ID RLA0_YEAST Reviewed; 312 AA. AC P05317; D6VYX8; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S acidic ribosomal protein P0 {ECO:0000303|PubMed:9559554}; DE Short=A0; DE AltName: Full=L10e; GN Name=RPP0 {ECO:0000303|PubMed:9559554}; GN Synonyms=L10E, RPA0, RPL10E, RPLA0; OrderedLocusNames=YLR340W; GN ORFNames=L8300.8; 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 [MRNA]. RC STRAIN=IFO 40028; RX PubMed=3287327; DOI=10.1093/nar/16.8.3573; RA Mitsui K., Tsurugi K.; RT "cDNA and deduced amino acid sequence of 38 kDa-type acidic ribosomal RT protein A0 from Saccharomyces cerevisiae."; RL Nucleic Acids Res. 16:3573-3573(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2681177; DOI=10.1093/oxfordjournals.jbchem.a122836; RA Mitsui K., Nakagawa T., Tsurugi K.; RT "The gene and the primary structure of acidic ribosomal protein A0 from RT yeast Saccharomyces cerevisiae which shows partial homology to bacterial RT ribosomal protein L10."; RL J. Biochem. 106:223-227(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SR26-12C; RX PubMed=2404943; DOI=10.1128/jb.172.2.579-588.1990; RA Newton C.H., Shimmin L.C., Yee J., Dennis P.P.; RT "A family of genes encode the multiple forms of the Saccharomyces RT cerevisiae ribosomal proteins equivalent to the Escherichia coli L12 RT protein and a single form of the L10-equivalent ribosomal protein."; RL J. Bacteriol. 172:579-588(1990). RN [4] RP ERRATUM OF PUBMED:2404943. RX PubMed=2188966; DOI=10.1128/jb.172.6.3535.1990; RA Newton C.H., Shimmin L.C., Yee J., Dennis P.P.; RL J. Bacteriol. 172:3535-3535(1990). RN [5] 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 [6] 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 [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 PHOSPHORYLATION AT SER-302. RX PubMed=9843429; DOI=10.1021/bi981396i; RA Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G.; RT "Phosphorylation of ribosomal protein P0 is not essential for ribosome RT function but can affect translation."; RL Biochemistry 37:16620-16626(1998). RN [9] RP INTERACTION WITH YFL034W. RX PubMed=15286401; DOI=10.1007/bf02702559; RA Aruna K., Chakraborty T., Nambeesan S., Mannan A.B., Sehgal A., RA Balachandara S.R., Sharma S.; RT "Identification of a hypothetical membrane protein interactor of ribosomal RT phosphoprotein P0."; RL J. Biosci. 29:33-43(2004). RN [10] RP INTERACTION WITH RPP1A; RPP1B; RPP2A AND RPP2B. RX PubMed=16573688; DOI=10.1111/j.1365-2958.2006.05117.x; RA Krokowski D., Boguszewska A., Abramczyk D., Liljas A., Tchorzewski M., RA Grankowski N.; RT "Yeast ribosomal P0 protein has two separate binding sites for P1/P2 RT proteins."; RL Mol. Microbiol. 60:386-400(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, 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 SER-302, 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 SER-68 AND SER-302, 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-97 AND LYS-144, 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 [15] 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 [16] RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS). 