RS24_HUMAN
ID RS24_HUMAN Reviewed; 133 AA.
AC P62847; E7EPK6; P16632; Q5T0P7; Q5T0P8; Q7Z3D1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=40S ribosomal protein S24;
DE AltName: Full=Small ribosomal subunit protein eS24 {ECO:0000303|PubMed:24524803};
GN Name=RPS24;
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] (ISOFORM 1).
RX PubMed=2210388; DOI=10.1016/0378-1119(90)90103-x;
RA Brown S.J., Jewell A., Maki C.G., Roufa D.J.;
RT "A cDNA encoding human ribosomal protein S24.";
RL Gene 91:293-296(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=8647458; DOI=10.1016/0378-1119(96)88652-5;
RA Xu W.-B., Roufa D.J.;
RT "The gene encoding human ribosomal protein S24 and tissue-specific
RT expression of differentially spliced mRNAs.";
RL Gene 169:257-262(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and 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 MRNA] (ISOFORM 3).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney, and Muscle;
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 [9]
RP PROTEIN SEQUENCE OF 1-8; 50-61; 69-83 AND 119-132, ACETYLATION AT MET-1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Quadroni M.;
RL Submitted (OCT-2004) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 69-83.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [11]
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 [12]
RP INVOLVEMENT IN DBA3, AND TISSUE SPECIFICITY.
RX PubMed=17186470; DOI=10.1086/510020;
RA Gazda H.T., Grabowska A., Merida-Long L.B., Latawiec E., Schneider H.E.,
RA Lipton J.M., Vlachos A., Atsidaftos E., Ball S.E., Orfali K.A.,
RA Niewiadomska E., Da Costa L., Tchernia G., Niemeyer C., Meerpohl J.J.,
RA Stahl J., Schratt G., Glader B., Backer K., Wong C., Nathan D.G.,
RA Beggs A.H., Sieff C.A.;
RT "Ribosomal protein S24 gene is mutated in Diamond-Blackfan anemia.";
RL Am. J. Hum. Genet. 79:1110-1118(2006).
RN [13]
RP FUNCTION.
RX PubMed=18230666; DOI=10.1093/hmg/ddn015;
RA Choesmel V., Fribourg S., Aguissa-Toure A.H., Pinaud N., Legrand P.,
RA Gazda H.T., Gleizes P.E.;
RT "Mutation of ribosomal protein RPS24 in Diamond-Blackfan anemia results in
RT a ribosome biogenesis disorder.";
RL Hum. Mol. Genet. 17:1253-1263(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, AND IDENTIFICATION BY MASS
RP 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 [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [19]
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 [20]
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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS
RP 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 [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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).
CC -!- FUNCTION: Required for processing of pre-rRNA and maturation of 40S
CC ribosomal subunits. {ECO:0000269|PubMed:18230666}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P62847-1, P16632-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P62847-2, P16632-2;
CC Sequence=VSP_005724;
CC Name=3;
CC IsoId=P62847-3; Sequence=VSP_039113;
CC Name=4;
CC IsoId=P62847-4; Sequence=VSP_045672;
CC -!- TISSUE SPECIFICITY: Mature tissues, such as adult brain, skeletal
CC muscle, heart, and kidney, express low levels, whereas tissues and
CC organs with significant populations of proliferating cells, such as
CC fetal brain, placenta, bone marrow, and various glandular organs,
CC contain significantly higher levels. {ECO:0000269|PubMed:17186470}.
CC -!- DISEASE: Diamond-Blackfan anemia 3 (DBA3) [MIM:610629]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of developing leukemia. 30 to
CC 40% of Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies.
CC {ECO:0000269|PubMed:17186470}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS24 family.
CC {ECO:0000305}.
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DR EMBL; M31520; AAA36588.1; -; mRNA.
DR EMBL; U12202; AAB08007.1; -; Genomic_DNA.
DR EMBL; U12202; AAB08006.1; -; Genomic_DNA.
DR EMBL; BX336465; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK311776; BAG34719.1; -; mRNA.
DR EMBL; AK311910; BAG34851.1; -; mRNA.
DR EMBL; BX537975; CAD97939.1; -; mRNA.
DR EMBL; AL512628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54623.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54625.1; -; Genomic_DNA.
DR EMBL; BC000523; AAH00523.1; -; mRNA.
DR EMBL; BC003149; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC071926; AAH71926.1; -; mRNA.
DR CCDS; CCDS44443.1; -. [P62847-4]
DR CCDS; CCDS7355.1; -.
DR CCDS; CCDS7356.1; -. [P62847-2]
DR CCDS; CCDS86122.1; -. [P62847-3]
DR PIR; JC4671; JC4671.
DR PIR; JH0213; JH0213.
