RS18A_YEAST
ID RS18A_YEAST Reviewed; 146 AA.
AC P0CX55; D6VT75; P35271;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=40S ribosomal protein S18-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein uS13-A {ECO:0000303|PubMed:24524803};
GN Name=RPS18A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YDR450W;
GN ORFNames=D9461.35;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 2-36; 58-68 AND 81-88, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [4]
RP NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [5]
RP CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
RX PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
RA Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
RT "The action of N-terminal acetyltransferases on yeast ribosomal proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-49; LYS-80 AND LYS-96,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
RP METHYLATION AT LYS-48 BY RKM1.
RX PubMed=22522802; DOI=10.1002/pmic.201100570;
RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT "Methylation of translation-associated proteins in Saccharomyces
RT cerevisiae: Identification of methylated lysines and their
RT methyltransferases.";
RL Proteomics 12:960-972(2012).
RN [11]
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 [12]
RP 3D-STRUCTURE MODELING OF 15-145, AND ELECTRON MICROSCOPY.
RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA Frank J.;
RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT ribosome and subunit-subunit interactions.";
RL Cell 107:373-386(2001).
RN [13]
RP 3D-STRUCTURE MODELING OF 15-146, AND ELECTRON MICROSCOPY.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260, ECO:0000269|Ref.3}.
CC -!- MISCELLANEOUS: Present with 48100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS13 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC {ECO:0000305}.
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DR EMBL; U33007; AAB64891.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12285.1; -; Genomic_DNA.
DR PIR; S50886; S50886.
DR RefSeq; NP_010738.1; NM_001180758.1.
DR RefSeq; NP_013686.1; NM_001182384.1.
DR PDB; 3J6X; EM; 6.10 A; 18=1-146.
DR PDB; 3J6Y; EM; 6.10 A; 18=1-146.
DR PDB; 3J77; EM; 6.20 A; 18=1-146.
DR PDB; 3J78; EM; 6.30 A; 18=1-146.
DR PDB; 4U3M; X-ray; 3.00 A; C8/c8=2-146.
DR PDB; 4U3N; X-ray; 3.20 A; C8/c8=2-146.
DR PDB; 4U3U; X-ray; 2.90 A; C8/c8=2-146.
DR PDB; 4U4N; X-ray; 3.10 A; C8/c8=2-146.
DR PDB; 4U4O; X-ray; 3.60 A; C8/c8=2-146.
DR PDB; 4U4Q; X-ray; 3.00 A; C8/c8=2-146.
DR PDB; 4U4R; X-ray; 2.80 A; C8/c8=2-146.
DR PDB; 4U4U; X-ray; 3.00 A; C8/c8=2-146.
DR PDB; 4U4Y; X-ray; 3.20 A; C8/c8=2-146.
DR PDB; 4U4Z; X-ray; 3.10 A; C8/c8=2-146.
DR PDB; 4U50; X-ray; 3.20 A; C8/c8=2-146.
DR PDB; 4U51; X-ray; 3.20 A; C8/c8=2-146.
DR PDB; 4U52; X-ray; 3.00 A; C8/c8=2-146.
DR PDB; 4U53; X-ray; 3.30 A; C8/c8=2-146.
DR PDB; 4U55; X-ray; 3.20 A; C8/c8=2-146.
DR PDB; 4U56; X-ray; 3.45 A; C8/c8=2-146.
DR PDB; 4U6F; X-ray; 3.10 A; C8/c8=2-146.
DR PDB; 4V4B; EM; 11.70 A; AM=15-146.
DR PDB; 4V6I; EM; 8.80 A; AM=1-146.
DR PDB; 4V7R; X-ray; 4.00 A; AL/CL=1-146.
DR PDB; 4V88; X-ray; 3.00 A; AS/CS=1-146.
DR PDB; 4V8Y; EM; 4.30 A; AS=1-146.
DR PDB; 4V8Z; EM; 6.60 A; AS=1-146.
DR PDB; 4V92; EM; 3.70 A; S=2-141.
DR PDB; 5DAT; X-ray; 3.15 A; C8/c8=2-146.