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 (3.00 ANGSTROMS), SUBUNIT, AND 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. uL10 forms part of the P stalk that participates in recruiting CC G proteins to the ribosome. {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) (PubMed:9559554, PubMed:22096102). The 5 CC acidic ribosomal P-proteins form the stalk structure of the 60S CC subunit. They are organized as a pentameric complex in which uL10/P0 CC interacts with 2 heterodimers, P1A-P2B and P1B-P2A. uL10 directly CC interacts with 28S rRNA (PubMed:16573688). uL10 interacts with YFL034W CC (PubMed:15286401). {ECO:0000269|PubMed:15286401, CC ECO:0000269|PubMed:16573688, ECO:0000269|PubMed:22096102, CC ECO:0000305|PubMed:9559554}. CC -!- INTERACTION: CC P05317; P32324: EFT2; NbExp=3; IntAct=EBI-15447, EBI-6333; CC P05317; P05318: RPP1A; NbExp=3; IntAct=EBI-15447, EBI-15452; CC P05317; P10622: RPP1B; NbExp=2; IntAct=EBI-15447, EBI-15460; CC P05317; P05319: RPP2A; NbExp=2; IntAct=EBI-15447, EBI-15456; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 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; X06959; CAA30029.1; -; mRNA. DR EMBL; D00529; BAA00415.1; -; Genomic_DNA. DR EMBL; X13328; CAA31703.1; -; Genomic_DNA. DR EMBL; M26506; AAA34730.1; -; Genomic_DNA. DR EMBL; M37326; AAA34729.1; -; Genomic_DNA. DR EMBL; U19028; AAB67258.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09644.1; -; Genomic_DNA. DR PIR; S51343; R5BY0E. DR RefSeq; NP_013444.1; NM_001182229.1. DR PDB; 3J16; EM; -; G=1-312. DR PDB; 3J77; EM; 6.20 A; P0=1-312. DR PDB; 3J78; EM; 6.30 A; P0=1-312. DR PDB; 4U3M; X-ray; 3.00 A; p0=2-311. DR PDB; 4U3N; X-ray; 3.20 A; p0=2-312. DR PDB; 4U3U; X-ray; 2.90 A; p0=2-312. DR PDB; 4U4N; X-ray; 3.10 A; p0=2-312. DR PDB; 4U4O; X-ray; 3.60 A; p0=2-312. DR PDB; 4U4Q; X-ray; 3.00 A; p0=2-312. DR PDB; 4U4R; X-ray; 2.80 A; p0=2-312. DR PDB; 4U4U; X-ray; 3.00 A; p0=2-312. DR PDB; 4U4Y; X-ray; 3.20 A; p0=2-312. DR PDB; 4U4Z; X-ray; 3.10 A; p0=2-312. DR PDB; 4U50; X-ray; 3.20 A; p0=2-312. DR PDB; 4U51; X-ray; 3.20 A; p0=2-312. DR PDB; 4U52; X-ray; 3.00 A; p0=2-312. DR PDB; 4U53; X-ray; 3.30 A; p0=2-312. DR PDB; 4U55; X-ray; 3.20 A; p0=2-312. DR PDB; 4U56; X-ray; 3.45 A; p0=2-312. DR PDB; 4U6F; X-ray; 3.10 A; p0=2-312. DR PDB; 4V6I; EM; 8.80 A; Bs=1-312. DR PDB; 4V7R; X-ray; 4.00 A; DM=1-312. DR PDB; 4V88; X-ray; 3.00 A; Dq=1-312. DR PDB; 4V8T; EM; 8.10 A; q=1-312. DR PDB; 4V8Y; EM; 4.30 A; Bq=1-312. DR PDB; 4V8Z; EM; 6.60 A; Bq=1-237. DR PDB; 5APN; EM; 3.91 A; q=1-312. DR PDB; 5APO; EM; 3.41 A; q=1-312. DR PDB; 5DAT; X-ray; 3.15 A; p0=2-221. DR PDB; 5DC3; X-ray; 3.25 A; p0=2-312. DR PDB; 5DGE; X-ray; 3.45 A; p0=2-312. DR PDB; 5DGF; X-ray; 3.30 A; p0=1-312. DR PDB; 5DGV; X-ray; 3.10 A; p0=2-312. DR PDB; 5FCI; X-ray; 3.40 A; p0=2-311. DR PDB; 5FCJ; X-ray; 3.10 A; p0=2-312. DR PDB; 5I4L; X-ray; 3.10 A; p0=1-312. DR PDB; 5JUO; EM; 4.00 A; VA=1-312. DR PDB; 5JUP; EM; 3.50 A; VA=1-312. DR PDB; 5JUS; EM; 4.20 A; VA=1-312. DR PDB; 5JUT; EM; 4.00 A; VA=1-312. DR PDB; 5JUU; EM; 4.00 A; VA=1-312. DR PDB; 5LYB; X-ray; 3.25 A; p0=3-198. DR PDB; 5MEI; X-ray; 3.50 A; p0=2-221. DR PDB; 5NDG; X-ray; 3.70 A; p0=1-312. DR PDB; 5OBM; X-ray; 3.40 A; p0=1-312. DR PDB; 5ON6; X-ray; 3.10 A; p0=2-312. DR PDB; 5TBW; X-ray; 3.00 A; p0=3-221. DR PDB; 5TGA; X-ray; 3.30 A; p0=3-221. DR PDB; 5TGM; X-ray; 3.50 A; p0=1-312. DR PDB; 6GQ1; EM; 4.40 A; P0=5-193. DR PDB; 6GQB; EM; 3.90 A; P0=5-193. DR PDB; 6GQV; EM; 4.00 A; P0=5-193. DR PDB; 6HHQ; X-ray; 3.10 A; p0=1-312. DR PDB; 6I7O; EM; 5.30 A; BU/YU=1-312. DR PDB; 