RL25_YEAST
ID RL25_YEAST Reviewed; 142 AA.
AC P04456; D6W1U1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=60S ribosomal protein L25 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein uL23 {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP16L;
DE AltName: Full=YL25;
DE AltName: Full=YP42';
GN Name=RPL25 {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YOL127W;
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=Carlsbergensis;
RX PubMed=6091033; DOI=10.1093/nar/12.17.6685;
RA Leer R.J., van Raamsdonk-Duin M.M.C., Hagendoorn M.J.M., Mager W.H.,
RA Planta R.J.;
RT "Structural comparison of yeast ribosomal protein genes.";
RL Nucleic Acids Res. 12:6685-6700(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896265;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1013::aid-yea980%3e3.0.co;2-5;
RA Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E.,
RA Arino J.;
RT "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome
RT XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase,
RT the ribosomal L25 gene and four new open reading frames.";
RL Yeast 12:1013-1020(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 PROTEIN SEQUENCE OF 2-21.
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 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 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 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 [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 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 [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 3D-STRUCTURE MODELING OF 60-136, 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 [14]
RP 3D-STRUCTURE MODELING OF 60-142, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=EJY251-11b;
RX PubMed=15542864; DOI=10.1074/mcp.m400154-mcp200;
RA Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,
RA Gygi S.P.;
RT "A proteomic strategy for gaining insights into protein sumoylation in
RT yeast.";
RL Mol. Cell. Proteomics 4:246-254(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (4.0 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 [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 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. uL23 is a major component of the universal docking site for
CC these factors at the polypeptide exit tunnel.
CC {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU). 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). uL23 is associated with the polypeptide
CC exit tunnel (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- INTERACTION:
CC P04456; Q01560: NPL3; NbExp=2; IntAct=EBI-15308, EBI-12114;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000305}.
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DR EMBL; U41293; AAC49465.1; -; Genomic_DNA.
DR EMBL; X01014; CAA25506.1; -; Genomic_DNA.
DR EMBL; Z74869; CAA99146.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10657.1; -; Genomic_DNA.
DR PIR; S63443; R5BY25.
DR RefSeq; NP_014514.1; NM_001183381.1.
DR PDB; 2WW9; EM; 8.60 A; K=1-142.
DR PDB; 2WWA; EM; 8.90 A; K=1-142.
DR PDB; 2WWB; EM; 6.48 A; K=1-142.
DR PDB; 3J6X; EM; 6.10 A; 65=1-142.
DR PDB; 3J6Y; EM; 6.10 A; 65=1-142.
DR PDB; 3J77; EM; 6.20 A; 75=1-142.
DR PDB; 3J78; EM; 6.30 A; 75=1-142.
DR PDB; 3JCT; EM; 3.08 A; X=1-142.
DR PDB; 4U3M; X-ray; 3.00 A; N5/n5=2-142.
DR PDB; 4U3N; X-ray; 3.20 A; N5/n5=2-142.
DR PDB; 4U3U; X-ray; 2.90 A; N5/n5=2-142.
DR PDB; 4U4N; X-ray; 3.10 A; N5/n5=2-142.
DR PDB; 4U4O; X-ray; 3.60 A; N5/n5=2-142.
DR PDB; 4U4Q; X-ray; 3.00 A; N5/n5=2-142.
DR PDB; 4U4R; X-ray; 2.80 A; N5/n5=2-142.
DR PDB; 4U4U; X-ray; 3.00 A; N5/n5=2-142.
DR PDB; 4U4Y; X-ray; 3.20 A; N5/n5=2-142.
DR PDB; 4U4Z; X-ray; 3.10 A; N5/n5=2-142.
DR PDB; 4U50; X-ray; 3.20 A; N5/n5=2-142.
DR PDB; 4U51; X-ray; 3.20 A; N5/n5=2-142.
DR PDB; 4U52; X-ray; 3.00 A; N5/n5=2-142.
DR PDB; 4U53; X-ray; 3.30 A; N5/n5=2-142.
DR PDB; 4U55; X-ray; 3.20 A; N5/n5=2-142.
DR PDB; 4U56; X-ray; 3.45 A; N5/n5=2-142.
DR PDB; 4U6F; X-ray; 3.10 A; N5/n5=2-142.
DR PDB; 4V4B; EM; 11.70 A; BT=60-142.
DR PDB; 4V6I; EM; 8.80 A; BX=1-142.
DR PDB; 4V7F; EM; 8.70 A; W=1-142.
DR PDB; 4V7R; X-ray; 4.00 A; BW/DW=1-142.
DR PDB; 4V88; X-ray; 3.00 A; BX/DX=1-142.
DR PDB; 4V8T; EM; 8.10 A; X=1-142.
DR PDB; 4V8Y; EM; 4.30 A; BX=2-142.