DR RefSeq; NP_001017.1; NM_001026.4. [P62847-1]
DR RefSeq; NP_001135755.1; NM_001142283.1. [P62847-3]
DR RefSeq; NP_001135757.1; NM_001142285.1. [P62847-4]
DR RefSeq; NP_148982.1; NM_033022.3. [P62847-2]
DR PDB; 4UG0; EM; -; SY=1-133.
DR PDB; 4V6X; EM; 5.00 A; AY=1-133.
DR PDB; 5A2Q; EM; 3.90 A; Y=1-130.
DR PDB; 5AJ0; EM; 3.50 A; BY=1-133.
DR PDB; 5FLX; EM; 3.90 A; Y=1-133.
DR PDB; 5LKS; EM; 3.60 A; SY=1-133.
DR PDB; 5OA3; EM; 4.30 A; Y=1-130.
DR PDB; 5T2C; EM; 3.60 A; AQ=1-133.
DR PDB; 5VYC; X-ray; 6.00 A; Y1/Y2/Y3/Y4/Y5/Y6=1-133.
DR PDB; 6FEC; EM; 6.30 A; s=3-133.
DR PDB; 6G18; EM; 3.60 A; Y=1-133.
DR PDB; 6G4S; EM; 4.00 A; Y=1-133.
DR PDB; 6G4W; EM; 4.50 A; Y=1-133.
DR PDB; 6G51; EM; 4.10 A; Y=1-133.
DR PDB; 6G53; EM; 4.50 A; Y=1-133.
DR PDB; 6G5H; EM; 3.60 A; Y=1-133.
DR PDB; 6G5I; EM; 3.50 A; Y=1-133.
DR PDB; 6IP5; EM; 3.90 A; 3N=1-133.
DR PDB; 6IP6; EM; 4.50 A; 3N=1-133.
DR PDB; 6IP8; EM; 3.90 A; 3N=1-133.
DR PDB; 6OLE; EM; 3.10 A; SY=2-132.
DR PDB; 6OLF; EM; 3.90 A; SY=2-132.
DR PDB; 6OLG; EM; 3.40 A; BY=4-128.
DR PDB; 6OLI; EM; 3.50 A; SY=2-132.
DR PDB; 6OLZ; EM; 3.90 A; BY=4-128.
DR PDB; 6OM0; EM; 3.10 A; SY=2-132.
DR PDB; 6OM7; EM; 3.70 A; SY=2-132.
DR PDB; 6QZP; EM; 2.90 A; SY=2-132.
DR PDB; 6XA1; EM; 2.80 A; SY=4-125.
DR PDB; 6Y0G; EM; 3.20 A; SY=1-133.
DR PDB; 6Y2L; EM; 3.00 A; SY=1-133.
DR PDB; 6Y57; EM; 3.50 A; SY=1-133.
DR PDB; 6YBW; EM; 3.10 A; T=1-133.
DR PDB; 6Z6L; EM; 3.00 A; SY=1-133.
DR PDB; 6Z6M; EM; 3.10 A; SY=1-133.
DR PDB; 6Z6N; EM; 2.90 A; SY=1-133.
DR PDB; 6ZLW; EM; 2.60 A; Y=1-133.
DR PDB; 6ZM7; EM; 2.70 A; SY=1-133.
DR PDB; 6ZME; EM; 3.00 A; SY=1-133.
DR PDB; 6ZMI; EM; 2.60 A; SY=1-133.
DR PDB; 6ZMO; EM; 3.10 A; SY=1-133.
DR PDB; 6ZMT; EM; 3.00 A; Y=1-133.
DR PDB; 6ZMW; EM; 3.70 A; T=1-133.
DR PDB; 6ZN5; EM; 3.20 A; Y=3-126.
DR PDB; 6ZOJ; EM; 2.80 A; Y=1-130.
DR PDB; 6ZOK; EM; 2.80 A; Y=1-130.
DR PDB; 6ZON; EM; 3.00 A; z=1-133.
DR PDB; 6ZP4; EM; 2.90 A; z=1-133.
DR PDB; 6ZUO; EM; 3.10 A; Y=1-133.
DR PDB; 6ZV6; EM; 2.90 A; Y=1-133.
DR PDB; 6ZVH; EM; 2.90 A; Y=2-132.
DR PDB; 6ZXD; EM; 3.20 A; Y=1-133.
DR PDB; 6ZXE; EM; 3.00 A; Y=1-133.
DR PDB; 6ZXF; EM; 3.70 A; Y=1-133.
DR PDB; 6ZXG; EM; 2.60 A; Y=1-133.
DR PDB; 6ZXH; EM; 2.70 A; Y=1-133.
DR PDB; 7K5I; EM; 2.90 A; Y=1-133.
DR PDB; 7MQ8; EM; 3.60 A; LF=1-133.
DR PDB; 7MQ9; EM; 3.87 A; LF=1-133.
DR PDB; 7MQA; EM; 2.70 A; LF=1-133.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
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; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P62847; -.
DR SMR; P62847; -.
