ID RS29A_YEAST Reviewed; 56 AA.
AC P41057; A2TBM8; D6VZ23; P05761;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=Small ribosomal subunit protein uS14A {ECO:0000303|PubMed:24524803};
DE AltName: Full=40S ribosomal protein S29-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=S36;
DE AltName: Full=YS29;
GN Name=RPS29A {ECO:0000303|PubMed:9559554}; Synonyms=RPS36A, YS29A;
GN OrderedLocusNames=YLR388W; ORFNames=L8084.11;
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].
RA Suzuki K., Otaka E.;
RT "S.cerevisiae YS29A gene for ribosomal protein YS29.";
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 1-20.
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 PROTEIN SEQUENCE OF 2-10, 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 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 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 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 [13]
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 [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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
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 6490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS14 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC {ECO:0000305}.
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DR EMBL; D14676; BAA03507.1; -; Genomic_DNA.
DR EMBL; U19729; AAB82350.1; -; Genomic_DNA.
DR EMBL; EF123131; ABM97475.1; -; mRNA.
DR EMBL; BK006945; DAA09689.1; -; Genomic_DNA.
DR PIR; S48503; S48503.
DR RefSeq; NP_013492.3; NM_001182277.3.
DR PDB; 3J6X; EM; 6.10 A; 29=1-56.
DR PDB; 3J6Y; EM; 6.10 A; 29=1-56.
DR PDB; 3J77; EM; 6.20 A; 29=1-56.
DR PDB; 3J78; EM; 6.30 A; 29=1-56.
DR PDB; 4U3M; X-ray; 3.00 A; D9/d9=2-56.
DR PDB; 4U3N; X-ray; 3.20 A; D9/d9=2-56.
DR PDB; 4U3U; X-ray; 2.90 A; D9/d9=2-56.
DR PDB; 4U4N; X-ray; 3.10 A; D9/d9=2-56.
DR PDB; 4U4O; X-ray; 3.60 A; D9/d9=2-56.
DR PDB; 4U4Q; X-ray; 3.00 A; D9/d9=2-56.
DR PDB; 4U4R; X-ray; 2.80 A; D9/d9=2-56.
DR PDB; 4U4U; X-ray; 3.00 A; D9/d9=2-56.
DR PDB; 4U4Y; X-ray; 3.20 A; D9/d9=2-56.
DR PDB; 4U4Z; X-ray; 3.10 A; D9/d9=2-56.
DR PDB; 4U50; X-ray; 3.20 A; D9/d9=2-56.
DR PDB; 4U51; X-ray; 3.20 A; D9/d9=2-56.
DR PDB; 4U52; X-ray; 3.00 A; D9/d9=2-56.
DR PDB; 4U53; X-ray; 3.30 A; D9/d9=2-56.
DR PDB; 4U55; X-ray; 3.20 A; D9/d9=2-56.
DR PDB; 4U56; X-ray; 3.45 A; D9/d9=2-56.
DR PDB; 4U6F; X-ray; 3.10 A; D9/d9=2-56.
DR PDB; 4V6I; EM; 8.80 A; AN=1-56.
DR PDB; 4V7R; X-ray; 4.00 A; AS/CS=1-56.
DR PDB; 4V88; X-ray; 3.00 A; Ad/Cd=1-56.
DR PDB; 4V8Y; EM; 4.30 A; A3=1-56.
DR PDB; 4V8Z; EM; 6.60 A; A3=1-56.
DR PDB; 5DAT; X-ray; 3.15 A; D9/d9=2-56.
DR PDB; 5DC3; X-ray; 3.25 A; D9/d9=2-56.
DR PDB; 5DGE; X-ray; 3.45 A; D9/d9=2-56.
DR PDB; 5DGF; X-ray; 3.30 A; D9/d9=2-56.
DR PDB; 5DGV; X-ray; 3.10 A; D9/d9=2-56.
DR PDB; 5FCI; X-ray; 3.40 A; D9/d9=2-56.
DR PDB; 5FCJ; X-ray; 3.10 A; D9/d9=2-56.
DR PDB; 5I4L; X-ray; 3.10 A; D9/d9=4-56.
DR PDB; 5JUO; EM; 4.00 A; AC=1-56.
DR PDB; 5JUP; EM; 3.50 A; AC=1-56.
DR PDB; 5JUS; EM; 4.20 A; AC=1-56.
DR PDB; 5JUT; EM; 4.00 A; AC=1-56.
