RS3A1_YEAST
ID RS3A1_YEAST Reviewed; 255 AA.
AC P33442; D6VZ76;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=40S ribosomal protein S1-A {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000303|PubMed:9559554};
DE AltName: Full=RP10A;
DE AltName: Full=Small ribosomal subunit protein eS1-A {ECO:0000303|PubMed:24524803};
GN Name=RPS1A {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000303|PubMed:9559554};
GN Synonyms=PLC1, RPS10A; OrderedLocusNames=YLR441C; ORFNames=L9753.9;
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=1451783; DOI=10.1016/0014-5793(92)80203-s;
RA Ito M., Yasui A., Komamine A.;
RT "A gene family homologous to the S-phase specific gene in higher plants is
RT essential for cell proliferation in Saccharomyces cerevisiae.";
RL FEBS Lett. 301:29-33(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8143753; DOI=10.1111/j.1432-1033.1994.tb18704.x;
RA Auclair D., Lang B.L., Desgroseillers L., Forest P.;
RT "Analysis of genes encoding highly conserved lysine-rich proteins in
RT Aplysia californica and Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 220:997-1003(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
RX PubMed=6098447; DOI=10.1002/j.1460-2075.1984.tb02214.x;
RA Shore D., Squire M., Nasmyth K.A.;
RT "Characterization of two genes required for the position-effect control of
RT yeast mating-type genes.";
RL EMBO J. 3:2817-2823(1984).
RN [7]
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 [8]
RP CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT ALA-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 [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-245, 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-254, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-245 AND THR-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [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). eS1 interacts directly with uS11 and
CC eS26, which form part of the mRNA exit tunnel (PubMed:9559554,
CC PubMed:22096102). {ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260}.
CC -!- MISCELLANEOUS: Present with 92400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS1 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03122}.
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DR EMBL; X65802; CAA46676.1; -; Genomic_DNA.
DR EMBL; X68556; CAA48559.1; -; Genomic_DNA.
DR EMBL; U21094; AAB67521.1; -; Genomic_DNA.
DR EMBL; AY693148; AAT93167.1; -; Genomic_DNA.
DR EMBL; X01420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006945; DAA09742.1; -; Genomic_DNA.
DR PIR; S21121; S21121.
DR RefSeq; NP_013546.1; NM_001182329.1.
DR PDB; 3J6X; EM; 6.10 A; S1=1-255.
DR PDB; 3J6Y; EM; 6.10 A; S1=1-255.
DR PDB; 3J77; EM; 6.20 A; S1=1-255.
DR PDB; 3J78; EM; 6.30 A; S1=1-255.
DR PDB; 4U3M; X-ray; 3.00 A; S1/s1=2-255.
DR PDB; 4U3N; X-ray; 3.20 A; S1/s1=2-255.
DR PDB; 4U3U; X-ray; 2.90 A; S1/s1=2-255.
DR PDB; 4U4N; X-ray; 3.10 A; S1/s1=2-255.
DR PDB; 4U4O; X-ray; 3.60 A; S1/s1=2-255.
DR PDB; 4U4Q; X-ray; 3.00 A; S1/s1=2-255.
DR PDB; 4U4R; X-ray; 2.80 A; S1/s1=2-255.
DR PDB; 4U4U; X-ray; 3.00 A; S1/s1=2-255.
DR PDB; 4U4Y; X-ray; 3.20 A; S1/s1=2-255.
DR PDB; 4U4Z; X-ray; 3.10 A; S1/s1=2-255.
DR PDB; 4U50; X-ray; 3.20 A; S1/s1=2-255.
DR PDB; 4U51; X-ray; 3.20 A; S1/s1=2-255.
DR PDB; 4U52; X-ray; 3.00 A; S1/s1=2-255.
DR PDB; 4U53; X-ray; 3.30 A; S1/s1=2-255.
DR PDB; 4U55; X-ray; 3.20 A; S1/s1=2-255.
DR PDB; 4U56; X-ray; 3.45 A; S1/s1=2-255.
DR PDB; 4U6F; X-ray; 3.10 A; S1/s1=2-255.
DR PDB; 4V88; X-ray; 3.00 A; AB/CB=1-255.
DR PDB; 4V8Y; EM; 4.30 A; AB=1-255.
DR PDB; 4V8Z; EM; 6.60 A; AB=1-255.
