RL24_MOUSE
ID RL24_MOUSE Reviewed; 157 AA.
AC Q8BP67; P38663; Q58EA4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=60S ribosomal protein L24;
GN Name=Rpl24;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, Eye, and Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-131, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:0000250|UniProtKB:P83731}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P83731}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P83731}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02110.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK018731; BAB31374.1; -; mRNA.
DR EMBL; AK077617; BAC36903.1; -; mRNA.
DR EMBL; BC002110; AAH02110.2; ALT_INIT; mRNA.
DR EMBL; BC053377; AAH53377.1; -; mRNA.
DR EMBL; BC058114; AAH58114.1; -; mRNA.
DR EMBL; BC092008; AAH92008.1; -; mRNA.
DR CCDS; CCDS28218.1; -.
DR RefSeq; NP_077180.1; NM_024218.4.
DR PDB; 6SWA; EM; 3.10 A; U=1-157.
DR PDB; 7CPU; EM; 2.82 A; LW=1-157.
DR PDB; 7CPV; EM; 3.03 A; LW=1-157.
DR PDB; 7LS1; EM; 3.30 A; Q2=1-157.
DR PDB; 7LS2; EM; 3.10 A; Q2=1-157.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; Q8BP67; -.
DR SMR; Q8BP67; -.
DR BioGRID; 212718; 87.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; Q8BP67; 5.
DR MINT; Q8BP67; -.
DR STRING; 10090.ENSMUSP00000023269; -.
DR iPTMnet; Q8BP67; -.
DR PhosphoSitePlus; Q8BP67; -.
DR SwissPalm; Q8BP67; -.
DR EPD; Q8BP67; -.
DR jPOST; Q8BP67; -.
DR MaxQB; Q8BP67; -.
DR PeptideAtlas; Q8BP67; -.
DR PRIDE; Q8BP67; -.
DR ProteomicsDB; 255018; -.
DR TopDownProteomics; Q8BP67; -.
DR Antibodypedia; 32294; 80 antibodies from 24 providers.
DR DNASU; 68193; -.
DR Ensembl; ENSMUST00000023269; ENSMUSP00000023269; ENSMUSG00000098274.
DR GeneID; 68193; -.
DR KEGG; mmu:68193; -.
DR UCSC; uc007zlv.2; mouse.
DR CTD; 6152; -.
DR MGI; MGI:1915443; Rpl24.
DR VEuPathDB; HostDB:ENSMUSG00000098274; -.
DR eggNOG; KOG1722; Eukaryota.
DR GeneTree; ENSGT00950000183105; -.
DR HOGENOM; CLU_106411_1_0_1; -.
DR InParanoid; Q8BP67; -.
DR OMA; PGKGKIY; -.
DR OrthoDB; 1502432at2759; -.
DR PhylomeDB; Q8BP67; -.
DR TreeFam; TF312933; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 68193; 27 hits in 70 CRISPR screens.
DR ChiTaRS; Rpl24; mouse.
DR PRO; PR:Q8BP67; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BP67; protein.
DR Bgee; ENSMUSG00000098274; Expressed in epiblast (generic) and 73 other tissues.
DR Genevisible; Q8BP67; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:MGI.
DR GO; GO:0010458; P:exit from mitosis; IMP:MGI.
DR GO; GO:0021554; P:optic nerve development; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:MGI.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR CDD; cd00472; Ribosomal_L24e_L24; 1.
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; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..157
FT /note="60S ribosomal protein L24"
FT /id="PRO_0000136869"
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:23806337"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 131
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT CONFLICT 14
FT /note="Y -> N (in Ref. 1; BAC36903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 17779 MW; 1D48EEB7C0652574 CRC64;
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN WTVLYRRKHK
KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV RKAQREQAIR AAKEAKKAKQ
ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA PRVGGKR
