RS11A_YEAST
ID RS11A_YEAST Reviewed; 156 AA.
AC P0CX47; D6VQ48; O11852; P26781;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=40S ribosomal protein S11-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP41;
DE AltName: Full=S18;
DE AltName: Full=Small ribosomal subunit protein uS17-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS12;
GN Name=RPS11A {ECO:0000303|PubMed:9559554}; Synonyms=RPS18A;
GN OrderedLocusNames=YDR025W; ORFNames=YD9813.03;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8070651; DOI=10.1093/genetics/137.2.369;
RA Folley L.S., Fox T.D.;
RT "Reduced dosage of genes encoding ribosomal protein S18 suppresses a
RT mitochondrial initiation codon mutation in Saccharomyces cerevisiae.";
RL Genetics 137:369-379(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896275;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA Eide L.G., Sander C., Prydz H.;
RT "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL Yeast 12:1085-1090(1996).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-21, AND ACETYLATION AT SER-2 BY NATA.
RX PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 267:5442-5445(1992).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-46; LYS-56; LYS-57;
RP LYS-79; LYS-96; LYS-105; LYS-133; LYS-141 AND LYS-148, AND IDENTIFICATION
RP 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 [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 69-144, 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 69-144, 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, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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|PubMed:1544921}.
CC -!- MISCELLANEOUS: There are 2 genes for uS17 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC {ECO:0000305}.
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DR EMBL; L15408; AAC37411.1; -; Unassigned_DNA.
DR EMBL; X95966; CAA65218.1; -; Genomic_DNA.
DR EMBL; Z47814; CAA87804.1; -; Genomic_DNA.
DR EMBL; Z74321; CAA98846.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11870.1; -; Genomic_DNA.
DR PIR; S41784; S41784.
DR RefSeq; NP_009604.1; NM_001178396.1.
DR RefSeq; NP_010308.3; NM_001180333.3.
DR PDB; 3J6X; EM; 6.10 A; 11=1-156.
DR PDB; 3J6Y; EM; 6.10 A; 11=1-156.
DR PDB; 3J77; EM; 6.20 A; 11=1-156.
DR PDB; 3J78; EM; 6.30 A; 11=1-156.
DR PDB; 4U3M; X-ray; 3.00 A; C1/c1=2-156.
DR PDB; 4U3N; X-ray; 3.20 A; C1/c1=2-156.
DR PDB; 4U3U; X-ray; 2.90 A; C1/c1=2-156.
DR PDB; 4U4N; X-ray; 3.10 A; C1/c1=2-156.
DR PDB; 4U4O; X-ray; 3.60 A; C1/c1=2-156.
DR PDB; 4U4Q; X-ray; 3.00 A; C1/c1=2-156.
DR PDB; 4U4R; X-ray; 2.80 A; C1/c1=2-156.
DR PDB; 4U4U; X-ray; 3.00 A; C1/c1=2-156.
DR PDB; 4U4Y; X-ray; 3.20 A; C1/c1=2-156.
DR PDB; 4U4Z; X-ray; 3.10 A; C1/c1=2-156.
DR PDB; 4U50; X-ray; 3.20 A; C1/c1=2-156.
DR PDB; 4U51; X-ray; 3.20 A; C1/c1=2-156.
DR PDB; 4U52; X-ray; 3.00 A; C1/c1=2-156.
DR PDB; 4U53; X-ray; 3.30 A; C1/c1=2-156.
DR PDB; 4U55; X-ray; 3.20 A; C1/c1=2-156.
DR PDB; 4U56; X-ray; 3.45 A; C1/c1=2-156.
DR PDB; 4U6F; X-ray; 3.10 A; C1/c1=2-156.
DR PDB; 4V4B; EM; 11.70 A; AQ=69-144.
DR PDB; 4V6I; EM; 8.80 A; AP=1-156.
DR PDB; 4V7R; X-ray; 4.00 A; AF/CF=1-156.
DR PDB; 4V88; X-ray; 3.00 A; AL/CL=1-156.
DR PDB; 4V8Y; EM; 4.30 A; AL=1-156.
DR PDB; 4V8Z; EM; 6.60 A; AL=1-156.
DR PDB; 4V92; EM; 3.70 A; L=4-145.
