ID RS9_HUMAN Reviewed; 194 AA. AC P46781; A9C4C1; Q4QRK7; Q9BVZ0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 226. DE RecName: Full=Small ribosomal subunit protein uS4 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S9; GN Name=RPS9 {ECO:0000312|HGNC:HGNC:10442}; 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]. RC TISSUE=Colon; RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-i; RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.; RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 RT and S29 human ribosomal protein mRNAs."; RL Biochim. Biophys. Acta 1262:64-68(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11875025; DOI=10.1101/gr.214202; RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.; RT "The human ribosomal protein genes: sequencing and comparative analysis of RT 73 genes."; RL Genome Res. 12:379-390(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Muscle, Placenta, and Skin; 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 PROTEIN SEQUENCE OF 2-19. 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-73. RX PubMed=9582194; DOI=10.1101/gr.8.5.509; RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., RA Tanaka T., Page D.C.; RT "A map of 75 human ribosomal protein genes."; RL Genome Res. 8:509-523(1998). RN [8] 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 [9] 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 [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155, 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 [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-163, 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 [14] 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 [15] 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 [16] 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 [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-93 AND LYS-139, 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 [18] RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S 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 [19] {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). RN [20] RP VARIANT [LARGE SCALE ANALYSIS] PHE-137. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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 P46781; P40763: STAT3; NbExp=2; IntAct=EBI-351206, EBI-518675; 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 universal ribosomal protein uS4 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; U14971; AAA85659.1; -; mRNA. DR EMBL; AB061839; BAB79477.1; -; Genomic_DNA. DR EMBL; CU457734; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU151838; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471135; EAW72209.1; -; Genomic_DNA. DR EMBL; BC000802; AAH00802.1; -; mRNA. DR EMBL; BC007410; AAH07410.1; -; mRNA. DR EMBL; BC007434; AAH07434.1; -; mRNA. DR EMBL; BC007857; AAH07857.1; -; mRNA. DR EMBL; BC068055; AAH68055.1; -; mRNA. DR EMBL; BC071940; AAH71940.1; -; mRNA. DR EMBL; BC096756; AAH96756.1; -; mRNA. DR EMBL; AB007150; BAA25816.1; -; Genomic_DNA. DR CCDS; CCDS12884.1; -. DR PIR; S55917; S55917. DR RefSeq; NP_001004.2; NM_001013.3. DR RefSeq; NP_001308630.1; NM_001321701.1. DR RefSeq; NP_001308631.1; NM_001321702.1. DR RefSeq; NP_001308633.1; NM_001321704.1. DR PDB; 4UG0; EM; -; SJ=1-194. DR PDB; 4V6X; EM; 5.00 A; AJ=1-194. DR PDB; 5A2Q; EM; 3.90 