ID RS11_HUMAN Reviewed; 158 AA.
AC P62280; B2R4F5; P04643; Q498Y6; Q6IRY0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 196.
DE RecName: Full=Small ribosomal subunit protein uS17 {ECO:0000303|PubMed:24524803};
DE AltName: Full=40S ribosomal protein S11;
GN Name=RPS11 {ECO:0000312|HGNC:HGNC:10384};
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=3267208; DOI=10.1093/nar/16.3.1205;
RA Lott J.B., Mackie G.A.;
RT "Sequence of a cloned cDNA encoding human ribosomal protein S11.";
RL Nucleic Acids Res. 16:1205-1205(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10580157; DOI=10.1016/s0378-1119(99)00429-1;
RA Higa S., Yoshihama M., Tanaka T., Kenmochi N.;
RT "Gene organization and sequence of the region containing the ribosomal
RT protein genes RPL13A and RPS11 in the human genome and conserved features
RT in the mouse genome.";
RL Gene 240:371-377(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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=B-cell, Eye, Lung, and Prostate;
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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 39-45 AND 137-143.
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-158.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38 AND LYS-45, AND IDENTIFICATION
RP BY MASS 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 [11]
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 [12]
RP MUTAGENESIS OF CYS-60, AND PALMITOYLATION AT CYS-60.
RX PubMed=21044946; DOI=10.1194/jlr.d011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND SER-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 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 [18]
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 [19]
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 [20] {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. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. Part of the small subunit (SSU) processome, first
CC precursor of the small eukaryotic ribosomal subunit. During the
CC assembly of the SSU processome in the nucleolus, many ribosome
CC biogenesis factors, an RNA chaperone and ribosomal proteins associate
CC with the nascent pre-rRNA and work in concert to generate RNA folding,
CC modifications, rearrangements and cleavage as well as targeted
CC degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797).
CC {ECO:0000269|PubMed:23636399, 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 P62280; Q5S007: LRRK2; NbExp=5; IntAct=EBI-1047710, EBI-5323863;
CC P62280; Q99558: MAP3K14; NbExp=3; IntAct=EBI-1047710, EBI-358011;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:34516797}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P62281}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC {ECO:0000305}.
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DR EMBL; X06617; CAA29834.1; -; mRNA.
DR EMBL; AB028893; BAA88215.1; -; Genomic_DNA.
DR EMBL; AK311809; BAG34752.1; -; mRNA.
DR EMBL; CH471177; EAW52497.1; -; Genomic_DNA.
DR EMBL; BC007283; AAH07283.1; -; mRNA.
DR EMBL; BC007603; AAH07603.1; -; mRNA.
DR EMBL; BC007945; AAH07945.1; -; mRNA.
DR EMBL; BC010028; AAH10028.1; -; mRNA.
DR EMBL; BC016378; AAH16378.1; -; mRNA.
DR EMBL; BC070224; AAH70224.1; -; mRNA.
DR EMBL; BC100025; AAI00026.1; -; mRNA.
DR EMBL; AB007152; BAA25818.1; -; Genomic_DNA.
DR CCDS; CCDS12769.1; -.
DR PIR; S02133; R3HU11.
DR RefSeq; NP_001006.1; NM_001015.4.
DR PDB; 4UG0; EM; -; SL=1-158.
DR PDB; 4V6X; EM; 5.00 A; AL=1-158.
DR PDB; 5A2Q; EM; 3.90 A; L=1-158.
DR PDB; 5AJ0; EM; 3.50 A; BL=1-158.
DR PDB; 5FLX; EM; 3.90 A; L=1-158.
DR PDB; 5LKS; EM; 3.60 A; SL=1-158.
DR PDB; 5OA3; EM; 4.30 A; L=1-158.
DR PDB; 5T2C; EM; 3.60 A; Aw=1-158.
DR PDB; 5VYC; X-ray; 6.00 A; L1/L2/L3/L4/L5/L6=1-158.
DR PDB; 6FEC; EM; 6.30 A; G=1-158.
DR PDB; 6G18; EM; 3.60 A; L=1-158.
DR PDB; 6G4S; EM; 4.00 A; L=1-158.
DR PDB; 6G4W; EM; 4.50 A; L=1-158.
DR PDB; 6G51; EM; 4.10 A; L=1-158.
DR PDB; 6G53; EM; 4.50 A; L=1-158.
DR PDB; 6G5H; EM; 3.60 A; L=1-158.
DR PDB; 6G5I; EM; 3.50 A; L=1-158.
DR PDB; 6IP5; EM; 3.90 A; 2v=1-158.
DR PDB; 6IP6; EM; 4.50 A; 2v=1-158.
DR PDB; 6IP8; EM; 3.90 A; 2v=1-158.
DR PDB; 6OLE; EM; 3.10 A; SL=2-154.
DR PDB; 6OLF; EM; 3.90 A; SL=2-154.
DR PDB; 6OLG; EM; 3.40 A; BL=6-158.
DR PDB; 6OLI; EM; 3.50 A; SL=2-154.
