ID RM46_HUMAN Reviewed; 279 AA. AC Q9H2W6; B2RD75; Q9HBU8; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 176. DE RecName: Full=Large ribosomal subunit protein mL46 {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L46, mitochondrial; DE Short=L46mt; DE Short=MRP-L46; DE AltName: Full=P2ECSL; DE Flags: Precursor; GN Name=MRPL46; Synonyms=C15orf4, LIECG2; 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 {ECO:0000312|EMBL:AAG43507.1}; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11761714; DOI=10.3109/10425170109047561; RA Carim-Todd L., Sumoy L., Andreu N., Estivill X., Escarceller M.; RT "Cloning, mapping and expression analysis of C15orf4, a novel human gene RT with homology to the yeast mitochondrial ribosomal protein Ym130 gene."; RL DNA Seq. 12:91-96(2001). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG43507.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhang K.M., Chen B.S.; RT "A novel gene identified in vascular endothelial cells."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] {ECO:0000305, ECO:0000312|EMBL:AAG43507.1} 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal 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 [6] RP IDENTIFICATION, AND SUBUNIT. RX PubMed=11551941; DOI=10.1074/jbc.m106510200; RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M., RA Moseley A., Spremulli L.L.; RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the RT complement of ribosomal proteins present."; RL J. Biol. Chem. 276:43958-43969(2001). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). 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 IDENTIFICATION BY 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. mL46 is located at the central protuberance. CC {ECO:0000269|PubMed:11551941, 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 mitochondrion-specific ribosomal protein CC mL46 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG33698.1; Type=Erroneous initiation; Evidence={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; AF210056; AAG43507.1; -; mRNA. DR EMBL; AF205435; AAG33698.1; ALT_INIT; mRNA. DR EMBL; AK315434; BAG37822.1; -; mRNA. DR EMBL; CH471101; EAX01995.1; -; Genomic_DNA. DR EMBL; BC017883; AAH17883.1; -; mRNA. DR CCDS; CCDS10341.1; -. DR RefSeq; NP_071446.2; NM_022163.3. DR PDB; 3J7Y; EM; 3.40 A; e=1-279. DR PDB; 3J9M; EM; 3.50 A; e=1-279. DR PDB; 5OOL; EM; 3.06 A; e=1-279. DR PDB; 5OOM; EM; 3.03 A; e=1-279. DR PDB; 6I9R; EM; 3.90 A; e=1-279. DR PDB; 6NU2; EM; 3.90 A; e=43-279. DR PDB; 6NU3; EM; 4.40 A; e=1-279. DR PDB; 6VLZ; EM; 2.97 A; e=1-279. DR PDB; 6VMI; EM; 2.96 A; e=1-279. DR PDB; 6ZM5; EM; 2.89 A; e=1-279. DR PDB; 6ZM6; EM; 2.59 A; e=1-279. DR PDB; 6ZS9; EM; 4.00 A; e=1-279. DR PDB; 6ZSA; EM; 4.00 A; e=1-279. DR PDB; 6ZSB; EM; 4.50 A; e=1-279. DR PDB; 6ZSC; EM; 3.50 A; e=1-279. DR PDB; 6ZSD; EM; 3.70 A; e=1-279. DR PDB; 6ZSE; EM; 5.00 A; e=1-279. DR PDB; 6ZSG; EM; 4.00 A; e=1-279. DR PDB; 7A5F; EM; 4.40 A; e3=1-279. DR PDB; 7A5G; EM; 4.33 A; e3=1-279. DR PDB; 7A5H; EM; 3.30 A; e=1-279. DR PDB; 7A5I; EM; 3.70 A; e3=1-279. DR PDB; 7A5J; EM; 3.10 A; e=1-279. DR PDB; 7A5K; EM; 3.70 A; e3=1-279. DR PDB; 7L08; EM; 3.49 A; e=1-279. DR PDB; 7L20; EM; 3.15 A; e=1-279. DR PDB; 7O9K; EM; 3.10 A; e=1-279. DR PDB; 7O9M; EM; 2.50 A; e=1-279. DR PDB; 7ODR; EM; 2.90 A; e=1-279. DR PDB; 7ODS; EM; 3.10 A; e=1-279. DR PDB; 7ODT; EM; 3.10 A; e=1-279. DR PDB; 7OF0; EM; 2.20 A; e=1-279. DR PDB; 7OF2; EM; 2.70 A; e=1-279. DR PDB; 7OF3; EM; 2.70 A; e=1-279. DR PDB; 7OF4; EM; 2.70 A; e=1-279. DR PDB; 7OF5; EM; 2.90 A; e=1-279. DR PDB; 7OF6; EM; 2.60 A; e=1-279. DR PDB; 7OF7; EM; 2.50 A; e=1-279. DR PDB; 7OG4; EM; 3.80 A; e=1-279. DR PDB; 7OI7; EM; 3.50 A; e=1-279. DR PDB; 7OI8; EM; 3.50 A; e=1-279. DR PDB; 7OI9; EM; 3.30 A; e=1-279. DR PDB; 7OIA; EM; 3.20 A; e=1-279. DR PDB; 7OIB; EM; 3.30 A; e=1-279. DR PDB; 7OIC; EM; 3.10 A; e=1-279. DR PDB; 7OID; EM; 3.70 A; e=1-279. DR PDB; 7OIE; EM; 3.50 A; e=1-279. DR PDB; 7PD3; EM; 3.40 A; e=1-279. DR PDB; 7PO4; EM; 2.56 A; e=1-279. DR PDB; 7QI4; EM; 2.21 A; e=1-279. DR PDB; 7QI5; EM; 2.63 A; e=1-279. DR PDB; 7QI6; EM; 2.98 A; e=1-279. DR PDB; 8ANY; EM; 2.85 A; e=1-279. DR PDB; 8OIR; EM; 3.10 A; Bv=1-279. DR PDB; 8OIT; EM; 2.90 A; Bv=1-279. 