ID RM24_HUMAN Reviewed; 216 AA. AC Q96A35; D3DVC8; Q53G65; Q53HT0; Q5SYZ9; Q5SZ00; Q5SZ02; Q96Q70; Q9H7G3; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 169. DE RecName: Full=Large ribosomal subunit protein uL24m {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L24, mitochondrial; DE Short=L24mt; DE Short=MRP-L24; DE Flags: Precursor; GN Name=MRPL24; 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 [LARGE SCALE MRNA]. RC TISSUE=Adipose tissue; 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Adipose tissue; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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=Bone marrow, and Ovary; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-216. RX PubMed=11543634; DOI=10.1006/geno.2001.6622; RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., RA Watanabe K., Tanaka T.; RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes to RT the chromosomes and implications for human disorders."; RL Genomics 77:65-70(2001). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [10] 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 [11] {ECO:0007744|PDB:3J7Y} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25278503; DOI=10.1126/science.1258026; RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G., RA Scheres S.H., Ramakrishnan V.; RT "Structure of the large ribosomal subunit from human mitochondria."; RL Science 346:718-722(2014). RN [12] {ECO:0007744|PDB:3J9M} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25838379; DOI=10.1126/science.aaa1193; RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.; RT "Ribosome. The structure of the human mitochondrial ribosome."; RL Science 348:95-98(2015). RN [13] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM} RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=28892042; DOI=10.1038/nsmb.3464; RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J., RA Amunts A., Ramakrishnan V.; RT "Structures of the human mitochondrial ribosome in native states of RT assembly."; RL Nat. Struct. Mol. Biol. 24:866-869(2017). CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt- CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA CC (mt-tRNA(Val)), which plays an integral structural role, and 52 CC different proteins. {ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK024570; BAB14929.1; -; mRNA. DR EMBL; CR457329; CAG33610.1; -; mRNA. DR EMBL; AK222500; BAD96220.1; -; mRNA. DR EMBL; AK223066; BAD96786.1; -; mRNA. DR EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52913.1; -; Genomic_DNA. DR EMBL; CH471121; EAW52914.1; -; Genomic_DNA. DR EMBL; BC012440; AAH12440.1; -; mRNA. DR EMBL; BC016700; AAH16700.1; -; mRNA. DR EMBL; AB051341; BAB54931.2; -; Genomic_DNA. DR CCDS; CCDS1155.1; -. DR RefSeq; NP_078816.2; NM_024540.3. DR RefSeq; NP_663781.1; NM_145729.2. DR RefSeq; XP_011508283.1; XM_011509981.2. DR RefSeq; XP_011508284.1; XM_011509982.2. DR