RM24_HUMAN
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 03-AUG-2022, entry version 161.
DE RecName: Full=39S ribosomal protein L24, mitochondrial;
DE Short=L24mt;
DE Short=MRP-L24;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL24m {ECO:0000303|PubMed:25278503};
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}.
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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; 7QH6; EM; 3.08 A; V=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; 7QH6; -.
DR AlphaFoldDB; Q96A35; -.
DR SMR; Q96A35; -.
DR BioGRID; 122732; 199.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q96A35; -.
DR IntAct; Q96A35; 52.
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; Q96A35; -.
DR PeptideAtlas; Q96A35; -.
DR PRIDE; Q96A35; -.
DR ProteomicsDB; 75904; -.
DR TopDownProteomics; Q96A35; -.
DR Antibodypedia; 34225; 199 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 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; 1007373at2759; -.
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; 250 hits in 1092 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 192 other tissues.
DR ExpressionAtlas; Q96A35; baseline and differential.
DR Genevisible; Q96A35; HS.
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; IC: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; IPR041988; KOW_RPL26/RPL24.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR003256; Ribosomal_L24.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR12903; PTHR12903; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF17136; ribosomal_L24; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01079; rplX_bact; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
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="39S ribosomal protein L24, mitochondrial"
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
