ID RS5_HUMAN Reviewed; 204 AA. AC P46782; B2R4T2; Q96BN0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 220. DE RecName: Full=Small ribosomal subunit protein uS7 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S5; DE Contains: DE RecName: Full=Small ribosomal subunit protein uS7, N-terminally processed; DE AltName: Full=40S ribosomal protein S5, N-terminally processed; GN Name=RPS5 {ECO:0000312|HGNC:HGNC:10426}; 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 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=Bone, and Ovary; 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 2-18; 23-42; 48-55; 137-145 AND 168-182, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 1-18; 23-42; 137-159 AND 168-182, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-204. 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 [9] RP PROTEIN SEQUENCE OF 192-197. 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 [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, 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 [13] 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-142, 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14, AND IDENTIFICATION BY RP 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-47, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [20] 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 [21] {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 P46782; P54253: ATXN1; NbExp=3; IntAct=EBI-350569, EBI-930964; CC P46782; P42858: HTT; NbExp=3; IntAct=EBI-350569, EBI-466029; CC P46782; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-350569, EBI-1055254; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, CC nucleolus {ECO:0000269|PubMed:34516797}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 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; U14970; AAA85658.1; -; mRNA. DR EMBL; AB061853; BAB79493.1; -; Genomic_DNA. DR EMBL; AK311938; BAG34879.1; -; mRNA. DR EMBL; CH471135; EAW72581.1; -; Genomic_DNA. DR EMBL; BC015405; AAH15405.1; -; mRNA. DR EMBL; BC018151; AAH18151.1; -; mRNA. DR EMBL; AB007149; BAA25815.1; -; Genomic_DNA. DR CCDS; CCDS12978.1; -. DR PIR; S55916; S55916. DR RefSeq; NP_001000.2; NM_001009.3. DR PDB; 4UG0; EM; -; SF=1-204. DR PDB; 4V6X; EM; 5.00 A; AF=1-204. DR PDB; 5A2Q; EM; 3.90 A; F=1-204. DR PDB; 5AJ0; EM; 3.50 A; BF=1-204. DR PDB; 5FLX; EM; 3.90 A; F=1-204. DR PDB; 5LKS; EM; 3.60 A; SF=1-204. DR PDB; 5OA3; EM; 4.30 A; F=1-204. DR PDB; 5T2C; EM; 3.60 A; As=1-204. DR PDB; 5VYC; X-ray; 6.00 A; F1/F2/F3/F4/F5/F6=1-204. DR PDB; 6FEC; EM; 6.30 A; U=14-204. DR PDB; 6G18; EM; 3.60 A; F=1-204. DR PDB; 6G4S; EM; 4.00 A; F=1-204. DR PDB; 6G4W; EM; 4.50 A; F=1-204. DR PDB; 6G51; EM; 4.10 A; F=1-204. DR PDB; 6G53; EM; 4.50 A; F=1-204. DR PDB; 6G5H; EM; 3.60 A; F=1-204. DR PDB; 6G5I; EM; 3.50 A; F=1-204. DR PDB; 6IP5; EM; 3.90 A; 2r=1-204. DR PDB; 6IP6; EM; 4.50 A; 2r=1-204. DR PDB; 6IP8; EM; 3.90 A; 2r=1-204. DR PDB; 6OLE; EM; 3.10 A; SF=16-204. DR PDB; 6OLF; EM; 3.90 A; SF=16-204. DR PDB; 6OLG; EM; 3.40 A; BF=15-204. DR PDB; 6OLI; EM; 3.50 A; SF=16-204. DR PDB; 6OLZ; EM; 3.90 A; BF=15-204. DR PDB; 6OM0; EM; 3.10 A; SF=16-204. DR PDB; 6OM7; EM; 3.70 A; SF=16-204. DR PDB; 6QZP; EM; 2.90 A; SF=16-204. DR PDB; 6XA1; EM; 2.80 A; SF=16-204. DR PDB; 6Y0G; EM; 3.20 A; SF=1-204. DR PDB; 6Y2L; EM; 3.00 A; SF=1-204. DR PDB; 6Y57; EM; 3.50 A; SF=1-204. DR PDB; 6YBS; EM; 3.10 A; V=1-204. DR PDB; 6Z6L; EM; 3.00 A; SF=1-204. DR PDB; 6Z6M; EM; 3.10 A; SF=1-204. DR PDB; 6Z6N; EM; 2.90 A; SF=1-204. DR PDB; 6ZLW; EM; 2.60 