PDB; 3J7Y; EM; 3.40 A; V=1-216. DR PDB; 3J9M; EM; 3.50 A; V=1-216. DR PDB; 5OOL; EM; 3.06 A; V=1-216. DR PDB; 5OOM; EM; 3.03 A; V=1-216. DR PDB; 6I9R; EM; 3.90 A; V=1-216. DR PDB; 6NU2; EM; 3.90 A; V=15-216. DR PDB; 6NU3; EM; 4.40 A; V=1-216. DR PDB; 6VLZ; EM; 2.97 A; V=1-216. DR PDB; 6VMI; EM; 2.96 A; V=1-216. DR PDB; 6ZM5; EM; 2.89 A; V=1-216. DR PDB; 6ZM6; EM; 2.59 A; V=1-216. DR PDB; 6ZS9; EM; 4.00 A; XV=1-216. DR PDB; 6ZSA; EM; 4.00 A; XV=1-216. DR PDB; 6ZSB; EM; 4.50 A; XV=1-216. DR PDB; 6ZSC; EM; 3.50 A; XV=1-216. DR PDB; 6ZSD; EM; 3.70 A; XV=1-216. DR PDB; 6ZSE; EM; 5.00 A; XV=1-216. DR PDB; 6ZSG; EM; 4.00 A; XV=1-216. DR PDB; 7A5F; EM; 4.40 A; V3=1-216. DR PDB; 7A5G; EM; 4.33 A; V3=1-216. DR PDB; 7A5H; EM; 3.30 A; V=1-216. DR PDB; 7A5I; EM; 3.70 A; V3=1-216. DR PDB; 7A5J; EM; 3.10 A; V=1-216. DR PDB; 7A5K; EM; 3.70 A; V3=1-216. DR PDB; 7L08; EM; 3.49 A; V=1-216. DR PDB; 7L20; EM; 3.15 A; V=1-216. DR PDB; 7O9K; EM; 3.10 A; V=1-216. DR PDB; 7O9M; EM; 2.50 A; V=1-216. DR PDB; 7ODR; EM; 2.90 A; V=1-216. DR PDB; 7ODS; EM; 3.10 A; V=1-216. DR PDB; 7ODT; EM; 3.10 A; V=1-216. DR PDB; 7OF0; EM; 2.20 A; V=1-216. DR PDB; 7OF2; EM; 2.70 A; V=1-216. DR PDB; 7OF3; EM; 2.70 A; V=1-216. DR PDB; 7OF4; EM; 2.70 A; V=1-216. DR PDB; 7OF5; EM; 2.90 A; V=1-216. DR PDB; 7OF6; EM; 2.60 A; V=1-216. DR PDB; 7OF7; EM; 2.50 A; V=1-216. DR PDB; 7OG4; EM; 3.80 A; XV=1-216. DR PDB; 7OI6; EM; 5.70 A; V=1-216. DR PDB; 7OI7; EM; 3.50 A; V=1-216. DR PDB; 7OI8; EM; 3.50 A; V=1-216. DR PDB; 7OI9; EM; 3.30 A; V=1-216. DR PDB; 7OIA; EM; 3.20 A; V=1-216. DR PDB; 7OIB; EM; 3.30 A; V=1-216. DR PDB; 7OIC; EM; 3.10 A; V=1-216. DR PDB; 7OID; EM; 3.70 A; V=1-216. DR PDB; 7OIE; EM; 3.50 A; V=1-216. DR PDB; 7PD3; EM; 3.40 A; V=1-216. DR PDB; 7PO4; EM; 2.56 A; V=1-216. DR PDB; 7QH6; EM; 3.08 A; V=1-216. DR PDB; 7QH7; EM; 2.89 A; V=169-216. DR PDB; 7QI4; EM; 2.21 A; V=1-216. DR PDB; 7QI5; EM; 2.63 A; V=1-216. DR PDB; 7QI6; EM; 2.98 A; V=1-216. DR PDB; 8ANY; EM; 2.85 A; V=1-216. DR PDB; 8OIR; EM; 3.10 A; BC=1-216. DR PDB; 8OIT; EM; 2.90 A; BC=1-216. DR PDBsum; 3J7Y; -. DR PDBsum; 3J9M; -. DR PDBsum; 5OOL; -. DR PDBsum; 5OOM; -. DR PDBsum; 6I9R; -. DR PDBsum; 6NU2; -. DR PDBsum; 6NU3; -. DR PDBsum; 6VLZ; -. DR PDBsum; 6VMI; -. DR PDBsum; 6ZM5; -. DR PDBsum; 6ZM6; -. DR PDBsum; 6ZS9; -. DR PDBsum; 6ZSA; -. DR PDBsum; 6ZSB; -. DR PDBsum; 6ZSC; -. DR PDBsum; 6ZSD; -. DR PDBsum; 6ZSE; -. DR PDBsum; 6ZSG; -. DR PDBsum; 7A5F; -. DR PDBsum; 7A5G; -. DR PDBsum; 7A5H; -. DR PDBsum; 7A5I; -. DR PDBsum; 7A5J; -. DR PDBsum; 7A5K; -. DR PDBsum; 7L08; -. DR PDBsum; 7L20; -. DR PDBsum; 7O9K; -. DR PDBsum; 7O9M; -. DR PDBsum; 7ODR; -. DR PDBsum; 7ODS; -. DR PDBsum; 7ODT; -. DR PDBsum; 7OF0; -. DR PDBsum; 7OF2; -. DR PDBsum; 7OF3; -. DR PDBsum; 7OF4; -. DR PDBsum; 7OF5; -. DR PDBsum; 7OF6; -. DR PDBsum; 7OF7; -. DR PDBsum; 7OG4; -. DR PDBsum; 7OI6; -. DR PDBsum; 7OI7; -. DR PDBsum; 7OI8; -. DR PDBsum; 7OI9; -. DR