A; J=1-194. DR PDB; 5AJ0; EM; 3.50 A; BJ=1-194. DR PDB; 5FLX; EM; 3.90 A; J=1-194. DR PDB; 5LKS; EM; 3.60 A; SJ=1-194. DR PDB; 5OA3; EM; 4.30 A; J=1-194. DR PDB; 5T2C; EM; 3.60 A; AL=1-194. DR PDB; 5VYC; X-ray; 6.00 A; J1/J2/J3/J4/J5/J6=1-194. DR PDB; 6FEC; EM; 6.30 A; K=7-188. DR PDB; 6G18; EM; 3.60 A; J=1-194. DR PDB; 6G4S; EM; 4.00 A; J=1-194. DR PDB; 6G4W; EM; 4.50 A; J=1-194. DR PDB; 6G51; EM; 4.10 A; J=1-194. DR PDB; 6G53; EM; 4.50 A; J=1-194. DR PDB; 6G5H; EM; 3.60 A; J=1-194. DR PDB; 6G5I; EM; 3.50 A; J=1-194. DR PDB; 6IP5; EM; 3.90 A; 3I=1-194. DR PDB; 6IP6; EM; 4.50 A; 3I=1-194. DR PDB; 6IP8; EM; 3.90 A; 3I=1-194. DR PDB; 6OLE; EM; 3.10 A; SJ=2-186. DR PDB; 6OLF; EM; 3.90 A; SJ=2-186. DR PDB; 6OLG; EM; 3.40 A; BJ=2-180. DR PDB; 6OLI; EM; 3.50 A; SJ=2-186. DR PDB; 6OLZ; EM; 3.90 A; BJ=2-180. DR PDB; 6OM0; EM; 3.10 A; SJ=2-186. DR PDB; 6OM7; EM; 3.70 A; SJ=2-186. DR PDB; 6QZP; EM; 2.90 A; SJ=2-186. DR PDB; 6XA1; EM; 2.80 A; SJ=2-181. DR PDB; 6Y0G; EM; 3.20 A; SJ=1-194. DR PDB; 6Y2L; EM; 3.00 A; SJ=1-194. DR PDB; 6Y57; EM; 3.50 A; SJ=1-194. DR PDB; 6YBW; EM; 3.10 A; D=1-194. DR PDB; 6Z6L; EM; 3.00 A; SJ=1-194. DR PDB; 6Z6M; EM; 3.10 A; SJ=1-194. DR PDB; 6Z6N; EM; 2.90 A; SJ=1-194. DR PDB; 6ZLW; EM; 2.60 A; J=1-194. DR PDB; 6ZM7; EM; 2.70 A; SJ=1-194. DR PDB; 6ZME; EM; 3.00 A; SJ=1-194. DR PDB; 6ZMI; EM; 2.60 A; SJ=1-194. DR PDB; 6ZMO; EM; 3.10 A; SJ=1-194. DR PDB; 6ZMT; EM; 3.00 A; J=1-194. DR PDB; 6ZMW; EM; 3.70 A; D=1-194. DR PDB; 6ZN5; EM; 3.20 A; J=2-181. DR PDB; 6ZOJ; EM; 2.80 A; J=1-194. DR PDB; 6ZOK; EM; 2.80 A; J=1-194. DR PDB; 6ZON; EM; 3.00 A; c=1-194. DR PDB; 6ZP4; EM; 2.90 A; c=1-194. DR PDB; 6ZUO; EM; 3.10 A; J=1-194. DR PDB; 6ZV6; EM; 2.90 A; J=1-194. DR PDB; 6ZVH; EM; 2.90 A; J=2-186. DR PDB; 6ZVJ; EM; 3.80 A; c=2-181. DR PDB; 6ZXD; EM; 3.20 A; J=1-194. DR PDB; 6ZXE; EM; 3.00 A; J=1-194. DR PDB; 6ZXF; EM; 3.70 A; J=1-194. DR PDB; 6ZXG; EM; 2.60 A; J=1-194. DR PDB; 6ZXH; EM; 2.70 A; J=1-194. DR PDB; 7A09; EM; 3.50 A; c=1-194. DR PDB; 7K5I; EM; 2.90 A; J=1-194. DR PDB; 7MQ8; EM; 3.60 A; L9=1-194. DR PDB; 7MQ9; EM; 3.87 A; L9=1-194. DR PDB; 7MQA; EM; 2.70 A; L9=1-194. DR PDB; 7QP6; EM; 4.70 A; D=1-194. DR PDB; 7QP7; EM; 3.70 A; D=1-194. DR PDB; 7R4X; EM; 2.15 A; J=1-194. DR PDB; 7TQL; EM; 3.40 A; J=2-181. DR PDB; 7WTS; EM; 3.20 A; J=1-194. DR PDB; 7WTT; EM; 3.10 A; J=1-194. DR PDB; 7WTU; EM; 3.00 A; J=1-194. DR PDB; 7WTV; EM; 3.50 A; J=1-194. DR PDB; 7WTW; EM; 3.20 A; J=1-194. DR PDB; 7WTX; EM; 3.10 A; J=1-194. DR PDB; 7WTZ; EM; 3.00 A; J=1-194. DR PDB; 7WU0; EM; 3.30 A; J=1-194. DR PDB; 7XNX; EM; 2.70 A; SJ=1-194. DR PDB; 7XNY; EM; 2.50 A; SJ=1-194. DR PDB; 8G5Y; EM; 2.29 A; SJ=1-194. DR PDB; 8G5Z; EM; 2.64 A; SJ=2-186. DR PDB; 8G60; EM; 2.54 A; SJ=1-194. DR PDB; 8G61; EM; 2.94 A; SJ=1-194. DR PDB; 8G6J; EM; 2.80 A; SJ=1-194. DR PDB; 8GLP; EM; 1.67 A; SJ=1-194. DR PDB; 8JDJ; EM; 2.50 A; 6=1-194. DR PDB; 8JDK; EM; 2.26 A; 6=1-194. DR PDB; 8JDL; EM; 2.42 A; 6=1-194. DR PDB; 8JDM; EM; 2.67 A; 6=1-194. DR PDB; 8PPK; EM; 2.98 A; J=1-194. DR PDB; 8PPL; EM; 2.65 A; AJ=1-194. DR PDB; 8T4S; EM; 2.60 A; J=1-194. 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; 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; P46781; -. 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-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; P46781; -. DR BioGRID; 112117; 570. