RM50_HUMAN
ID RM50_HUMAN Reviewed; 158 AA.
AC Q8N5N7; B7Z358; Q5T7E0; Q9NX15;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=39S ribosomal protein L50, mitochondrial;
DE Short=L50mt;
DE Short=MRP-L50;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL50 {ECO:0000303|PubMed:25278503};
GN Name=MRPL50;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Carcinoma, Hepatoma, and Hippocampus;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-127.
RC TISSUE=Skin;
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 [4]
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 [5]
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 [6] {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 [7] {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 [8] {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. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N5N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5N7-2; Sequence=VSP_056091;
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL50 family. {ECO:0000305}.
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DR EMBL; AK000500; BAA91207.1; -; mRNA.
DR EMBL; AK025643; BAB15200.1; -; mRNA.
DR EMBL; AK295521; BAH12094.1; -; mRNA.
DR EMBL; AL353621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032008; AAH32008.1; -; mRNA.
DR CCDS; CCDS6753.1; -. [Q8N5N7-1]
DR RefSeq; NP_061924.1; NM_019051.2. [Q8N5N7-1]
DR PDB; 3J7Y; EM; 3.40 A; h=1-158.
DR PDB; 3J9M; EM; 3.50 A; h=1-158.
DR PDB; 5OOL; EM; 3.06 A; h=1-158.
DR PDB; 5OOM; EM; 3.03 A; h=1-158.
DR PDB; 6I9R; EM; 3.90 A; h=1-158.
DR PDB; 6NU2; EM; 3.90 A; h=56-158.
DR PDB; 6NU3; EM; 4.40 A; h=1-158.
DR PDB; 6VLZ; EM; 2.97 A; h=1-158.
DR PDB; 6VMI; EM; 2.96 A; h=1-158.
DR PDB; 6ZM5; EM; 2.89 A; h=1-158.
DR PDB; 6ZM6; EM; 2.59 A; h=1-158.
DR PDB; 6ZS9; EM; 4.00 A; h=1-158.
DR PDB; 6ZSA; EM; 4.00 A; h=1-158.
DR PDB; 6ZSB; EM; 4.50 A; h=1-158.
DR PDB; 6ZSC; EM; 3.50 A; h=1-158.
DR PDB; 6ZSD; EM; 3.70 A; h=1-158.
DR PDB; 6ZSE; EM; 5.00 A; h=1-158.
DR PDB; 6ZSG; EM; 4.00 A; h=1-158.
DR PDB; 7A5F; EM; 4.40 A; h3=1-158.
DR PDB; 7A5G; EM; 4.33 A; h3=1-158.
DR PDB; 7A5H; EM; 3.30 A; h=1-158.
DR PDB; 7A5I; EM; 3.70 A; h3=1-158.
DR PDB; 7A5J; EM; 3.10 A; h=1-158.
DR PDB; 7A5K; EM; 3.70 A; h3=1-158.
DR PDB; 7L08; EM; 3.49 A; h=1-158.
DR PDB; 7L20; EM; 3.15 A; h=1-158.
DR PDB; 7O9K; EM; 3.10 A; h=1-158.
DR PDB; 7O9M; EM; 2.50 A; h=1-158.
DR PDB; 7ODR; EM; 2.90 A; h=1-158.
DR PDB; 7ODS; EM; 3.10 A; h=1-158.
DR PDB; 7ODT; EM; 3.10 A; h=1-158.
DR PDB; 7OF0; EM; 2.20 A; h=1-158.
DR PDB; 7OF2; EM; 2.70 A; h=1-158.
DR PDB; 7OF3; EM; 2.70 A; h=1-158.
DR PDB; 7OF4; EM; 2.70 A; h=1-158.
DR PDB; 7OF5; EM; 2.90 A; h=1-158.
DR PDB; 7OF6; EM; 2.60 A; h=1-158.
DR PDB; 7OF7; EM; 2.50 A; h=1-158.
DR PDB; 7OG4; EM; 3.80 A; h=1-158.
DR PDB; 7OI6; EM; 5.70 A; h=1-158.
DR PDB; 7OI7; EM; 3.50 A; h=1-158.
DR PDB; 7OI8; EM; 3.50 A; h=1-158.
DR PDB; 7OI9; EM; 3.30 A; h=1-158.
DR PDB; 7OIA; EM; 3.20 A; h=1-158.
DR PDB; 7OIB; EM; 3.30 A; h=1-158.
