RS5_HUMAN
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 03-AUG-2022, entry version 211.
DE RecName: Full=40S ribosomal protein S5;
DE AltName: Full=Small ribosomal subunit protein uS7 {ECO:0000303|PubMed:24524803};
DE Contains:
DE RecName: Full=40S ribosomal protein S5, N-terminally processed;
GN Name=RPS5;
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).
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 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 -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000305}.
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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 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; P46782; -.
DR SMR; P46782; -.
DR BioGRID; 112107; 322.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P46782; -.
DR IntAct; P46782; 76.
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 SWISS-2DPAGE; P46782; -.
DR EPD; P46782; -.
DR jPOST; P46782; -.
DR MassIVE; P46782; -.
DR MaxQB; P46782; -.
DR PaxDb; P46782; -.
DR PeptideAtlas; P46782; -.
DR PRIDE; P46782; -.
DR ProteomicsDB; 55764; -.
DR TopDownProteomics; P46782; -.
DR Antibodypedia; 33338; 262 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 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; KMNIVER; -.
DR OrthoDB; 1532160at2759; -.
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-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; 825 hits in 1065 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 adult organism and 212 other tissues.
DR ExpressionAtlas; P46782; baseline and differential.
DR Genevisible; P46782; 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:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
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; IC:FlyBase.
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: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; -; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005716; Ribosomal_S5/S7_euk/arc.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01028; uS7_euk_arch; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..204
FT /note="40S ribosomal protein S5"
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="40S ribosomal protein S5, N-terminally 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:6ZLW"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 86..103
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 143..161
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:7K5I"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 197..203
FT /evidence="ECO:0007829|PDB:6ZLW"
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