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P46781; -. DR IntAct; P46781; 90. DR MINT; P46781; -. DR STRING; 9606.ENSP00000375632; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P46781; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P46781; -. DR MetOSite; P46781; -. DR PhosphoSitePlus; P46781; -. DR SwissPalm; P46781; -. DR BioMuta; RPS9; -. DR DMDM; 20178311; -. DR EPD; P46781; -. DR jPOST; P46781; -. DR MassIVE; P46781; -. DR MaxQB; P46781; -. DR PaxDb; 9606-ENSP00000302896; -. DR PeptideAtlas; P46781; -. DR ProteomicsDB; 55763; -. DR Pumba; P46781; -. DR TopDownProteomics; P46781; -. DR Antibodypedia; 35226; 276 antibodies from 29 providers. DR DNASU; 6203; -. DR Ensembl; ENST00000302907.9; ENSP00000302896.4; ENSG00000170889.14. DR Ensembl; ENST00000391752.5; ENSP00000375632.1; ENSG00000170889.14. DR Ensembl; ENST00000391753.6; ENSP00000375633.2; ENSG00000170889.14. DR Ensembl; ENST00000610826.4; ENSP00000481764.1; ENSG00000278270.4. DR Ensembl; ENST00000610953.3; ENSP00000482023.1; ENSG00000278081.3. DR Ensembl; ENST00000611921.4; ENSP00000480662.1; ENSG00000274950.4. DR Ensembl; ENST00000614737.4; ENSP00000482338.1; ENSG00000278270.4. DR Ensembl; ENST00000615346.4; ENSP00000481553.1; ENSG00000274646.4. DR Ensembl; ENST00000616082.3; ENSP00000482475.1; ENSG00000274646.4. DR Ensembl; ENST00000616536.4; ENSP00000481822.1; ENSG00000274950.4. DR Ensembl; ENST00000616839.3; ENSP00000484394.1; ENSG00000277359.3. DR Ensembl; ENST00000616877.3; ENSP00000481194.1; ENSG00000274950.4. DR Ensembl; ENST00000616928.3; ENSP00000481655.1; ENSG00000274626.3. DR Ensembl; ENST00000617291.3; ENSP00000482274.1; ENSG00000274005.3. DR Ensembl; ENST00000618751.3; ENSP00000480135.1; ENSG00000275323.3. DR Ensembl; ENST00000619229.4; ENSP00000479917.1; ENSG00000278270.4. DR Ensembl; ENST00000620720.3; ENSP00000478449.1; ENSG00000277079.3. DR Ensembl; ENST00000620940.4; ENSP00000483179.1; ENSG00000274646.4. DR GeneID; 6203; -. DR KEGG; hsa:6203; -. DR MANE-Select; ENST00000302907.9; ENSP00000302896.4; NM_001013.4; NP_001004.2. DR UCSC; uc002qdx.4; human. DR AGR; HGNC:10442; -. DR CTD; 6203; -. DR DisGeNET; 6203; -. DR GeneCards; RPS9; -. DR HGNC; HGNC:10442; RPS9. DR HPA; ENSG00000170889; Low tissue specificity. DR MIM; 603631; gene. DR neXtProt; NX_P46781; -. DR OpenTargets; ENSG00000170889; -. DR PharmGKB; PA34857; -. DR VEuPathDB; HostDB:ENSG00000170889; -. DR eggNOG; KOG3301; Eukaryota. DR GeneTree; ENSGT00550000074829; -. DR HOGENOM; CLU_089738_0_0_1; -. DR InParanoid; P46781; -. DR OMA; RQFITHG; -. DR OrthoDB; 1086372at2759; -. DR PhylomeDB; P46781; -. DR TreeFam; TF300795; -. DR PathwayCommons; P46781; -. 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-6790901; rRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-HSA-72649; Translation initiation complex formation. DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits. DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex. DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency. DR Reactome; R-HSA-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; P46781; -. DR SIGNOR; P46781; -. DR BioGRID-ORCS; 6203; 842 hits in 1159 CRISPR screens. DR ChiTaRS; RPS9; human. DR GeneWiki; RPS9; -. DR GenomeRNAi; 6203; -. DR Pharos; P46781; Tbio. DR PRO; PR:P46781; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P46781; Protein. DR Bgee; ENSG00000170889; Expressed in monocyte and 99 other cell types or tissues. DR ExpressionAtlas; P46781; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 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; IDA:UniProtKB. 