DR PDB; 7OIC; EM; 3.10 A; h=1-158.
DR PDB; 7OID; EM; 3.70 A; h=1-158.
DR PDB; 7OIE; EM; 3.50 A; h=1-158.
DR PDB; 7PD3; EM; 3.40 A; h=1-158.
DR PDB; 7QH6; EM; 3.08 A; h=1-158.
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; Q8N5N7; -.
DR SMR; Q8N5N7; -.
DR BioGRID; 120021; 235.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q8N5N7; -.
DR IntAct; Q8N5N7; 118.
DR MINT; Q8N5N7; -.
DR STRING; 9606.ENSP00000363999; -.
DR GlyGen; Q8N5N7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N5N7; -.
DR PhosphoSitePlus; Q8N5N7; -.
DR BioMuta; MRPL50; -.
DR DMDM; 118573685; -.
DR EPD; Q8N5N7; -.
DR jPOST; Q8N5N7; -.
DR MassIVE; Q8N5N7; -.
DR MaxQB; Q8N5N7; -.
DR PaxDb; Q8N5N7; -.
DR PeptideAtlas; Q8N5N7; -.
DR PRIDE; Q8N5N7; -.
DR ProteomicsDB; 6492; -.
DR ProteomicsDB; 72078; -. [Q8N5N7-1]
DR TopDownProteomics; Q8N5N7-1; -. [Q8N5N7-1]
DR Antibodypedia; 14646; 144 antibodies from 24 providers.
DR DNASU; 54534; -.
DR Ensembl; ENST00000374865.5; ENSP00000363999.4; ENSG00000136897.8. [Q8N5N7-1]
DR GeneID; 54534; -.
DR KEGG; hsa:54534; -.
DR MANE-Select; ENST00000374865.5; ENSP00000363999.4; NM_019051.3; NP_061924.1.
DR UCSC; uc004bbe.3; human. [Q8N5N7-1]
DR CTD; 54534; -.
DR GeneCards; MRPL50; -.
DR HGNC; HGNC:16654; MRPL50.
DR HPA; ENSG00000136897; Low tissue specificity.
DR MIM; 611854; gene.
DR neXtProt; NX_Q8N5N7; -.
DR OpenTargets; ENSG00000136897; -.
DR PharmGKB; PA30983; -.
DR VEuPathDB; HostDB:ENSG00000136897; -.
DR eggNOG; ENOG502S27V; Eukaryota.
DR GeneTree; ENSGT00390000004279; -.
DR HOGENOM; CLU_137129_0_0_1; -.
DR InParanoid; Q8N5N7; -.
DR OMA; NLKITWN; -.
DR OrthoDB; 1586864at2759; -.
DR PhylomeDB; Q8N5N7; -.
DR TreeFam; TF105895; -.
DR PathwayCommons; Q8N5N7; -.
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; Q8N5N7; -.
DR SIGNOR; Q8N5N7; -.
DR BioGRID-ORCS; 54534; 269 hits in 1083 CRISPR screens.
DR ChiTaRS; MRPL50; human.
DR GenomeRNAi; 54534; -.
DR Pharos; Q8N5N7; Tdark.
DR PRO; PR:Q8N5N7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N5N7; protein.
DR Bgee; ENSG00000136897; Expressed in left ventricle myocardium and 194 other tissues.
DR Genevisible; Q8N5N7; HS.
DR GO; GO:0005829; C:cytosol; 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:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR018305; Ribosomal_L50_mt.
DR PANTHER; PTHR31542; PTHR31542; 1.
DR Pfam; PF10501; Ribosomal_L50; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..158
FT /note="39S ribosomal protein L50, mitochondrial"
FT /id="PRO_0000261659"
FT VAR_SEQ 123..158
FT /note="VRDVLDFYNVPIQDRSKFDELSASNLPPNLKITWSY -> GYSFEEGKIQLG
FT I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056091"
FT VARIANT 127
FT /note="L -> F (in dbSNP:rs8131)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029474"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 158 AA; 18325 MW; F8FD54809C08EF0E CRC64;
MAARSVSGIT RRVFMWTVSG TPCREFWSRF RKEKEPVVVE TVEEKKEPIL VCPPLRSRAY
TPPEDLQSRL ESYVKEVFGS SLPSNWQDIS LEDSRLKFNL LAHLADDLGH VVPNSRLHQM
CRVRDVLDFY NVPIQDRSKF DELSASNLPP NLKITWSY