A; K=1-204. DR PDB; 6ZM7; EM; 2.70 A; SF=1-204. DR PDB; 6ZME; EM; 3.00 A; SF=1-204. DR PDB; 6ZMI; EM; 2.60 A; SF=1-204. DR PDB; 6ZMO; EM; 3.10 A; SF=1-204. DR PDB; 6ZMT; EM; 3.00 A; K=1-204. DR PDB; 6ZMW; EM; 3.70 A; V=1-204. DR PDB; 6ZN5; EM; 3.20 A; K=16-204. DR PDB; 6ZOJ; EM; 2.80 A; F=1-204. DR PDB; 6ZOL; EM; 2.80 A; F=1-204. DR PDB; 6ZON; EM; 3.00 A; e=1-204. DR PDB; 6ZP4; EM; 2.90 A; e=1-204. DR PDB; 6ZUO; EM; 3.10 A; F=1-204. DR PDB; 6ZV6; EM; 2.90 A; F=1-204. DR PDB; 6ZVH; EM; 2.90 A; F=16-204. DR PDB; 6ZVJ; EM; 3.80 A; e=16-204. DR PDB; 6ZXD; EM; 3.20 A; F=1-204. DR PDB; 6ZXE; EM; 3.00 A; F=1-204. DR PDB; 6ZXF; EM; 3.70 A; F=1-204. DR PDB; 6ZXG; EM; 2.60 A; F=1-204. DR PDB; 6ZXH; EM; 2.70 A; F=1-204. DR PDB; 7A09; EM; 3.50 A; e=1-204. DR PDB; 7K5I; EM; 2.90 A; F=1-204. DR PDB; 7MQ8; EM; 3.60 A; L5=1-204. DR PDB; 7MQ9; EM; 3.87 A; L5=1-204. DR PDB; 7MQA; EM; 2.70 A; L5=1-204. DR PDB; 7QP6; EM; 4.70 A; V=1-204. DR PDB; 7QP7; EM; 3.70 A; V=1-204. DR PDB; 7R4X; EM; 2.15 A; F=1-204. DR PDB; 7TQL; EM; 3.40 A; K=16-204. DR PDB; 7WTT; EM; 3.10 A; F=1-204. DR PDB; 7WTU; EM; 3.00 A; F=1-204. DR PDB; 7WTV; EM; 3.50 A; F=1-204. DR PDB; 7WTW; EM; 3.20 A; F=1-204. DR PDB; 7WTX; EM; 3.10 A; F=1-204. DR PDB; 7WTZ; EM; 3.00 A; F=1-204. DR PDB; 7WU0; EM; 3.30 A; F=1-204. DR PDB; 7XNX; EM; 2.70 A; SF=1-204. DR PDB; 7XNY; EM; 2.50 A; SF=1-204. DR PDB; 8G5Y; EM; 2.29 A; SF=1-204. DR PDB; 8G5Z; EM; 2.64 A; SF=16-204. DR PDB; 8G60; EM; 2.54 A; SF=1-204. DR PDB; 8G61; EM; 2.94 A; SF=1-204. DR PDB; 8G6J; EM; 2.80 A; SF=1-204. DR PDB; 8GLP; EM; 1.67 A; SF=1-204. DR PDB; 8JDJ; EM; 2.50 A; 2=1-204. DR PDB; 8JDK; EM; 2.26 A; 2=1-204. DR PDB; 8JDL; EM; 2.42 A; 2=1-204. DR PDB; 8JDM; EM; 2.67 A; 2=1-204. DR PDB; 8PPK; EM; 2.98 A; F=1-204. DR PDB; 8PPL; EM; 2.65 A; AF=1-204. DR PDB; 8T4S; EM; 2.60 A; F=1-204. 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; 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; P46782; -. 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; P46782; -. DR BioGRID; 112107; 392. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P46782; -. DR IntAct; P46782; 78. DR MINT; P46782; -. DR STRING; 9606.ENSP00000472985; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P46782; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P46782; -. DR MetOSite; P46782; -. DR PhosphoSitePlus; P46782; -. DR SwissPalm; P46782; -. DR BioMuta; RPS5; -. DR EPD; P46782; -. DR jPOST; P46782; -. DR MassIVE; P46782; -. DR MaxQB; P46782; -. DR PaxDb; 9606-ENSP00000472985; -. DR PeptideAtlas; P46782; -. DR PRIDE; P46782; -. DR ProteomicsDB; 55764; -. DR Pumba; P46782; -. DR TopDownProteomics; P46782; -. DR Antibodypedia; 33338; 279 antibodies from 28 providers. DR DNASU; 6193; -. DR Ensembl; ENST00000196551.8; ENSP00000196551.3; ENSG00000083845.9. DR Ensembl; ENST00000596046.1; ENSP00000472985.1; ENSG00000083845.9. DR Ensembl; ENST00000601521.5; ENSP00000470114.1; ENSG00000083845.9. DR GeneID; 6193; -. DR KEGG; hsa:6193; -. DR MANE-Select; ENST00000196551.8; ENSP00000196551.3; NM_001009.4; NP_001000.2. DR UCSC; uc002qsn.4; human. DR AGR; HGNC:10426; -. DR CTD; 6193; -. DR DisGeNET; 6193; -. DR GeneCards; RPS5; -. DR HGNC; HGNC:10426; RPS5. DR HPA; ENSG00000083845; Low tissue specificity. DR MIM; 603630; gene. DR neXtProt; NX_P46782; -. DR OpenTargets; ENSG00000083845; -. DR PharmGKB; PA34841; -. DR VEuPathDB; HostDB:ENSG00000083845; -. DR eggNOG; KOG3291; Eukaryota. DR GeneTree; ENSGT00390000010806; -. DR HOGENOM; CLU_063975_0_0_1; -. DR InParanoid; P46782; -. DR OMA; ASTMMMH; -. DR OrthoDB; 5473800at2759; -. DR PhylomeDB; P46782; -. DR TreeFam; TF300872; -. DR PathwayCommons; P46782; -. 