RS13_YEAST
ID RS13_YEAST Reviewed; 151 AA.
AC P05756; D6VS50;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=40S ribosomal protein S13 {ECO:0000303|PubMed:9559554};
DE AltName: Full=S27a;
DE AltName: Full=Small ribosomal subunit protein uS15 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS15;
GN Name=RPS13 {ECO:0000303|PubMed:9559554}; Synonyms=RPS13C;
GN OrderedLocusNames=YDR064W; ORFNames=D4252, YD9609.18;
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=8789263;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA Brandt P., Ramlow S., Otto B., Bloecker H.;
RT "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT Saccharomyces cerevisiae chromosome IV.";
RL Yeast 12:85-90(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PROTEIN SEQUENCE OF 2-41.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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 [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-39 AND LYS-43, AND
RP IDENTIFICATION BY MASS 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 [9]
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 [10]
RP 3D-STRUCTURE MODELING OF 66-130, 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 [11]
RP 3D-STRUCTURE MODELING OF 66-130, 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 [12]
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 [13]
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:22096102}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000305}.
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DR EMBL; X84162; CAA58980.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89093.1; -; Genomic_DNA.
DR EMBL; Z74360; CAA98882.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11910.1; -; Genomic_DNA.
DR PIR; S54048; S54048.
DR RefSeq; NP_010349.3; NM_001180372.3.
DR PDB; 3J6X; EM; 6.10 A; 13=1-151.
DR PDB; 3J6Y; EM; 6.10 A; 13=1-151.
DR PDB; 3J77; EM; 6.20 A; 13=1-151.
DR PDB; 3J78; EM; 6.30 A; 13=1-151.
DR PDB; 4U3M; X-ray; 3.00 A; C3/c3=2-151.
DR PDB; 4U3N; X-ray; 3.20 A; C3/c3=2-151.
DR PDB; 4U3U; X-ray; 2.90 A; C3/c3=2-151.
DR PDB; 4U4N; X-ray; 3.10 A; C3/c3=2-151.
DR PDB; 4U4O; X-ray; 3.60 A; C3/c3=2-151.
DR PDB; 4U4Q; X-ray; 3.00 A; C3/c3=2-151.
DR PDB; 4U4R; X-ray; 2.80 A; C3/c3=2-151.
DR PDB; 4U4U; X-ray; 3.00 A; C3/c3=2-151.
DR PDB; 4U4Y; X-ray; 3.20 A; C3/c3=2-151.
DR PDB; 4U4Z; X-ray; 3.10 A; C3/c3=2-151.
DR PDB; 4U50; X-ray; 3.20 A; C3/c3=2-151.
DR PDB; 4U51; X-ray; 3.20 A; C3/c3=2-151.
DR PDB; 4U52; X-ray; 3.00 A; C3/c3=2-151.
DR PDB; 4U53; X-ray; 3.30 A; C3/c3=2-151.
DR PDB; 4U55; X-ray; 3.20 A; C3/c3=2-151.
DR PDB; 4U56; X-ray; 3.45 A; C3/c3=2-151.
DR PDB; 4U6F; X-ray; 3.10 A; C3/c3=2-151.
DR PDB; 4V4B; EM; 11.70 A; AO=66-130.
DR PDB; 4V6I; EM; 8.80 A; AO=1-151.
DR PDB; 4V7R; X-ray; 4.00 A; AG/CG=1-151.
DR PDB; 4V88; X-ray; 3.00 A; AN/CN=1-151.
DR PDB; 4V8Y; EM; 4.30 A; AN=1-151.
DR PDB; 4V8Z; EM; 6.60 A; AN=1-151.
DR PDB; 4V92; EM; 3.70 A; N=2-151.
DR PDB; 5DAT; X-ray; 3.15 A; C3/c3=2-151.
DR PDB; 5DC3; X-ray; 3.25 A; C3/c3=2-151.
DR PDB; 5DGE; X-ray; 3.45 A; C3/c3=2-151.
DR PDB; 5DGF; X-ray; 3.30 A; C3/c3=2-151.
DR PDB; 5DGV; X-ray; 3.10 A; C3/c3=2-151.
DR PDB; 5FCI; X-ray; 3.40 A; C3/c3=2-151.
