ID RL24_RAT Reviewed; 157 AA.
AC P83732; P38663;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 10-JUN-2026, entry version 146.
DE RecName: Full=Large ribosomal subunit protein eL24 {ECO:0000305};
DE AltName: Full=60S ribosomal protein L24;
DE AltName: Full=L30;
GN Name=Rpl24;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8048931; DOI=10.1006/bbrc.1994.2052;
RA Chan Y.-L., Olvera J., Wool I.G.;
RT "The primary structure of rat ribosomal protein L24.";
RL Biochem. Biophys. Res. Commun. 202:1176-1180(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
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 -!- PTM: Mono-ADP-ribosylation at Glu-4 by PARP16 inhibits polysome
CC assembly and mRNA loading, thereby inhibiting protein translation.
CC {ECO:0000250|UniProtKB:P83731}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000305}.
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DR EMBL; X78443; CAA55203.1; -; mRNA.
DR EMBL; BC058473; AAH58473.1; -; mRNA.
DR PIR; JC2444; JC2444.
DR RefSeq; NP_071960.1; NM_022515.2.
DR AlphaFoldDB; P83732; -.
DR SMR; P83732; -.
DR BioGRID; 249022; 7.
DR FunCoup; P83732; 2987.
DR IntAct; P83732; 10.
DR STRING; 10116.ENSRNOP00000002194; -.
DR GlyGen; P83732; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P83732; -.
DR PhosphoSitePlus; P83732; -.
DR jPOST; P83732; -.
DR PaxDb; 10116-ENSRNOP00000002194; -.
DR Ensembl; ENSRNOT00000002194.9; ENSRNOP00000002194.7; ENSRNOG00000001611.9.
DR Ensembl; ENSRNOT00055023705; ENSRNOP00055019307; ENSRNOG00055013790.
DR Ensembl; ENSRNOT00060022312; ENSRNOP00060017696; ENSRNOG00060013081.
DR Ensembl; ENSRNOT00065003010; ENSRNOP00065002075; ENSRNOG00065002287.
DR GeneID; 64307; -.
DR KEGG; rno:64307; -.
DR UCSC; RGD:621191; rat.
DR AGR; RGD:621191; -.
DR CTD; 6152; -.
DR RGD; 621191; Rpl24.
DR eggNOG; KOG1722; Eukaryota.
DR GeneTree; ENSGT00950000183105; -.
DR HOGENOM; CLU_106411_1_0_1; -.
DR InParanoid; P83732; -.
DR OMA; PGHGKKM; -.
DR OrthoDB; 1727108at2759; -.
DR PhylomeDB; P83732; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Reactome; R-RNO-9954709; Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide.
DR Reactome; R-RNO-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA.
DR Reactome; R-RNO-9954716; ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA.
DR PRO; PR:P83732; -.
DR Proteomes; UP000002494; Chromosome 11.
DR ExpressionAtlas; P83732; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0010458; P:exit from mitosis; ISO:RGD.
DR GO; GO:0021554; P:optic nerve development; ISO:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISO:RGD.
DR GO; GO:0006412; P:translation; ISO:RGD.
DR CDD; cd00472; Ribosomal_L24e_L24; 1.
DR FunFam; 2.30.170.20:FF:000004; 60S ribosomal protein l24; 1.
DR Gene3D; 6.10.250.1270; -; 1.
DR Gene3D; 2.30.170.20; Ribosomal protein L24e; 1.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR056366; Ribosomal_eL24.
DR InterPro; IPR000988; Ribosomal_eL24-rel_N.
DR InterPro; IPR023442; Ribosomal_eL24_CS.
DR InterPro; IPR011017; TRASH_dom.
DR PANTHER; PTHR10792; 60S RIBOSOMAL PROTEIN L24; 1.
DR PANTHER; PTHR10792:SF1; RIBOSOMAL PROTEIN L24; 1.
DR Pfam; PF01246; Ribosomal_L24e; 1.
DR SMART; SM00746; TRASH; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ADP-ribosylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..157
FT /note="Large ribosomal subunit protein eL24"
FT /id="PRO_0000136870"
FT REGION 106..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 27
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83731"
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:0000250|UniProtKB:Q8BP67"
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"
SQ SEQUENCE 157 AA; 17779 MW; 1D48EEB7C0652574 CRC64;
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN WTVLYRRKHK
KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV RKAQREQAIR AAKEAKKAKQ
ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA PRVGGKR
//
