RS14A_YEAST
ID RS14A_YEAST Reviewed; 137 AA.
AC P06367; D6VR41; Q96VG9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=40S ribosomal protein S14-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP59A;
DE AltName: Full=Small ribosomal subunit protein uS11-A {ECO:0000303|PubMed:24524803};
GN Name=RPS14A {ECO:0000303|PubMed:9559554}; Synonyms=CRY1, RPL59;
GN OrderedLocusNames=YCR031C; ORFNames=YCR31C;
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=3037334; DOI=10.1128/mcb.7.5.1764-1775.1987;
RA Larkin J.C., Thompson J.R., Woolford J.L. Jr.;
RT "Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a
RT highly conserved ribosomal protein gene.";
RL Mol. Cell. Biol. 7:1764-1775(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO 72 AND 123.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 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 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 FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME, AND SUBCELLULAR LOCATION.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
RN [10]
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 [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 9-133, 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, 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 (PubMed:22096102). uS11 is involved in nucleolar processing of
CC pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
CC {ECO:0000269|PubMed:15590835, 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). uS11 interacts with eS1 forming part of
CC the mRNA exit tunnel (PubMed:9559554, PubMed:22096102). uS11 interacts
CC with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal
CC small subunit (SSU) processome composed of at least 40 protein subunits
CC and snoRNA U3 (PubMed:15590835). {ECO:0000269|PubMed:15590835,
CC ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15590835}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:1544921}.
CC -!- MISCELLANEOUS: Present with 29600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS11 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M16126; AAA34530.1; -; Genomic_DNA.
DR EMBL; X59720; CAC42981.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07510.1; -; Genomic_DNA.
DR PIR; A02726; R5BY59.
DR RefSeq; NP_009960.2; NM_001178745.1.
DR PDB; 3J6X; EM; 6.10 A; 14=1-137.
DR PDB; 3J6Y; EM; 6.10 A; 14=1-137.
DR PDB; 3J77; EM; 6.20 A; 14=1-137.
DR PDB; 3J78; EM; 6.30 A; 14=1-137.
DR PDB; 4U3M; X-ray; 3.00 A; C4/c4=2-137.
DR PDB; 4U3N; X-ray; 3.20 A; C4/c4=2-137.
DR PDB; 4U3U; X-ray; 2.90 A; C4/c4=2-137.
DR PDB; 4U4N; X-ray; 3.10 A; C4/c4=2-137.
DR PDB; 4U4O; X-ray; 3.60 A; C4/c4=2-137.
DR PDB; 4U4Q; X-ray; 3.00 A; C4/c4=2-137.
DR PDB; 4U4R; X-ray; 2.80 A; C4/c4=2-137.
DR PDB; 4U4U; X-ray; 3.00 A; C4/c4=2-137.
DR PDB; 4U4Y; X-ray; 3.20 A; C4/c4=2-137.
DR PDB; 4U4Z; X-ray; 3.10 A; C4/c4=2-137.
DR PDB; 4U50; X-ray; 3.20 A; C4/c4=2-137.
DR PDB; 4U51; X-ray; 3.20 A; C4/c4=2-137.
DR PDB; 4U52; X-ray; 3.00 A; C4/c4=2-137.
DR PDB; 4U53; X-ray; 3.30 A; C4/c4=2-137.
DR PDB; 4U55; X-ray; 3.20 A; C4/c4=2-137.
DR PDB; 4U56; X-ray; 3.45 A; C4/c4=2-137.
DR PDB; 4U6F; X-ray; 3.10 A; C4/c4=2-137.
DR PDB; 4V4B; EM; 11.70 A; AK=2-137.
DR PDB; 4V6I; EM; 8.80 A; AK=1-137.
DR PDB; 4V7R; X-ray; 4.00 A; AH/CH=1-137.
DR PDB; 4V88; X-ray; 3.00 A; AO/CO=1-137.
DR PDB; 4V8Y; EM; 4.30 A; AO=1-137.
DR PDB; 4V8Z; EM; 6.60 A; AO=1-137.
DR PDB; 4V92; EM; 3.70 A; O=11-137.
DR PDB; 5DAT; X-ray; 3.15 A; C4/c4=2-137.
DR PDB; 5DC3; X-ray; 3.25 A; C4/c4=2-137.
DR PDB; 5DGE; X-ray; 3.45 A; C4/c4=2-137.
DR PDB; 5DGF; X-ray; 3.30 A; C4/c4=2-137.
DR PDB; 5DGV; X-ray; 3.10 A; C4/c4=2-137.
DR PDB; 5FCI; X-ray; 3.40 A; C4/c4=2-137.
DR PDB; 5FCJ; X-ray; 3.10 A; C4/c4=2-137.
DR PDB; 5JPQ; EM; 7.30 A; w=1-137.
DR PDB; 5JUO; EM; 4.00 A; LB=1-137.
DR PDB; 5JUP; EM; 3.50 A; LB=1-137.
DR PDB; 5JUS; EM; 4.20 A; LB=1-137.
DR PDB; 5JUT; EM; 4.00 A; LB=1-137.
DR PDB; 5JUU; EM; 4.00 A; LB=1-137.
DR PDB; 5LL6; EM; 3.90 A; Z=1-137.
DR PDB; 5LYB; X-ray; 3.25 A; C4/c4=10-137.
