RL10_YEAST
ID RL10_YEAST Reviewed; 221 AA.
AC P41805; D6VY76;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=60S ribosomal protein L10 {ECO:0000303|PubMed:9559554};
DE AltName: Full=L9;
DE AltName: Full=Large ribosomal subunit protein uL16 {ECO:0000303|PubMed:24524803};
DE AltName: Full=Ubiquinol-cytochrome C reductase complex subunit VI-requiring protein;
GN Name=RPL10 {ECO:0000303|PubMed:9559554}; Synonyms=GRC5, QSR1;
GN OrderedLocusNames=YLR075W;
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], AND MUTAGENESIS OF GLY-194.
RX PubMed=7730379; DOI=10.1074/jbc.270.17.9961;
RA Tron T., Yang M., Dick F.A., Schmitt M.E., Trumpower B.L.;
RT "QSR1, an essential yeast gene with a genetic relationship to a subunit of
RT the mitochondrial cytochrome bc1 complex, is homologous to a gene
RT implicated in eukaryotic cell differentiation.";
RL J. Biol. Chem. 270:9961-9970(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8789260;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<53::aid-yea886>3.0.co;2-m;
RA Koller H.T., Klade T., Ellinger A., Breitenbach M.;
RT "The yeast growth control gene GRC5 is highly homologous to the mammalian
RT putative tumor suppressor gene QM.";
RL Yeast 12:53-65(1996).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP IDENTIFICATION AS A RIBOSOMAL PROTEIN.
RX PubMed=9301022;
RX DOI=10.1002/(sici)1097-0061(19970930)13:12<1155::aid-yea166>3.0.co;2-o;
RA Nika J., Erickson F.L., Hannig E.M.;
RT "Ribosomal protein L9 is the product of GRC5, a homolog of the putative
RT tumor suppressor QM in S. cerevisiae.";
RL Yeast 13:1155-1166(1997).
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 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-205, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP 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 [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-40 AND LYS-101, 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 [13]
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 [14]
RP 3D-STRUCTURE MODELING OF 4-168, 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 [15]
RP 3D-STRUCTURE MODELING OF 2-169, 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 [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. {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).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC {ECO:0000305}.
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DR EMBL; U06952; AAA81534.1; -; Genomic_DNA.
DR EMBL; X78887; CAA55485.1; -; Genomic_DNA.
DR EMBL; Z73247; CAA97632.1; -; Genomic_DNA.
DR EMBL; AY693034; AAT93053.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09392.1; -; Genomic_DNA.
DR PIR; A57296; A57296.
DR RefSeq; NP_013176.1; NM_001181962.1.
DR PDB; 3J6X; EM; 6.10 A; 50=1-221.
DR PDB; 3J6Y; EM; 6.10 A; 50=1-221.
DR PDB; 3J77; EM; 6.20 A; 60=1-221.
DR PDB; 3J78; EM; 6.30 A; 60=1-221.
DR PDB; 4U3M; X-ray; 3.00 A; M0/m0=2-221.
DR PDB; 4U3N; X-ray; 3.20 A; M0/m0=2-221.
DR PDB; 4U3U; X-ray; 2.90 A; M0/m0=2-221.
DR PDB; 4U4N; X-ray; 3.10 A; M0/m0=2-221.
DR PDB; 4U4O; X-ray; 3.60 A; M0/m0=2-221.
DR PDB; 4U4Q; X-ray; 3.00 A; M0/m0=2-221.
DR PDB; 4U4R; X-ray; 2.80 A; M0/m0=2-221.
DR PDB; 4U4U; X-ray; 3.00 A; M0/m0=2-221.
DR PDB; 4U4Y; X-ray; 3.20 A; M0/m0=2-221.
DR PDB; 4U4Z; X-ray; 3.10 A; M0/m0=2-221.
DR PDB; 4U50; X-ray; 3.20 A; M0/m0=2-221.
DR PDB; 4U51; X-ray; 3.20 A; M0/m0=2-221.
DR PDB; 4U52; X-ray; 3.00 A; M0/m0=2-221.
DR PDB; 4U53; X-ray; 3.30 A; M0/m0=2-221.
DR PDB; 4U55; X-ray; 3.20 A; M0/m0=2-221.
DR PDB; 4U56; X-ray; 3.45 A; M0/m0=2-221.
