RM54_HUMAN
ID RM54_HUMAN Reviewed; 138 AA.
AC Q6P161;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=39S ribosomal protein L54, mitochondrial;
DE Short=L54mt;
DE Short=MRP-L54;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL54 {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=MRPL54;
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].
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 [2]
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 [3]
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 [4] {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 [5] {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:25838379, PubMed:28892042). 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. {ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC Q6P161; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-7825248, EBI-5453723;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL54 family. {ECO:0000305}.
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DR EMBL; BC065273; AAH65273.1; -; mRNA.
DR CCDS; CCDS12111.1; -.
DR RefSeq; NP_758455.1; NM_172251.2.
DR PDB; 3J9M; EM; 3.50 A; l=1-138.
DR PDB; 5OOL; EM; 3.06 A; l=1-138.
DR PDB; 5OOM; EM; 3.03 A; l=1-138.
DR PDB; 6I9R; EM; 3.90 A; l=1-138.
DR PDB; 6NU2; EM; 3.90 A; l=114-136.
DR PDB; 6NU3; EM; 4.40 A; l=1-138.
DR PDB; 6VLZ; EM; 2.97 A; l=1-138.
DR PDB; 6VMI; EM; 2.96 A; l=1-138.
DR PDB; 6ZM5; EM; 2.89 A; l=1-138.
DR PDB; 6ZM6; EM; 2.59 A; l=1-138.
DR PDB; 6ZS9; EM; 4.00 A; l=1-138.
DR PDB; 6ZSA; EM; 4.00 A; l=1-138.
DR PDB; 6ZSB; EM; 4.50 A; l=1-138.
DR PDB; 6ZSC; EM; 3.50 A; l=1-138.
DR PDB; 6ZSD; EM; 3.70 A; l=1-138.
DR PDB; 6ZSE; EM; 5.00 A; l=1-138.
DR PDB; 6ZSG; EM; 4.00 A; l=1-138.
DR PDB; 7A5F; EM; 4.40 A; l3=1-138.
DR PDB; 7A5G; EM; 4.33 A; l3=1-138.
DR PDB; 7A5H; EM; 3.30 A; l=1-138.
DR PDB; 7A5I; EM; 3.70 A; l3=1-138.
DR PDB; 7A5J; EM; 3.10 A; l=1-138.
DR PDB; 7A5K; EM; 3.70 A; l3=1-138.
DR PDB; 7L08; EM; 3.49 A; l=1-138.
DR PDB; 7L20; EM; 3.15 A; l=1-138.
DR PDB; 7O9K; EM; 3.10 A; l=1-138.
DR PDB; 7O9M; EM; 2.50 A; l=1-138.
DR PDB; 7ODR; EM; 2.90 A; l=1-138.
DR PDB; 7ODS; EM; 3.10 A; l=1-138.
DR PDB; 7ODT; EM; 3.10 A; l=1-138.
DR PDB; 7OF2; EM; 2.70 A; l=1-138.
DR PDB; 7OF4; EM; 2.70 A; l=1-138.
DR PDB; 7OF6; EM; 2.60 A; l=1-138.
DR PDB; 7OG4; EM; 3.80 A; l=1-138.
DR PDB; 7OI6; EM; 5.70 A; l=1-138.
DR PDB; 7OI7; EM; 3.50 A; l=1-138.
DR PDB; 7OI8; EM; 3.50 A; l=1-138.
DR PDB; 7OI9; EM; 3.30 A; l=1-138.
DR PDB; 7OIA; EM; 3.20 A; l=1-138.
DR PDB; 7OIB; EM; 3.30 A; l=1-138.
DR PDB; 7OIC; EM; 3.10 A; l=1-138.
DR PDB; 7OID; EM; 3.70 A; l=1-138.
DR PDB; 7OIE; EM; 3.50 A; l=1-138.
DR PDB; 7PD3; EM; 3.40 A; l=1-138.
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; 7OF2; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF6; -.
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 AlphaFoldDB; Q6P161; -.
DR SMR; Q6P161; -.
DR BioGRID; 125522; 43.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q6P161; -.
DR IntAct; Q6P161; 17.
DR MINT; Q6P161; -.
DR STRING; 9606.ENSP00000331849; -.
DR iPTMnet; Q6P161; -.
DR PhosphoSitePlus; Q6P161; -.
DR BioMuta; MRPL54; -.
DR DMDM; 74737109; -.
DR EPD; Q6P161; -.
DR jPOST; Q6P161; -.
DR MassIVE; Q6P161; -.
DR MaxQB; Q6P161; -.
DR PaxDb; Q6P161; -.
DR PeptideAtlas; Q6P161; -.
DR PRIDE; Q6P161; -.
DR ProteomicsDB; 66822; -.
DR TopDownProteomics; Q6P161; -.
DR Antibodypedia; 23347; 178 antibodies from 23 providers.
DR DNASU; 116541; -.
DR Ensembl; ENST00000330133.5; ENSP00000331849.3; ENSG00000183617.5.
DR GeneID; 116541; -.
DR KEGG; hsa:116541; -.
DR MANE-Select; ENST00000330133.5; ENSP00000331849.3; NM_172251.3; NP_758455.1.
DR UCSC; uc002lyq.5; human.
DR CTD; 116541; -.
DR DisGeNET; 116541; -.
DR GeneCards; MRPL54; -.
DR HGNC; HGNC:16685; MRPL54.
DR HPA; ENSG00000183617; Low tissue specificity.
DR MIM; 611858; gene.
DR neXtProt; NX_Q6P161; -.
DR OpenTargets; ENSG00000183617; -.
DR PharmGKB; PA30987; -.
DR VEuPathDB; HostDB:ENSG00000183617; -.
DR eggNOG; KOG3435; Eukaryota.
DR GeneTree; ENSGT00390000001201; -.
DR HOGENOM; CLU_143073_1_1_1; -.
DR InParanoid; Q6P161; -.
DR OMA; WLFQMNV; -.
DR OrthoDB; 1538612at2759; -.
DR PhylomeDB; Q6P161; -.
DR TreeFam; TF314007; -.
DR PathwayCommons; Q6P161; -.
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; Q6P161; -.
DR SIGNOR; Q6P161; -.
DR BioGRID-ORCS; 116541; 346 hits in 1082 CRISPR screens.
DR GenomeRNAi; 116541; -.
DR Pharos; Q6P161; Tdark.
DR PRO; PR:Q6P161; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6P161; protein.
DR Bgee; ENSG00000183617; Expressed in granulocyte and 176 other tissues.
DR ExpressionAtlas; Q6P161; baseline and differential.
DR Genevisible; Q6P161; 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:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR013870; Ribosomal_L37_mit.
DR PANTHER; PTHR28595; PTHR28595; 1.
DR Pfam; PF08561; Ribosomal_L37; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..138
FT /note="39S ribosomal protein L54, mitochondrial"
FT /id="PRO_0000278280"
FT HELIX 115..132
FT /evidence="ECO:0007829|PDB:5OOM"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7OIE"
SQ SEQUENCE 138 AA; 15819 MW; 98E0FCA10592B064 CRC64;
MATKRLFGAT RTWAGWGAWE LLNPATSGRL LARDYAKKPV MKGAKSGKGA VTSEALKDPD
VCTDPVQLTT YAMGVNIYKE GQDVPLKPDA EYPEWLFEMN LGPPKTLEEL DPESREYWRR
LRKQNIWRHN RLSKNKRL
