ID RS16_HUMAN Reviewed; 146 AA.
AC P62249; B2RDD5; P17008;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 179.
DE RecName: Full=Small ribosomal subunit protein uS9 {ECO:0000303|PubMed:24524803};
DE AltName: Full=40S ribosomal protein S16;
GN Name=RPS16 {ECO:0000312|HGNC:HGNC:10396};
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=2016298; DOI=10.1016/s0021-9258(20)89575-1;
RA Batra S.K., Metzgar R.S., Hollingsworth M.A.;
RT "Molecular cloning and sequence analysis of the human ribosomal protein
RT S16.";
RL J. Biol. Chem. 266:6830-6833(1991).
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 MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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, and Kidney;
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 2-11.
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 [7]
RP PROTEIN SEQUENCE OF 2-15 AND 51-62, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Lourenco F., Olson M.F.;
RL Submitted (DEC-2009) to UniProtKB.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [13]
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 [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [17] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=34516797; DOI=10.1126/science.abj5338;
RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT "Nucleolar maturation of the human small subunit processome.";
RL Science 373:eabj5338-eabj5338(2021).
CC -!- FUNCTION: Component of the small ribosomal subunit (PubMed:23636399).
CC The ribosome is a large ribonucleoprotein complex responsible for the
CC synthesis of proteins in the cell (PubMed:23636399). Part of the small
CC subunit (SSU) processome, first precursor of the small eukaryotic
CC ribosomal subunit. During the assembly of the SSU processome in the
CC nucleolus, many ribosome biogenesis factors, an RNA chaperone and
CC ribosomal proteins associate with the nascent pre-rRNA and work in
CC concert to generate RNA folding, modifications, rearrangements and
CC cleavage as well as targeted degradation of pre-ribosomal RNA by the
CC RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:34516797}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Part of the small
CC subunit (SSU) processome, composed of more than 70 proteins and the RNA
CC chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}.
CC -!- INTERACTION:
CC P62249; Q5S007: LRRK2; NbExp=4; IntAct=EBI-352480, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:34516797}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC {ECO:0000305}.
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DR EMBL; M60854; AAA60583.1; -; mRNA.
DR EMBL; AB061841; BAB79479.1; -; Genomic_DNA.
DR EMBL; AK315498; BAG37882.1; -; mRNA.
DR EMBL; CH471126; EAW56894.1; -; Genomic_DNA.
DR EMBL; BC004324; AAH04324.1; -; mRNA.
DR EMBL; BC007977; AAH07977.1; -; mRNA.
DR CCDS; CCDS12535.1; -.
DR PIR; A39760; R3HU16.
DR RefSeq; NP_001011.1; NM_001020.5.
DR PDB; 4UG0; EM; -; SQ=1-146.
DR PDB; 4V6X; EM; 5.00 A; AQ=1-146.
DR PDB; 5A2Q; EM; 3.90 A; Q=1-146.
DR PDB; 5AJ0; EM; 3.50 A; BQ=1-146.
DR PDB; 5FLX; EM; 3.90 A; Q=1-146.
DR PDB; 5LKS; EM; 3.60 A; SQ=1-146.
DR PDB; 5OA3; EM; 4.30 A; Q=1-146.
DR PDB; 5T2C; EM; 3.60 A; Ay=1-146.
DR PDB; 5VYC; X-ray; 6.00 A; Q1/Q2/Q3/Q4/Q5/Q6=1-146.
DR PDB; 6FEC; EM; 6.30 A; H=6-146.
DR PDB; 6G18; EM; 3.60 A; Q=1-146.
DR PDB; 6G4S; EM; 4.00 A; Q=1-146.
DR PDB; 6G4W; EM; 4.50 A; Q=1-146.
DR PDB; 6G51; EM; 4.10 A; Q=1-146.
DR PDB; 6G53; EM; 4.50 A; Q=1-146.
DR PDB; 6G5H; EM; 3.60 A; Q=1-146.
DR PDB; 6G5I; EM; 3.50 A; Q=1-146.
DR PDB; 6IP5; EM; 3.90 A; 2x=1-146.
DR PDB; 6IP6; EM; 4.50 A; 2x=1-146.
DR PDB; 6IP8; EM; 3.90 A; 2x=1-146.
DR PDB; 6OLE; EM; 3.10 A; SQ=1-146.
DR PDB; 6OLF; EM; 3.90 A; SQ=1-146.
DR PDB; 6OLG; EM; 3.40 A; BQ=8-146.