DR PDB; 4U6F; X-ray; 3.10 A; M0/m0=2-221.
DR PDB; 4V4B; EM; 11.70 A; BI=1-168.
DR PDB; 4V6I; EM; 8.80 A; BI=1-221.
DR PDB; 4V7R; X-ray; 4.00 A; BJ/DJ=1-221.
DR PDB; 4V88; X-ray; 3.00 A; BI/DI=1-221.
DR PDB; 4V8T; EM; 8.10 A; I=1-221.
DR PDB; 4V8Y; EM; 4.30 A; BI=2-221.
DR PDB; 4V8Z; EM; 6.60 A; BI=2-221.
DR PDB; 4V91; EM; 3.70 A; I=1-221.
DR PDB; 4ZOX; X-ray; 1.60 A; B=1-20.
DR PDB; 5APN; EM; 3.91 A; I=1-221.
DR PDB; 5APO; EM; 3.41 A; I=1-221.
DR PDB; 5DAT; X-ray; 3.15 A; M0/m0=2-221.
DR PDB; 5DC3; X-ray; 3.25 A; M0/m0=2-221.
DR PDB; 5DGE; X-ray; 3.45 A; M0/m0=2-221.
DR PDB; 5DGF; X-ray; 3.30 A; M0/m0=2-221.
DR PDB; 5DGV; X-ray; 3.10 A; M0/m0=2-221.
DR PDB; 5FCI; X-ray; 3.40 A; M0/m0=2-221.
DR PDB; 5FCJ; X-ray; 3.10 A; M0/m0=2-221.
DR PDB; 5GAK; EM; 3.88 A; s=1-221.
DR PDB; 5I4L; X-ray; 3.10 A; M0/m0=1-221.
DR PDB; 5JUO; EM; 4.00 A; N=1-221.
DR PDB; 5JUP; EM; 3.50 A; N=1-221.
DR PDB; 5JUS; EM; 4.20 A; N=1-221.
DR PDB; 5JUT; EM; 4.00 A; N=1-221.
DR PDB; 5JUU; EM; 4.00 A; N=1-221.
DR PDB; 5LYB; X-ray; 3.25 A; M0/m0=2-221.
DR PDB; 5M1J; EM; 3.30 A; I5=2-221.
DR PDB; 5MC6; EM; 3.80 A; BD=1-221.
DR PDB; 5MEI; X-ray; 3.50 A; CL/r=2-221.
DR PDB; 5NDG; X-ray; 3.70 A; M0/m0=1-221.
DR PDB; 5NDV; X-ray; 3.30 A; M0/m0=1-221.
DR PDB; 5NDW; X-ray; 3.70 A; M0/m0=1-221.
DR PDB; 5OBM; X-ray; 3.40 A; M0/m0=1-221.
DR PDB; 5ON6; X-ray; 3.10 A; CL/r=2-221.
DR PDB; 5T62; EM; 3.30 A; L=1-221.
DR PDB; 5T6R; EM; 4.50 A; L=1-221.
DR PDB; 5TBW; X-ray; 3.00 A; CL/r=2-221.
DR PDB; 5TGA; X-ray; 3.30 A; M0/m0=2-221.
DR PDB; 5TGM; X-ray; 3.50 A; M0/m0=2-221.
DR PDB; 6GQ1; EM; 4.40 A; I=2-221.
DR PDB; 6GQB; EM; 3.90 A; I=2-221.
DR PDB; 6GQV; EM; 4.00 A; I=2-221.
DR PDB; 6HD7; EM; 3.40 A; s=1-221.
DR PDB; 6HHQ; X-ray; 3.10 A; CL/r=1-221.
DR PDB; 6I7O; EM; 5.30 A; BD/YD=1-221.
DR PDB; 6N8O; EM; 3.50 A; Z=1-221.
DR PDB; 6OIG; EM; 3.80 A; I=2-221.
DR PDB; 6Q8Y; EM; 3.10 A; BD=2-221.
DR PDB; 6QT0; EM; 3.40 A; q=1-221.
DR PDB; 6QTZ; EM; 3.50 A; q=1-221.
DR PDB; 6R84; EM; 3.60 A; s=2-221.
DR PDB; 6R86; EM; 3.40 A; s=2-221.