DR PDB; 4V92; EM; 3.70 A; B=21-233.
DR PDB; 5DAT; X-ray; 3.15 A; S1/s1=2-255.
DR PDB; 5DC3; X-ray; 3.25 A; S1/s1=2-255.
DR PDB; 5DGE; X-ray; 3.45 A; S1/s1=2-255.
DR PDB; 5DGF; X-ray; 3.30 A; S1/s1=2-255.
DR PDB; 5DGV; X-ray; 3.10 A; S1/s1=2-255.
DR PDB; 5FCI; X-ray; 3.40 A; S1/s1=2-255.
DR PDB; 5FCJ; X-ray; 3.10 A; S1/s1=2-255.
DR PDB; 5I4L; X-ray; 3.10 A; S1/s1=20-235.
DR PDB; 5JUO; EM; 4.00 A; YA=1-255.
DR PDB; 5JUP; EM; 3.50 A; YA=1-255.
DR PDB; 5JUS; EM; 4.20 A; YA=1-255.
DR PDB; 5JUT; EM; 4.00 A; YA=1-255.
DR PDB; 5JUU; EM; 4.00 A; YA=1-255.
DR PDB; 5LL6; EM; 3.90 A; Q=1-255.
DR PDB; 5LYB; X-ray; 3.25 A; S1/s1=20-235.
DR PDB; 5M1J; EM; 3.30 A; B2=20-233.
DR PDB; 5MC6; EM; 3.80 A; Q=1-255.
DR PDB; 5MEI; X-ray; 3.50 A; C/s1=20-235.
DR PDB; 5NDG; X-ray; 3.70 A; S1/s1=20-235.
DR PDB; 5NDV; X-ray; 3.30 A; S1/s1=20-235.
DR PDB; 5NDW; X-ray; 3.70 A; S1/s1=20-235.
DR PDB; 5OBM; X-ray; 3.40 A; S1/s1=20-235.
DR PDB; 5ON6; X-ray; 3.10 A; C/s1=20-235.
DR PDB; 5TBW; X-ray; 3.00 A; C/s1=20-235.
DR PDB; 5TGA; X-ray; 3.30 A; S1/s1=20-235.
DR PDB; 5TGM; X-ray; 3.50 A; S1/s1=20-235.
DR PDB; 5WYJ; EM; 8.70 A; SC=1-255.
DR PDB; 5WYK; EM; 4.50 A; SC=1-255.
DR PDB; 6EML; EM; 3.60 A; Q=1-255.
DR PDB; 6FAI; EM; 3.40 A; B=1-255.
DR PDB; 6GQ1; EM; 4.40 A; r=20-233.
DR PDB; 6GQB; EM; 3.90 A; r=20-233.
DR PDB; 6GQV; EM; 4.00 A; r=20-233.
DR PDB; 6HHQ; X-ray; 3.10 A; C/s1=1-255.
DR PDB; 6I7O; EM; 5.30 A; Q/Qb=20-235.
DR PDB; 6KE6; EM; 3.40 A; SC=1-255.
DR PDB; 6LQP; EM; 3.20 A; SC=1-255.
DR PDB; 6LQQ; EM; 4.10 A; SC=1-255.
DR PDB; 6LQR; EM; 8.60 A; SC=1-255.
DR PDB; 6LQS; EM; 3.80 A; SC=1-255.
DR PDB; 6LQT; EM; 4.90 A; SC=1-255.
DR PDB; 6Q8Y; EM; 3.10 A; Q=20-233.
DR PDB; 6RBD; EM; 3.47 A; B=1-255.
DR PDB; 6RBE; EM; 3.80 A; B=1-255.
DR PDB; 6S47; EM; 3.28 A; BC=2-255.
DR PDB; 6SNT; EM; 2.80 A; B=1-255.
DR PDB; 6SV4; EM; 3.30 A; Q/Qb/Qc=1-255.
DR PDB; 6T4Q; EM; 2.60 A; SB=2-233.
DR PDB; 6T7I; EM; 3.20 A; SB=1-255.
DR PDB; 6T83; EM; 4.00 A; Ba/c=1-255.
DR PDB; 6TB3; EM; 2.80 A; Q=2-233.
DR PDB; 6Y7C; EM; 3.80 A; B=1-255.
DR PDB; 6Z6J; EM; 3.40 A; SB=1-255.
