RL24_HUMAN
ID RL24_HUMAN Reviewed; 157 AA.
AC P83731; B2R4Y3; P38663; Q6IBS3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=60S ribosomal protein L24;
DE AltName: Full=60S ribosomal protein L30;
DE AltName: Full=Large ribosomal subunit protein eL24 {ECO:0000303|PubMed:24524803};
GN Name=RPL24;
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].
RX PubMed=8428672; DOI=10.1016/0378-1119(93)90139-t;
RA Johnson K.R.;
RT "Characterization of cDNA clones encoding the human homologue of
RT Saccharomyces cerevisiae ribosomal protein L30.";
RL Gene 123:283-285(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [7]
RP PROTEIN SEQUENCE OF 1-12; 28-44; 48-56 AND 81-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-157.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-77 AND LYS-93, AND
RP IDENTIFICATION BY MASS 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83; SER-86 AND SER-149, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, AND
RP IDENTIFICATION BY 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 [18]
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2; LYS-27; LYS-35 AND LYS-147,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
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 [21] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR}
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. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000305}.
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DR EMBL; M94314; AAC28251.1; -; mRNA.
DR EMBL; AB061828; BAB79466.1; -; Genomic_DNA.
DR EMBL; CR456729; CAG33010.1; -; mRNA.
DR EMBL; AK311992; BAG34930.1; -; mRNA.
DR EMBL; CH471052; EAW79780.1; -; Genomic_DNA.
DR EMBL; BC000690; AAH00690.1; -; mRNA.
DR EMBL; BC070193; AAH70193.1; -; mRNA.
DR EMBL; AB007177; BAA25836.1; -; Genomic_DNA.
DR CCDS; CCDS33809.1; -.
DR PIR; JN0549; JN0549.
DR RefSeq; NP_000977.1; NM_000986.3.
DR PDB; 4UG0; EM; -; LW=1-157.
DR PDB; 4V6X; EM; 5.00 A; CW=1-157.
DR PDB; 5A2Q; EM; 3.90 A; w=79-126.
DR PDB; 5AJ0; EM; 3.50 A; AW=1-157.
DR PDB; 5LKS; EM; 3.60 A; LW=1-157.
DR PDB; 5T2C; EM; 3.60 A; Q=1-157.
DR PDB; 6IP5; EM; 3.90 A; 2Q=1-157.
DR PDB; 6IP6; EM; 4.50 A; 2Q=1-157.
DR PDB; 6IP8; EM; 3.90 A; 2Q=1-157.
DR PDB; 6LQM; EM; 3.09 A; f=1-157.
DR PDB; 6LSR; EM; 3.13 A; f=1-157.
DR PDB; 6OLE; EM; 3.10 A; X=2-62.
DR PDB; 6OLF; EM; 3.90 A; X=2-122.
DR PDB; 6OLG; EM; 3.40 A; AW=2-122.
DR PDB; 6OLI; EM; 3.50 A; X=2-62.
DR PDB; 6OLZ; EM; 3.90 A; AW=2-122.
DR PDB; 6OM0; EM; 3.10 A; X=2-62.
DR PDB; 6OM7; EM; 3.70 A; X=2-122.
DR PDB; 6QZP; EM; 2.90 A; LW=1-124.
DR PDB; 6W6L; EM; 3.84 A; X=1-157.
DR PDB; 6XA1; EM; 2.80 A; LW=1-124.
DR PDB; 6Y0G; EM; 3.20 A; LW=1-157.
DR PDB; 6Y2L; EM; 3.00 A; LW=1-157.
DR PDB; 6Y57; EM; 3.50 A; LW=1-157.
DR PDB; 6Y6X; EM; 2.80 A; LW=1-124.
DR PDB; 6Z6L; EM; 3.00 A; LW=1-157.
DR PDB; 6Z6M; EM; 3.10 A; LW=1-157.
DR PDB; 6Z6N; EM; 2.90 A; LW=1-157.
DR PDB; 6ZM7; EM; 2.70 A; LW=1-157.
