RS4X_HUMAN
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 03-AUG-2022, entry version 175.
DE RecName: Full=40S ribosomal protein S4, X isoform;
DE AltName: Full=SCR10;
DE AltName: Full=Single copy abundant mRNA protein;
DE AltName: Full=Small ribosomal subunit protein eS4 {ECO:0000303|PubMed:24524803};
GN Name=RPS4X; 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).
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 -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}.
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 Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs.
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 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 AlphaFoldDB; P62701; -.
DR SMR; P62701; -.
DR BioGRID; 112105; 376.
DR CORUM; P62701; -.
DR IntAct; P62701; 111.
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 SWISS-2DPAGE; P62701; -.
DR EPD; P62701; -.
DR jPOST; P62701; -.
DR MassIVE; P62701; -.
DR MaxQB; P62701; -.
DR PaxDb; P62701; -.
DR PeptideAtlas; P62701; -.
DR PRIDE; P62701; -.
DR ProteomicsDB; 57417; -.
DR TopDownProteomics; P62701; -.
DR Antibodypedia; 27877; 189 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 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; PARASIC; -.
DR OrthoDB; 1065966at2759; -.
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-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; 443 hits in 668 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 215 other tissues.
DR ExpressionAtlas; P62701; baseline and differential.
DR Genevisible; P62701; HS.
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:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; HDA:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; IDA:MGI.
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:0045471; P:response to ethanol; IEA:Ensembl.
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; -; 1.
DR HAMAP; MF_00485; Ribosomal_S4e; 1.
DR InterPro; IPR032277; 40S_S4_C.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041982; KOW_RPS4.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR000876; Ribosomal_S4e.
DR InterPro; IPR013845; Ribosomal_S4e_central_region.
DR InterPro; IPR038237; Ribosomal_S4e_central_sf.
DR InterPro; IPR013843; Ribosomal_S4e_N.
DR InterPro; IPR018199; Ribosomal_S4e_N_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11581; PTHR11581; 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 Pfam; PF01479; S4; 1.
DR PIRSF; PIRSF002116; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR PROSITE; PS00528; RIBOSOMAL_S4E; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW 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="40S ribosomal protein S4, 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:6ZXH"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6ZN5"
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