DR PDB; 5DC3; X-ray; 3.25 A; C8/c8=2-146.
DR PDB; 5DGE; X-ray; 3.45 A; C8/c8=2-146.
DR PDB; 5DGF; X-ray; 3.30 A; C8/c8=2-146.
DR PDB; 5DGV; X-ray; 3.10 A; C8/c8=2-146.
DR PDB; 5FCI; X-ray; 3.40 A; C8/c8=2-146.
DR PDB; 5FCJ; X-ray; 3.10 A; C8/c8=2-146.
DR PDB; 5I4L; X-ray; 3.10 A; C8/c8=2-146.
DR PDB; 5JUO; EM; 4.00 A; PB=1-146.
DR PDB; 5JUP; EM; 3.50 A; PB=1-146.
DR PDB; 5JUS; EM; 4.20 A; PB=1-146.
DR PDB; 5JUT; EM; 4.00 A; PB=1-146.
DR PDB; 5JUU; EM; 4.00 A; PB=1-146.
DR PDB; 5LYB; X-ray; 3.25 A; C8/c8=2-146.
DR PDB; 5M1J; EM; 3.30 A; S2=2-146.
DR PDB; 5MC6; EM; 3.80 A; H=1-146.
DR PDB; 5MEI; X-ray; 3.50 A; T/c8=2-146.
DR PDB; 5NDG; X-ray; 3.70 A; C8/c8=2-146.
DR PDB; 5NDV; X-ray; 3.30 A; C8/c8=2-146.
DR PDB; 5NDW; X-ray; 3.70 A; C8/c8=2-146.
DR PDB; 5OBM; X-ray; 3.40 A; C8/c8=2-146.
DR PDB; 5ON6; X-ray; 3.10 A; T/c8=2-146.
DR PDB; 5TBW; X-ray; 3.00 A; T/c8=2-146.
DR PDB; 5TGA; X-ray; 3.30 A; C8/c8=2-146.
DR PDB; 5TGM; X-ray; 3.50 A; C8/c8=2-146.
DR PDB; 5WLC; EM; 3.80 A; L3=1-146.
DR PDB; 6EML; EM; 3.60 A; H=1-146.
DR PDB; 6FAI; EM; 3.40 A; S=1-146.
DR PDB; 6GQ1; EM; 4.40 A; AI=2-146.
DR PDB; 6GQB; EM; 3.90 A; AI=2-146.
DR PDB; 6GQV; EM; 4.00 A; AI=2-146.
DR PDB; 6HHQ; X-ray; 3.10 A; T/c8=1-146.
DR PDB; 6I7O; EM; 5.30 A; H/Hb=2-146.
DR PDB; 6KE6; EM; 3.40 A; ST=1-146.
DR PDB; 6LQP; EM; 3.20 A; ST=1-146.
DR PDB; 6LQU; EM; 3.70 A; ST=1-146.
DR PDB; 6Q8Y; EM; 3.10 A; H=2-140.
DR PDB; 6RBD; EM; 3.47 A; S=1-146.
DR PDB; 6RBE; EM; 3.80 A; S=1-146.
DR PDB; 6S47; EM; 3.28 A; BT=2-146.
DR PDB; 6SNT; EM; 2.80 A; S=1-146.
DR PDB; 6SV4; EM; 3.30 A; H/Hb/Hc=1-146.
DR PDB; 6T4Q; EM; 2.60 A; SS=2-146.
DR PDB; 6T7I; EM; 3.20 A; SS=1-146.
DR PDB; 6T7T; EM; 3.10 A; SS=1-146.
DR PDB; 6T83; EM; 4.00 A; Sb/t=1-146.
DR PDB; 6TB3; EM; 2.80 A; H=2-146.
DR PDB; 6TNU; EM; 3.10 A; H=2-146.
DR PDB; 6WDR; EM; 3.70 A; S=2-136.
DR PDB; 6WOO; EM; 2.90 A; SS=9-144.
DR PDB; 6XIQ; EM; 4.20 A; AI=1-146.
DR PDB; 6XIR; EM; 3.20 A; AI=1-146.
DR PDB; 6Y7C; EM; 3.80 A; S=1-146.