DR PDB; 6R87; EM; 3.40 A; s=2-221.
DR PDB; 6RI5; EM; 3.30 A; q=1-221.
DR PDB; 6S47; EM; 3.28 A; AL=2-221.
DR PDB; 6SNT; EM; 2.80 A; p=1-221.
DR PDB; 6SV4; EM; 3.30 A; BD/YD/ZD=1-221.
DR PDB; 6T4Q; EM; 2.60 A; LI=2-219.
DR PDB; 6T7I; EM; 3.20 A; LI=1-221.
DR PDB; 6T7T; EM; 3.10 A; LI=1-221.
DR PDB; 6T83; EM; 4.00 A; Iy/La=1-221.
DR PDB; 6TB3; EM; 2.80 A; BD=2-219.
DR PDB; 6TNU; EM; 3.10 A; BD=2-219.
DR PDB; 6WOO; EM; 2.90 A; I=3-218.
DR PDB; 6Z6J; EM; 3.40 A; LI=1-221.
DR PDB; 6Z6K; EM; 3.40 A; LI=1-221.
DR PDB; 7AZY; EM; 2.88 A; o=1-221.
DR PDB; 7B7D; EM; 3.30 A; LL=2-219.
DR PDB; 7NRC; EM; 3.90 A; LL=2-219.
DR PDB; 7NRD; EM; 4.36 A; LL=2-219.
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; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V91; -.
DR PDBsum; 4ZOX; -.
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; 5GAK; -.
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; 5T62; -.
DR PDBsum; 5T6R; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6RI5; -.
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; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P41805; -.
DR SMR; P41805; -.
DR BioGRID; 31349; 420.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-2507N; -.
DR IntAct; P41805; 93.
DR MINT; P41805; -.
DR STRING; 4932.YLR075W; -.
DR CarbonylDB; P41805; -.
DR iPTMnet; P41805; -.
DR MaxQB; P41805; -.
DR PaxDb; P41805; -.
DR PRIDE; P41805; -.
DR EnsemblFungi; YLR075W_mRNA; YLR075W; YLR075W.
DR GeneID; 850764; -.
DR KEGG; sce:YLR075W; -.
DR SGD; S000004065; RPL10.
DR VEuPathDB; FungiDB:YLR075W; -.
DR eggNOG; KOG0857; Eukaryota.
DR GeneTree; ENSGT00390000003897; -.
DR HOGENOM; CLU_084051_0_0_1; -.
DR InParanoid; P41805; -.
DR OMA; HHVIREN; -.
DR BioCyc; YEAST:G3O-32227-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 ChiTaRS; RPL10; yeast.
DR EvolutionaryTrace; P41805; -.
DR PRO; PR:P41805; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P41805; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
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 GO; GO:0006415; P:translational termination; IMP:SGD.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR InterPro; IPR001197; Ribosomal_L10e.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR018255; Ribosomal_L10e_CS.
DR PANTHER; PTHR11726; PTHR11726; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PIRSF; PIRSF005590; Ribosomal_L10; 1.
DR SUPFAM; SSF54686; SSF54686; 1.
DR TIGRFAMs; TIGR00279; uL16_euk_arch; 1.
DR PROSITE; PS01257; RIBOSOMAL_L10E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..221
FT /note="60S ribosomal protein L10"
FT /id="PRO_0000147129"
FT REPEAT 167..181
FT /note="1"
FT REPEAT 200..216
FT /note="2"
FT REGION 167..216
FT /note="2 X 15-17 AA approximate repeats"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 194
FT /note="G->D: In QSR1-1; synthetic lethal."
FT /evidence="ECO:0000269|PubMed:7730379"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:4ZOX"
SQ SEQUENCE 221 AA; 25361 MW; 6FF976A3800F347D CRC64;
MARRPARCYR YQKNKPYPKS RYNRAVPDSK IRIYDLGKKK ATVDEFPLCV HLVSNELEQL
SSEALEAARI CANKYMTTVS GRDAFHLRVR VHPFHVLRIN KMLSCAGADR LQQGMRGAWG
KPHGLAARVD IGQIIFSVRT KDSNKDVVVE GLRRARYKFP GQQKIILSKK WGFTNLDRPE
YLKKREAGEV KDDGAFVKFL SKKGSLENNI REFPEYFAAQ A
