RS9_HUMAN
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 03-AUG-2022, entry version 217.
DE RecName: Full=40S ribosomal protein S9;
DE AltName: Full=Small ribosomal subunit protein uS4 {ECO:0000303|PubMed:24524803};
GN Name=RPS9;
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).
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]
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 -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}.
CC -!- INTERACTION:
CC P46781; P40763: STAT3; NbExp=2; IntAct=EBI-351206, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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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 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 AlphaFoldDB; P46781; -.
DR SMR; P46781; -.
DR BioGRID; 112117; 483.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P46781; -.
DR IntAct; P46781; 108.
DR MINT; P46781; -.
DR STRING; 9606.ENSP00000302896; -.
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; P46781; -.
DR PeptideAtlas; P46781; -.
DR PRIDE; P46781; -.
DR ProteomicsDB; 55763; -.
DR TopDownProteomics; P46781; -.
DR Antibodypedia; 35226; 248 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 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; ARQFITH; -.
DR OrthoDB; 1310788at2759; -.
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-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; 805 hits in 1081 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 97 other tissues.
DR ExpressionAtlas; P46781; baseline and differential.
DR Genevisible; P46781; HS.
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:0015935; C:small ribosomal subunit; IBA:GO_Central.
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; IC:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01018; uS4_arch; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; 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..194
FT /note="40S ribosomal protein S9"
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 TURN 22..24
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6ZOK"
FT HELIX 41..60
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 151..155
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:6ZLW"
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