DR PDB; 5M1J; EM; 3.30 A; O2=11-137.
DR PDB; 5MC6; EM; 3.80 A; Z=1-137.
DR PDB; 5NDG; X-ray; 3.70 A; C4/c4=10-137.
DR PDB; 5TGM; X-ray; 3.50 A; C4/c4=10-126.
DR PDB; 5WLC; EM; 3.80 A; NG=1-137.
DR PDB; 5WYJ; EM; 8.70 A; SP=1-137.
DR PDB; 5WYK; EM; 4.50 A; SP=1-137.
DR PDB; 6EML; EM; 3.60 A; Z=1-137.
DR PDB; 6FAI; EM; 3.40 A; O=1-137.
DR PDB; 6KE6; EM; 3.40 A; SP=1-137.
DR PDB; 6LQP; EM; 3.20 A; SP=1-137.
DR PDB; 6LQQ; EM; 4.10 A; SP=1-137.
DR PDB; 6LQR; EM; 8.60 A; SP=1-137.
DR PDB; 6LQS; EM; 3.80 A; SP=1-137.
DR PDB; 6LQT; EM; 4.90 A; SP=1-137.
DR PDB; 6LQU; EM; 3.70 A; SP=1-137.
DR PDB; 6RBD; EM; 3.47 A; O=1-137.
DR PDB; 6RBE; EM; 3.80 A; O=1-137.
DR PDB; 6S47; EM; 3.28 A; BP=2-137.
DR PDB; 6SNT; EM; 2.80 A; O=1-137.
DR PDB; 6SV4; EM; 3.30 A; Z/Zb/Zc=1-137.
DR PDB; 6T7I; EM; 3.20 A; SO=1-137.
DR PDB; 6T7T; EM; 3.10 A; SO=1-137.
DR PDB; 6T83; EM; 4.00 A; Ob/p=1-137.
DR PDB; 6Y7C; EM; 3.80 A; O=1-137.
DR PDB; 6Z6J; EM; 3.40 A; SO=1-137.
DR PDB; 6Z6K; EM; 3.40 A; SO=1-137.
DR PDB; 6ZCE; EM; 5.30 A; P=2-137.
DR PDB; 6ZQA; EM; 4.40 A; DO=1-137.
DR PDB; 6ZQB; EM; 3.90 A; DO=1-137.
DR PDB; 6ZQC; EM; 3.80 A; DO=1-137.
DR PDB; 6ZQD; EM; 3.80 A; DO=1-137.
DR PDB; 6ZQE; EM; 7.10 A; DO=1-137.
DR PDB; 6ZQF; EM; 4.90 A; DO=1-137.
DR PDB; 6ZQG; EM; 3.50 A; DO=1-137.
DR PDB; 6ZU9; EM; 6.20 A; Z=2-137.
DR PDB; 7AJT; EM; 4.60 A; DO=1-137.
DR PDB; 7AJU; EM; 3.80 A; DO=1-137.
DR PDB; 7D4I; EM; 4.00 A; SP=1-137.
DR PDB; 7D5S; EM; 4.60 A; SP=1-137.
DR PDB; 7D5T; EM; 6.00 A; SP=1-137.
DR PDB; 7D63; EM; 12.30 A; SP=1-137.
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; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5JPQ; -.
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; 5NDG; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
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; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P06367; -.
DR SMR; P06367; -.
DR BioGRID; 31014; 771.
DR IntAct; P06367; 32.
DR STRING; 4932.YCR031C; -.
DR MoonProt; P06367; -.
DR iPTMnet; P06367; -.
DR MaxQB; P06367; -.
DR PaxDb; P06367; -.
DR PRIDE; P06367; -.
DR TopDownProteomics; P06367; -.
DR EnsemblFungi; YCR031C_mRNA; YCR031C; YCR031C.
DR GeneID; 850397; -.
DR KEGG; sce:YCR031C; -.
DR SGD; S000000627; RPS14A.
DR VEuPathDB; FungiDB:YCR031C; -.
DR eggNOG; KOG0407; Eukaryota.
DR GeneTree; ENSGT00390000000703; -.
DR HOGENOM; CLU_072439_6_0_1; -.
DR InParanoid; P06367; -.
DR OMA; HIYASTN; -.
DR BioCyc; YEAST:G3O-29345-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; P06367; -.
DR PRO; PR:P06367; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P06367; protein.
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; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
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); IMP:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ribosome biogenesis; rRNA processing.
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..137
FT /note="40S ribosomal protein S14-A"
FT /id="PRO_0000123359"
FT REGION 117..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT CONFLICT 72
FT /note="K -> R (in Ref. 1; AAA34530)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="S -> C (in Ref. 1; AAA34530)"
FT /evidence="ECO:0000305"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6FAI"
FT TURN 129..133
FT /evidence="ECO:0007829|PDB:6RBD"
SQ SEQUENCE 137 AA; 14537 MW; 65A9212E10340A95 CRC64;
MSNVVQARDN SQVFGVARIY ASFNDTFVHV TDLSGKETIA RVTGGMKVKA DRDESSPYAA
MLAAQDVAAK CKEVGITAVH VKIRATGGTR TKTPGPGGQA ALRALARSGL RIGRIEDVTP
VPSDSTRKKG GRRGRRL