PDBsum; 7OIA; -. DR PDBsum; 7OIB; -. DR PDBsum; 7OIC; -. DR PDBsum; 7OID; -. DR PDBsum; 7OIE; -. DR PDBsum; 7PD3; -. DR PDBsum; 7PO4; -. DR PDBsum; 7QH6; -. DR PDBsum; 7QH7; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q96A35; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11391; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-11641; -. DR EMDB; EMD-11642; -. DR EMDB; EMD-11643; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11645; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12763; -. DR EMDB; EMD-12764; -. DR EMDB; EMD-12845; -. DR EMDB; EMD-12846; -. DR EMDB; EMD-12847; -. DR EMDB; EMD-12865; -. DR EMDB; EMD-12867; -. DR EMDB; EMD-12868; -. DR EMDB; EMD-12869; -. DR EMDB; EMD-12870; -. DR EMDB; EMD-12871; -. DR EMDB; EMD-12872; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-12919; -. DR EMDB; EMD-12920; -. DR EMDB; EMD-12921; -. DR EMDB; EMD-12922; -. DR EMDB; EMD-12923; -. DR EMDB; EMD-12924; -. DR EMDB; EMD-12925; -. DR EMDB; EMD-12926; -. DR EMDB; EMD-12927; -. DR EMDB; EMD-13329; -. DR EMDB; EMD-13562; -. DR EMDB; EMD-13965; -. DR EMDB; EMD-13967; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16899; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-23121; -. DR EMDB; EMD-3842; -. DR EMDB; EMD-3843; -. DR EMDB; EMD-4434; -. DR SMR; Q96A35; -. DR BioGRID; 122732; 216. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q96A35; -. DR IntAct; Q96A35; 54. DR MINT; Q96A35; -. DR STRING; 9606.ENSP00000354525; -. DR GlyGen; Q96A35; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96A35; -. DR PhosphoSitePlus; Q96A35; -. DR SwissPalm; Q96A35; -. DR BioMuta; MRPL24; -. DR DMDM; 74751733; -. DR EPD; Q96A35; -. DR jPOST; Q96A35; -. DR MassIVE; Q96A35; -. DR MaxQB; Q96A35; -. DR PaxDb; 9606-ENSP00000354525; -. DR PeptideAtlas; Q96A35; -. DR ProteomicsDB; 75904; -. DR Pumba; Q96A35; -. DR TopDownProteomics; Q96A35; -. DR Antibodypedia; 34225; 232 antibodies from 27 providers. DR DNASU; 79590; -. DR Ensembl; ENST00000361531.6; ENSP00000354525.2; ENSG00000143314.12. DR Ensembl; ENST00000368211.8; ENSP00000357194.4; ENSG00000143314.12. DR GeneID; 79590; -. DR KEGG; hsa:79590; -. DR MANE-Select; ENST00000361531.6; ENSP00000354525.2; NM_145729.3; NP_663781.1. DR UCSC; uc001fpw.2; human. DR AGR; HGNC:14037; -. DR CTD; 79590; -. DR DisGeNET; 79590; -. DR GeneCards; MRPL24; -. DR HGNC; HGNC:14037; MRPL24. DR HPA; ENSG00000143314; Low tissue specificity. DR MIM; 611836; gene. DR neXtProt; NX_Q96A35; -. DR OpenTargets; ENSG00000143314; -. DR PharmGKB; PA30954; -. DR VEuPathDB; HostDB:ENSG00000143314; -. DR eggNOG; KOG1708; Eukaryota. DR GeneTree; ENSGT00390000014542; -. DR HOGENOM; CLU_093315_0_1_1; -. DR InParanoid; Q96A35; -. DR OMA; DFEWRFT; -. DR OrthoDB; 36159at2759; -. DR PhylomeDB; Q96A35; -. DR TreeFam; TF105984; -. DR PathwayCommons; Q96A35; -. DR Reactome; R-HSA-5368286; Mitochondrial translation initiation. DR