DR BioGRID; 112143; 461.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62847; -.
DR IntAct; P62847; 83.
DR MINT; P62847; -.
DR STRING; 9606.ENSP00000414321; -.
DR GlyGen; P62847; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62847; -.
DR MetOSite; P62847; -.
DR PhosphoSitePlus; P62847; -.
DR SwissPalm; P62847; -.
DR BioMuta; RPS24; -.
DR DMDM; 51338645; -.
DR EPD; P62847; -.
DR jPOST; P62847; -.
DR MassIVE; P62847; -.
DR MaxQB; P62847; -.
DR PaxDb; P62847; -.
DR PeptideAtlas; P62847; -.
DR PRIDE; P62847; -.
DR ProteomicsDB; 17381; -.
DR ProteomicsDB; 57434; -.
DR ProteomicsDB; 57435; -. [P62847-2]
DR ProteomicsDB; 57436; -. [P62847-3]
DR TopDownProteomics; P62847-1; -. [P62847-1]
DR TopDownProteomics; P62847-2; -. [P62847-2]
DR TopDownProteomics; P62847-4; -. [P62847-4]
DR Antibodypedia; 1244; 159 antibodies from 26 providers.
DR DNASU; 6229; -.
DR Ensembl; ENST00000372360.9; ENSP00000361435.4; ENSG00000138326.21. [P62847-2]
DR Ensembl; ENST00000440692.6; ENSP00000414321.1; ENSG00000138326.21. [P62847-4]
DR Ensembl; ENST00000464716.6; ENSP00000494231.1; ENSG00000138326.21. [P62847-3]
DR Ensembl; ENST00000613865.5; ENSP00000478869.2; ENSG00000138326.21. [P62847-1]
DR GeneID; 6229; -.
DR KEGG; hsa:6229; -.
DR MANE-Select; ENST00000372360.9; ENSP00000361435.4; NM_033022.4; NP_148982.1. [P62847-2]
DR UCSC; uc001jzp.4; human.
DR CTD; 6229; -.
DR DisGeNET; 6229; -.
DR GeneCards; RPS24; -.
DR GeneReviews; RPS24; -.
DR HGNC; HGNC:10411; RPS24.
DR HPA; ENSG00000138326; Low tissue specificity.
DR MalaCards; RPS24; -.
DR MIM; 602412; gene.
DR MIM; 610629; phenotype.
DR neXtProt; NX_P62847; -.
DR OpenTargets; ENSG00000138326; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34815; -.
DR VEuPathDB; HostDB:ENSG00000138326; -.
DR eggNOG; KOG3424; Eukaryota.
DR GeneTree; ENSGT00390000000153; -.
DR HOGENOM; CLU_086546_0_0_1; -.
DR InParanoid; P62847; -.
DR OMA; TFGFRTH; -.
DR OrthoDB; 1465790at2759; -.
DR PhylomeDB; P62847; -.
DR TreeFam; TF314134; -.
DR PathwayCommons; P62847; -.
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-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
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-9754678; SARS-CoV-2 modulates host translation machinery.
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; P62847; -.
DR SIGNOR; P62847; -.
DR BioGRID-ORCS; 6229; 749 hits in 1037 CRISPR screens.
DR ChiTaRS; RPS24; human.
DR GeneWiki; RPS24; -.
DR GenomeRNAi; 6229; -.
DR Pharos; P62847; Tbio.
DR PRO; PR:P62847; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P62847; protein.
DR Bgee; ENSG00000138326; Expressed in mucosa of sigmoid colon and 204 other tissues.
DR ExpressionAtlas; P62847; baseline and differential.
DR Genevisible; P62847; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0031369; F:translation initiation factor binding; ISS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:UniProtKB.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
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; Diamond-Blackfan anemia;
KW Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..133
FT /note="40S ribosomal protein S24"
FT /id="PRO_0000137623"
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:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 131..133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005724"
FT VAR_SEQ 131..133
FT /note="PKE -> KK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039113"
FT VAR_SEQ 131..133
FT /note="PKE -> MRELGLGVQALGRISQEERCTDVKNSKARESRGVVWQVEVPGPWS
FT VWTCGRLRRGCGKYLQVAVTWRKTENREQCCQACLLERALVRNGAFMSPASPAPAGSPH
FT PVDGDLVLHLPEALSATLTLSPHIQAINKSFGPFFEIHQESSCFSPPSCLSGLGH (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045672"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6ZUO"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6ZVH"
SQ SEQUENCE 133 AA; 15423 MW; CE9065C0764D60A6 CRC64;
MNDTVTIRTR KFMTNRLLQR KQMVIDVLHP GKATVPKTEI REKLAKMYKT TPDVIFVFGF
RTHFGGGKTT GFGMIYDSLD YAKKNEPKHR LARHGLYEKK KTSRKQRKER KNRMKKVRGT
AKANVGAGKK PKE
