RS8A_YEAST
ID RS8A_YEAST Reviewed; 200 AA.
AC P0CX39; A2TBM0; A2TBP0; D3DM09; P05754; P22801;
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 S8-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP19;
DE AltName: Full=S14;
DE AltName: Full=Small ribosomal subunit protein eS8-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS9;
GN Name=RPS8A {ECO:0000303|PubMed:9559554}; Synonyms=RPS14A;
GN OrderedLocusNames=YBL072C; ORFNames=YBL06.05, YBL0613;
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=7992509; DOI=10.1002/yea.320100811;
RA Logghe M., Molemans F., Fiers W., Contreras R.;
RT "The two genes encoding yeast ribosomal protein S8 reside on different
RT chromosomes, and are closely linked to the hsp70 stress protein genes SSA3
RT and SSA4.";
RL Yeast 10:1093-1100(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-102.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [5]
RP PARTIAL PROTEIN SEQUENCE OF 2-51, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=18782943; DOI=10.1007/bf00341461;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence
RT characterization of twenty-four proteins from cytoplasmic ribosomes.";
RL Mol. Gen. Genet. 195:544-546(1984).
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.
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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-69 AND SER-73, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107 AND SER-158, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62; SER-69; SER-73; SER-86;
RP SER-154; SER-155 AND SER-161, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
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 [14]
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 -!- MISCELLANEOUS: Present with 15900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS8 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family.
CC {ECO:0000305}.
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DR EMBL; Z26879; CAA81525.1; -; Genomic_DNA.
DR EMBL; Z35833; CAA84893.1; -; Genomic_DNA.
DR EMBL; EF123123; ABM97467.1; -; mRNA.
DR EMBL; BK006936; DAA07049.1; -; Genomic_DNA.
DR PIR; S45591; S45591.
DR RefSeq; NP_009481.1; NM_001178312.1.
DR RefSeq; NP_011028.1; NM_001178993.1.
DR PDB; 3J6X; EM; 6.10 A; S8=1-200.
DR PDB; 3J6Y; EM; 6.10 A; S8=1-200.
DR PDB; 3J77; EM; 6.20 A; S8=1-200.
DR PDB; 3J78; EM; 6.30 A; S8=1-200.
DR PDB; 4U3M; X-ray; 3.00 A; S8/s8=1-200.
DR PDB; 4U3N; X-ray; 3.20 A; S8/s8=1-200.
DR PDB; 4U3U; X-ray; 2.90 A; S8/s8=1-200.
DR PDB; 4U4N; X-ray; 3.10 A; S8/s8=1-200.
DR PDB; 4U4O; X-ray; 3.60 A; S8/s8=1-200.
DR PDB; 4U4Q; X-ray; 3.00 A; S8/s8=1-200.
DR PDB; 4U4R; X-ray; 2.80 A; S8/s8=1-200.
DR PDB; 4U4U; X-ray; 3.00 A; S8/s8=1-200.
DR PDB; 4U4Y; X-ray; 3.20 A; S8/s8=1-200.
DR PDB; 4U4Z; X-ray; 3.10 A; S8/s8=1-200.
DR PDB; 4U50; X-ray; 3.20 A; S8/s8=1-200.
DR PDB; 4U51; X-ray; 3.20 A; S8/s8=1-200.
DR PDB; 4U52; X-ray; 3.00 A; S8/s8=1-200.
DR PDB; 4U53; X-ray; 3.30 A; S8/s8=1-200.
DR PDB; 4U55; X-ray; 3.20 A; S8/s8=1-200.
DR PDB; 4U56; X-ray; 3.45 A; S8/s8=1-200.
DR PDB; 4U6F; X-ray; 3.10 A; S8/s8=1-200.
DR PDB; 4V88; X-ray; 3.00 A; AI/CI=1-200.
DR PDB; 4V8Y; EM; 4.30 A; AI=1-200.
DR PDB; 4V8Z; EM; 6.60 A; AI=1-200.
DR PDB; 4V92; EM; 3.70 A; I=2-199.
DR PDB; 5DAT; X-ray; 3.15 A; S8/s8=1-200.
DR PDB; 5DC3; X-ray; 3.25 A; S8/s8=1-200.
DR PDB; 5DGE; X-ray; 3.45 A; S8/s8=1-200.
DR PDB; 5DGF; X-ray; 3.30 A; S8/s8=1-200.
