RT63_HUMAN
ID RT63_HUMAN Reviewed; 102 AA.
AC Q9BQC6; A2A332;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ribosomal protein 63, mitochondrial;
DE Short=hMRP63;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL63 {ECO:0000303|PubMed:25278503};
DE AltName: Full=Mitochondrial ribosomal protein 63;
DE AltName: Full=Mitochondrial ribosomal protein L57;
GN Name=MRPL57; Synonyms=MRP63;
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 GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Hypothalamus;
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 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 [6]
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 [7]
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 [8]
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 [9] {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 -!- INTERACTION:
CC Q9BQC6; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-1055359, EBI-7062247;
CC Q9BQC6; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-1055359, EBI-17490413;
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 mL63 family. {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; AB049957; BAB41010.1; -; mRNA.
DR EMBL; AL158032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08296.1; -; Genomic_DNA.
DR EMBL; BC023616; AAH23616.1; -; mRNA.
DR EMBL; BC068492; AAH68492.1; -; mRNA.
DR CCDS; CCDS9296.1; -.
DR RefSeq; NP_076931.1; NM_024026.4.
DR RefSeq; XP_016876229.1; XM_017020740.1.
DR PDB; 3J7Y; EM; 3.40 A; o=1-102.
DR PDB; 3J9M; EM; 3.50 A; o=1-102.
DR PDB; 5OOL; EM; 3.06 A; o=1-102.
DR PDB; 5OOM; EM; 3.03 A; o=1-102.
DR PDB; 6I9R; EM; 3.90 A; o=1-102.
DR PDB; 6NU2; EM; 3.90 A; o=9-102.
DR PDB; 6NU3; EM; 4.40 A; o=1-102.
DR PDB; 6VLZ; EM; 2.97 A; o=1-102.
DR PDB; 6VMI; EM; 2.96 A; o=1-102.
DR PDB; 6ZM5; EM; 2.89 A; o=1-102.
DR PDB; 6ZM6; EM; 2.59 A; o=1-102.
DR PDB; 6ZS9; EM; 4.00 A; o=1-102.
DR PDB; 6ZSA; EM; 4.00 A; o=1-102.
DR PDB; 6ZSB; EM; 4.50 A; o=1-102.
DR PDB; 6ZSC; EM; 3.50 A; o=1-102.
DR PDB; 6ZSD; EM; 3.70 A; o=1-102.
DR PDB; 6ZSE; EM; 5.00 A; o=1-102.
DR PDB; 6ZSG; EM; 4.00 A; o=1-102.
DR PDB; 7A5F; EM; 4.40 A; o3=1-102.
DR PDB; 7A5G; EM; 4.33 A; o3=1-102.
DR PDB; 7A5H; EM; 3.30 A; o=1-102.
DR PDB; 7A5I; EM; 3.70 A; o3=1-102.
DR PDB; 7A5J; EM; 3.10 A; o=1-102.
DR PDB; 7A5K; EM; 3.70 A; o3=1-102.
DR PDB; 7L08; EM; 3.49 A; o=1-102.
DR PDB; 7L20; EM; 3.15 A; o=1-102.
DR PDB; 7O9K; EM; 3.10 A; o=1-102.
DR PDB; 7O9M; EM; 2.50 A; o=1-102.
DR PDB; 7ODR; EM; 2.90 A; o=1-102.
DR PDB; 7ODS; EM; 3.10 A; o=1-102.
DR PDB; 7ODT; EM; 3.10 A; o=1-102.
DR PDB; 7OF0; EM; 2.20 A; o=1-102.
DR PDB; 7OF2; EM; 2.70 A; o=1-102.
DR PDB; 7OF3; EM; 2.70 A; o=1-102.
DR PDB; 7OF4; EM; 2.70 A; o=1-102.
DR PDB; 7OF5; EM; 2.90 A; o=1-102.
DR PDB; 7OF6; EM; 2.60 A; o=1-102.
DR PDB; 7OF7; EM; 2.50 A; o=1-102.
DR PDB; 7OG4; EM; 3.80 A; o=1-102.
DR PDB; 7OI6; EM; 5.70 A; o=1-102.
DR PDB; 7OI7; EM; 3.50 A; o=1-102.