DR PDB; 5JUU; EM; 4.00 A; AC=1-56.
DR PDB; 5LYB; X-ray; 3.25 A; D9/d9=4-56.
DR PDB; 5M1J; EM; 3.30 A; d2=4-56.
DR PDB; 5MC6; EM; 3.80 A; M=1-56.
DR PDB; 5MEI; X-ray; 3.50 A; d9/e=4-56.
DR PDB; 5NDG; X-ray; 3.70 A; D9/d9=4-56.
DR PDB; 5NDV; X-ray; 3.30 A; D9/d9=4-56.
DR PDB; 5NDW; X-ray; 3.70 A; D9/d9=4-56.
DR PDB; 5OBM; X-ray; 3.40 A; D9/d9=4-56.
DR PDB; 5ON6; X-ray; 3.10 A; d9/e=4-56.
DR PDB; 5TBW; X-ray; 3.00 A; d9/e=4-56.
DR PDB; 5TGA; X-ray; 3.30 A; D9/d9=4-56.
DR PDB; 5TGM; X-ray; 3.50 A; D9/d9=4-56.
DR PDB; 6FAI; EM; 3.40 A; d=1-56.
DR PDB; 6GQ1; EM; 4.40 A; AT=4-56.
DR PDB; 6GQB; EM; 3.90 A; AT=4-56.
DR PDB; 6GQV; EM; 4.00 A; AT=4-56.
DR PDB; 6HHQ; X-ray; 3.10 A; d9/e=1-56.
DR PDB; 6I7O; EM; 5.30 A; M/Mb=4-56.
DR PDB; 6Q8Y; EM; 3.10 A; M=4-56.
DR PDB; 6RBD; EM; 3.47 A; d=1-56.
DR PDB; 6RBE; EM; 3.80 A; d=1-56.
DR PDB; 6S47; EM; 3.28 A; Be=2-56.
DR PDB; 6SNT; EM; 2.80 A; d=1-56.
DR PDB; 6SV4; EM; 3.30 A; M/Mb/Mc=1-56.
DR PDB; 6T4Q; EM; 2.60 A; Sd=4-56.
DR PDB; 6T7I; EM; 3.20 A; Sd=1-56.
DR PDB; 6T7T; EM; 3.10 A; Sd=1-56.
DR PDB; 6T83; EM; 4.00 A; 4/db=1-56.
DR PDB; 6TB3; EM; 2.80 A; M=4-56.
DR PDB; 6TNU; EM; 3.10 A; M=4-56.
DR PDB; 6WDR; EM; 3.70 A; d=20-56.
DR PDB; 6WOO; EM; 2.90 A; dd=4-56.
DR PDB; 6Y7C; EM; 3.80 A; d=1-56.
DR PDB; 6Z6J; EM; 3.40 A; Sd=1-56.
DR PDB; 6Z6K; EM; 3.40 A; Sd=1-56.
DR PDB; 6ZCE; EM; 5.30 A; e=1-56.
DR PDB; 6ZU9; EM; 6.20 A; N=1-56.
DR PDB; 6ZVI; EM; 3.00 A; O=4-56.
DR PDB; 7A1G; EM; 3.00 A; M=4-56.
DR PDB; 7B7D; EM; 3.30 A; M=4-56.
DR PDB; 7MPI; EM; 3.05 A; Bd=4-56.
DR PDB; 7MPJ; EM; 2.70 A; Bd=4-56.
DR PDB; 7N8B; EM; 3.05 A; Bd=4-56.
DR PDB; 7NRC; EM; 3.90 A; SM=4-56.
DR PDB; 7NRD; EM; 4.36 A; SM=4-56.
DR PDB; 7ZPQ; EM; 3.47 A; Ad=4-56.
DR PDB; 7ZRS; EM; 4.80 A; Ad=4-56.
DR PDB; 7ZUW; EM; 4.30 A; Ad=4-56.
DR PDB; 7ZUX; EM; 2.50 A; Dd=4-56.
DR PDB; 7ZW0; EM; 2.40 A; sM=1-56.
DR PDB; 8BQD; EM; 3.90 A; M=4-56.
DR PDB; 8BQX; EM; 3.80 A; M=4-56.
DR PDB; 8CAH; EM; 3.00 A; M=1-56.
DR PDB; 8CAS; EM; 3.30 A; N=1-56.
DR PDB; 8CBJ; EM; 3.80 A; d=1-56.
