RL29_HUMAN
ID RL29_HUMAN Reviewed; 159 AA.
AC P47914; A8K0H3; B2R4M8; Q6IPY3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=60S ribosomal protein L29;
DE AltName: Full=Cell surface heparin-binding protein HIP;
DE AltName: Full=Large ribosomal subunit protein eL29 {ECO:0000303|PubMed:24524803};
GN Name=RPL29;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Law P.T., Tsui S.K., Lee C.Y., Waye M.M.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8597591; DOI=10.1016/0167-4781(95)00224-3;
RA Law P.T., Tsui S.K.W., Lam W.Y., Luk S.C., Hwang D.M., Liew C.C.,
RA Lee C.-Y., Fung K.-P., Waye M.M.Y.;
RT "A novel cDNA encoding a human homologue of ribosomal protein L29.";
RL Biochim. Biophys. Acta 1305:105-108(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8662616; DOI=10.1074/jbc.271.20.11817;
RA Liu S., Smith S.E., Julian J., Rohde L.H., Karin N.J., Carson D.D.;
RT "cDNA cloning and expression of HIP, a novel cell surface heparan
RT sulfate/heparin-binding protein of human uterine epithelial cells and cell
RT lines.";
RL J. Biol. Chem. 271:11817-11823(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-15, IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION
RP AT LYS-5, FUNCTION, AND SUBUNIT.
RX PubMed=12962325; DOI=10.1023/a:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of the
RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and
RT Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-142, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [18] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). The ribosome is a large
CC ribonucleoprotein complex responsible for the synthesis of proteins in
CC the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family.
CC {ECO:0000305}.
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DR EMBL; U10248; AAC50499.1; -; mRNA.
DR EMBL; Z49148; CAA89008.1; -; mRNA.
DR EMBL; U49083; AAC50647.1; -; mRNA.
DR EMBL; AK289538; BAF82227.1; -; mRNA.
DR EMBL; AK311884; BAG34825.1; -; mRNA.
DR EMBL; BC008926; AAH08926.1; -; mRNA.
DR EMBL; BC070190; AAH70190.1; -; mRNA.
DR EMBL; BC070481; AAH70481.1; -; mRNA.
DR EMBL; BC071663; AAH71663.1; -; mRNA.
DR CCDS; CCDS2845.1; -.
DR PIR; S65784; S65784.
DR RefSeq; NP_000983.1; NM_000992.2.
DR PDB; 4UG0; EM; -; Lb=1-159.
DR PDB; 4V6X; EM; 5.00 A; Cb=1-159.
DR PDB; 5AJ0; EM; 3.50 A; Ab=1-159.
DR PDB; 5T2C; EM; 3.60 A; V=1-159.
DR PDB; 6IP5; EM; 3.90 A; 2V=1-159.
DR PDB; 6IP6; EM; 4.50 A; 2V=1-159.
DR PDB; 6IP8; EM; 3.90 A; 2V=1-159.
DR PDB; 6LQM; EM; 3.09 A; C=1-159.
DR PDB; 6LSR; EM; 3.13 A; C=1-159.
DR PDB; 6LSS; EM; 3.23 A; C=1-159.
DR PDB; 6LU8; EM; 3.13 A; C=1-159.
DR PDB; 6OLE; EM; 3.10 A; c=2-122.
DR PDB; 6OLF; EM; 3.90 A; c=2-122.
DR PDB; 6OLG; EM; 3.40 A; Ab=2-122.
DR PDB; 6OLI; EM; 3.50 A; c=2-122.
DR PDB; 6OLZ; EM; 3.90 A; Ab=2-119.
DR PDB; 6OM0; EM; 3.10 A; c=2-122.
DR PDB; 6OM7; EM; 3.70 A; c=2-122.
DR PDB; 6QZP; EM; 2.90 A; Lb=2-122.
DR PDB; 6W6L; EM; 3.84 A; c=1-159.
DR PDB; 6XA1; EM; 2.80 A; Lb=2-122.
DR PDB; 6Y0G; EM; 3.20 A; Lb=1-159.
DR PDB; 6Y2L; EM; 3.00 A; Lb=1-159.
DR PDB; 6Y57; EM; 3.50 A; Lb=1-159.
DR PDB; 6Y6X; EM; 2.80 A; Lb=2-122.
DR PDB; 6Z6L; EM; 3.00 A; Lb=1-159.
