RM51_HUMAN
ID RM51_HUMAN Reviewed; 128 AA.
AC Q4U2R6; Q96Q57; Q9BQ36; Q9P0N7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=39S ribosomal protein L51, mitochondrial;
DE Short=L51mt;
DE Short=MRP-L51;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL51 {ECO:0000303|PubMed:25278503};
DE AltName: Full=bMRP-64;
DE Short=bMRP64;
DE Flags: Precursor;
GN Name=MRPL51; Synonyms=MRP64; ORFNames=CDA09, HSPC241;
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=11402041; DOI=10.1074/jbc.m103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-63.
RX PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA Watanabe K., Tanaka T.;
RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes to
RT the chromosomes and implications for human disorders.";
RL Genomics 77:65-70(2001).
RN [6]
RP IDENTIFICATION.
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 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 [8]
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 [9] {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 [10] {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 [11] {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 (PubMed:25278503, PubMed:25838379). Interacts with
CC OXA1L (By similarity). {ECO:0000250|UniProtKB:P0C2B6,
CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC 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 mL51 family. {ECO:0000305}.
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DR EMBL; AB049959; BAB41012.1; -; mRNA.
DR EMBL; AF212248; AAK14931.1; -; mRNA.
DR EMBL; AF151075; AAF36161.1; -; mRNA.
DR EMBL; BC000191; AAH00191.1; -; mRNA.
DR EMBL; BC014329; AAH14329.1; -; mRNA.
DR EMBL; AB051355; BAB54944.1; -; Genomic_DNA.
DR CCDS; CCDS8547.1; -.
DR RefSeq; NP_057581.2; NM_016497.3.
DR PDB; 3J7Y; EM; 3.40 A; i=1-128.
DR PDB; 3J9M; EM; 3.50 A; i=1-128.
DR PDB; 5OOL; EM; 3.06 A; i=1-128.
DR PDB; 5OOM; EM; 3.03 A; i=1-128.
DR PDB; 6I9R; EM; 3.90 A; i=1-128.
DR PDB; 6NU2; EM; 3.90 A; i=32-128.
DR PDB; 6NU3; EM; 4.40 A; i=1-128.
DR PDB; 6VLZ; EM; 2.97 A; i=1-128.
DR PDB; 6VMI; EM; 2.96 A; i=1-128.
DR PDB; 6ZM5; EM; 2.89 A; i=1-128.
DR PDB; 6ZM6; EM; 2.59 A; i=1-128.
DR PDB; 6ZS9; EM; 4.00 A; i=1-128.
DR PDB; 6ZSA; EM; 4.00 A; i=1-128.
DR PDB; 6ZSB; EM; 4.50 A; i=1-128.
DR PDB; 6ZSC; EM; 3.50 A; i=1-128.
DR PDB; 6ZSD; EM; 3.70 A; i=1-128.
DR PDB; 6ZSE; EM; 5.00 A; i=1-128.
DR PDB; 6ZSG; EM; 4.00 A; i=1-128.
DR PDB; 7A5F; EM; 4.40 A; i3=1-128.
DR PDB; 7A5G; EM; 4.33 A; i3=1-128.
DR PDB; 7A5H; EM; 3.30 A; i=1-128.
DR PDB; 7A5I; EM; 3.70 A; i3=1-128.
DR PDB; 7A5J; EM; 3.10 A; i=1-128.
DR PDB; 7A5K; EM; 3.70 A; i3=1-128.
DR PDB; 7L08; EM; 3.49 A; i=1-128.
DR PDB; 7L20; EM; 3.15 A; i=1-128.
DR PDB; 7O9K; EM; 3.10 A; i=1-128.
DR PDB; 7O9M; EM; 2.50 A; i=1-128.
DR PDB; 7ODR; EM; 2.90 A; i=1-128.
DR PDB; 7ODS; EM; 3.10 A; i=1-128.
DR PDB; 7ODT; EM; 3.10 A; i=1-128.
DR PDB; 7OF0; EM; 2.20 A; i=1-128.
DR PDB; 7OF2; EM; 2.70 A; i=1-128.
DR PDB; 7OF3; EM; 2.70 A; i=1-128.
DR PDB; 7OF4; EM; 2.70 A; i=1-128.
DR PDB; 7OF5; EM; 2.90 A; i=1-128.
DR PDB; 7OF6; EM; 2.60 A; i=1-128.
DR PDB; 7OF7; EM; 2.50 A; i=1-128.
DR PDB; 7OG4; EM; 3.80 A; i=1-128.
