ID RM13_HUMAN Reviewed; 178 AA. AC Q9BYD1; B2R4R8; Q9UI04; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=Large ribosomal subunit protein uL13m {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L13, mitochondrial; DE Short=L13mt; DE Short=MRP-L13; GN Name=MRPL13; 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]. RX PubMed=11279069; DOI=10.1074/jbc.m100432200; RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., RA Watanabe K.; RT "Structural compensation for the deficit of rRNA with proteins in the RT mammalian mitochondrial ribosome. Systematic analysis of protein components RT of the large ribosomal subunit from mammalian mitochondria."; RL J. Biol. Chem. 276:21724-21736(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Adrenal gland; RA Ren S., Jiang C., Huang C., Li Y., Lin W., Zhou J., Yu Y., Xu S., Wang Y., RA Han Z., Chen Z., Fu G.; RT "A novel gene expressed in human adrenal gland."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; 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] 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=Brain, and Placenta; 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 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 [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [8] {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 [9] {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 [10] {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:25278503, PubMed:25838379, PubMed:28892042). 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 (PubMed:25278503, PubMed:25838379). Interacts with CC OXA1L (By similarity). {ECO:0000250|UniProtKB:Q3SYS1, CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042}. CC -!- INTERACTION: CC Q9BYD1; P42858: HTT; NbExp=3; IntAct=EBI-1054936, EBI-466029; 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 uL13 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF17202.1; Type=Frameshift; 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; AB049640; BAB40845.1; -; mRNA. DR EMBL; AF112214; AAF17202.1; ALT_FRAME; mRNA. DR EMBL; AK311924; BAG34865.1; -; mRNA. DR EMBL; CH471060; EAW92004.1; -; Genomic_DNA. DR EMBL; BC009190; AAH09190.1; -; mRNA. DR EMBL; BC021744; AAH21744.1; -; mRNA. DR CCDS; CCDS6332.1; -. DR RefSeq; NP_054797.2; NM_014078.5. DR PDB; 3J7Y; EM; 3.40 A; K=1-178. DR PDB; 3J9M; EM; 3.50 A; K=1-178. DR PDB; 5OOL; EM; 3.06 A; K=1-178. DR PDB; 5OOM; EM; 3.03 A; K=1-178. DR PDB; 6I9R; EM; 3.90 A; K=1-178. DR PDB; 6NU2; EM; 3.90 A; K=2-178. DR PDB; 6NU3; EM; 4.40 A; K=1-178. DR PDB; 6VLZ; EM; 2.97 A; K=1-178. DR PDB; 6VMI; EM; 2.96 A; K=1-178. DR PDB; 6ZM5; EM; 2.89 A; K=2-178. DR PDB; 6ZM6; EM; 2.59 A; K=2-178. DR PDB; 6ZS9; EM; 4.00 A; XK=1-178. DR PDB; 6ZSA; EM; 4.00 A; XK=1-178. DR PDB; 6ZSB; EM; 4.50 A; XK=1-178. DR PDB; 6ZSC; EM; 3.50 A; XK=1-178. DR PDB; 6ZSD; EM; 3.70 A; XK=1-178. DR PDB; 6ZSE; EM; 5.00 A; XK=1-178. DR PDB; 6ZSG; EM; 4.00 A; XK=1-178. DR PDB; 7A5F; EM; 4.40 A; K3=1-178. DR PDB; 7A5G; EM; 4.33 A; K3=1-178. DR PDB; 7A5H; EM; 3.30 A; K=1-178. DR PDB; 7A5I; EM; 3.70 A; K3=1-178. DR PDB; 7A5J; EM; 3.10 A; K=1-178. DR PDB; 7A5K; EM; 3.70 A; K3=1-178. DR PDB; 7L08; EM; 3.49 A; K=1-178. DR PDB; 7L20; EM; 3.15 A; K=1-178. DR PDB; 7O9K; EM; 3.10 A; K=1-178. DR PDB; 7O9M; EM; 2.50 A; K=1-178. DR PDB; 7ODR; EM; 2.90 A; K=1-178. DR PDB; 7ODS; EM; 3.10 A; K=1-178. DR PDB; 7ODT; EM; 3.10 A; K=1-178. DR PDB; 7OF0; EM; 2.20 A; K=1-178. DR PDB; 7OF2; EM; 2.70 A; K=1-178. DR PDB; 7OF3; EM; 2.70 A; K=1-178. DR PDB; 7OF4; EM; 2.70 A; K=1-178. DR PDB; 7OF5; EM; 2.90 A; K=1-178. DR PDB; 7OF6; EM; 2.60 A; K=1-178. DR PDB; 7OF7; EM; 2.50 A; K=1-178. DR PDB; 7OG4; EM; 3.80 A; XK=1-178. DR PDB; 7OI6; EM; 5.70 A; K=1-178. DR PDB; 7OI7; EM; 3.50 A; K=1-178. DR PDB; 7OI8; EM; 3.50 A; K=1-178. DR PDB; 7OI9; EM; 3.30 A; K=1-178. DR PDB; 7OIA; EM; 3.20 A; K=1-178. DR PDB; 7OIB; EM; 3.30 A; K=1-178. DR PDB; 7OIC; EM; 3.10 A; K=1-178. DR PDB; 7OID; EM; 3.70 A; K=1-178. DR PDB; 7OIE; EM; 3.50 A; K=1-178. DR PDB; 7PD3; EM; 3.40 A; K=1-178. DR PDB; 7PO4; EM; 2.56 A; K=2-178. DR PDB; 7QH6; EM; 3.08 A; K=1-178. DR PDB; 7QH7; EM; 2.89 A; K=2-178. DR PDB; 7QI4; EM; 2.21 A; K=1-178. DR PDB; 7QI5; EM; 2.63 A; K=1-178. DR PDB; 7QI6; EM; 2.98 A; K=1-178. DR PDB; 8ANY; EM; 2.85 A; K=1-178. DR PDB; 8OIR; EM; 3.10 A; BR=1-178. DR PDB; 8OIT; EM; 2.90 A; BR=1-178. 