DR PDB; 5FCJ; X-ray; 3.10 A; C3/c3=2-151.
DR PDB; 5I4L; X-ray; 3.10 A; C3/c3=2-151.
DR PDB; 5JPQ; EM; 7.30 A; v=1-151.
DR PDB; 5JUO; EM; 4.00 A; KB=1-151.
DR PDB; 5JUP; EM; 3.50 A; KB=1-151.
DR PDB; 5JUS; EM; 4.20 A; KB=1-151.
DR PDB; 5JUT; EM; 4.00 A; KB=1-151.
DR PDB; 5JUU; EM; 4.00 A; KB=1-151.
DR PDB; 5LL6; EM; 3.90 A; Y=1-151.
DR PDB; 5LYB; X-ray; 3.25 A; C3/c3=2-151.
DR PDB; 5M1J; EM; 3.30 A; N2=2-151.
DR PDB; 5MC6; EM; 3.80 A; Y=1-151.
DR PDB; 5MEI; X-ray; 3.50 A; O/c3=2-151.
DR PDB; 5NDG; X-ray; 3.70 A; C3/c3=2-151.
DR PDB; 5NDV; X-ray; 3.30 A; C3/c3=2-151.
DR PDB; 5NDW; X-ray; 3.70 A; C3/c3=2-151.
DR PDB; 5OBM; X-ray; 3.40 A; C3/c3=2-151.
DR PDB; 5ON6; X-ray; 3.10 A; O/c3=2-151.
DR PDB; 5TBW; X-ray; 3.00 A; O/c3=2-151.
DR PDB; 5TGA; X-ray; 3.30 A; C3/c3=2-151.
DR PDB; 5TGM; X-ray; 3.50 A; C3/c3=2-151.
DR PDB; 5WLC; EM; 3.80 A; NF=1-151.
DR PDB; 5WYJ; EM; 8.70 A; SO=1-151.
DR PDB; 5WYK; EM; 4.50 A; SO=1-151.
DR PDB; 6EML; EM; 3.60 A; Y=1-151.
DR PDB; 6FAI; EM; 3.40 A; N=1-151.
DR PDB; 6GQ1; EM; 4.40 A; AD=2-151.
DR PDB; 6GQB; EM; 3.90 A; AD=2-151.
DR PDB; 6GQV; EM; 4.00 A; AD=2-151.
DR PDB; 6HHQ; X-ray; 3.10 A; O/c3=1-151.
DR PDB; 6I7O; EM; 5.30 A; Y/Yb=2-151.
DR PDB; 6KE6; EM; 3.40 A; SO=1-151.
DR PDB; 6LQP; EM; 3.20 A; SO=1-151.
DR PDB; 6LQQ; EM; 4.10 A; SO=1-151.
DR PDB; 6LQR; EM; 8.60 A; SO=1-151.
DR PDB; 6LQS; EM; 3.80 A; SO=1-151.
DR PDB; 6LQT; EM; 4.90 A; SO=1-151.
DR PDB; 6LQU; EM; 3.70 A; SO=1-151.
DR PDB; 6Q8Y; EM; 3.10 A; Y=2-151.
DR PDB; 6RBD; EM; 3.47 A; N=1-151.
DR PDB; 6RBE; EM; 3.80 A; N=1-151.
DR PDB; 6S47; EM; 3.28 A; BO=2-151.
DR PDB; 6SNT; EM; 2.80 A; N=1-151.
DR PDB; 6SV4; EM; 3.30 A; Y/Yb/Yc=1-151.
DR PDB; 6T4Q; EM; 2.60 A; SN=2-151.
DR PDB; 6T7I; EM; 3.20 A; SN=1-151.
DR PDB; 6T7T; EM; 3.10 A; SN=1-151.
DR PDB; 6T83; EM; 4.00 A; Nb/o=1-151.
DR PDB; 6TB3; EM; 2.80 A; Y=2-151.
DR PDB; 6TNU; EM; 3.10 A; Y=2-151.
DR PDB; 6WDR; EM; 3.70 A; N=2-151.
DR PDB; 6WOO; EM; 2.90 A; NN=2-151.