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; 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; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q9H2W6; -. 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-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-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; Q9H2W6; -. DR BioGRID; 117757; 197. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q9H2W6; -. DR IntAct; Q9H2W6; 47. DR MINT; Q9H2W6; -. DR STRING; 9606.ENSP00000312311; -. DR GlyGen; Q9H2W6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H2W6; -. DR MetOSite; Q9H2W6; -. DR PhosphoSitePlus; Q9H2W6; -. DR SwissPalm; Q9H2W6; -. DR BioMuta; MRPL46; -. DR DMDM; 52783325; -. DR EPD; Q9H2W6; -. DR jPOST; Q9H2W6; -. DR MassIVE; Q9H2W6; -. DR MaxQB; Q9H2W6; -. DR PaxDb; 9606-ENSP00000312311; -. DR PeptideAtlas; Q9H2W6; -. DR ProteomicsDB; 80610; -. DR Pumba; Q9H2W6; -. DR Antibodypedia; 58578; 214 antibodies from 27 providers. DR DNASU; 26589; -. DR Ensembl; ENST00000312475.5; ENSP00000312311.4; ENSG00000259494.2. DR GeneID; 26589; -. DR KEGG; hsa:26589; -. DR MANE-Select; ENST00000312475.5; ENSP00000312311.4; NM_022163.4; NP_071446.2. DR UCSC; uc002bmj.3; human. DR AGR; HGNC:1192; -. DR CTD; 26589; -. DR DisGeNET; 26589; -. DR GeneCards; MRPL46; -. DR HGNC; HGNC:1192; MRPL46. DR HPA; ENSG00000259494; Low tissue specificity. DR MIM; 611851; gene. DR neXtProt; NX_Q9H2W6; -. DR PharmGKB; PA30978; -. DR VEuPathDB; HostDB:ENSG00000259494; -. DR eggNOG; KOG4548; Eukaryota. DR GeneTree; ENSGT00390000015400; -. DR HOGENOM; CLU_079736_1_0_1; -. DR InParanoid; Q9H2W6; -. DR OMA; EKWDLYA; -. DR OrthoDB; 36305at2759; -. DR PhylomeDB; Q9H2W6; -. DR PathwayCommons; Q9H2W6; -. 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; Q9H2W6; -. DR SIGNOR; Q9H2W6; -. DR BioGRID-ORCS; 26589; 335 hits in 1163 CRISPR screens. DR ChiTaRS; MRPL46; human. DR GenomeRNAi; 26589; -. DR Pharos; Q9H2W6; Tdark. DR PRO; PR:Q9H2W6; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9H2W6; Protein. DR Bgee; ENSG00000259494; Expressed in adrenal tissue and 99 other cell types or tissues. DR ExpressionAtlas; Q9H2W6; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. 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:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR CDD; cd04661; MRP_L46; 1. DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR040008; Ribosomal_mL46. DR InterPro; IPR021757; Ribosomal_mL46_N. DR InterPro; IPR033650; Ribosomal_mL46_NUDIX. DR PANTHER; PTHR13124:SF12; 39S RIBOSOMAL PROTEIN L46, MITOCHONDRIAL; 1. DR PANTHER; PTHR13124; 39S RIBOSOMAL PROTEIN L46, MITOCHONDRIAL PRECURSOR-RELATED; 1. DR Pfam; PF11788; MRP-L46; 1. DR SUPFAM; SSF55811; Nudix; 1. DR Genevisible; Q9H2W6; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Mitochondrion; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..279 FT /note="Large ribosomal subunit protein mL46" FT /id="PRO_0000030576" FT MOD_RES 230 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 106 FT /note="H -> Y (in dbSNP:rs16941888)" FT /id="VAR_052046" FT CONFLICT 197 FT /note="E -> K (in Ref. 2; AAG33698)" FT /evidence="ECO:0000305" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 65..81 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 86..89 FT /evidence="ECO:0007829|PDB:5OOM" FT HELIX 92..103 FT /evidence="ECO:0007829|PDB:5OOM" FT HELIX 117..130 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:7OI7" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:3J7Y" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:7OIA" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:3J7Y" FT STRAND 228..233 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:3J7Y" FT HELIX 259..263 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 267..270 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 279 AA; 31705 MW; EDA966D758715378 CRC64; MAAPVRRTLL GVAGGWRRFE RLWAGSLSSR SLALAAAPSS NGSPWRLLGA LCLQRPPVVS KPLTPLQEEM ASLLQQIEIE RSLYSDHELR ALDENQRLAK KKADLHDEED EQDILLAQDL EDMWEQKFLQ FKLGARITEA DEKNDRTSLN RKLDRNLVLL VREKFGDQDV WILPQAEWQP GETLRGTAER TLATLSENNM EAKFLGNAPC GHYTFKFPQA MRTESNLGAK VFFFKALLLT GDFSQAGNKG HHVWVTKDEL GDYLKPKYLA QVRRFVSDL //