Reactome; R-HSA-5389840; Mitochondrial translation elongation. DR Reactome; R-HSA-5419276; Mitochondrial translation termination. DR SignaLink; Q96A35; -. DR SIGNOR; Q96A35; -. DR BioGRID-ORCS; 79590; 272 hits in 1171 CRISPR screens. DR ChiTaRS; MRPL24; human. DR GeneWiki; MRPL24; -. DR GenomeRNAi; 79590; -. DR Pharos; Q96A35; Tdark. DR PRO; PR:Q96A35; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96A35; Protein. DR Bgee; ENSG00000143314; Expressed in body of pancreas and 194 other cell types or tissues. DR ExpressionAtlas; Q96A35; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR CDD; cd06089; KOW_RPL26; 1. DR Gene3D; 2.30.30.30; -; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR003256; Ribosomal_uL24. DR InterPro; IPR005825; Ribosomal_uL24_CS. DR InterPro; IPR041988; Ribosomal_uL24_KOW. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR NCBIfam; TIGR01079; rplX_bact; 1. DR PANTHER; PTHR12903:SF0; 39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL; 1. DR PANTHER; PTHR12903; MITOCHONDRIAL RIBOSOMAL PROTEIN L24; 1. DR Pfam; PF00467; KOW; 1. DR Pfam; PF17136; ribosomal_L24; 1. DR SMART; SM00739; KOW; 1. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR PROSITE; PS01108; RIBOSOMAL_L24; 1. DR Genevisible; Q96A35; HS. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Transit peptide. FT TRANSIT 1..9 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 10..216 FT /note="Large ribosomal subunit protein uL24m" FT /id="PRO_0000270488" FT DOMAIN 56..89 FT /note="KOW" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CONFLICT 109 FT /note="I -> V (in Ref. 1; BAB14929 and 3; BAD96220)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="Q -> H (in Ref. 1; BAB14929)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="E -> D (in Ref. 1; BAB14929)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="E -> Q (in Ref. 1; BAB14929)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="R -> Q (in Ref. 3; BAD96786)" FT /evidence="ECO:0000305" FT HELIX 29..34 FT /evidence="ECO:0007829|PDB:5OOM" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:5OOM" FT TURN 68..71 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 73..80 FT /evidence="ECO:0007829|PDB:5OOM" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:5OOL" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:7OIE" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:5OOM" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:5OOL" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:3J7Y" FT HELIX 179..183 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 194..202 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 216 AA; 24915 MW; 2A1F5C88001557D0 CRC64; MRLSALLALA SKVTLPPHYR YGMSPPGSVA DKRKNPPWIR RRPVVVEPIS DEDWYLFCGD TVEILEGKDA GKQGKVVQVI RQRNWVVVGG LNTHYRYIGK TMDYRGTMIP SEAPLLHRQV KLVDPMDRKP TEIEWRFTEA GERVRVSTRS GRIIPKPEFP RADGIVPETW IDGPKDTSVE DALERTYVPC LKTLQEEVME AMGIKETRKY KKVYWY //