DR PDB; 6OLI; EM; 3.50 A; SQ=1-146.
DR PDB; 6OLZ; EM; 3.90 A; BQ=8-146.
DR PDB; 6OM0; EM; 3.10 A; SQ=1-146.
DR PDB; 6OM7; EM; 3.70 A; SQ=1-146.
DR PDB; 6QZP; EM; 2.90 A; SQ=6-146.
DR PDB; 6XA1; EM; 2.80 A; SQ=7-146.
DR PDB; 6Y0G; EM; 3.20 A; SQ=1-146.
DR PDB; 6Y2L; EM; 3.00 A; SQ=1-146.
DR PDB; 6Y57; EM; 3.50 A; SQ=1-146.
DR PDB; 6YBS; EM; 3.10 A; Y=1-146.
DR PDB; 6Z6L; EM; 3.00 A; SQ=1-146.
DR PDB; 6Z6M; EM; 3.10 A; SQ=1-146.
DR PDB; 6Z6N; EM; 2.90 A; SQ=1-146.
DR PDB; 6ZLW; EM; 2.60 A; R=1-146.
DR PDB; 6ZM7; EM; 2.70 A; SQ=1-146.
DR PDB; 6ZME; EM; 3.00 A; SQ=1-146.
DR PDB; 6ZMI; EM; 2.60 A; SQ=1-146.
DR PDB; 6ZMO; EM; 3.10 A; SQ=1-146.
DR PDB; 6ZMT; EM; 3.00 A; R=1-146.
DR PDB; 6ZMW; EM; 3.70 A; Y=1-146.
DR PDB; 6ZN5; EM; 3.20 A; R=8-146.
DR PDB; 6ZOJ; EM; 2.80 A; Q=1-146.
DR PDB; 6ZOL; EM; 2.80 A; Q=1-146.
DR PDB; 6ZON; EM; 3.00 A; g=1-146.
DR PDB; 6ZP4; EM; 2.90 A; g=1-146.
DR PDB; 6ZUO; EM; 3.10 A; Q=1-146.
DR PDB; 6ZV6; EM; 2.90 A; Q=1-146.
DR PDB; 6ZVH; EM; 2.90 A; Q=3-146.
DR PDB; 6ZVJ; EM; 3.80 A; g=9-146.
DR PDB; 6ZXD; EM; 3.20 A; Q=1-146.
DR PDB; 6ZXE; EM; 3.00 A; Q=1-146.
DR PDB; 6ZXF; EM; 3.70 A; Q=1-146.
DR PDB; 6ZXG; EM; 2.60 A; Q=1-146.
DR PDB; 6ZXH; EM; 2.70 A; Q=1-146.
DR PDB; 7A09; EM; 3.50 A; g=1-146.
DR PDB; 7K5I; EM; 2.90 A; Q=1-146.
DR PDB; 7MQ8; EM; 3.60 A; LC=1-146.
DR PDB; 7MQ9; EM; 3.87 A; LC=1-146.
DR PDB; 7MQA; EM; 2.70 A; LC=1-146.
DR PDB; 7QP6; EM; 4.70 A; Y=1-146.
DR PDB; 7QP7; EM; 3.70 A; Y=1-146.
DR PDB; 7R4X; EM; 2.15 A; Q=1-146.
DR PDB; 7TQL; EM; 3.40 A; R=8-146.
DR PDB; 7WTT; EM; 3.10 A; Q=1-146.
DR PDB; 7WTU; EM; 3.00 A; Q=1-146.
DR PDB; 7WTV; EM; 3.50 A; Q=1-146.
DR PDB; 7WTW; EM; 3.20 A; Q=1-146.
DR PDB; 7WTX; EM; 3.10 A; Q=1-146.
DR PDB; 7WTZ; EM; 3.00 A; Q=1-146.
DR PDB; 7WU0; EM; 3.30 A; Q=1-146.
DR PDB; 7XNX; EM; 2.70 A; SQ=1-146.
DR PDB; 7XNY; EM; 2.50 A; SQ=1-146.
DR PDB; 8G5Y; EM; 2.29 A; SQ=1-146.
DR PDB; 8G60; EM; 2.54 A; SQ=1-146.
DR PDB; 8G61; EM; 2.94 A; SQ=1-146.
DR PDB; 8G6J; EM; 2.80 A; SQ=1-146.
DR PDB; 8GLP; EM; 1.67 A; SQ=1-146.
DR PDB; 8JDJ; EM; 2.50 A; AC=1-146.
DR PDB; 8JDK; EM; 2.26 A; AC=1-146.