6OIG; EM; 3.80 A; q=3-198. DR PDB; 6R84; EM; 3.60 A; r=3-199. DR PDB; 6R86; EM; 3.40 A; r=3-199. DR PDB; 6R87; EM; 3.40 A; r=3-199. DR PDB; 6SV4; EM; 3.30 A; BU/YU/ZU=1-312. DR PDB; 6T83; EM; 4.00 A; ba=2-312. DR PDB; 6WOO; EM; 2.90 A; r=6-200. DR PDB; 7TOO; EM; 2.70 A; ALP0=1-198. DR PDB; 7TOP; EM; 2.40 A; ALP0=1-198. DR PDB; 7U6V; EM; 4.10 A; P=307-312. DR PDB; 8AAF; EM; 2.50 A; 0=1-312. DR PDB; 8AGT; EM; 2.60 A; 0=1-312. DR PDB; 8AGU; EM; 2.70 A; 0=1-312. DR PDB; 8AGV; EM; 2.60 A; 0=1-312. DR PDB; 8AGW; EM; 2.60 A; 0=1-312. DR PDB; 8AGX; EM; 2.40 A; 0=1-312. DR PDB; 8AGZ; EM; 2.60 A; 0=1-312. DR PDB; 8CCS; EM; 1.97 A; DD=1-312. DR PDB; 8CDL; EM; 2.72 A; DD=1-312. DR PDB; 8CDR; EM; 2.04 A; DD=1-312. DR PDB; 8CEH; EM; 2.05 A; DD=1-312. DR PDB; 8CF5; EM; 2.71 A; DD=1-312. DR PDB; 8CG8; EM; 2.57 A; DD=1-312. DR PDB; 8CGN; EM; 2.28 A; DD=1-312. DR PDB; 8CIV; EM; 2.47 A; DD=1-312. DR PDB; 8CKU; EM; 3.11 A; DD=1-312. DR PDB; 8CMJ; EM; 3.79 A; DD=1-312. DR PDB; 8EUB; EM; 2.52 A; VA=1-312. DR PDB; 8EVQ; EM; 2.72 A; V=1-312. DR PDB; 8EVR; EM; 2.87 A; V=1-312. DR PDB; 8EVS; EM; 2.62 A; V=1-312. DR PDB; 8EWB; EM; 2.87 A; V=1-312. DR PDBsum; 3J16; -. 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; 4V8T; -. DR PDBsum; 4V8Y; -. DR PDBsum; 4V8Z; -. 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; 5I4L; -. DR PDBsum; 5JUO; -. DR PDBsum; 5JUP; -. DR PDBsum; 5JUS; -. DR PDBsum; 5JUT; -. DR PDBsum; 5JUU; -. DR PDBsum; 5LYB; -. DR PDBsum; 5MEI; -. DR PDBsum; 5NDG; -. DR PDBsum; 5OBM; -. DR PDBsum; 5ON6; -. DR PDBsum; 5TBW; -. DR PDBsum; 5TGA; -. DR PDBsum; 5TGM; -. DR PDBsum; 6GQ1; -. DR PDBsum; 6GQB; -. DR PDBsum; 6GQV; -. DR PDBsum; 6HHQ; -. DR PDBsum; 6I7O; -. DR PDBsum; 6OIG; -. DR PDBsum; 6R84; -. DR PDBsum; 6R86; -. DR PDBsum; 6R87; -. DR PDBsum; 6SV4; -. DR PDBsum; 6T83; -. DR PDBsum; 6WOO; -. DR PDBsum; 7TOO; -. DR PDBsum; 7TOP; -. DR PDBsum; 7U6V; -. DR PDBsum; 8AAF; -. DR PDBsum; 8AGT; -. DR PDBsum; 8AGU; -. DR PDBsum; 8AGV; -. DR PDBsum; 8AGW; -. DR PDBsum; 8AGX; -. DR PDBsum; 8AGZ; -. DR PDBsum; 8CCS; -. DR PDBsum; 8CDL; -. DR PDBsum; 8CDR; -. DR PDBsum; 8CEH; -. DR PDBsum; 8CF5; -. DR PDBsum; 8CG8; -. DR PDBsum; 8CGN; -. DR PDBsum; 8CIV; -. DR PDBsum; 8CKU; -. DR PDBsum; 8CMJ; -. DR PDBsum; 8EUB; -. DR PDBsum; 8EVQ; -. DR PDBsum; 8EVR; -. DR PDBsum; 8EVS; -. DR PDBsum; 8EWB; -. DR AlphaFoldDB; P05317; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-16563; -. DR EMDB; EMD-16591; -. DR EMDB; EMD-16594; -. DR EMDB; EMD-16609; -. DR EMDB; EMD-16616; -. DR EMDB; EMD-16634; -. DR EMDB; EMD-16648; -. DR EMDB; EMD-16684; -. DR EMDB; EMD-16702; -. DR EMDB; EMD-16729; -. DR EMDB; EMD-20077; -. DR EMDB; EMD-21859; -. DR EMDB; EMD-26033; -. DR EMDB; EMD-26034; -. DR EMDB; EMD-28610; -. DR EMDB; EMD-28633; -. DR EMDB; EMD-28634; -. DR EMDB; EMD-28635; -. DR EMDB; EMD-28642; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4751; -. DR EMDB; EMD-4752; -. DR EMDB; EMD-4753; -. DR SMR; P05317; -. DR BioGRID; 31602; 459. DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit. DR DIP; DIP-1582N; -. DR IntAct; P05317; 289. DR MINT; P05317; -. DR STRING; 4932.YLR340W; -. DR iPTMnet; P05317; -. DR MaxQB; P05317; -. DR PaxDb; 4932-YLR340W; -. DR PeptideAtlas; P05317; -. DR TopDownProteomics; P05317; -. DR EnsemblFungi; YLR340W_mRNA; YLR340W; YLR340W. DR GeneID; 851052; -. DR KEGG; sce:YLR340W; -. DR