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:0005840; C:ribosome; NAS:UniProtKB. 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; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:0045182; F:translation regulator activity; IMP:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. 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:0006412; P:translation; IMP:UniProtKB. DR CDD; cd00165; S4; 1. DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1. DR InterPro; IPR022801; Ribosomal_uS4. DR InterPro; IPR018079; Ribosomal_uS4_CS. DR InterPro; IPR005710; Ribosomal_uS4_euk/arc. DR InterPro; IPR001912; Ribosomal_uS4_N. DR InterPro; IPR002942; S4_RNA-bd. DR InterPro; IPR036986; S4_RNA-bd_sf. DR NCBIfam; TIGR01018; uS4_arch; 1. DR PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1. DR PANTHER; PTHR11831:SF5; 40S RIBOSOMAL PROTEIN S9; 1. DR Pfam; PF00163; Ribosomal_S4; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM01390; Ribosomal_S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1. DR PROSITE; PS00632; RIBOSOMAL_S4; 1. DR PROSITE; PS50889; S4; 1. DR Genevisible; P46781; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8706699" FT CHAIN 2..194 FT /note="Small ribosomal subunit protein uS4" FT /id="PRO_0000132689" FT DOMAIN 108..182 FT /note="S4 RNA-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182" FT REGION 162..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 66 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6ZWN5" FT MOD_RES 116 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6ZWN5" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 155 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 163 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 93 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 139 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 137 FT /note="V -> F (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036543" FT CONFLICT 84 FT /note="I -> L (in Ref. 1; AAA85659)" FT /evidence="ECO:0000305" FT CONFLICT 165..167 FT /note="YGG -> TGV (in Ref. 1; AAA85659)" FT /evidence="ECO:0000305" FT STRAND 17..20 FT /evidence="ECO:0007829|PDB:6ZLW" FT HELIX 22..35 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 40..61 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 68..83 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:6ZLW" FT HELIX 94..97 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 102..106 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 110..116 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 119..122 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 123..131 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 151..154 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:6YBW" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 172..177 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:7R4X" SQ SEQUENCE 194 AA; 22591 MW; E9CE3CBD59524F81 CRC64; MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL AKIRKAAREL LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL KIEDFLERRL QTQVFKLGLA KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK GQGGAGAGDD EEED //