DR PDB; 8JDL; EM; 2.42 A; AC=1-146.
DR PDB; 8JDM; EM; 2.67 A; AC=1-146.
DR PDB; 8PPK; EM; 2.98 A; Q=1-146.
DR PDB; 8PPL; EM; 2.65 A; AQ=1-146.
DR PDB; 8T4S; EM; 2.60 A; Q=1-146.
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; 6YBS; -.
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; 6ZOL; -.
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; 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; P62249; -.
DR EMDB; EMD-10668; -.
DR EMDB; EMD-10674; -.
DR EMDB; EMD-10690; -.
DR EMDB; EMD-10772; -.
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-11322; -.
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-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; P62249; -.
DR BioGRID; 112131; 713.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62249; -.
DR DIP; DIP-33200N; -.
DR IntAct; P62249; 92.
DR MINT; P62249; -.
DR STRING; 9606.ENSP00000367806; -.
DR GlyCosmos; P62249; 1 site, 2 glycans.
DR GlyGen; P62249; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P62249; -.
DR MetOSite; P62249; -.
DR PhosphoSitePlus; P62249; -.
DR SwissPalm; P62249; -.
DR BioMuta; RPS16; -.
DR DMDM; 50403607; -.
DR EPD; P62249; -.
DR jPOST; P62249; -.
DR MassIVE; P62249; -.
DR MaxQB; P62249; -.
DR PaxDb; 9606-ENSP00000251453; -.
DR PeptideAtlas; P62249; -.
DR ProteomicsDB; 57374; -.
DR Pumba; P62249; -.
DR TopDownProteomics; P62249; -.
DR Antibodypedia; 30342; 227 antibodies from 25 providers.
DR DNASU; 6217; -.
DR Ensembl; ENST00000251453.8; ENSP00000251453.2; ENSG00000105193.9.
DR GeneID; 6217; -.
DR KEGG; hsa:6217; -.
DR MANE-Select; ENST00000251453.8; ENSP00000251453.2; NM_001020.6; NP_001011.1.
DR UCSC; uc002olk.4; human.
DR AGR; HGNC:10396; -.
DR CTD; 6217; -.
DR DisGeNET; 6217; -.
DR GeneCards; RPS16; -.
DR HGNC; HGNC:10396; RPS16.
DR HPA; ENSG00000105193; Low tissue specificity.
DR MIM; 603675; gene.
DR neXtProt; NX_P62249; -.
DR OpenTargets; ENSG00000105193; -.
DR PharmGKB; PA34796; -.
DR VEuPathDB; HostDB:ENSG00000105193; -.
DR eggNOG; KOG1753; Eukaryota.
DR GeneTree; ENSGT00390000013067; -.
DR InParanoid; P62249; -.
DR OMA; WPIEMAR; -.
DR OrthoDB; 22228at2759; -.
DR PhylomeDB; P62249; -.
DR TreeFam; TF300088; -.
DR PathwayCommons; P62249; -.
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; P62249; -.
DR SIGNOR; P62249; -.
DR BioGRID-ORCS; 6217; 819 hits in 1175 CRISPR screens.
DR ChiTaRS; RPS16; human.
DR GeneWiki; RPS16; -.
DR GenomeRNAi; 6217; -.
DR Pharos; P62249; Tbio.
DR PRO; PR:P62249; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P62249; Protein.
DR Bgee; ENSG00000105193; Expressed in adult organism and 215 other cell types or tissues.
DR ExpressionAtlas; P62249; baseline and differential.
DR Genevisible; P62249; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
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:0015935; C:small ribosomal subunit; HDA: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; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR000754; Ribosomal_uS9.
DR InterPro; IPR020574; Ribosomal_uS9_CS.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR21569:SF16; 40S RIBOSOMAL PROTEIN S16; 1.
DR PANTHER; PTHR21569; RIBOSOMAL PROTEIN S9; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699, ECO:0000269|Ref.7"
FT CHAIN 2..146
FT /note="Small ribosomal subunit protein uS9"
FT /id="PRO_0000111479"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 19..30
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:7R4X"
FT TURN 60..65
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 77..99
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:7R4X"
SQ SEQUENCE 146 AA; 16445 MW; 519BCFB91BB68A15 CRC64;
MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK LLEPVLLLGK
ERFAGVDIRV RVKGGGHVAQ IYAIRQSISK ALVAYYQKYV DEASKKEIKD ILIQYDRTLL
VADPRRCESK KFGGPGARAR YQKSYR
//
