RM53_HUMAN
ID RM53_HUMAN Reviewed; 112 AA.
AC Q96EL3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=39S ribosomal protein L53, mitochondrial;
DE Short=L53mt;
DE Short=MRP-L53;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL53 {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL53;
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: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 [5] {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 [6] {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. mL53 is located at the L7/L12 stalk.
CC {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC Q96EL3; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-2513715, EBI-17439331;
CC Q96EL3; Q15370: ELOB; NbExp=5; IntAct=EBI-2513715, EBI-301238;
CC Q96EL3; A0A0B4J2D5: GATD3B; NbExp=3; IntAct=EBI-2513715, EBI-23705910;
CC Q96EL3; O15499: GSC2; NbExp=3; IntAct=EBI-2513715, EBI-19954058;
CC Q96EL3; P31943: HNRNPH1; NbExp=3; IntAct=EBI-2513715, EBI-351590;
CC Q96EL3; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2513715, EBI-747204;
CC Q96EL3; O00139: KIF2A; NbExp=3; IntAct=EBI-2513715, EBI-2692369;
CC Q96EL3; O00139-1: KIF2A; NbExp=3; IntAct=EBI-2513715, EBI-12197879;
CC Q96EL3; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2513715, EBI-10271199;
CC Q96EL3; P26367: PAX6; NbExp=3; IntAct=EBI-2513715, EBI-747278;
CC Q96EL3; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-2513715, EBI-358436;
CC Q96EL3; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-2513715, EBI-2212028;
CC Q96EL3; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-2513715, EBI-529518;
CC Q96EL3; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-2513715, EBI-741515;
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 mL53 family. {ECO:0000305}.
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DR EMBL; BC012163; AAH12163.1; -; mRNA.
DR CCDS; CCDS1944.1; -.
DR RefSeq; NP_444278.1; NM_053050.4.
DR PDB; 3J7Y; EM; 3.40 A; k=1-112.
DR PDB; 3J9M; EM; 3.50 A; k=1-112.
DR PDB; 5OOL; EM; 3.06 A; k=1-112.
DR PDB; 5OOM; EM; 3.03 A; k=1-112.
DR PDB; 6I9R; EM; 3.90 A; k=1-112.
DR PDB; 6NU2; EM; 3.90 A; k=13-96.
DR PDB; 6NU3; EM; 4.40 A; k=1-112.
DR PDB; 6VLZ; EM; 2.97 A; k=1-112.
DR PDB; 6VMI; EM; 2.96 A; k=1-112.
DR PDB; 6ZM5; EM; 2.89 A; k=2-112.
DR PDB; 6ZM6; EM; 2.59 A; k=2-112.
DR PDB; 6ZS9; EM; 4.00 A; k=1-112.
DR PDB; 6ZSA; EM; 4.00 A; k=1-112.
DR PDB; 6ZSB; EM; 4.50 A; k=1-112.
DR PDB; 6ZSC; EM; 3.50 A; k=1-112.
DR PDB; 6ZSD; EM; 3.70 A; k=1-112.
DR PDB; 6ZSE; EM; 5.00 A; k=1-112.
DR PDB; 6ZSG; EM; 4.00 A; k=1-112.
DR PDB; 7A5F; EM; 4.40 A; k3=1-112.
DR PDB; 7A5G; EM; 4.33 A; k3=1-112.
DR PDB; 7A5H; EM; 3.30 A; k=1-112.
DR PDB; 7A5I; EM; 3.70 A; k3=1-112.
DR PDB; 7A5J; EM; 3.10 A; k=1-112.
DR PDB; 7A5K; EM; 3.70 A; k3=1-112.
DR PDB; 7L08; EM; 3.49 A; k=1-112.
DR PDB; 7L20; EM; 3.15 A; k=1-112.
DR PDB; 7O9K; EM; 3.10 A; k=1-112.
DR PDB; 7O9M; EM; 2.50 A; k=1-112.
DR PDB; 7ODR; EM; 2.90 A; k=1-112.
DR PDB; 7ODS; EM; 3.10 A; k=1-112.
DR PDB; 7ODT; EM; 3.10 A; k=1-112.
DR PDB; 7OF0; EM; 2.20 A; k=1-112.
DR PDB; 7OF2; EM; 2.70 A; k=1-112.
