RL29_YEAST
ID RL29_YEAST Reviewed; 59 AA.
AC P05747; A2TBN8; D6VTR4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=60S ribosomal protein L29 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL29 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YL43;
GN Name=RPL29 {ECO:0000303|PubMed:9559554}; Synonyms=YL43;
GN OrderedLocusNames=YFR032C-A; ORFNames=YFR032BW;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-47.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [5]
RP PROTEIN SEQUENCE OF 2-40, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=18782943; DOI=10.1007/bf00341461;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence
RT characterization of twenty-four proteins from cytoplasmic ribosomes.";
RL Mol. Gen. Genet. 195:544-546(1984).
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.
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 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 [9]
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 [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY MASS
RP 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 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 [14]
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 -!- MISCELLANEOUS: Present with 51100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family.
CC {ECO:0000305}.
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DR EMBL; D50617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY558472; AAS56798.1; -; Genomic_DNA.
DR EMBL; EF123141; ABM97485.1; -; mRNA.
DR EMBL; BK006940; DAA12474.1; -; Genomic_DNA.
DR PIR; S71066; S71066.
DR RefSeq; NP_116690.3; NM_001184311.3.
DR PDB; 3J6X; EM; 6.10 A; 69=1-59.
DR PDB; 3J6Y; EM; 6.10 A; 69=1-59.
DR PDB; 3J77; EM; 6.20 A; 79=1-59.
DR PDB; 3J78; EM; 6.30 A; 79=1-59.
DR PDB; 4U3M; X-ray; 3.00 A; N9/n9=2-59.
DR PDB; 4U3N; X-ray; 3.20 A; N9/n9=2-59.
DR PDB; 4U3U; X-ray; 2.90 A; N9/n9=2-59.
DR PDB; 4U4N; X-ray; 3.10 A; N9/n9=2-59.
DR PDB; 4U4O; X-ray; 3.60 A; N9/n9=2-59.
DR PDB; 4U4Q; X-ray; 3.00 A; N9/n9=2-59.
DR PDB; 4U4R; X-ray; 2.80 A; N9/n9=2-59.
DR PDB; 4U4U; X-ray; 3.00 A; N9/n9=2-59.
DR PDB; 4U4Y; X-ray; 3.20 A; N9/n9=2-59.
DR PDB; 4U4Z; X-ray; 3.10 A; N9/n9=2-59.
DR PDB; 4U50; X-ray; 3.20 A; N9/n9=2-59.
DR PDB; 4U51; X-ray; 3.20 A; N9/n9=2-59.
DR PDB; 4U52; X-ray; 3.00 A; N9/n9=2-59.
DR PDB; 4U53; X-ray; 3.30 A; N9/n9=2-59.
DR PDB; 4U55; X-ray; 3.20 A; N9/n9=2-59.
DR PDB; 4U56; X-ray; 3.45 A; N9/n9=2-59.
DR PDB; 4U6F; X-ray; 3.10 A; N9/n9=2-59.
DR PDB; 4V6I; EM; 8.80 A; Bd=1-59.
DR PDB; 4V88; X-ray; 3.00 A; Bb/Db=1-59.
DR PDB; 4V8T; EM; 8.10 A; b=1-59.
DR PDB; 4V8Y; EM; 4.30 A; Bb=2-59.
DR PDB; 4V8Z; EM; 6.60 A; Bb=2-59.
DR PDB; 4V91; EM; 3.70 A; b=1-59.
DR PDB; 5APN; EM; 3.91 A; b=1-59.
DR PDB; 5APO; EM; 3.41 A; b=1-59.
DR PDB; 5DAT; X-ray; 3.15 A; N9/n9=2-59.
DR PDB; 5DC3; X-ray; 3.25 A; N9/n9=2-59.
DR PDB; 5DGE; X-ray; 3.45 A; N9/n9=2-59.
DR PDB; 5DGF; X-ray; 3.30 A; N9/n9=2-59.
DR PDB; 5DGV; X-ray; 3.10 A; N9/n9=2-59.
DR PDB; 5FCI; X-ray; 3.40 A; N9/n9=2-59.
DR PDB; 5FCJ; X-ray; 3.10 A; N9/n9=2-59.
DR PDB; 5GAK; EM; 3.88 A; d=1-59.
DR PDB; 5H4P; EM; 3.07 A; b=1-59.
DR PDB; 5I4L; X-ray; 3.10 A; N9/n9=2-59.
DR PDB; 5JUO; EM; 4.00 A; GA=1-59.
DR PDB; 5JUP; EM; 3.50 A; GA=1-59.
DR PDB; 5JUS; EM; 4.20 A; GA=1-59.
DR PDB; 5JUT; EM; 4.00 A; GA=1-59.
DR PDB; 5JUU; EM; 4.00 A; GA=1-59.
DR PDB; 5LYB; X-ray; 3.25 A; N9/n9=2-59.
DR PDB; 5M1J; EM; 3.30 A; b5=2-59.
DR PDB; 5MC6; EM; 3.80 A; AV=1-59.
DR PDB; 5MEI; X-ray; 3.50 A; AC/DD=2-59.
DR PDB; 5NDG; X-ray; 3.70 A; N9/n9=2-59.
DR PDB; 5NDV; X-ray; 3.30 A; N9/n9=2-59.