DR PDB; 7OI8; EM; 3.50 A; o=1-102.
DR PDB; 7OI9; EM; 3.30 A; o=1-102.
DR PDB; 7OIA; EM; 3.20 A; o=1-102.
DR PDB; 7OIB; EM; 3.30 A; o=1-102.
DR PDB; 7OIC; EM; 3.10 A; o=1-102.
DR PDB; 7OID; EM; 3.70 A; o=1-102.
DR PDB; 7OIE; EM; 3.50 A; o=1-102.
DR PDB; 7PD3; EM; 3.40 A; o=1-102.
DR PDB; 7QH6; EM; 3.08 A; o=1-102.
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; Q9BQC6; -.
DR SMR; Q9BQC6; -.
DR BioGRID; 122459; 102.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR IntAct; Q9BQC6; 28.
DR MINT; Q9BQC6; -.
DR STRING; 9606.ENSP00000310726; -.
DR GlyGen; Q9BQC6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQC6; -.
DR PhosphoSitePlus; Q9BQC6; -.
DR BioMuta; MRPL57; -.
DR EPD; Q9BQC6; -.
DR jPOST; Q9BQC6; -.
DR MassIVE; Q9BQC6; -.
DR MaxQB; Q9BQC6; -.
DR PaxDb; Q9BQC6; -.
DR PeptideAtlas; Q9BQC6; -.
DR PRIDE; Q9BQC6; -.
DR ProteomicsDB; 78656; -.
DR TopDownProteomics; Q9BQC6; -.
DR Antibodypedia; 49702; 19 antibodies from 7 providers.
DR DNASU; 78988; -.
DR Ensembl; ENST00000309594.5; ENSP00000310726.4; ENSG00000173141.5.
DR GeneID; 78988; -.
DR KEGG; hsa:78988; -.
DR MANE-Select; ENST00000309594.5; ENSP00000310726.4; NM_024026.5; NP_076931.1.
DR UCSC; uc001unw.4; human.
DR CTD; 78988; -.
DR GeneCards; MRPL57; -.
DR HGNC; HGNC:14514; MRPL57.
DR HPA; ENSG00000173141; Low tissue specificity.
DR MIM; 611997; gene.
DR neXtProt; NX_Q9BQC6; -.
DR OpenTargets; ENSG00000173141; -.
DR PharmGKB; PA30937; -.
DR VEuPathDB; HostDB:ENSG00000173141; -.
DR eggNOG; ENOG502S44A; Eukaryota.
DR GeneTree; ENSGT00390000008171; -.
DR HOGENOM; CLU_175792_1_0_1; -.
DR InParanoid; Q9BQC6; -.
DR OMA; QEFGHAA; -.
DR OrthoDB; 1622855at2759; -.
DR PhylomeDB; Q9BQC6; -.
DR TreeFam; TF324466; -.
DR PathwayCommons; Q9BQC6; -.
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; Q9BQC6; -.
DR SIGNOR; Q9BQC6; -.
DR BioGRID-ORCS; 78988; 559 hits in 1095 CRISPR screens.
DR ChiTaRS; MRPL57; human.
DR GenomeRNAi; 78988; -.
DR Pharos; Q9BQC6; Tdark.
DR PRO; PR:Q9BQC6; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9BQC6; protein.
DR Bgee; ENSG00000173141; Expressed in endothelial cell and 212 other tissues.
DR ExpressionAtlas; Q9BQC6; baseline and differential.
DR Genevisible; Q9BQC6; 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; ISS: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 InterPro; IPR016576; Ribosomal_MRP63_mit.
DR PANTHER; PTHR14520; PTHR14520; 1.
DR Pfam; PF14978; MRP-63; 1.
DR PIRSF; PIRSF011124; MRP63; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..102
FT /note="Ribosomal protein 63, mitochondrial"
FT /id="PRO_0000253541"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:5OOL"
FT HELIX 29..49
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 64..79
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 102 AA; 12266 MW; 2456F3E663C6F683 CRC64;
MFLTALLWRG RIPGRQWIGK HRRPRFVSLR AKQNMIRRLE IEAENHYWLS MPYMTREQER
GHAAVRRREA FEAIKAAATS KFPPHRFIAD QLDHLNVTKK WS