DR PDB; 7OI6; EM; 5.70 A; i=1-128.
DR PDB; 7OI7; EM; 3.50 A; i=1-128.
DR PDB; 7OI8; EM; 3.50 A; i=1-128.
DR PDB; 7OI9; EM; 3.30 A; i=1-128.
DR PDB; 7OIA; EM; 3.20 A; i=1-128.
DR PDB; 7OIB; EM; 3.30 A; i=1-128.
DR PDB; 7OIC; EM; 3.10 A; i=1-128.
DR PDB; 7OID; EM; 3.70 A; i=1-128.
DR PDB; 7OIE; EM; 3.50 A; i=1-128.
DR PDB; 7PD3; EM; 3.40 A; i=1-128.
DR PDB; 7QH6; EM; 3.08 A; i=1-128.
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; Q4U2R6; -.
DR SMR; Q4U2R6; -.
DR BioGRID; 119414; 140.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q4U2R6; -.
DR IntAct; Q4U2R6; 23.
DR MINT; Q4U2R6; -.
DR STRING; 9606.ENSP00000229238; -.
DR BioMuta; MRPL51; -.
DR DMDM; 74762954; -.
DR EPD; Q4U2R6; -.
DR jPOST; Q4U2R6; -.
DR MassIVE; Q4U2R6; -.
DR MaxQB; Q4U2R6; -.
DR PaxDb; Q4U2R6; -.
DR PeptideAtlas; Q4U2R6; -.
DR PRIDE; Q4U2R6; -.
DR ProteomicsDB; 62262; -.
DR TopDownProteomics; Q4U2R6; -.
DR Antibodypedia; 22416; 161 antibodies from 24 providers.
DR DNASU; 51258; -.
DR Ensembl; ENST00000229238.5; ENSP00000229238.3; ENSG00000111639.8.
DR GeneID; 51258; -.
DR KEGG; hsa:51258; -.
DR MANE-Select; ENST00000229238.5; ENSP00000229238.3; NM_016497.4; NP_057581.2.
DR UCSC; uc001qom.3; human.
DR CTD; 51258; -.
DR GeneCards; MRPL51; -.
DR HGNC; HGNC:14044; MRPL51.
DR HPA; ENSG00000111639; Low tissue specificity.
DR MIM; 611855; gene.
DR neXtProt; NX_Q4U2R6; -.
DR OpenTargets; ENSG00000111639; -.
DR PharmGKB; PA30984; -.
DR VEuPathDB; HostDB:ENSG00000111639; -.
DR eggNOG; KOG4045; Eukaryota.
DR GeneTree; ENSGT00390000018821; -.
DR HOGENOM; CLU_150741_0_0_1; -.
DR InParanoid; Q4U2R6; -.
DR OMA; LIIAPCW; -.
DR OrthoDB; 1197004at2759; -.
DR PhylomeDB; Q4U2R6; -.
DR TreeFam; TF106130; -.
DR PathwayCommons; Q4U2R6; -.
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; Q4U2R6; -.
DR SIGNOR; Q4U2R6; -.
DR BioGRID-ORCS; 51258; 235 hits in 1082 CRISPR screens.
DR ChiTaRS; MRPL51; human.
DR GenomeRNAi; 51258; -.
DR Pharos; Q4U2R6; Tdark.
DR PRO; PR:Q4U2R6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q4U2R6; protein.
DR Bgee; ENSG00000111639; Expressed in left ventricle myocardium and 183 other tissues.
DR ExpressionAtlas; Q4U2R6; baseline and differential.
DR Genevisible; Q4U2R6; 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:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; ISS:UniProtKB.
DR InterPro; IPR019373; Ribosomal_L51_mit.
DR PANTHER; PTHR13409; PTHR13409; 1.
DR Pfam; PF10244; MRP-L51; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..128
FT /note="39S ribosomal protein L51, mitochondrial"
FT /id="PRO_0000273082"
FT VARIANT 102
FT /note="M -> I (in dbSNP:rs9526)"
FT /id="VAR_030079"
FT CONFLICT 79
FT /note="W -> R (in Ref. 3; AAF36161)"
FT /evidence="ECO:0000305"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 53..59
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 104..123
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 128 AA; 15095 MW; 9DB4720D5B387A5D CRC64;
MAGNLLSGAG RRLWDWVPLA CRSFSLGVPR LIGIRLTLPP PKVVDRWNEK RAMFGVYDNI
GILGNFEKHP KELIRGPIWL RGWKGNELQR CIRKRKMVGS RMFADDLHNL NKRIRYLYKH
FNRHGKFR