DR PDB; 6OLZ; EM; 3.90 A; BL=6-158.
DR PDB; 6OM0; EM; 3.10 A; SL=2-154.
DR PDB; 6OM7; EM; 3.70 A; SL=2-154.
DR PDB; 6QZP; EM; 2.90 A; SL=2-154.
DR PDB; 6XA1; EM; 2.80 A; SL=2-151.
DR PDB; 6Y0G; EM; 3.20 A; SL=1-158.
DR PDB; 6Y2L; EM; 3.00 A; SL=1-158.
DR PDB; 6Y57; EM; 3.50 A; SL=1-158.
DR PDB; 6YBW; EM; 3.10 A; B=1-157.
DR PDB; 6Z6L; EM; 3.00 A; SL=1-158.
DR PDB; 6Z6M; EM; 3.10 A; SL=1-158.
DR PDB; 6Z6N; EM; 2.90 A; SL=1-158.
DR PDB; 6ZLW; EM; 2.60 A; L=1-158.
DR PDB; 6ZM7; EM; 2.70 A; SL=1-158.
DR PDB; 6ZME; EM; 3.00 A; SL=1-158.
DR PDB; 6ZMI; EM; 2.60 A; SL=1-158.
DR PDB; 6ZMO; EM; 3.10 A; SL=1-158.
DR PDB; 6ZMT; EM; 3.00 A; L=1-158.
DR PDB; 6ZMW; EM; 3.70 A; B=1-158.
DR PDB; 6ZN5; EM; 3.20 A; L=2-152.
DR PDB; 6ZOJ; EM; 2.80 A; L=1-158.
DR PDB; 6ZOK; EM; 2.80 A; L=1-158.
DR PDB; 6ZON; EM; 3.00 A; n=1-158.
DR PDB; 6ZP4; EM; 2.90 A; n=1-158.
DR PDB; 6ZUO; EM; 3.10 A; L=1-158.
DR PDB; 6ZV6; EM; 2.90 A; L=1-158.
DR PDB; 6ZVH; EM; 2.90 A; L=2-154.
DR PDB; 6ZVJ; EM; 3.80 A; n=4-147.
DR PDB; 6ZXD; EM; 3.20 A; L=1-158.
DR PDB; 6ZXE; EM; 3.00 A; L=1-158.
DR PDB; 6ZXF; EM; 3.70 A; L=1-158.
DR PDB; 6ZXG; EM; 2.60 A; L=1-158.
DR PDB; 6ZXH; EM; 2.70 A; L=1-158.
DR PDB; 7A09; EM; 3.50 A; n=1-158.
DR PDB; 7K5I; EM; 2.90 A; L=1-158.
DR PDB; 7MQ8; EM; 3.60 A; LD=1-158.
DR PDB; 7MQ9; EM; 3.87 A; LD=1-158.
DR PDB; 7MQA; EM; 2.70 A; LD=1-158.
DR PDB; 7QP6; EM; 4.70 A; B=1-158.
DR PDB; 7QP7; EM; 3.70 A; B=1-158.
DR PDB; 7R4X; EM; 2.15 A; L=1-158.
DR PDB; 7TQL; EM; 3.40 A; L=2-148.
DR PDB; 7WTS; EM; 3.20 A; L=1-158.
DR PDB; 7WTT; EM; 3.10 A; L=1-158.
DR PDB; 7WTU; EM; 3.00 A; L=1-158.
DR PDB; 7WTV; EM; 3.50 A; L=1-158.
DR PDB; 7WTW; EM; 3.20 A; L=1-158.
DR PDB; 7WTX; EM; 3.10 A; L=1-158.
DR PDB; 7WTZ; EM; 3.00 A; L=1-158.
DR PDB; 7WU0; EM; 3.30 A; L=1-158.
DR PDB; 7XNX; EM; 2.70 A; SL=1-158.
DR PDB; 7XNY; EM; 2.50 A; SL=1-158.
DR PDB; 8G5Y; EM; 2.29 A; SL=1-158.
DR PDB; 8G60; EM; 2.54 A; SL=1-158.
DR PDB; 8G61; EM; 2.94 A; SL=1-158.
DR PDB; 8G6J; EM; 2.80 A; SL=1-158.
DR PDB; 8GLP; EM; 1.67 A; SL=1-158.
DR PDB; 8JDJ; EM; 2.50 A; 8=1-158.
DR PDB; 8JDK; EM; 2.26 A; 8=1-158.
DR PDB; 8JDL; EM; 2.42 A; 8=1-158.
DR PDB; 8JDM; EM; 2.67 A; 8=1-158.
DR PDB; 8PPK; EM; 2.98 A; L=1-158.
DR PDB; 8PPL; EM; 2.65 A; AL=1-158.
DR PDB; 8T4S; EM; 2.60 A; L=1-158.
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 PDBsum; 7QP6; -.
DR PDBsum; 7QP7; -.
DR PDBsum; 7R4X; -.
DR PDBsum; 7TQL; -.
DR PDBsum; 7WTS; -.
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; P62280; -.
