RS24_MOUSE
ID RS24_MOUSE Reviewed; 133 AA.
AC P62849; P16632; Q642L0; Q6PDB5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=40S ribosomal protein S24;
GN Name=Rps24;
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 [MRNA] (ISOFORM 2).
RX PubMed=1840675; DOI=10.1093/nar/19.23.6647;
RA Ro H.-S., Xu L.;
RT "Nucleotide sequences of a cDNA clone encoding mouse ribosomal protein
RT S24.";
RL Nucleic Acids Res. 19:6647-6647(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND
RP 3), AND INDUCTION.
RX PubMed=8127713; DOI=10.1093/nar/22.4.646;
RA Xu L., He G.-P., Li A., Ro H.-S.;
RT "Molecular characterization of the mouse ribosomal protein S24 multigene
RT family: a uniquely expressed intron-containing gene with cell-specific
RT expression of three alternatively spliced mRNAs.";
RL Nucleic Acids Res. 22:646-655(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Kidney, and Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C3H/He, and C57BL/6J; TISSUE=Brain, and Osteoblast;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
CC -!- FUNCTION: Required for processing of pre-rRNA and maturation of 40S
CC ribosomal subunits. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=S24c;
CC IsoId=P62849-1, P16632-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=S24a;
CC IsoId=P62849-2, P16632-2;
CC Sequence=VSP_011365;
CC Name=3; Synonyms=S24b;
CC IsoId=P62849-3; Sequence=VSP_011366;
CC -!- INDUCTION: Down-regulated during adipocyte differentiation and up-
CC regulated during cellular transformation. {ECO:0000269|PubMed:8127713}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS24 family.
CC {ECO:0000305}.
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DR EMBL; X60289; CAA42829.1; -; mRNA.
DR EMBL; X71972; CAA50792.1; -; Genomic_DNA.
DR EMBL; AK005358; BAB23973.1; -; mRNA.
DR EMBL; AK007776; BAB25248.1; -; mRNA.
DR EMBL; AK012537; BAB28304.1; -; mRNA.
DR EMBL; AK018704; BAB31355.1; -; mRNA.
DR EMBL; AK049387; BAC33727.1; -; mRNA.
DR EMBL; BC058817; AAH58817.1; -; mRNA.
DR EMBL; BC081457; AAH81457.1; -; mRNA.
DR CCDS; CCDS36829.1; -.
DR CCDS; CCDS36830.1; -. [P62849-2]
DR CCDS; CCDS88597.1; -. [P62849-3]
DR RefSeq; NP_035427.2; NM_011297.2. [P62849-2]
DR RefSeq; NP_997517.1; NM_207634.1. [P62849-1]
DR RefSeq; NP_997518.1; NM_207635.1. [P62849-3]
DR RefSeq; XP_006518797.1; XM_006518734.1.
DR PDB; 7CPU; EM; 2.82 A; SY=1-133.
DR PDB; 7CPV; EM; 3.03 A; SY=1-133.
DR PDB; 7LS1; EM; 3.30 A; Q3=1-133.
DR PDB; 7LS2; EM; 3.10 A; Q3=1-133.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62849; -.
DR SMR; P62849; -.
DR BioGRID; 203008; 75.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; P62849; 4.
DR MINT; P62849; -.
DR STRING; 10090.ENSMUSP00000125977; -.
DR iPTMnet; P62849; -.
DR PhosphoSitePlus; P62849; -.
DR SwissPalm; P62849; -.
DR EPD; P62849; -.
DR jPOST; P62849; -.
DR MaxQB; P62849; -.
DR PaxDb; P62849; -.
DR PeptideAtlas; P62849; -.
DR PRIDE; P62849; -.
DR ProteomicsDB; 299818; -.
DR ProteomicsDB; 299819; -. [P62849-2]
DR ProteomicsDB; 299820; -. [P62849-3]
DR DNASU; 20088; -.
DR Ensembl; ENSMUST00000112384; ENSMUSP00000108003; ENSMUSG00000025290. [P62849-2]
DR Ensembl; ENSMUST00000169826; ENSMUSP00000125977; ENSMUSG00000025290. [P62849-2]
DR Ensembl; ENSMUST00000223999; ENSMUSP00000153659; ENSMUSG00000025290. [P62849-3]
DR Ensembl; ENSMUST00000225023; ENSMUSP00000152944; ENSMUSG00000025290. [P62849-1]
DR GeneID; 20088; -.
DR KEGG; mmu:20088; -.
DR UCSC; uc007sra.1; mouse.
DR UCSC; uc007src.1; mouse. [P62849-3]
DR CTD; 6229; -.
DR MGI; MGI:98147; Rps24.
DR VEuPathDB; HostDB:ENSMUSG00000025290; -.
DR eggNOG; KOG3424; Eukaryota.
DR GeneTree; ENSGT00390000000153; -.
DR HOGENOM; CLU_107248_1_0_1; -.
DR InParanoid; P62849; -.
DR OMA; TFGFRTH; -.
DR OrthoDB; 1465790at2759; -.
DR PhylomeDB; P62849; -.
DR TreeFam; TF314134; -.
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-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
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; 20088; 14 hits in 53 CRISPR screens.
DR ChiTaRS; Rps24; mouse.
DR PRO; PR:P62849; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P62849; protein.
DR Bgee; ENSMUSG00000025290; Expressed in ventricular zone and 238 other tissues.
DR ExpressionAtlas; P62849; baseline and differential.
DR Genevisible; P62849; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0015935; C:small ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0031369; F:translation initiation factor binding; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0034101; P:erythrocyte homeostasis; ISO:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR HAMAP; MF_00545; Ribosomal_S24e; 1.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001976; Ribosomal_S24e.
DR InterPro; IPR018098; Ribosomal_S24e_CS.
DR PANTHER; PTHR10496; PTHR10496; 1.
DR Pfam; PF01282; Ribosomal_S24e; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS00529; RIBOSOMAL_S24E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..133
FT /note="40S ribosomal protein S24"
FT /id="PRO_0000137625"
FT REGION 92..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..118
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P62847"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62847"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62847"
FT VAR_SEQ 131..133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:1840675"
FT /id="VSP_011365"
FT VAR_SEQ 131..133
FT /note="PKE -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011366"
SQ SEQUENCE 133 AA; 15423 MW; CE9065C0764D60A6 CRC64;
MNDTVTIRTR KFMTNRLLQR KQMVIDVLHP GKATVPKTEI REKLAKMYKT TPDVIFVFGF
RTHFGGGKTT GFGMIYDSLD YAKKNEPKHR LARHGLYEKK KTSRKQRKER KNRMKKVRGT
AKANVGAGKK PKE
