RS4A_YEAST
ID RS4A_YEAST Reviewed; 261 AA.
AC P0CX35; D3DLF2; P05753;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=40S ribosomal protein S4-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP5;
DE AltName: Full=S7;
DE AltName: Full=Small ribosomal subunit protein eS4-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS6;
GN Name=RPS4A {ECO:0000303|PubMed:9559554}; Synonyms=RPS7B;
GN OrderedLocusNames=YJR145C; ORFNames=J2186;
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].
RX PubMed=1737755; DOI=10.1016/s0021-9258(19)50687-1;
RA Synetos D., Dabeva M.D., Warner J.R.;
RT "The yeast ribosomal protein S7 and its genes.";
RL J. Biol. Chem. 267:3008-3013(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 PRELIMINARY PROTEIN SEQUENCE OF 2-29.
RX PubMed=6814480; DOI=10.1021/bi00262a005;
RA Otaka E., Higo K., Osawa S.;
RT "Isolation of seventeen proteins and amino-terminal amino acid sequences of
RT eight proteins from cytoplasmic ribosomes of yeast.";
RL Biochemistry 21:4545-4550(1982).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115, AND IDENTIFICATION BY
RP 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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-134; LYS-161; LYS-168;
RP LYS-174; LYS-179; LYS-211 AND LYS-233, AND IDENTIFICATION BY MASS
RP 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 [14]
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 [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 -!- MISCELLANEOUS: Present with 573 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS4 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family.
CC {ECO:0000305}.
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DR EMBL; M64293; AAA35011.1; -; Genomic_DNA.
DR EMBL; Z49645; CAA89678.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08930.1; -; Genomic_DNA.
DR PIR; S20054; S20054.
DR RefSeq; NP_012073.1; NM_001179334.1.
DR RefSeq; NP_012679.3; NM_001181803.3.
DR PDB; 3J6X; EM; 6.10 A; S4=1-261.
DR PDB; 3J6Y; EM; 6.10 A; S4=1-261.
DR PDB; 3J77; EM; 6.20 A; S4=1-261.
DR PDB; 3J78; EM; 6.30 A; S4=1-261.
DR PDB; 4U3M; X-ray; 3.00 A; S4/s4=2-261.
DR PDB; 4U3N; X-ray; 3.20 A; S4/s4=2-261.
DR PDB; 4U3U; X-ray; 2.90 A; S4/s4=2-261.
DR PDB; 4U4N; X-ray; 3.10 A; S4/s4=2-261.
DR PDB; 4U4O; X-ray; 3.60 A; S4/s4=2-261.
DR PDB; 4U4Q; X-ray; 3.00 A; S4/s4=2-261.
DR PDB; 4U4R; X-ray; 2.80 A; S4/s4=2-261.
DR PDB; 4U4U; X-ray; 3.00 A; S4/s4=2-261.
DR PDB; 4U4Y; X-ray; 3.20 A; S4/s4=2-261.
DR PDB; 4U4Z; X-ray; 3.10 A; S4/s4=2-261.
DR PDB; 4U50; X-ray; 3.20 A; S4/s4=2-261.
DR PDB; 4U51; X-ray; 3.20 A; S4/s4=2-261.
DR PDB; 4U52; X-ray; 3.00 A; S4/s4=2-261.
DR PDB; 4U53; X-ray; 3.30 A; S4/s4=2-261.
DR PDB; 4U55; X-ray; 3.20 A; S4/s4=2-261.
DR PDB; 4U56; X-ray; 3.45 A; S4/s4=2-261.
DR PDB; 4U6F; X-ray; 3.10 A; S4/s4=2-261.
DR PDB; 4V6I; EM; 8.80 A; AD=1-261.
DR PDB; 4V88; X-ray; 3.00 A; AE/CE=1-261.
DR PDB; 4V8Y; EM; 4.30 A; AE=1-261.
DR PDB; 4V8Z; EM; 6.60 A; AE=1-261.
DR PDB; 4V92; EM; 3.70 A; E=2-261.
DR PDB; 5DAT; X-ray; 3.15 A; S4/s4=2-261.
DR PDB; 5DC3; X-ray; 3.25 A; S4/s4=2-261.
DR PDB; 5DGE; X-ray; 3.45 A; S4/s4=2-261.
DR PDB; 5DGF; X-ray; 3.30 A; S4/s4=2-261.
DR PDB; 5DGV; X-ray; 3.10 A; S4/s4=2-261.
DR PDB; 5FCI; X-ray; 3.40 A; S4/s4=2-261.
DR PDB; 5FCJ; X-ray; 3.10 A; S4/s4=2-261.
