位置:首页 > 蛋白库 > RS11_HUMAN
RS11_HUMAN
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   03-AUG-2022, entry version 187.
DE   RecName: Full=40S ribosomal protein S11;
DE   AltName: Full=Small ribosomal subunit protein uS17 {ECO:0000303|PubMed:24524803};
GN   Name=RPS11;
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).
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       P62280; Q5S007: LRRK2; NbExp=5; IntAct=EBI-1047710, EBI-5323863;
CC       P62280; Q99558: MAP3K14; NbExp=3; IntAct=EBI-1047710, EBI-358011;
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
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   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   AlphaFoldDB; P62280; -.
DR   SMR; P62280; -.
DR   BioGRID; 112119; 325.
DR   ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR   CORUM; P62280; -.
DR   IntAct; P62280; 111.
DR   MINT; P62280; -.
DR   STRING; 9606.ENSP00000270625; -.
DR   GlyGen; P62280; 1 site, 1 O-linked glycan (1 site).
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; P62280; -.
DR   PeptideAtlas; P62280; -.
DR   PRIDE; P62280; -.
DR   ProteomicsDB; 57385; -.
DR   TopDownProteomics; P62280; -.
DR   Antibodypedia; 32033; 205 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   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; KKYERYE; -.
DR   OrthoDB; 1325168at2759; -.
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-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; 829 hits in 1055 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 216 other 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: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; IC:FlyBase.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR032440; Ribosomal_S11_N.
DR   InterPro; IPR000266; Ribosomal_S17/S11.
DR   InterPro; IPR028333; Ribosomal_S17_arc-typ.
DR   InterPro; IPR019979; Ribosomal_S17_CS.
DR   PANTHER; PTHR10744; PTHR10744; 1.
DR   Pfam; PF00366; Ribosomal_S17; 1.
DR   Pfam; PF16205; Ribosomal_S17_N; 1.
DR   PRINTS; PR00973; RIBOSOMALS17.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR03630; uS17_arch; 1.
DR   PROSITE; PS00056; RIBOSOMAL_S17; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Citrullination; Direct protein sequencing;
KW   Lipoprotein; Methylation; Palmitate; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; 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="40S ribosomal protein S11"
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"
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:6ZLW"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:6YBW"
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:6ZLW"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:6ZLW"
FT   STRAND          72..79
FT                   /evidence="ECO:0007829|PDB:6ZLW"
FT   STRAND          82..96
FT                   /evidence="ECO:0007829|PDB:6ZLW"
FT   TURN            97..100
FT                   /evidence="ECO:0007829|PDB:6ZLW"
FT   STRAND          101..112
FT                   /evidence="ECO:0007829|PDB:6ZLW"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:6ZLW"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:6ZLW"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:6ZLW"
SQ   SEQUENCE   158 AA;  18431 MW;  9FB75DC1D99614B0 CRC64;
     MADIQTERAY QKQPTIFQNK KRVLLGETGK EKLPRYYKNI GLGFKTPKEA IEGTYIDKKC
     PFTGNVSIRG RILSGVVTKM KMQRTIVIRR DYLHYIRKYN RFEKRHKNMS VHLSPCFRDV
     QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG TKKQFQKF
 
 
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