DR PDB; 5NDW; X-ray; 3.70 A; N9/n9=2-59.
DR PDB; 5OBM; X-ray; 3.40 A; N9/n9=2-59.
DR PDB; 5ON6; X-ray; 3.10 A; AC/DD=2-59.
DR PDB; 5T62; EM; 3.30 A; o=1-59.
DR PDB; 5T6R; EM; 4.50 A; o=1-59.
DR PDB; 5TBW; X-ray; 3.00 A; AC/DD=2-59.
DR PDB; 5TGA; X-ray; 3.30 A; N9/n9=2-59.
DR PDB; 5TGM; X-ray; 3.50 A; N9/n9=2-59.
DR PDB; 6GQ1; EM; 4.40 A; b=2-59.
DR PDB; 6GQB; EM; 3.90 A; b=2-59.
DR PDB; 6GQV; EM; 4.00 A; b=2-59.
DR PDB; 6HD7; EM; 3.40 A; d=1-59.
DR PDB; 6HHQ; X-ray; 3.10 A; AC/DD=1-59.
DR PDB; 6I7O; EM; 5.30 A; AV/XV=2-59.
DR PDB; 6N8J; EM; 3.50 A; o=1-59.
DR PDB; 6N8K; EM; 3.60 A; o=1-59.
DR PDB; 6N8L; EM; 3.60 A; o=1-59.
DR PDB; 6N8M; EM; 3.50 A; o=1-59.
DR PDB; 6N8N; EM; 3.80 A; o=1-59.
DR PDB; 6N8O; EM; 3.50 A; o=1-59.
DR PDB; 6OIG; EM; 3.80 A; b=2-59.
DR PDB; 6Q8Y; EM; 3.10 A; AV=2-59.
DR PDB; 6QIK; EM; 3.10 A; a=1-59.
DR PDB; 6QT0; EM; 3.40 A; a=1-59.
DR PDB; 6QTZ; EM; 3.50 A; a=1-59.
DR PDB; 6R84; EM; 3.60 A; d=2-59.
DR PDB; 6R86; EM; 3.40 A; d=2-59.
DR PDB; 6R87; EM; 3.40 A; d=2-59.
DR PDB; 6RI5; EM; 3.30 A; a=1-59.
DR PDB; 6RZZ; EM; 3.20 A; a=1-59.
DR PDB; 6S05; EM; 3.90 A; a=1-59.
DR PDB; 6S47; EM; 3.28 A; Ad=2-59.
DR PDB; 6SNT; EM; 2.80 A; ao=1-59.
DR PDB; 6SV4; EM; 3.30 A; AV/XV/zV=1-59.
DR PDB; 6T4Q; EM; 2.60 A; Lb=2-59.
DR PDB; 6T7I; EM; 3.20 A; Lb=1-59.
DR PDB; 6T7T; EM; 3.10 A; Lb=1-59.
DR PDB; 6T83; EM; 4.00 A; M/by=1-59.
DR PDB; 6TB3; EM; 2.80 A; AV=2-59.
DR PDB; 6TNU; EM; 3.10 A; AV=2-59.
DR PDB; 6WOO; EM; 2.90 A; b=3-59.
DR PDB; 6Z6J; EM; 3.40 A; Lb=1-59.
DR PDB; 6Z6K; EM; 3.40 A; Lb=1-59.
DR PDB; 7AZY; EM; 2.88 A; W=1-59.
DR PDB; 7B7D; EM; 3.30 A; LX=2-59.
DR PDB; 7NRC; EM; 3.90 A; Ld=2-59.
DR PDB; 7NRD; EM; 4.36 A; Ld=2-59.
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; 4V6I; -.
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; 5GAK; -.
DR PDBsum; 5H4P; -.
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; 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; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P05747; -.
DR SMR; P05747; -.
DR BioGRID; 31189; 206.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR IntAct; P05747; 5.
DR STRING; 4932.YFR032C-A; -.
DR iPTMnet; P05747; -.
DR MaxQB; P05747; -.
DR PaxDb; P05747; -.
DR PRIDE; P05747; -.
DR EnsemblFungi; YFR032C-A_mRNA; YFR032C-A; YFR032C-A.
DR GeneID; 850592; -.
DR KEGG; sce:YFR032C-A; -.
DR SGD; S000006437; RPL29.
DR VEuPathDB; FungiDB:YFR032C-A; -.
DR eggNOG; KOG3504; Eukaryota.
DR GeneTree; ENSGT00390000007084; -.
DR HOGENOM; CLU_169255_2_0_1; -.
DR InParanoid; P05747; -.
DR OMA; RNQKFCK; -.
DR BioCyc; YEAST:G3O-30506-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; RPL29; yeast.
DR PRO; PR:P05747; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P05747; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD.
DR InterPro; IPR002673; Ribosomal_L29e.
DR PANTHER; PTHR12884; PTHR12884; 1.
DR Pfam; PF01779; Ribosomal_L29e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:18782943"
FT CHAIN 2..59
FT /note="60S ribosomal protein L29"
FT /id="PRO_0000219141"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 37..55
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 59 AA; 6669 MW; ACED5822295F53F7 CRC64;
MAKSKNHTAH NQTRKAHRNG IKKPKTYKYP SLKGVDPKFR RNHKHALHGT AKALAAAKK