DR EMDB; EMD-10668; -.
DR EMDB; EMD-10674; -.
DR EMDB; EMD-10690; -.
DR EMDB; EMD-10775; -.
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-11321; -.
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-32799; -.
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; P62280; -.
DR BioGRID; 112119; 480.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62280; -.
DR IntAct; P62280; 116.
DR MINT; P62280; -.
DR STRING; 9606.ENSP00000270625; -.
DR GlyGen; P62280; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P62280; -.
DR PhosphoSitePlus; P62280; -.
DR SwissPalm; P62280; -.
DR BioMuta; RPS11; -.
DR DMDM; 50403609; -.
DR SWISS-2DPAGE; P62280; -.
DR EPD; P62280; -.
DR jPOST; P62280; -.
DR MassIVE; P62280; -.
DR MaxQB; P62280; -.
DR PaxDb; 9606-ENSP00000270625; -.
DR PeptideAtlas; P62280; -.
DR ProteomicsDB; 57385; -.
DR Pumba; P62280; -.
DR TopDownProteomics; P62280; -.
DR Antibodypedia; 32033; 226 antibodies from 26 providers.
DR DNASU; 6205; -.
DR Ensembl; ENST00000270625.7; ENSP00000270625.1; ENSG00000142534.7.
DR GeneID; 6205; -.
DR KEGG; hsa:6205; -.
DR MANE-Select; ENST00000270625.7; ENSP00000270625.1; NM_001015.5; NP_001006.1.
DR UCSC; uc002pob.3; human.
DR AGR; HGNC:10384; -.
DR CTD; 6205; -.
DR DisGeNET; 6205; -.
DR GeneCards; RPS11; -.
DR HGNC; HGNC:10384; RPS11.
DR HPA; ENSG00000142534; Low tissue specificity.
DR MIM; 180471; gene.
DR neXtProt; NX_P62280; -.
DR OpenTargets; ENSG00000142534; -.
DR PharmGKB; PA34782; -.
DR VEuPathDB; HostDB:ENSG00000142534; -.
DR eggNOG; KOG1728; Eukaryota.
DR GeneTree; ENSGT00390000002732; -.
DR HOGENOM; CLU_073626_0_2_1; -.
DR InParanoid; P62280; -.
DR OMA; DYEKCPF; -.
DR OrthoDB; 982046at2759; -.
DR PhylomeDB; P62280; -.
DR TreeFam; TF300126; -.
DR PathwayCommons; P62280; -.
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; P62280; -.
DR SIGNOR; P62280; -.
DR BioGRID-ORCS; 6205; 870 hits in 1142 CRISPR screens.
DR ChiTaRS; RPS11; human.
DR GeneWiki; RPS11; -.
DR GenomeRNAi; 6205; -.
DR Pharos; P62280; Tbio.
DR PRO; PR:P62280; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P62280; Protein.
DR Bgee; ENSG00000142534; Expressed in upper leg skin and 218 other cell types or tissues.
DR ExpressionAtlas; P62280; baseline and differential.
DR Genevisible; P62280; HS.
DR GO; GO:0005737; C:cytoplasm; HDA: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; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005840; C:ribosome; NAS: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; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 2.40.50.1000; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000266; Ribosomal_uS17.
DR InterPro; IPR028333; Ribosomal_uS17_arc/euk.
DR InterPro; IPR019979; Ribosomal_uS17_CS.
DR InterPro; IPR032440; Ribosomal_uS17_N.
DR NCBIfam; TIGR03630; uS17_arch; 1.
DR PANTHER; PTHR10744:SF9; 40S RIBOSOMAL PROTEIN S11; 1.
DR PANTHER; PTHR10744; 40S RIBOSOMAL PROTEIN S11 FAMILY MEMBER; 1.
DR Pfam; PF00366; Ribosomal_S17; 1.
DR Pfam; PF16205; Ribosomal_S17_N; 1.
DR PRINTS; PR00973; RIBOSOMALS17.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00056; RIBOSOMAL_S17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Cytoplasm;
KW Direct protein sequencing; Lipoprotein; Methylation; Nucleus; Palmitate;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..158
FT /note="Small ribosomal subunit protein uS17"
FT /id="PRO_0000128509"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 22
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P62281"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62281"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 69
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P62281"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 60
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:21044946"
FT MUTAGEN 60
FT /note="C->S: Abolishes S-acylation."
FT /evidence="ECO:0000269|PubMed:21044946"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:7WTZ"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:7R4X"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:7WTW"
FT STRAND 85..96
FT /evidence="ECO:0007829|PDB:7R4X"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 101..112
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:7R4X"
SQ SEQUENCE 158 AA; 18431 MW; 9FB75DC1D99614B0 CRC64;
MADIQTERAY QKQPTIFQNK KRVLLGETGK EKLPRYYKNI GLGFKTPKEA IEGTYIDKKC
PFTGNVSIRG RILSGVVTKM KMQRTIVIRR DYLHYIRKYN RFEKRHKNMS VHLSPCFRDV
QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG TKKQFQKF
//