DR PDB; 5DAT; X-ray; 3.15 A; C1/c1=2-156.
DR PDB; 5DC3; X-ray; 3.25 A; C1/c1=2-156.
DR PDB; 5DGE; X-ray; 3.45 A; C1/c1=2-156.
DR PDB; 5DGV; X-ray; 3.10 A; C1/c1=2-156.
DR PDB; 5FCI; X-ray; 3.40 A; C1/c1=2-147.
DR PDB; 5FCJ; X-ray; 3.10 A; C1/c1=2-146.
DR PDB; 5I4L; X-ray; 3.10 A; C1/c1=1-156.
DR PDB; 5JUO; EM; 4.00 A; IB=1-156.
DR PDB; 5JUP; EM; 3.50 A; IB=1-156.
DR PDB; 5JUS; EM; 4.20 A; IB=1-156.
DR PDB; 5JUT; EM; 4.00 A; IB=1-156.
DR PDB; 5JUU; EM; 4.00 A; IB=1-156.
DR PDB; 5LL6; EM; 3.90 A; X=1-156.
DR PDB; 5LYB; X-ray; 3.25 A; C1/c1=2-146.
DR PDB; 5M1J; EM; 3.30 A; L2=2-156.
DR PDB; 5MC6; EM; 3.80 A; X=1-156.
DR PDB; 5MEI; X-ray; 3.50 A; M/c1=2-156.
DR PDB; 5NDG; X-ray; 3.70 A; C1/c1=1-156.
DR PDB; 5NDV; X-ray; 3.30 A; C1/c1=2-147.
DR PDB; 5NDW; X-ray; 3.70 A; C1/c1=1-156.
DR PDB; 5OBM; X-ray; 3.40 A; C1/c1=1-156.
DR PDB; 5ON6; X-ray; 3.10 A; M/c1=2-156.
DR PDB; 5TBW; X-ray; 3.00 A; M/c1=2-156.
DR PDB; 5TGA; X-ray; 3.30 A; C1/c1=2-156.
DR PDB; 5TGM; X-ray; 3.50 A; C1/c1=2-146.
DR PDB; 5TZS; EM; 5.10 A; D=1-156.
DR PDB; 5WLC; EM; 3.80 A; LD=1-156.
DR PDB; 5WYJ; EM; 8.70 A; SM=1-156.
DR PDB; 5WYK; EM; 4.50 A; SM=1-156.
DR PDB; 6EML; EM; 3.60 A; X=1-156.
DR PDB; 6FAI; EM; 3.40 A; L=1-156.
DR PDB; 6GQ1; EM; 4.40 A; AB=2-154.
DR PDB; 6GQB; EM; 3.90 A; AB=2-154.
DR PDB; 6GQV; EM; 4.00 A; AB=2-154.
DR PDB; 6HHQ; X-ray; 3.10 A; M/c1=1-156.
DR PDB; 6I7O; EM; 5.30 A; X/Xb=2-147.
DR PDB; 6KE6; EM; 3.40 A; SM=1-156.
DR PDB; 6LQP; EM; 3.20 A; SM=1-156.
DR PDB; 6LQQ; EM; 4.10 A; SM=1-156.
DR PDB; 6LQR; EM; 8.60 A; SM=1-156.
DR PDB; 6LQS; EM; 3.80 A; SM=1-156.
DR PDB; 6LQT; EM; 4.90 A; SM=1-156.
DR PDB; 6LQU; EM; 3.70 A; SM=1-156.
DR PDB; 6LQV; EM; 4.80 A; SM=1-156.
DR PDB; 6Q8Y; EM; 3.10 A; X=2-156.
DR PDB; 6RBD; EM; 3.47 A; L=1-156.
DR PDB; 6RBE; EM; 3.80 A; L=1-156.
DR PDB; 6S47; EM; 3.28 A; BM=2-156.
DR PDB; 6SNT; EM; 2.80 A; L=1-156.
DR PDB; 6SV4; EM; 3.30 A; X/Xb/Xc=1-156.
DR PDB; 6T4Q; EM; 2.60 A; SL=2-145.
DR PDB; 6T7I; EM; 3.20 A; SL=1-156.
DR PDB; 6T7T; EM; 3.10 A; SL=1-156.