DR PDB; 6ZME; EM; 3.00 A; LW=1-157.
DR PDB; 6ZMI; EM; 2.60 A; LW=1-157.
DR PDB; 6ZMO; EM; 3.10 A; LW=1-157.
DR PDB; 7BHP; EM; 3.30 A; LW=1-157.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
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; P83731; -.
DR SMR; P83731; -.
DR BioGRID; 112071; 292.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P83731; -.
DR IntAct; P83731; 82.
DR MINT; P83731; -.
DR STRING; 9606.ENSP00000377640; -.
DR GlyGen; P83731; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P83731; -.
DR MetOSite; P83731; -.
DR PhosphoSitePlus; P83731; -.
DR SwissPalm; P83731; -.
DR BioMuta; RPL24; -.
DR DMDM; 41393532; -.
DR EPD; P83731; -.
DR jPOST; P83731; -.
DR MassIVE; P83731; -.
DR PaxDb; P83731; -.
DR PeptideAtlas; P83731; -.
DR PRIDE; P83731; -.
DR ProteomicsDB; 57738; -.
DR TopDownProteomics; P83731; -.
DR Antibodypedia; 32294; 80 antibodies from 24 providers.
DR DNASU; 6152; -.
DR Ensembl; ENST00000394077.8; ENSP00000377640.3; ENSG00000114391.13.
DR GeneID; 6152; -.
DR KEGG; hsa:6152; -.
DR MANE-Select; ENST00000394077.8; ENSP00000377640.3; NM_000986.4; NP_000977.1.
DR CTD; 6152; -.
DR DisGeNET; 6152; -.
DR GeneCards; RPL24; -.
DR HGNC; HGNC:10325; RPL24.
DR HPA; ENSG00000114391; Low tissue specificity.
DR MIM; 604180; gene.
DR neXtProt; NX_P83731; -.
DR OpenTargets; ENSG00000114391; -.
DR PharmGKB; PA34701; -.
DR VEuPathDB; HostDB:ENSG00000114391; -.
DR eggNOG; KOG1722; Eukaryota.
DR GeneTree; ENSGT00950000183105; -.
DR HOGENOM; CLU_106411_1_0_1; -.
DR InParanoid; P83731; -.
DR OMA; PGKGKIY; -.
DR OrthoDB; 1502432at2759; -.
DR PhylomeDB; P83731; -.
DR TreeFam; TF312933; -.
DR PathwayCommons; P83731; -.
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; P83731; -.
DR SIGNOR; P83731; -.
DR BioGRID-ORCS; 6152; 715 hits in 1021 CRISPR screens.
DR ChiTaRS; RPL24; human.
DR GeneWiki; RPL24; -.
DR GenomeRNAi; 6152; -.
DR Pharos; P83731; Tbio.
DR PRO; PR:P83731; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P83731; protein.
DR Bgee; ENSG00000114391; Expressed in calcaneal tendon and 97 other tissues.
DR ExpressionAtlas; P83731; baseline and differential.
DR Genevisible; P83731; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0010458; P:exit from mitosis; IEA:Ensembl.
DR GO; GO:0021554; P:optic nerve development; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:Ensembl.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd00472; Ribosomal_L24e_L24; 1.
DR DisProt; DP01935; -.
DR Gene3D; 2.30.170.20; -; 1.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR000988; Ribosomal_L24e-rel.
DR InterPro; IPR023442; Ribosomal_L24e_CS.
DR InterPro; IPR011017; TRASH_dom.
DR PANTHER; PTHR10792; PTHR10792; 1.
DR Pfam; PF01246; Ribosomal_L24e; 1.
DR SMART; SM00746; TRASH; 1.
DR PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..157
FT /note="60S ribosomal protein L24"
FT /id="PRO_0000136867"
FT REGION 106..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 131
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP67"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 157 AA; 17779 MW; 1D48EEB7C0652574 CRC64;
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN WTVLYRRKHK
KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV RKAQREQAIR AAKEAKKAKQ
ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA PRVGGKR