DR PDB; 5I4L; X-ray; 3.10 A; S4/s4=2-261.
DR PDB; 5JUO; EM; 4.00 A; BB=1-261.
DR PDB; 5JUP; EM; 3.50 A; BB=1-261.
DR PDB; 5JUS; EM; 4.20 A; BB=1-261.
DR PDB; 5JUT; EM; 4.00 A; BB=1-261.
DR PDB; 5JUU; EM; 4.00 A; BB=1-261.
DR PDB; 5LL6; EM; 3.90 A; S=1-261.
DR PDB; 5LYB; X-ray; 3.25 A; S4/s4=2-261.
DR PDB; 5M1J; EM; 3.30 A; E2=2-261.
DR PDB; 5MC6; EM; 3.80 A; S=1-261.
DR PDB; 5MEI; X-ray; 3.50 A; F/s4=2-261.
DR PDB; 5NDG; X-ray; 3.70 A; S4/s4=2-261.
DR PDB; 5NDV; X-ray; 3.30 A; S4/s4=2-261.
DR PDB; 5NDW; X-ray; 3.70 A; S4/s4=2-261.
DR PDB; 5OBM; X-ray; 3.40 A; S4/s4=2-261.
DR PDB; 5ON6; X-ray; 3.10 A; F/s4=2-261.
DR PDB; 5TBW; X-ray; 3.00 A; F/s4=2-261.
DR PDB; 5TGA; X-ray; 3.30 A; S4/s4=2-261.
DR PDB; 5TGM; X-ray; 3.50 A; S4/s4=2-261.
DR PDB; 5TZS; EM; 5.10 A; 5=1-261.
DR PDB; 5WLC; EM; 3.80 A; L4=1-261.
DR PDB; 5WYJ; EM; 8.70 A; SF=1-261.
DR PDB; 5WYK; EM; 4.50 A; SF=1-261.
DR PDB; 6EML; EM; 3.60 A; S=1-261.
DR PDB; 6FAI; EM; 3.40 A; E=1-261.
DR PDB; 6GQ1; EM; 4.40 A; u=2-261.
DR PDB; 6GQB; EM; 3.90 A; u=2-261.
DR PDB; 6GQV; EM; 4.00 A; u=2-261.
DR PDB; 6HHQ; X-ray; 3.10 A; F/s4=1-261.
DR PDB; 6I7O; EM; 5.30 A; S/Sb=2-261.
DR PDB; 6KE6; EM; 3.40 A; SF=1-261.
DR PDB; 6LQP; EM; 3.20 A; SF=1-261.
DR PDB; 6LQQ; EM; 4.10 A; SF=1-261.
DR PDB; 6LQR; EM; 8.60 A; SF=1-261.
DR PDB; 6LQS; EM; 3.80 A; SF=1-261.
DR PDB; 6LQT; EM; 4.90 A; SF=1-261.
DR PDB; 6LQU; EM; 3.70 A; SF=1-261.
DR PDB; 6LQV; EM; 4.80 A; SF=1-261.
DR PDB; 6Q8Y; EM; 3.10 A; S=2-261.
DR PDB; 6RBD; EM; 3.47 A; E=1-261.
DR PDB; 6RBE; EM; 3.80 A; E=1-261.
DR PDB; 6S47; EM; 3.28 A; BF=2-261.
DR PDB; 6SNT; EM; 2.80 A; E=1-261.
DR PDB; 6SV4; EM; 3.30 A; S/Sb/Sc=1-261.
DR PDB; 6T4Q; EM; 2.60 A; SE=2-259.
DR PDB; 6T7I; EM; 3.20 A; SE=1-261.
DR PDB; 6T7T; EM; 3.10 A; SE=1-261.
DR PDB; 6T83; EM; 4.00 A; Eb/f=1-261.
DR PDB; 6TB3; EM; 2.80 A; S=2-259.
DR PDB; 6TNU; EM; 3.10 A; S=2-259.
DR PDB; 6WDR; EM; 3.70 A; E=2-261.
DR PDB; 6WOO; EM; 2.90 A; EE=2-258.
DR PDB; 6XIQ; EM; 4.20 A; u=1-261.
DR PDB; 6XIR; EM; 3.20 A; u=1-261.
DR PDB; 6Y7C; EM; 3.80 A; E=1-261.
DR PDB; 6Z6J; EM; 3.40 A; SE=1-261.
DR PDB; 6Z6K; EM; 3.40 A; SE=1-261.
DR PDB; 6ZCE; EM; 5.30 A; F=1-261.
