RS16_HUMAN
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 03-AUG-2022, entry version 170.
DE RecName: Full=40S ribosomal protein S16;
DE AltName: Full=Small ribosomal subunit protein uS9 {ECO:0000303|PubMed:24524803};
GN Name=RPS16;
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).
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 -!- INTERACTION:
CC P62249; Q5S007: LRRK2; NbExp=4; IntAct=EBI-352480, EBI-5323863;
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 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 AlphaFoldDB; P62249; -.
DR SMR; P62249; -.
DR BioGRID; 112131; 448.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62249; -.
DR DIP; DIP-33200N; -.
DR IntAct; P62249; 87.
DR MINT; P62249; -.
DR STRING; 9606.ENSP00000251453; -.
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; P62249; -.
DR PeptideAtlas; P62249; -.
DR PRIDE; P62249; -.
DR ProteomicsDB; 57374; -.
DR TopDownProteomics; P62249; -.
DR Antibodypedia; 30342; 207 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 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; FMGQAEA; -.
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-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; 783 hits in 1090 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 213 other tissues.
DR ExpressionAtlas; P62249; baseline and differential.
DR Genevisible; P62249; HS.
DR GO; GO:0005737; C:cytoplasm; IC: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:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0015935; C:small ribosomal subunit; HDA:UniProtKB.
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; IC:FlyBase.
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; IMP: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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein;
KW 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="40S ribosomal protein S16"
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..18
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 20..34
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 77..99
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 146 AA; 16445 MW; 519BCFB91BB68A15 CRC64;
MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK LLEPVLLLGK
ERFAGVDIRV RVKGGGHVAQ IYAIRQSISK ALVAYYQKYV DEASKKEIKD ILIQYDRTLL
VADPRRCESK KFGGPGARAR YQKSYR