DR PDB; 6Z6K; EM; 3.40 A; SB=1-255.
DR PDB; 6ZCE; EM; 5.30 A; C=1-255.
DR PDB; 6ZQA; EM; 4.40 A; DA=1-255.
DR PDB; 6ZQB; EM; 3.90 A; DA=1-255.
DR PDB; 6ZQC; EM; 3.80 A; DA=1-255.
DR PDB; 6ZQD; EM; 3.80 A; DA=1-255.
DR PDB; 6ZQE; EM; 7.10 A; DA=1-255.
DR PDB; 6ZQF; EM; 4.90 A; DA=1-255.
DR PDB; 6ZQG; EM; 3.50 A; DA=1-255.
DR PDB; 6ZU9; EM; 6.20 A; Q=1-255.
DR PDB; 6ZVI; EM; 3.00 A; j=20-235.
DR PDB; 7A1G; EM; 3.00 A; Q=2-233.
DR PDB; 7AJT; EM; 4.60 A; DA=1-255.
DR PDB; 7AJU; EM; 3.80 A; DA=1-255.
DR PDB; 7B7D; EM; 3.30 A; Q=2-233.
DR PDB; 7D4I; EM; 4.00 A; SC=1-255.
DR PDB; 7D5T; EM; 6.00 A; SC=1-255.
DR PDB; 7D63; EM; 12.30 A; SC=1-255.
DR PDB; 7NRC; EM; 3.90 A; SQ=2-233.
DR PDB; 7NRD; EM; 4.36 A; SQ=20-235.
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; 5TGM; -.
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; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
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; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P33442; -.
DR SMR; P33442; -.
DR BioGRID; 31700; 738.
DR DIP; DIP-4147N; -.
DR IntAct; P33442; 65.
DR MINT; P33442; -.
DR STRING; 4932.YLR441C; -.
DR CarbonylDB; P33442; -.
DR iPTMnet; P33442; -.
DR MaxQB; P33442; -.
DR PaxDb; P33442; -.
DR PRIDE; P33442; -.
DR TopDownProteomics; P33442; -.
DR EnsemblFungi; YLR441C_mRNA; YLR441C; YLR441C.
DR GeneID; 851162; -.
DR KEGG; sce:YLR441C; -.
DR SGD; S000004433; RPS1A.
DR VEuPathDB; FungiDB:YLR441C; -.
DR eggNOG; KOG1628; Eukaryota.
DR GeneTree; ENSGT00940000165721; -.
DR HOGENOM; CLU_062507_0_0_1; -.
DR InParanoid; P33442; -.
DR OMA; KCEDVQG; -.
DR BioCyc; YEAST:G3O-32497-MON; -.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-936440; Negative regulators of DDX58/IFIH1 signaling.
DR PRO; PR:P33442; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P33442; protein.
DR GO; GO:0030686; C:90S preribosome; 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:0003735; F:structural constituent of ribosome; NAS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1.
DR InterPro; IPR027500; Ribosomal_S1/3_euk.
DR InterPro; IPR001593; Ribosomal_S3Ae.
DR InterPro; IPR018281; Ribosomal_S3Ae_CS.
DR Pfam; PF01015; Ribosomal_S3Ae; 1.
DR SMART; SM01397; Ribosomal_S3Ae; 1.
DR PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03122,
FT ECO:0000269|PubMed:10601260"
FT CHAIN 2..255
FT /note="40S ribosomal protein S1-A"
FT /id="PRO_0000153541"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine; partial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03122,
FT ECO:0000269|PubMed:10601260"
FT MOD_RES 245
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P23248"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:7A1G"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 158..177
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 255 AA; 28743 MW; 2629D022EDBDE885 CRC64;
MAVGKNKRLS KGKKGQKKRV VDPFTRKEWF DIKAPSTFEN RNVGKTLVNK STGLKSASDA
LKGRVVEVCL ADLQGSEDHS FRKIKLRVDE VQGKNLLTNF HGMDFTTDKL RSMVRKWQTL
IEANVTVKTS DDYVLRIFAI AFTRKQANQV KRHSYAQSSH IRAIRKVISE ILTKEVQGST
LAQLTSKLIP EVINKEIENA TKDIFPLQNI HVRKVKLLKQ PKFDVGALMA LHGEGSGEEK
GKKVTGFKDE VLETV