DR PDB; 5DGV; X-ray; 3.10 A; S8/s8=1-200.
DR PDB; 5FCI; X-ray; 3.40 A; S8/s8=1-200.
DR PDB; 5FCJ; X-ray; 3.10 A; S8/s8=1-200.
DR PDB; 5I4L; X-ray; 3.10 A; S8/s8=1-200.
DR PDB; 5JUO; EM; 4.00 A; FB=1-200.
DR PDB; 5JUP; EM; 3.50 A; FB=1-200.
DR PDB; 5JUS; EM; 4.20 A; FB=1-200.
DR PDB; 5JUT; EM; 4.00 A; FB=1-200.
DR PDB; 5JUU; EM; 4.00 A; FB=1-200.
DR PDB; 5LL6; EM; 3.90 A; V=1-200.
DR PDB; 5LYB; X-ray; 3.25 A; S8/s8=2-200.
DR PDB; 5M1J; EM; 3.30 A; I2=2-200.
DR PDB; 5MC6; EM; 3.80 A; V=1-200.
DR PDB; 5MEI; X-ray; 3.50 A; J/s8=2-200.
DR PDB; 5NDG; X-ray; 3.70 A; S8/s8=1-200.
DR PDB; 5NDV; X-ray; 3.30 A; S8/s8=1-200.
DR PDB; 5NDW; X-ray; 3.70 A; S8/s8=1-200.
DR PDB; 5OBM; X-ray; 3.40 A; S8/s8=1-200.
DR PDB; 5ON6; X-ray; 3.10 A; J/s8=2-200.
DR PDB; 5TBW; X-ray; 3.00 A; J/s8=2-200.
DR PDB; 5TGA; X-ray; 3.30 A; S8/s8=2-200.
DR PDB; 5TZS; EM; 5.10 A; 8=1-200.
DR PDB; 5WLC; EM; 3.80 A; L8=1-200.
DR PDB; 5WYJ; EM; 8.70 A; SJ=1-200.
DR PDB; 5WYK; EM; 4.50 A; SJ=1-200.
DR PDB; 6EML; EM; 3.60 A; V=1-200.
DR PDB; 6FAI; EM; 3.40 A; I=1-200.
DR PDB; 6GQ1; EM; 4.40 A; y=2-200.
DR PDB; 6GQB; EM; 3.90 A; y=2-200.
DR PDB; 6GQV; EM; 4.00 A; y=2-200.
DR PDB; 6HHQ; X-ray; 3.10 A; J/s8=1-200.
DR PDB; 6I7O; EM; 5.30 A; V/Vb=1-200.
DR PDB; 6KE6; EM; 3.40 A; SJ=1-200.
DR PDB; 6LQP; EM; 3.20 A; SJ=1-200.
DR PDB; 6LQQ; EM; 4.10 A; SJ=1-200.
DR PDB; 6LQR; EM; 8.60 A; SJ=1-200.
DR PDB; 6LQS; EM; 3.80 A; SJ=1-200.
DR PDB; 6LQT; EM; 4.90 A; SJ=1-200.
DR PDB; 6LQU; EM; 3.70 A; SJ=1-200.
DR PDB; 6LQV; EM; 4.80 A; SJ=1-200.
DR PDB; 6Q8Y; EM; 3.10 A; V=2-200.
DR PDB; 6RBD; EM; 3.47 A; I=1-200.
DR PDB; 6RBE; EM; 3.80 A; I=1-200.
DR PDB; 6S47; EM; 3.28 A; BJ=2-200.
DR PDB; 6SNT; EM; 2.80 A; I=1-200.
DR PDB; 6SV4; EM; 3.30 A; V/Vb/Vc=1-200.
DR PDB; 6T4Q; EM; 2.60 A; SI=2-199.
DR PDB; 6T7I; EM; 3.20 A; SI=1-200.
DR PDB; 6T7T; EM; 3.10 A; SI=1-200.
DR PDB; 6T83; EM; 4.00 A; Ib/j=1-200.
DR PDB; 6WDR; EM; 3.70 A; I=2-200.
DR PDB; 6WOO; EM; 2.90 A; II=2-200.
DR PDB; 6Y7C; EM; 3.80 A; I=1-200.
DR PDB; 6Z6J; EM; 3.40 A; SI=1-200.