AGR; SGD:S000004332; -. DR SGD; S000004332; RPP0. DR VEuPathDB; FungiDB:YLR340W; -. DR eggNOG; KOG0815; Eukaryota. DR GeneTree; ENSGT00390000017839; -. DR HOGENOM; CLU_053173_1_1_1; -. DR InParanoid; P05317; -. DR OMA; DMNPFKL; -. DR OrthoDB; 168365at2759; -. DR BioCyc; YEAST:G3O-32417-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-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 BioGRID-ORCS; 851052; 6 hits in 10 CRISPR screens. DR PRO; PR:P05317; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P05317; Protein. DR GO; GO:0030686; C:90S preribosome; HDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:SGD. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD. DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD. DR CDD; cd05795; Ribosomal_P0_L10e; 1. DR Gene3D; 3.30.70.1730; -; 1. DR Gene3D; 3.90.105.20; -; 1. DR InterPro; IPR001790; Ribosomal_uL10. DR InterPro; IPR040637; Ribosomal_uL10-like_insert. DR InterPro; IPR043164; Ribosomal_uL10-like_insert_sf. DR InterPro; IPR043141; Ribosomal_uL10-like_sf. DR InterPro; IPR030670; uL10_eukaryotes. DR PANTHER; PTHR45699; 60S ACIDIC RIBOSOMAL PROTEIN P0; 1. DR PANTHER; PTHR45699:SF3; 60S ACIDIC RIBOSOMAL PROTEIN P0; 1. DR Pfam; PF00428; Ribosomal_60s; 1. DR Pfam; PF00466; Ribosomal_L10; 1. DR Pfam; PF17777; RL10P_insert; 1. DR PIRSF; PIRSF039087; L10E; 1. DR SUPFAM; SSF160369; Ribosomal protein L10-like; 1. DR SWISS-2DPAGE; P05317; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT CHAIN 1..312 FT /note="Large ribosomal subunit protein uL10" FT /id="PRO_0000154786" FT REGION 199..230 FT /note="Interaction with P1A-P2B" FT REGION 231..258 FT /note="Interaction with P1B-P2A" FT REGION 278..312 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 292..312 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 68 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 302 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:9843429, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT CROSSLNK 14 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 97 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 144 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CONFLICT 83 FT /note="N -> Y (in Ref. 1; CAA30029 and 2; FT BAA00415/CAA31703)" FT /evidence="ECO:0000305" FT HELIX 4..21 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 23..29 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 35..43 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:4U3U" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 56..64 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 82..89 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 93..102 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 186..194 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:4U3M" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 210..213 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 214..219 FT /evidence="ECO:0007829|PDB:4U4R" SQ SEQUENCE 312 AA; 33717 MW; 109ECC90F7C8B68E CRC64; MGGIREKKAE YFAKLREYLE EYKSLFVVGV DNVSSQQMHE VRKELRGRAV VLMGKNTMVR RAIRGFLSDL PDFEKLLPFV KGNVGFVFTN EPLTEIKNVI VSNRVAAPAR AGAVAPEDIW VRAVNTGMEP GKTSFFQALG VPTKIARGTI EIVSDVKVVD AGNKVGQSEA SLLNLLNISP FTFGLTVVQV YDNGQVFPSS ILDITDEELV SHFVSAVSTI ASISLAIGYP TLPSVGHTLI NNYKDLLAVA IAASYHYPEI EDLVDRIENP EKYAAAAPAA TSAASGDAAP AEEAAAEEEE ESDDDMGFGL FD //