; PF00467; KOW; 1. DR Pfam; PF00900; Ribosomal_S4e; 1. DR Pfam; PF08071; RS4NT; 1. DR PIRSF; PIRSF002116; Ribosomal_S4; 1. DR SMART; SM00363; S4; 1. DR PROSITE; PS00528; RIBOSOMAL_S4E; 1. DR PROSITE; PS50889; S4; 1. DR SWISS-2DPAGE; P62701; -. DR Genevisible; P62701; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Nucleus; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8706699" FT CHAIN 2..263 FT /note="Small ribosomal subunit protein eS4, X isoform" FT /id="PRO_0000130805" FT DOMAIN 42..104 FT /note="S4 RNA-binding" FT MOD_RES 233 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62702" FT CROSSLNK 230 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CONFLICT 33 FT /note="Missing (in Ref. 8; AAA36597)" FT /evidence="ECO:0000305" FT CONFLICT 57..59 FT /note="TGD -> DRR (in Ref. 6; CAA94808)" FT /evidence="ECO:0000305" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:6ZV6" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 44..49 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 58..66 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 93..96 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 121..132 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 136..141 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:6ZVH" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 159..163 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 187..190 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:6ZVH" FT STRAND 207..211 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:6ZXG" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 233..236 FT /evidence="ECO:0007829|PDB:6ZLW" FT TURN 240..243 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 248..256 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 258..261 FT /evidence="ECO:0007829|PDB:6ZMT" SQ SEQUENCE 263 AA; 29598 MW; 87200E545A8958B0 CRC64; MARGPKKHLK RVAAPKHWML DKLTGVFAPR PSTGPHKLRE CLPLIIFLRN RLKYALTGDE VKKICMQRFI KIDGKVRTDI TYPAGFMDVI SIDKTGENFR LIYDTKGRFA VHRITPEEAK YKLCKVRKIF VGTKGIPHLV THDARTIRYP DPLIKVNDTI QIDLETGKIT DFIKFDTGNL CMVTGGANLG RIGVITNRER HPGSFDVVHV KDANGNSFAT RLSNIFVIGK GNKPWISLPR GKGIRLTIAE ERDKRLAAKQ SSG //