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; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
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; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
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; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7MPI; -.
DR PDBsum; 7MPJ; -.
DR PDBsum; 7N8B; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7ZPQ; -.
DR PDBsum; 7ZRS; -.
DR PDBsum; 7ZUW; -.
DR PDBsum; 7ZUX; -.
DR PDBsum; 7ZW0; -.
DR PDBsum; 8BQD; -.
DR PDBsum; 8BQX; -.
DR PDBsum; 8CAH; -.
DR PDBsum; 8CAS; -.
DR PDBsum; 8CBJ; -.
DR AlphaFoldDB; P41057; -.
DR EMDB; EMD-0047; -.
DR EMDB; EMD-0048; -.
DR EMDB; EMD-0049; -.
DR EMDB; EMD-10098; -.
DR EMDB; EMD-10262; -.
DR EMDB; EMD-10315; -.
DR EMDB; EMD-10377; -.
DR EMDB; EMD-10396; -.
DR EMDB; EMD-10397; -.
DR EMDB; EMD-10398; -.
DR EMDB; EMD-10431; -.
DR EMDB; EMD-10537; -.
DR EMDB; EMD-10713; -.
DR EMDB; EMD-11096; -.
DR EMDB; EMD-11097; -.
DR EMDB; EMD-11160; -.
DR EMDB; EMD-11439; -.
DR EMDB; EMD-11608; -.
DR EMDB; EMD-12081; -.
DR EMDB; EMD-12534; -.
DR EMDB; EMD-12535; -.
DR EMDB; EMD-21644; -.
DR EMDB; EMD-21859; -.
DR EMDB; EMD-23934; -.
DR EMDB; EMD-23935; -.
DR EMDB; EMD-24235; -.
DR EMDB; EMD-3461; -.
DR EMDB; EMD-4140; -.
DR EMDB; EMD-4214; -.
DR EMDB; EMD-4427; -.
DR EMDB; EMD-4474; -.
DR EMDB; EMD-4792; -.
DR EMDB; EMD-4793; -.
DR SMR; P41057; -.
DR BioGRID; 31647; 285.
DR DIP; DIP-4643N; -.
DR IntAct; P41057; 7.
DR STRING; 4932.YLR388W; -.
DR iPTMnet; P41057; -.
DR MaxQB; P41057; -.
DR PaxDb; 4932-YLR388W; -.
DR PeptideAtlas; P41057; -.
DR EnsemblFungi; YLR388W_mRNA; YLR388W; YLR388W.
DR GeneID; 851104; -.
DR KEGG; sce:YLR388W; -.
DR AGR; SGD:S000004380; -.
DR SGD; S000004380; RPS29A.
DR VEuPathDB; FungiDB:YLR388W; -.
DR eggNOG; KOG3506; Eukaryota.
DR GeneTree; ENSGT00940000170141; -.
DR HOGENOM; CLU_177289_1_1_1; -.
DR InParanoid; P41057; -.
DR OMA; CFRQCAK; -.
DR OrthoDB; 5476442at2759; -.
DR BioCyc; YEAST:G3O-32454-MONOMER; -.
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-72649; Translation initiation complex formation.
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 BioGRID-ORCS; 851104; 3 hits in 10 CRISPR screens.
DR PRO; PR:P41057; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P41057; Protein.
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:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR InterPro; IPR001209; Ribosomal_uS14.
DR InterPro; IPR018271; Ribosomal_uS14_CS.
DR InterPro; IPR039744; RIbosomal_uS14_euk_arc.
DR InterPro; IPR043140; Ribosomal_uS14_sf.
DR PANTHER; PTHR12010; 40S RIBOSOMAL PROTEIN S29; 1.
DR PANTHER; PTHR12010:SF2; 40S RIBOSOMAL PROTEIN S29; 1.
DR Pfam; PF00253; Ribosomal_S14; 1.
DR PROSITE; PS00527; RIBOSOMAL_S14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:18782943"
FT CHAIN 2..56
FT /note="Small ribosomal subunit protein uS14A"
FT /id="PRO_0000131032"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41058"
FT CONFLICT 7
FT /note="W -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="Y -> F (in Ref. 4; ABM97475)"
FT /evidence="ECO:0000305"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 56 AA; 6661 MW; F1A6900EE27748C2 CRC64;
MAHENVWFSH PRRYGKGSRQ CRVCSSHTGL IRKYGLNICR QCFREKANDI GFNKFR
//
