ID RM20_HUMAN Reviewed; 149 AA. AC Q9BYC9; B2RE41; B7Z746; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=Large ribosomal subunit protein bL20m {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L20, mitochondrial; DE Short=L20mt; DE Short=MRP-L20; DE Flags: Precursor; GN Name=MRPL20; 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), AND SUBCELLULAR LOCATION. 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Synovium, and Uterus; 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 [3] 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 [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] (ISOFORM 1). RC TISSUE=Bone marrow, Lymph, and Mammary gland; 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 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 [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:28892042, PubMed:25838379). Mature mammalian 55S CC mitochondrial ribosomes consist of a small (28S) and a large (39S) CC subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt- CC rRNA) and 30 different proteins. The 39S large subunit contains a 16S CC rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt- CC tRNA(Val)), which plays an integral structural role, and 52 different CC proteins (PubMed:25278503, PubMed:25838379). Interacts with OXA1L (By CC similarity). {ECO:0000250|UniProtKB:Q2TBR2, CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069, CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BYC9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BYC9-2; Sequence=VSP_056084; CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL20 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; AB049644; BAB40849.1; -; mRNA. DR EMBL; AK301440; BAH13482.1; -; mRNA. DR EMBL; AK315794; BAG38138.1; -; mRNA. DR EMBL; AL391244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471183; EAW56207.1; -; Genomic_DNA. DR EMBL; BC009515; AAH09515.1; -; mRNA. DR EMBL; BC014316; AAH14316.1; -; mRNA. DR EMBL; BC059945; AAH59945.1; -; mRNA. DR CCDS; CCDS26.1; -. [Q9BYC9-1] DR RefSeq; NP_060441.2; NM_017971.3. [Q9BYC9-1] DR PDB; 3J7Y; EM; 3.40 A; R=1-149. DR PDB; 3J9M; EM; 3.50 A; R=1-149. DR PDB; 5OOL; EM; 3.06 A; R=1-149. DR PDB; 5OOM; EM; 3.03 A; R=1-149. DR PDB; 6I9R; EM; 3.90 A; R=1-149. DR PDB; 6NU2; EM; 3.90 A; R=10-149. DR PDB; 6NU3; EM; 4.40 A; R=1-149. DR PDB; 6VLZ; EM; 2.97 A; R=1-149. DR PDB; 6VMI; EM; 2.96 A; R=1-149. DR PDB; 6ZM5; EM; 2.89 A; R=1-149. DR PDB; 6ZM6; EM; 2.59 A; R=1-149. DR PDB; 6ZS9; EM; 4.00 A; XR=1-149. DR PDB; 6ZSA; EM; 4.00 A; XR=1-149. DR PDB; 6ZSB; EM; 4.50 A; XR=1-149. DR PDB; 6ZSC; EM; 3.50 A; XR=1-149. DR PDB; 6ZSD; EM; 3.70 A; XR=1-149. DR PDB; 6ZSE; EM; 5.00 A; XR=1-149. DR PDB; 6ZSG; EM; 4.00 A; XR=1-149. DR PDB; 7A5F; EM; 4.40 A; R3=1-149. DR PDB; 7A5G; EM; 4.33 A; R3=1-149. DR PDB; 7A5H; EM; 3.30 A; R=1-149. DR PDB; 7A5I; EM; 3.70 A; R3=1-149. DR PDB; 7A5J; EM; 3.10 A; R=1-149. DR PDB; 7A5K; EM; 3.70 A; R3=1-149. DR PDB; 7L08; EM; 3.49 A; R=1-149. DR PDB; 7L20; EM; 3.15 A; R=1-149. DR PDB; 7O9K; EM; 3.10 A; R=1-149. DR PDB; 7O9M; EM; 2.50 A; R=1-149. DR PDB; 7ODR; EM; 2.90 A; R=1-149. DR PDB; 7ODS; EM; 3.10 A; R=1-149. DR PDB; 7ODT; EM; 3.10 A; R=1-149. DR PDB; 7OF0; EM; 2.20 A; R=1-149. DR PDB; 7OF2; EM; 2.70 A; R=1-149. DR PDB; 7OF3; EM; 2.70 A; R=1-149. DR PDB; 7OF4; EM; 2.70 A; R=1-149. DR PDB; 7OF5; EM; 2.90 A; R=1-149. DR PDB; 7OF6; EM; 2.60 A; R=1-149. DR PDB; 7OF7; EM; 2.50 A; R=1-149. DR PDB; 7OG4; EM; 3.80 A; XR=1-149. DR PDB; 7OI6; EM; 5.70 A; R=1-149. DR PDB; 7OI7; EM; 3.50 A; R=1-149. DR PDB; 7OI8; EM; 3.50 A; R=1-149. DR PDB; 7OI9; EM; 3.30 A; R=1-149. DR PDB; 7OIA; EM; 3.20 A; R=1-149. DR PDB; 7OIB; EM; 3.30 A; R=1-149. DR PDB; 7OIC; EM; 3.10 A; R=1-149. DR PDB; 7OID; EM; 3.70 A; R=1-149. DR PDB; 7OIE; EM; 3.50 A; R=1-149. DR PDB; 7PD3; EM; 3.40 A; R=1-149. DR PDB; 7PO4; EM; 2.56 A; R=1-149. DR PDB; 7QH6; EM; 3.08 A; R=1-149. DR PDB; 7QH7; EM; 2.89 A; R=10-148. DR PDB; 7QI4; EM; 2.21 A; R=1-149. DR PDB; 7QI5; EM; 2.63 A; R=1-149. DR PDB; 7QI6; EM; 2.98 A; R=1-149. DR PDB; 8ANY; EM; 2.85 A; R=1-149. DR PDB; 8OIR; EM; 3.10 A; BY=1-149. DR PDB; 8OIT; EM; 2.90 A; BY=1-149. 