DR PDB; 4V8Z; EM; 6.60 A; BX=2-142.
DR PDB; 4V91; EM; 3.70 A; X=1-142.
DR PDB; 5APN; EM; 3.91 A; X=1-142.
DR PDB; 5APO; EM; 3.41 A; X=1-142.
DR PDB; 5DAT; X-ray; 3.15 A; N5/n5=2-142.
DR PDB; 5DC3; X-ray; 3.25 A; N5/n5=2-142.
DR PDB; 5DGE; X-ray; 3.45 A; N5/n5=2-142.
DR PDB; 5DGF; X-ray; 3.30 A; N5/n5=2-142.
DR PDB; 5DGV; X-ray; 3.10 A; N5/n5=2-142.
DR PDB; 5FCI; X-ray; 3.40 A; N5/n5=2-142.
DR PDB; 5FCJ; X-ray; 3.10 A; N5/n5=2-142.
DR PDB; 5FL8; EM; 9.50 A; X=1-142.
DR PDB; 5GAK; EM; 3.88 A; Z=1-142.
DR PDB; 5H4P; EM; 3.07 A; X=1-142.
DR PDB; 5I4L; X-ray; 3.10 A; N5/n5=22-142.
DR PDB; 5JCS; EM; 9.50 A; X=1-142.
DR PDB; 5JUO; EM; 4.00 A; CA=1-142.
DR PDB; 5JUP; EM; 3.50 A; CA=1-142.
DR PDB; 5JUS; EM; 4.20 A; CA=1-142.
DR PDB; 5JUT; EM; 4.00 A; CA=1-142.
DR PDB; 5JUU; EM; 4.00 A; CA=1-142.
DR PDB; 5LYB; X-ray; 3.25 A; N5/n5=22-142.
DR PDB; 5M1J; EM; 3.30 A; X5=22-142.
DR PDB; 5MC6; EM; 3.80 A; AH=1-142.
DR PDB; 5MEI; X-ray; 3.50 A; 8/CZ=22-142.
DR PDB; 5NDG; X-ray; 3.70 A; N5/n5=22-142.
DR PDB; 5NDV; X-ray; 3.30 A; N5/n5=23-142.
DR PDB; 5NDW; X-ray; 3.70 A; N5/n5=22-142.
DR PDB; 5OBM; X-ray; 3.40 A; N5/n5=22-142.
DR PDB; 5ON6; X-ray; 3.10 A; 8/CZ=22-142.
DR PDB; 5T62; EM; 3.30 A; k=1-142.
DR PDB; 5T6R; EM; 4.50 A; k=1-142.
DR PDB; 5TBW; X-ray; 3.00 A; 8/CZ=22-142.
DR PDB; 5TGA; X-ray; 3.30 A; N5/n5=22-142.
DR PDB; 5TGM; X-ray; 3.50 A; N5/n5=22-142.
DR PDB; 6CB1; EM; 4.60 A; X=1-142.
DR PDB; 6ELZ; EM; 3.30 A; X=1-142.
DR PDB; 6EM5; EM; 4.30 A; X=1-142.
DR PDB; 6FT6; EM; 3.90 A; X=1-142.
DR PDB; 6GQ1; EM; 4.40 A; X=22-142.
DR PDB; 6GQB; EM; 3.90 A; X=22-142.
DR PDB; 6GQV; EM; 4.00 A; X=22-142.
DR PDB; 6HD7; EM; 3.40 A; Z=1-142.
DR PDB; 6HHQ; X-ray; 3.10 A; 8/CZ=1-142.
DR PDB; 6I7O; EM; 5.30 A; AH/XH=23-142.
DR PDB; 6M62; EM; 3.20 A; X=1-142.
DR PDB; 6N8J; EM; 3.50 A; X=1-142.
DR PDB; 6N8K; EM; 3.60 A; X=1-142.
DR PDB; 6N8L; EM; 3.60 A; X=1-142.
DR PDB; 6N8M; EM; 3.50 A; k=1-142.
DR PDB; 6N8N; EM; 3.80 A; k=1-142.
DR PDB; 6N8O; EM; 3.50 A; k=1-142.
DR PDB; 6OIG; EM; 3.80 A; X=22-142.
DR PDB; 6Q8Y; EM; 3.10 A; AH=22-142.
DR PDB; 6QIK; EM; 3.10 A; W=1-142.
DR PDB; 6QT0; EM; 3.40 A; W=1-142.
DR PDB; 6QTZ; EM; 3.50 A; W=1-142.
DR PDB; 6R84; EM; 3.60 A; Z=22-142.
DR PDB; 6R86; EM; 3.40 A; Z=22-142.
DR PDB; 6R87; EM; 3.40 A; Z=22-142.
DR PDB; 6RI5; EM; 3.30 A; W=1-142.
