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RM20_HUMAN
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   03-AUG-2022, entry version 172.
DE   RecName: Full=39S ribosomal protein L20, mitochondrial;
DE            Short=L20mt;
DE            Short=MRP-L20;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein bL20m {ECO:0000303|PubMed:25278503};
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}.
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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; 7QH6; EM; 3.08 A; R=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; 7QH6; -.
DR   AlphaFoldDB; Q9BYC9; -.
DR   SMR; Q9BYC9; -.
DR   BioGRID; 120374; 169.
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; Q9BYC9; -.
DR   PeptideAtlas; Q9BYC9; -.
DR   PRIDE; Q9BYC9; -.
DR   ProteomicsDB; 6831; -.
DR   ProteomicsDB; 79614; -. [Q9BYC9-1]
DR   Antibodypedia; 51971; 94 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   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; 1582185at2759; -.
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; 312 hits in 1082 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 205 other tissues.
DR   ExpressionAtlas; Q9BYC9; baseline and differential.
DR   Genevisible; Q9BYC9; 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:0005761; C:mitochondrial ribosome; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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; IC:ComplexPortal.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   CDD; cd07026; Ribosomal_L20; 1.
DR   Gene3D; 1.10.1900.20; -; 1.
DR   InterPro; IPR005813; Ribosomal_L20.
DR   InterPro; IPR035566; Ribosomal_protein_L20_C.
DR   PANTHER; PTHR10986; PTHR10986; 1.
DR   Pfam; PF00453; Ribosomal_L20; 1.
DR   PRINTS; PR00062; RIBOSOMALL20.
DR   SUPFAM; SSF74731; SSF74731; 1.
DR   TIGRFAMs; TIGR01032; rplT_bact; 1.
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="39S ribosomal protein L20, mitochondrial"
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:3J7Y"
SQ   SEQUENCE   149 AA;  17443 MW;  53AD05B3BBD9AE6B CRC64;
     MVFLTAQLWL RNRVTDRYFR IQEVLKHARH FRGRKNRCYR LAVRTVIRAF VKCTKARYLK
     KKNMRTLWIN RITAASQEHG LKYPALIGNL VKCQVELNRK VLADLAIYEP KTFKSLAALA
     SRRRHEGFAA ALGDGKEPEG IFSRVVQYH
 
 
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