DR PDB; 6T83; EM; 4.00 A; Lb/m=1-156.
DR PDB; 6TB3; EM; 2.80 A; X=4-145.
DR PDB; 6TNU; EM; 3.10 A; X=4-145.
DR PDB; 6WDR; EM; 3.70 A; L=6-145.
DR PDB; 6WOO; EM; 2.90 A; LL=2-145.
DR PDB; 6XIQ; EM; 4.20 A; AB=1-156.
DR PDB; 6XIR; EM; 3.20 A; AB=1-156.
DR PDB; 6Y7C; EM; 3.80 A; L=1-156.
DR PDB; 6Z6J; EM; 3.40 A; SL=1-156.
DR PDB; 6Z6K; EM; 3.40 A; SL=1-156.
DR PDB; 6ZCE; EM; 5.30 A; M=2-156.
DR PDB; 6ZQB; EM; 3.90 A; DL=1-156.
DR PDB; 6ZQC; EM; 3.80 A; DL=1-156.
DR PDB; 6ZQD; EM; 3.80 A; DL=1-156.
DR PDB; 6ZQE; EM; 7.10 A; DL=1-156.
DR PDB; 6ZQF; EM; 4.90 A; DL=1-156.
DR PDB; 6ZQG; EM; 3.50 A; DL=1-156.
DR PDB; 6ZU9; EM; 6.20 A; X=2-156.
DR PDB; 6ZVI; EM; 3.00 A; t=2-147.
DR PDB; 7A1G; EM; 3.00 A; X=4-145.
DR PDB; 7AJT; EM; 4.60 A; DL=1-156.
DR PDB; 7AJU; EM; 3.80 A; DL=1-156.
DR PDB; 7B7D; EM; 3.30 A; X=4-145.
DR PDB; 7D4I; EM; 4.00 A; SM=1-156.
DR PDB; 7D5T; EM; 6.00 A; SM=1-156.
DR PDB; 7D63; EM; 12.30 A; SM=1-155.
DR PDB; 7NRC; EM; 3.90 A; SX=4-145.
DR PDB; 7NRD; EM; 4.36 A; SX=2-147.
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; 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; 5LL6; -.
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; 5TZS; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
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; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
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; 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; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0CX47; -.
DR SMR; P0CX47; -.
DR BioGRID; 32075; 235.
DR BioGRID; 32750; 341.
DR IntAct; P0CX47; 7.
DR MINT; P0CX47; -.
DR STRING; 4932.YBR048W; -.
DR iPTMnet; P0CX47; -.
DR MaxQB; P0CX47; -.
DR PaxDb; P0CX47; -.
DR PRIDE; P0CX47; -.
DR EnsemblFungi; YBR048W_mRNA; YBR048W; YBR048W.
DR EnsemblFungi; YDR025W_mRNA; YDR025W; YDR025W.
DR GeneID; 851589; -.
DR GeneID; 852337; -.
DR KEGG; sce:YBR048W; -.
DR KEGG; sce:YDR025W; -.
DR SGD; S000002432; RPS11A.
DR VEuPathDB; FungiDB:YBR048W; -.
DR VEuPathDB; FungiDB:YDR025W; -.
DR eggNOG; KOG1728; Eukaryota.
DR HOGENOM; CLU_073626_0_2_1; -.
DR InParanoid; P0CX47; -.
DR OMA; KKYERYE; -.
DR BioCyc; YEAST:G3O-29641-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; P0CX47; -.
DR PRO; PR:P0CX47; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P0CX47; protein.
DR ExpressionAtlas; P0CX47; baseline and differential.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
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; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT CHAIN 2..156
FT /note="40S ribosomal protein S11-A"
FT /id="PRO_0000128523"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 79
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 CROSSLNK 105
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 12..13
FT /note="AF -> FA (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 80..94
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 156 AA; 17749 MW; 6F7825FAE17EB084 CRC64;
MSTELTVQSE RAFQKQPHIF NNPKVKTSKR TKRWYKNAGL GFKTPKTAIE GSYIDKKCPF
TGLVSIRGKI LTGTVVSTKM HRTIVIRRAY LHYIPKYNRY EKRHKNVPVH VSPAFRVQVG
DIVTVGQCRP ISKTVRFNVV KVSAAAGKAN KQFAKF