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; P46782; -. DR SIGNOR; P46782; -. DR BioGRID-ORCS; 6193; 862 hits in 1149 CRISPR screens. DR ChiTaRS; RPS5; human. DR GeneWiki; RPS5; -. DR GenomeRNAi; 6193; -. DR Pharos; P46782; Tbio. DR PRO; PR:P46782; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P46782; Protein. DR Bgee; ENSG00000083845; Expressed in primordial germ cell in gonad and 214 other cell types or tissues. DR ExpressionAtlas; P46782; baseline and differential. 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:1990904; C:ribonucleoprotein complex; IDA:MGI. DR GO; GO:0005840; C:ribosome; IBA:GO_Central. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB. 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:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0006450; P:regulation of translational fidelity; IGI:UniProtKB. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0006412; P:translation; IGI:UniProtKB. DR GO; GO:0006413; P:translational initiation; IC:UniProtKB. DR CDD; cd14867; uS7_Eukaryote; 1. DR Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1. DR InterPro; IPR000235; Ribosomal_uS7. DR InterPro; IPR020606; Ribosomal_uS7_CS. DR InterPro; IPR023798; Ribosomal_uS7_dom. DR InterPro; IPR036823; Ribosomal_uS7_dom_sf. DR InterPro; IPR005716; Ribosomal_uS7_euk/arc. DR NCBIfam; TIGR01028; uS7_euk_arch; 1. DR PANTHER; PTHR11205:SF18; 40S RIBOSOMAL PROTEIN S5; 1. DR PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1. DR Pfam; PF00177; Ribosomal_S7; 1. DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1. DR SUPFAM; SSF47973; Ribosomal protein S7; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. DR SWISS-2DPAGE; P46782; -. DR Genevisible; P46782; 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; Ubl conjugation. FT CHAIN 1..204 FT /note="Small ribosomal subunit protein uS7" FT /id="PRO_0000370369" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..204 FT /note="Small ribosomal subunit protein uS7, N-terminally FT processed" FT /id="PRO_0000124526" FT MOD_RES 1 FT /note="N-acetylmethionine; in 40S ribosomal protein S5; FT alternate" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712" FT MOD_RES 2 FT /note="N-acetylthreonine; in 40S ribosomal protein S5, N- FT terminally processed" FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:25944712" FT MOD_RES 14 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 47 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 47 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CONFLICT 59..60 FT /note="KR -> NA (in Ref. 1; AAA85658)" FT /evidence="ECO:0000305" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:6ZLW" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 68..75 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 86..104 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 108..119 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 122..126 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:6ZLW" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 143..162 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 169..181 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:7K5I" FT HELIX 188..201 FT /evidence="ECO:0007829|PDB:7R4X" SQ SEQUENCE 204 AA; 22876 MW; DFE2FD5AAFCFD894 CRC64; MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII HLLTGENPLQ VLVNAIINSG PREDSTRIGR AGTVRRQAVD VSPLRRVNQA IWLLCTGARE AAFRNIKTIA ECLADELINA AKGSSNSYAI KKKDELERVA KSNR //