DR PDB; 6Z6M; EM; 3.10 A; Lb=1-159.
DR PDB; 6Z6N; EM; 2.90 A; Lb=1-159.
DR PDB; 6ZM7; EM; 2.70 A; Lb=1-159.
DR PDB; 6ZME; EM; 3.00 A; Lb=1-159.
DR PDB; 6ZMI; EM; 2.60 A; Lb=1-159.
DR PDB; 6ZMO; EM; 3.10 A; Lb=1-159.
DR PDB; 7BHP; EM; 3.30 A; Lb=1-159.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P47914; -.
DR SMR; P47914; -.
DR BioGRID; 112078; 271.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P47914; -.
DR IntAct; P47914; 55.
DR MINT; P47914; -.
DR STRING; 9606.ENSP00000418868; -.
DR GlyGen; P47914; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P47914; -.
DR PhosphoSitePlus; P47914; -.
DR SwissPalm; P47914; -.
DR BioMuta; RPL29; -.
DR EPD; P47914; -.
DR jPOST; P47914; -.
DR MassIVE; P47914; -.
DR MaxQB; P47914; -.
DR PaxDb; P47914; -.
DR PeptideAtlas; P47914; -.
DR PRIDE; P47914; -.
DR ProteomicsDB; 55822; -.
DR TopDownProteomics; P47914; -.
DR Antibodypedia; 31146; 75 antibodies from 23 providers.
DR DNASU; 6159; -.
DR Ensembl; ENST00000294189.11; ENSP00000294189.4; ENSG00000162244.12.
DR Ensembl; ENST00000466397.5; ENSP00000418868.1; ENSG00000162244.12.
DR Ensembl; ENST00000475248.5; ENSP00000417048.1; ENSG00000162244.12.
DR Ensembl; ENST00000479017.5; ENSP00000418153.1; ENSG00000162244.12.
DR Ensembl; ENST00000492277.5; ENSP00000418346.1; ENSG00000162244.12.
DR Ensembl; ENST00000495383.5; ENSP00000420673.1; ENSG00000162244.12.
DR GeneID; 6159; -.
DR KEGG; hsa:6159; -.
DR MANE-Select; ENST00000294189.11; ENSP00000294189.4; NM_000992.3; NP_000983.1.
DR UCSC; uc003dcs.4; human.
DR CTD; 6159; -.
DR DisGeNET; 6159; -.
DR GeneCards; RPL29; -.
DR HGNC; HGNC:10331; RPL29.
DR HPA; ENSG00000162244; Low tissue specificity.
DR MIM; 601832; gene.
DR neXtProt; NX_P47914; -.
DR OpenTargets; ENSG00000162244; -.
DR PharmGKB; PA34711; -.
DR VEuPathDB; HostDB:ENSG00000162244; -.
DR eggNOG; KOG3504; Eukaryota.
DR GeneTree; ENSGT00390000007084; -.
DR HOGENOM; CLU_139508_0_0_1; -.
DR InParanoid; P47914; -.
DR OMA; TYIAHPK; -.
DR OrthoDB; 1608986at2759; -.
DR PhylomeDB; P47914; -.
DR TreeFam; TF313858; -.
DR PathwayCommons; P47914; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P47914; -.
DR SIGNOR; P47914; -.
DR BioGRID-ORCS; 6159; 301 hits in 1026 CRISPR screens.
DR ChiTaRS; RPL29; human.
DR GeneWiki; RPL29; -.
DR GenomeRNAi; 6159; -.
DR Pharos; P47914; Tbio.
DR PRO; PR:P47914; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P47914; protein.
DR Bgee; ENSG00000162244; Expressed in stromal cell of endometrium and 108 other tissues.
DR ExpressionAtlas; P47914; baseline and differential.
DR Genevisible; P47914; HS.
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; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0007566; P:embryo implantation; TAS:ProtInc.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
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; Acetylation; Cytoplasm; Direct protein sequencing;
KW Heparin-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325"
FT CHAIN 2..159
FT /note="60S ribosomal protein L29"
FT /id="PRO_0000219134"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:12962325,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CONFLICT 5
FT /note="K -> R (in Ref. 4; BAF82227)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="R -> A (in Ref. 2; CAA89008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 17752 MW; 2A0C31984EF4FF95 CRC64;
MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN KKGLKKMQAN
NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA HPKLGKRARA RIAKGLRLCR
PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR TQAPTKASE