DR PDB; 6RZZ; EM; 3.20 A; W=1-142.
DR PDB; 6S05; EM; 3.90 A; W=1-142.
DR PDB; 6S47; EM; 3.28 A; AZ=2-142.
DR PDB; 6SNT; EM; 2.80 A; as=1-142.
DR PDB; 6SV4; EM; 3.30 A; AH/XH/zH=1-142.
DR PDB; 6T4Q; EM; 2.60 A; LX=22-142.
DR PDB; 6T7I; EM; 3.20 A; LX=1-142.
DR PDB; 6T7T; EM; 3.10 A; LX=1-142.
DR PDB; 6T83; EM; 4.00 A; I/Xy=1-142.
DR PDB; 6TB3; EM; 2.80 A; AH=22-142.
DR PDB; 6TNU; EM; 3.10 A; AH=22-142.
DR PDB; 6WOO; EM; 2.90 A; X=22-142.
DR PDB; 6XIQ; EM; 4.20 A; X=1-142.
DR PDB; 6XIR; EM; 3.20 A; X=1-142.
DR PDB; 6YLG; EM; 3.00 A; X=1-142.
DR PDB; 6YLH; EM; 3.10 A; X=1-142.
DR PDB; 6YLX; EM; 3.90 A; X=1-142.
DR PDB; 6YLY; EM; 3.80 A; X=1-142.
DR PDB; 6Z6J; EM; 3.40 A; LX=1-142.
DR PDB; 6Z6K; EM; 3.40 A; LX=1-142.
DR PDB; 7AZY; EM; 2.88 A; I=1-142.
DR PDB; 7B7D; EM; 3.30 A; LT=22-142.
DR PDB; 7BT6; EM; 3.12 A; X=1-142.
DR PDB; 7BTB; EM; 3.22 A; X=1-142.
DR PDB; 7NRC; EM; 3.90 A; LZ=22-142.
DR PDB; 7NRD; EM; 4.36 A; LZ=22-142.
DR PDB; 7OF1; EM; 3.10 A; X=1-142.
DR PDB; 7OH3; EM; 3.40 A; X=1-142.
DR PDB; 7OHQ; EM; 3.10 A; X=1-142.
DR PDB; 7OHR; EM; 4.72 A; X=1-142.
DR PDB; 7OHV; EM; 3.90 A; X=1-142.
DR PDBsum; 2WW9; -.
DR PDBsum; 2WWA; -.
DR PDBsum; 2WWB; -.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3JCT; -.
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; 4V7F; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JCS; -.
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; 5T62; -.
DR PDBsum; 5T6R; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6N8M; -.
DR PDBsum; 6N8N; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6QIK; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6RI5; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6S05; -.
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; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHV; -.
DR AlphaFoldDB; P04456; -.
DR SMR; P04456; -.
DR BioGRID; 34248; 587.
DR DIP; DIP-7137N; -.
DR IntAct; P04456; 56.
DR MINT; P04456; -.
DR STRING; 4932.YOL127W; -.
DR iPTMnet; P04456; -.
DR MaxQB; P04456; -.
DR PaxDb; P04456; -.
DR PRIDE; P04456; -.
DR TopDownProteomics; P04456; -.
DR EnsemblFungi; YOL127W_mRNA; YOL127W; YOL127W.
DR GeneID; 853993; -.
DR KEGG; sce:YOL127W; -.
DR SGD; S000005487; RPL25.
DR VEuPathDB; FungiDB:YOL127W; -.
DR eggNOG; KOG1751; Eukaryota.
DR GeneTree; ENSGT00940000171037; -.
DR HOGENOM; CLU_037562_0_1_1; -.
DR InParanoid; P04456; -.
DR OMA; IPHVPRM; -.
DR BioCyc; YEAST:G3O-33522-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-72689; Formation of a pool of free 40S subunits.
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; P04456; -.
DR PRO; PR:P04456; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P04456; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_A; Ribosomal_L23_A; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR005633; Ribosomal_L23/L25_N.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR Pfam; PF03939; Ribosomal_L23eN; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921"
FT CHAIN 2..142
FT /note="60S ribosomal protein L25"
FT /id="PRO_0000129483"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15542864"
FT CONFLICT 106..112
FT /note="DVLKVNT -> NI (in Ref. 1; CAA25506)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4U4U"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4U55"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 142 AA; 15758 MW; E40ED3A4FB8CA9F5 CRC64;
MAPSAKATAA KKAVVKGTNG KKALKVRTSA TFRLPKTLKL ARAPKYASKA VPHYNRLDSY
KVIEQPITSE TAMKKVEDGN ILVFQVSMKA NKYQIKKAVK ELYEVDVLKV NTLVRPNGTK
KAYVRLTADY DALDIANRIG YI