DR PDB; 6Z6J; EM; 3.40 A; SS=1-146.
DR PDB; 6Z6K; EM; 3.40 A; SS=1-146.
DR PDB; 6ZCE; EM; 5.30 A; T=1-146.
DR PDB; 6ZQA; EM; 4.40 A; DS=1-146.
DR PDB; 6ZQB; EM; 3.90 A; DS=1-122.
DR PDB; 6ZQC; EM; 3.80 A; DS=1-146.
DR PDB; 6ZQD; EM; 3.80 A; DS=1-146.
DR PDB; 6ZQE; EM; 7.10 A; DS=1-146.
DR PDB; 6ZQF; EM; 4.90 A; DS=1-146.
DR PDB; 6ZQG; EM; 3.50 A; DS=1-122.
DR PDB; 6ZU9; EM; 6.20 A; J=1-146.
DR PDB; 6ZVI; EM; 3.00 A; A=2-146.
DR PDB; 7A1G; EM; 3.00 A; I=2-146.
DR PDB; 7AJT; EM; 4.60 A; DS=1-146.
DR PDB; 7AJU; EM; 3.80 A; DS=1-146.
DR PDB; 7B7D; EM; 3.30 A; H=2-146.
DR PDB; 7D4I; EM; 4.00 A; ST=1-146.
DR PDB; 7D5S; EM; 4.60 A; ST=1-146.
DR PDB; 7D63; EM; 12.30 A; ST=1-146.
DR PDB; 7NRC; EM; 3.90 A; SH=2-146.
DR PDB; 7NRD; EM; 4.36 A; SH=2-146.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V4B; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0CX55; -.
DR SMR; P0CX55; -.
DR BioGRID; 32505; 660.
DR BioGRID; 35143; 217.
DR IntAct; P0CX55; 7.
DR MINT; P0CX55; -.
DR STRING; 4932.YDR450W; -.
DR CarbonylDB; P0CX55; -.
DR iPTMnet; P0CX55; -.
DR MaxQB; P0CX55; -.
DR PaxDb; P0CX55; -.
DR PRIDE; P0CX55; -.
DR TopDownProteomics; P0CX55; -.
DR EnsemblFungi; YDR450W_mRNA; YDR450W; YDR450W.
DR EnsemblFungi; YML026C_mRNA; YML026C; YML026C.
DR GeneID; 852061; -.
DR GeneID; 854982; -.
DR KEGG; sce:YDR450W; -.
DR KEGG; sce:YML026C; -.
DR SGD; S000002858; RPS18A.
DR VEuPathDB; FungiDB:YDR450W; -.
DR VEuPathDB; FungiDB:YML026C; -.
DR eggNOG; KOG3311; Eukaryota.
DR HOGENOM; CLU_103849_0_1_1; -.
DR InParanoid; P0CX55; -.
DR OMA; IRAYRGI; -.
DR BioCyc; YEAST:G3O-29981-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P0CX55; -.
DR PRO; PR:P0CX55; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P0CX55; protein.
DR ExpressionAtlas; P0CX55; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; NAS:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IGI:SGD.
DR Gene3D; 4.10.910.10; -; 1.
DR HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR InterPro; IPR001892; Ribosomal_S13.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR018269; Ribosomal_S13_CS.
DR Pfam; PF00416; Ribosomal_S13; 1.
DR PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260, ECO:0000269|Ref.3,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..146
FT /note="40S ribosomal protein S18-A"
FT /id="PRO_0000132227"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260, ECO:0000269|Ref.3,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 48
FT /note="N6-methyllysine; by RKM1"
FT /evidence="ECO:0000269|PubMed:22522802"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 116..120
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 146 AA; 17038 MW; 1F50BF9ADD20CA19 CRC64;
MSLVVQEQGS FQHILRLLNT NVDGNIKIVY ALTTIKGVGR RYSNLVCKKA DVDLHKRAGE
LTQEELERIV QIMQNPTHYK IPAWFLNRQN DITDGKDYHT LANNVESKLR DDLERLKKIR
AHRGIRHFWG LRVRGQHTKT TGRRRA