DR PDB; 6XIQ; EM; 4.20 A; AD=1-151.
DR PDB; 6XIR; EM; 3.20 A; AD=1-151.
DR PDB; 6Y7C; EM; 3.80 A; N=1-151.
DR PDB; 6Z6J; EM; 3.40 A; SN=1-151.
DR PDB; 6Z6K; EM; 3.40 A; SN=1-151.
DR PDB; 6ZCE; EM; 5.30 A; O=1-151.
DR PDB; 6ZQA; EM; 4.40 A; DN=1-151.
DR PDB; 6ZQB; EM; 3.90 A; DN=1-151.
DR PDB; 6ZQC; EM; 3.80 A; DN=1-151.
DR PDB; 6ZQD; EM; 3.80 A; DN=1-151.
DR PDB; 6ZQE; EM; 7.10 A; DN=1-151.
DR PDB; 6ZQF; EM; 4.90 A; DN=1-151.
DR PDB; 6ZQG; EM; 3.50 A; DN=1-151.
DR PDB; 6ZU9; EM; 6.20 A; Y=1-151.
DR PDB; 6ZVI; EM; 3.00 A; v=2-151.
DR PDB; 7A1G; EM; 3.00 A; Y=2-151.
DR PDB; 7AJT; EM; 4.60 A; DN=1-151.
DR PDB; 7AJU; EM; 3.80 A; DN=1-151.
DR PDB; 7B7D; EM; 3.30 A; Y=2-151.
DR PDB; 7D4I; EM; 4.00 A; SO=1-151.
DR PDB; 7D5S; EM; 4.60 A; SO=1-151.
DR PDB; 7D5T; EM; 6.00 A; SO=1-151.
DR PDB; 7D63; EM; 12.30 A; SO=1-151.
DR PDB; 7NRC; EM; 3.90 A; SY=2-151.
DR PDB; 7NRD; EM; 4.36 A; SY=2-151.
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; 5I4L; -.
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; 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; 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; 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; 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; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P05756; -.
DR SMR; P05756; -.
DR BioGRID; 32119; 670.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR IntAct; P05756; 60.
DR MINT; P05756; -.
DR STRING; 4932.YDR064W; -.
DR iPTMnet; P05756; -.
DR MaxQB; P05756; -.
DR PaxDb; P05756; -.
DR PRIDE; P05756; -.
DR TopDownProteomics; P05756; -.
DR EnsemblFungi; YDR064W_mRNA; YDR064W; YDR064W.
DR GeneID; 851636; -.
DR KEGG; sce:YDR064W; -.
DR SGD; S000002471; RPS13.
DR VEuPathDB; FungiDB:YDR064W; -.
DR eggNOG; KOG0400; Eukaryota.
DR GeneTree; ENSGT00390000017491; -.
DR HOGENOM; CLU_090139_1_0_1; -.
DR InParanoid; P05756; -.
DR OMA; EEHPKDM; -.
DR BioCyc; YEAST:G3O-29671-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; P05756; -.
DR PRO; PR:P05756; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P05756; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; 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); IMP:SGD.
DR CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR HAMAP; MF_01343_A; Ribosomal_S15_A; 1.
DR InterPro; IPR012606; Ribosomal_S13/S15_N.
DR InterPro; IPR000589; Ribosomal_S15.
DR InterPro; IPR023029; Ribosomal_S15P.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR PANTHER; PTHR11885; PTHR11885; 1.
DR Pfam; PF08069; Ribosomal_S13_N; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SMART; SM01386; Ribosomal_S13_N; 1.
DR SMART; SM01387; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:6814480"
FT CHAIN 2..151
FT /note="40S ribosomal protein S13"
FT /id="PRO_0000115689"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 25
FT /note="W -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> C (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 86..104
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 109..131
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 151 AA; 17029 MW; 9AA9EFBEC837053D CRC64;
MGRMHSAGKG ISSSAIPYSR NAPAWFKLSS ESVIEQIVKY ARKGLTPSQI GVLLRDAHGV
TQARVITGNK IMRILKSNGL APEIPEDLYY LIKKAVSVRK HLERNRKDKD AKFRLILIES
RIHRLARYYR TVAVLPPNWK YESATASALV N