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; Q9BYC9; -. 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; Q9BYC9; -. DR BioGRID; 120374; 183. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q9BYC9; -. DR IntAct; Q9BYC9; 46. DR MINT; Q9BYC9; -. DR STRING; 9606.ENSP00000341082; -. DR iPTMnet; Q9BYC9; -. DR PhosphoSitePlus; Q9BYC9; -. DR SwissPalm; Q9BYC9; -. DR BioMuta; MRPL20; -. DR DMDM; 74752447; -. DR EPD; Q9BYC9; -. DR jPOST; Q9BYC9; -. DR MassIVE; Q9BYC9; -. DR MaxQB; Q9BYC9; -. DR PaxDb; 9606-ENSP00000341082; -. DR PeptideAtlas; Q9BYC9; -. DR ProteomicsDB; 6831; -. DR ProteomicsDB; 79614; -. [Q9BYC9-1] DR Pumba; Q9BYC9; -. DR Antibodypedia; 51971; 113 antibodies from 19 providers. DR DNASU; 55052; -. DR Ensembl; ENST00000344843.12; ENSP00000341082.7; ENSG00000242485.6. [Q9BYC9-1] DR Ensembl; ENST00000482352.1; ENSP00000460924.1; ENSG00000242485.6. [Q9BYC9-2] DR GeneID; 55052; -. DR KEGG; hsa:55052; -. DR MANE-Select; ENST00000344843.12; ENSP00000341082.7; NM_017971.4; NP_060441.2. DR UCSC; uc001afo.5; human. [Q9BYC9-1] DR AGR; HGNC:14478; -. DR CTD; 55052; -. DR GeneCards; MRPL20; -. DR HGNC; HGNC:14478; MRPL20. DR HPA; ENSG00000242485; Low tissue specificity. DR MIM; 611833; gene. DR neXtProt; NX_Q9BYC9; -. DR OpenTargets; ENSG00000242485; -. DR PharmGKB; PA30950; -. DR VEuPathDB; HostDB:ENSG00000242485; -. DR eggNOG; KOG4707; Eukaryota. DR GeneTree; ENSGT00390000015823; -. DR HOGENOM; CLU_123265_1_1_1; -. DR InParanoid; Q9BYC9; -. DR OMA; GRRKNVW; -. DR OrthoDB; 5475236at2759; -. DR PhylomeDB; Q9BYC9; -. DR TreeFam; TF324702; -. DR PathwayCommons; Q9BYC9; -. 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; Q9BYC9; -. DR SIGNOR; Q9BYC9; -. DR BioGRID-ORCS; 55052; 324 hits in 1161 CRISPR screens. DR ChiTaRS; MRPL20; human. DR GeneWiki; MRPL20; -. DR GenomeRNAi; 55052; -. DR Pharos; Q9BYC9; Tdark. DR PRO; PR:Q9BYC9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BYC9; Protein. DR Bgee; ENSG00000242485; Expressed in palpebral conjunctiva and 207 other cell types or tissues. DR ExpressionAtlas; Q9BYC9; 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:HPA. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0019843; F:rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR CDD; cd07026; Ribosomal_L20; 1. DR Gene3D; 1.10.1900.20; Ribosomal protein L20; 1. DR InterPro; IPR005813; Ribosomal_bL20. DR InterPro; IPR035566; Ribosomal_protein_bL20_C. DR NCBIfam; TIGR01032; rplT_bact; 1. DR PANTHER; PTHR10986; 39S RIBOSOMAL PROTEIN L20; 1. DR PANTHER; PTHR10986:SF26; 39S RIBOSOMAL PROTEIN L20, MITOCHONDRIAL; 1. DR Pfam; PF00453; Ribosomal_L20; 1. DR PRINTS; PR00062; RIBOSOMALL20. DR SUPFAM; SSF74731; Ribosomal protein L20; 1. DR Genevisible; Q9BYC9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Mitochondrion; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Transit peptide. FT TRANSIT 1..9 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:Q2TBR2" FT CHAIN 10..149 FT /note="Large ribosomal subunit protein bL20m" FT /id="PRO_0000248279" FT VAR_SEQ 93..149 FT /note="CQVELNRKVLADLAIYEPKTFKSLAALASRRRHEGFAAALGDGKEPEGIFSR FT VVQYH -> VWVSMWVPLKFWTSAETIMRGVVVLPVVPANQEAEARGSLETDFWAVVCY FT ADGVSMLSVVSIW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056084" FT HELIX 17..28 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 33..36 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 39..77 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 99..108 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 110..124 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:7QH7" SQ SEQUENCE 149 AA; 17443 MW; 53AD05B3BBD9AE6B CRC64; MVFLTAQLWL RNRVTDRYFR IQEVLKHARH FRGRKNRCYR LAVRTVIRAF VKCTKARYLK KKNMRTLWIN RITAASQEHG LKYPALIGNL VKCQVELNRK VLADLAIYEP KTFKSLAALA SRRRHEGFAA ALGDGKEPEG IFSRVVQYH //