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; Q9BYD1; -. 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; Q9BYD1; -. DR BioGRID; 118817; 235. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q9BYD1; -. DR IntAct; Q9BYD1; 61. DR MINT; Q9BYD1; -. DR STRING; 9606.ENSP00000306548; -. DR GlyGen; Q9BYD1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BYD1; -. DR PhosphoSitePlus; Q9BYD1; -. DR SwissPalm; Q9BYD1; -. DR BioMuta; MRPL13; -. DR DMDM; 22257023; -. DR EPD; Q9BYD1; -. DR jPOST; Q9BYD1; -. DR MassIVE; Q9BYD1; -. DR MaxQB; Q9BYD1; -. DR PaxDb; 9606-ENSP00000306548; -. DR PeptideAtlas; Q9BYD1; -. DR ProteomicsDB; 79615; -. DR Pumba; Q9BYD1; -. DR TopDownProteomics; Q9BYD1; -. DR Antibodypedia; 26860; 224 antibodies from 26 providers. DR DNASU; 28998; -. DR Ensembl; ENST00000306185.8; ENSP00000306548.3; ENSG00000172172.8. DR GeneID; 28998; -. DR KEGG; hsa:28998; -. DR MANE-Select; ENST00000306185.8; ENSP00000306548.3; NM_014078.6; NP_054797.2. DR UCSC; uc003ypa.4; human. DR AGR; HGNC:14278; -. DR CTD; 28998; -. DR DisGeNET; 28998; -. DR GeneCards; MRPL13; -. DR HGNC; HGNC:14278; MRPL13. DR HPA; ENSG00000172172; Low tissue specificity. DR MIM; 610200; gene. DR neXtProt; NX_Q9BYD1; -. DR OpenTargets; ENSG00000172172; -. DR PharmGKB; PA30942; -. DR VEuPathDB; HostDB:ENSG00000172172; -. DR eggNOG; KOG3203; Eukaryota. DR GeneTree; ENSGT00390000001515; -. DR HOGENOM; CLU_082184_1_3_1; -. DR InParanoid; Q9BYD1; -. DR OMA; HKPIYTP; -. DR OrthoDB; 379801at2759; -. DR PhylomeDB; Q9BYD1; -. DR TreeFam; TF312914; -. DR PathwayCommons; Q9BYD1; -. 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; Q9BYD1; -. DR SIGNOR; Q9BYD1; -. DR BioGRID-ORCS; 28998; 341 hits in 1175 CRISPR screens. DR ChiTaRS; MRPL13; human. DR GenomeRNAi; 28998; -. DR Pharos; Q9BYD1; Tbio. DR PRO; PR:Q9BYD1; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9BYD1; Protein. DR Bgee; ENSG00000172172; Expressed in mucosa of transverse colon and 193 other cell types or tissues. DR ExpressionAtlas; Q9BYD1; 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:0005761; C:mitochondrial ribosome; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR GO; GO:0006412; P:translation; NAS:UniProtKB. DR CDD; cd00392; Ribosomal_L13; 1. DR Gene3D; 3.90.1180.10; Ribosomal protein L13; 1. DR HAMAP; MF_01366; Ribosomal_uL13; 1. DR InterPro; IPR005822; Ribosomal_uL13. DR InterPro; IPR005823; Ribosomal_uL13_bac-type. DR InterPro; IPR023563; Ribosomal_uL13_CS. DR InterPro; IPR036899; Ribosomal_uL13_sf. DR NCBIfam; TIGR01066; rplM_bact; 1. DR PANTHER; PTHR11545:SF2; 39S RIBOSOMAL PROTEIN L13, MITOCHONDRIAL; 1. DR PANTHER; PTHR11545; RIBOSOMAL PROTEIN L13; 1. DR Pfam; PF00572; Ribosomal_L13; 1. DR PIRSF; PIRSF002181; Ribosomal_L13; 1. DR SUPFAM; SSF52161; Ribosomal protein L13; 1. DR PROSITE; PS00783; RIBOSOMAL_L13; 1. DR Genevisible; Q9BYD1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Mitochondrion; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:25944712" FT CHAIN 2..178 FT /note="Large ribosomal subunit protein uL13m" FT /id="PRO_0000133793" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:25944712" FT HELIX 6..14 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 18..22 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 28..40 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 41..43 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 49..52 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 71..74 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 92..98 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 102..111 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 118..123 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 135..140 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 141..144 FT /evidence="ECO:0007829|PDB:7QH7" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 160..165 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:7QH7" SQ SEQUENCE 178 AA; 20692 MW; AF4FD524CC234D52 CRC64; MSSFSRAPQQ WATFARIWYL LDGKMQPPGK LAAMASIRLQ GLHKPVYHAL SDCGDHVVIM NTRHIAFSGN KWEQKVYSSH TGYPGGFRQV TAAQLHLRDP VAIVKLAIYG MLPKNLHRRT MMERLHLFPD EYIPEDILKN LVEELPQPRK IPKRLDEYTQ EEIDAFPRLW TPPEDYRL //