DR PDB; 6Z6K; EM; 3.40 A; SI=1-200.
DR PDB; 6ZCE; EM; 5.30 A; J=1-200.
DR PDB; 6ZQB; EM; 3.90 A; DI=1-200.
DR PDB; 6ZQC; EM; 3.80 A; DI=1-200.
DR PDB; 6ZQD; EM; 3.80 A; DI=1-200.
DR PDB; 6ZQE; EM; 7.10 A; DI=1-200.
DR PDB; 6ZQF; EM; 4.90 A; DI=1-200.
DR PDB; 6ZQG; EM; 3.50 A; DI=1-200.
DR PDB; 6ZU9; EM; 6.20 A; V=1-200.
DR PDB; 6ZVI; EM; 3.00 A; q=2-200.
DR PDB; 7A1G; EM; 3.00 A; V=1-200.
DR PDB; 7AJT; EM; 4.60 A; DI=1-200.
DR PDB; 7AJU; EM; 3.80 A; DI=1-200.
DR PDB; 7B7D; EM; 3.30 A; V=2-199.
DR PDB; 7D4I; EM; 4.00 A; SJ=1-200.
DR PDB; 7D5T; EM; 6.00 A; SJ=1-200.
DR PDB; 7D63; EM; 12.30 A; SJ=1-200.
DR PDB; 7NRC; EM; 3.90 A; SV=2-199.
DR PDB; 7NRD; EM; 4.36 A; SV=2-200.
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; 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; 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; 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; 6WDR; -.
DR PDBsum; 6WOO; -.
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; P0CX39; -.
DR SMR; P0CX39; -.
DR BioGRID; 32629; 941.
DR BioGRID; 36848; 68.
DR IntAct; P0CX39; 9.
DR MINT; P0CX39; -.
DR STRING; 4932.YBL072C; -.
DR CarbonylDB; P0CX39; -.
DR iPTMnet; P0CX39; -.
DR MaxQB; P0CX39; -.
DR PaxDb; P0CX39; -.
DR PRIDE; P0CX39; -.
DR EnsemblFungi; YBL072C_mRNA; YBL072C; YBL072C.
DR EnsemblFungi; YER102W_mRNA; YER102W; YER102W.
DR GeneID; 852206; -.
DR GeneID; 856839; -.
DR KEGG; sce:YBL072C; -.
DR KEGG; sce:YER102W; -.
DR SGD; S000000168; RPS8A.
DR VEuPathDB; FungiDB:YBL072C; -.
DR VEuPathDB; FungiDB:YER102W; -.
DR eggNOG; KOG3283; Eukaryota.
DR HOGENOM; CLU_080597_1_1_1; -.
DR InParanoid; P0CX39; -.
DR OMA; VGRCDGY; -.
DR BioCyc; YEAST:G3O-28965-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 ChiTaRS; RPS8A; yeast.
DR PRO; PR:P0CX39; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P0CX39; protein.
DR ExpressionAtlas; P0CX39; 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: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 Gene3D; 1.10.168.20; -; 1.
DR InterPro; IPR042563; Ribosomal_protein_S8e_euk.
DR InterPro; IPR001047; Ribosomal_S8e.
DR InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2.
DR InterPro; IPR018283; Ribosomal_S8e_CS.
DR PANTHER; PTHR10394; PTHR10394; 1.
DR Pfam; PF01201; Ribosomal_S8e; 1.
DR TIGRFAMs; TIGR00307; eS8; 1.
DR PROSITE; PS01193; RIBOSOMAL_S8E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:18782943"
FT CHAIN 2..200
FT /note="40S ribosomal protein S8-A"
FT /id="PRO_0000122258"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 49
FT /note="R -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..102
FT /note="IV -> MS (in Ref. 4; ABM97467)"
FT /evidence="ECO:0000305"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 200 AA; 22490 MW; 3DB5CD6B4970C457 CRC64;
MGISRDSRHK RSATGAKRAQ FRKKRKFELG RQPANTKIGA KRIHSVRTRG GNKKYRALRI
ETGNFSWASE GISKKTRIAG VVYHPSNNEL VRTNTLTKAA IVQIDATPFR QWFEAHYGQT
LGKKKNVKEE ETVAKSKNAE RKWAARAASA KIESSVESQF SAGRLYACIS SRPGQSGRCD
GYILEGEELA FYLRRLTAKK