DR PDB; 6ZQB; EM; 3.90 A; DE=1-261.
DR PDB; 6ZQC; EM; 3.80 A; DE=1-261.
DR PDB; 6ZQD; EM; 3.80 A; DE=1-261.
DR PDB; 6ZQE; EM; 7.10 A; DE=1-261.
DR PDB; 6ZQF; EM; 4.90 A; DE=1-261.
DR PDB; 6ZQG; EM; 3.50 A; DE=1-261.
DR PDB; 6ZU9; EM; 6.20 A; S=1-261.
DR PDB; 6ZVI; EM; 3.00 A; m=2-261.
DR PDB; 7A1G; EM; 3.00 A; S=2-259.
DR PDB; 7AJT; EM; 4.60 A; DE=1-261.
DR PDB; 7AJU; EM; 3.80 A; DE=1-261.
DR PDB; 7B7D; EM; 3.30 A; S=2-259.
DR PDB; 7D4I; EM; 4.00 A; SF=1-261.
DR PDB; 7D5T; EM; 6.00 A; SF=1-261.
DR PDB; 7D63; EM; 12.30 A; SF=1-261.
DR PDB; 7NRC; EM; 3.90 A; SS=2-259.
DR PDB; 7NRD; EM; 4.36 A; SS=2-261.
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; 4V6I; -.
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; 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; P0CX35; -.
DR SMR; P0CX35; -.
DR BioGRID; 33901; 179.
DR BioGRID; 36637; 323.
DR IntAct; P0CX35; 12.
DR MINT; P0CX35; -.
DR STRING; 4932.YHR203C; -.
DR iPTMnet; P0CX35; -.
DR MaxQB; P0CX35; -.
DR PaxDb; P0CX35; -.
DR PRIDE; P0CX35; -.
DR TopDownProteomics; P0CX35; -.
DR EnsemblFungi; YHR203C_mRNA; YHR203C; YHR203C.
DR EnsemblFungi; YJR145C_mRNA; YJR145C; YJR145C.
DR GeneID; 853610; -.
DR GeneID; 856610; -.
DR KEGG; sce:YHR203C; -.
DR KEGG; sce:YJR145C; -.
DR SGD; S000003906; RPS4A.
DR VEuPathDB; FungiDB:YHR203C; -.
DR VEuPathDB; FungiDB:YJR145C; -.
DR eggNOG; KOG0378; Eukaryota.
DR HOGENOM; CLU_060400_1_0_1; -.
DR InParanoid; P0CX35; -.
DR OMA; FPVGLMD; -.
DR BioCyc; YEAST:G3O-31759-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 PRO; PR:P0CX35; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P0CX35; protein.
DR ExpressionAtlas; P0CX35; baseline and differential.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0006412; P:translation; IBA:GO_Central.
DR CDD; cd06087; KOW_RPS4; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.740; -; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_00485; Ribosomal_S4e; 1.
DR InterPro; IPR032277; 40S_S4_C.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041982; KOW_RPS4.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR000876; Ribosomal_S4e.
DR InterPro; IPR013845; Ribosomal_S4e_central_region.
DR InterPro; IPR038237; Ribosomal_S4e_central_sf.
DR InterPro; IPR013843; Ribosomal_S4e_N.
DR InterPro; IPR018199; Ribosomal_S4e_N_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11581; PTHR11581; 2.
DR Pfam; PF16121; 40S_S4_C; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF00900; Ribosomal_S4e; 1.
DR Pfam; PF08071; RS4NT; 1.
DR Pfam; PF01479; S4; 1.
DR PIRSF; PIRSF002116; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR PROSITE; PS00528; RIBOSOMAL_S4E; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; 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 CHAIN 2..261
FT /note="40S ribosomal protein S4-A"
FT /id="PRO_0000130843"
FT DOMAIN 42..105
FT /note="S4 RNA-binding"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:6RBD"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6RBD"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:7A1G"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 119..132
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 261 AA; 29410 MW; F109594560F34734 CRC64;
MARGPKKHLK RLAAPHHWLL DKLSGCYAPR PSAGPHKLRE SLPLIVFLRN RLKYALNGRE
VKAILMQRHV KVDGKVRTDT TYPAGFMDVI TLDATNENFR LVYDVKGRFA VHRITDEEAS
YKLGKVKKVQ LGKKGVPYVV THDGRTIRYP DPNIKVNDTV KIDLASGKIT DFIKFDAGKL
VYVTGGRNLG RIGTIVHKER HDGGFDLVHI KDSLDNTFVT RLNNVFVIGE QGKPYISLPK
GKGIKLSIAE ERDRRRAQQG L