DR PDB; 7OF3; EM; 2.70 A; k=1-112.
DR PDB; 7OF4; EM; 2.70 A; k=1-112.
DR PDB; 7OF5; EM; 2.90 A; k=1-112.
DR PDB; 7OF6; EM; 2.60 A; k=1-112.
DR PDB; 7OF7; EM; 2.50 A; k=1-112.
DR PDB; 7OG4; EM; 3.80 A; k=1-112.
DR PDB; 7OI6; EM; 5.70 A; k=1-112.
DR PDB; 7OI7; EM; 3.50 A; k=1-112.
DR PDB; 7OI8; EM; 3.50 A; k=1-112.
DR PDB; 7OI9; EM; 3.30 A; k=1-112.
DR PDB; 7OIA; EM; 3.20 A; k=1-112.
DR PDB; 7OIB; EM; 3.30 A; k=1-112.
DR PDB; 7OIC; EM; 3.10 A; k=1-112.
DR PDB; 7OID; EM; 3.70 A; k=1-112.
DR PDB; 7OIE; EM; 3.50 A; k=1-112.
DR PDB; 7PD3; EM; 3.40 A; k=1-112.
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 AlphaFoldDB; Q96EL3; -.
DR SMR; Q96EL3; -.
DR BioGRID; 125521; 192.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q96EL3; -.
DR IntAct; Q96EL3; 41.
DR MINT; Q96EL3; -.
DR STRING; 9606.ENSP00000258105; -.
DR iPTMnet; Q96EL3; -.
DR PhosphoSitePlus; Q96EL3; -.
DR SwissPalm; Q96EL3; -.
DR BioMuta; MRPL53; -.
DR DMDM; 74731579; -.
DR EPD; Q96EL3; -.
DR jPOST; Q96EL3; -.
DR MassIVE; Q96EL3; -.
DR MaxQB; Q96EL3; -.
DR PaxDb; Q96EL3; -.
DR PeptideAtlas; Q96EL3; -.
DR PRIDE; Q96EL3; -.
DR ProteomicsDB; 76424; -.
DR TopDownProteomics; Q96EL3; -.
DR Antibodypedia; 70616; 48 antibodies from 15 providers.
DR DNASU; 116540; -.
DR Ensembl; ENST00000258105.8; ENSP00000258105.7; ENSG00000204822.7.
DR GeneID; 116540; -.
DR KEGG; hsa:116540; -.
DR MANE-Select; ENST00000258105.8; ENSP00000258105.7; NM_053050.5; NP_444278.1.
DR UCSC; uc002sln.4; human.
DR CTD; 116540; -.
DR GeneCards; MRPL53; -.
DR HGNC; HGNC:16684; MRPL53.
DR HPA; ENSG00000204822; Low tissue specificity.
DR MIM; 611857; gene.
DR neXtProt; NX_Q96EL3; -.
DR PharmGKB; PA30986; -.
DR VEuPathDB; HostDB:ENSG00000204822; -.
DR eggNOG; ENOG502S5X4; Eukaryota.
DR GeneTree; ENSGT00390000001440; -.
DR HOGENOM; CLU_175193_0_0_1; -.
DR InParanoid; Q96EL3; -.
DR OMA; RATNLNC; -.
DR OrthoDB; 1502821at2759; -.
DR PhylomeDB; Q96EL3; -.
DR TreeFam; TF300292; -.
DR PathwayCommons; Q96EL3; -.
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; Q96EL3; -.
DR SIGNOR; Q96EL3; -.
DR BioGRID-ORCS; 116540; 488 hits in 1083 CRISPR screens.
DR ChiTaRS; MRPL53; human.
DR GenomeRNAi; 116540; -.
DR Pharos; Q96EL3; Tdark.
DR PRO; PR:Q96EL3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96EL3; protein.
DR Bgee; ENSG00000204822; Expressed in right adrenal gland and 96 other tissues.
DR ExpressionAtlas; Q96EL3; baseline and differential.
DR Genevisible; Q96EL3; 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:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR019716; Ribosomal_L53_mit.
DR Pfam; PF10780; MRP_L53; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..112
FT /note="39S ribosomal protein L53, mitochondrial"
FT /id="PRO_0000261664"
FT VARIANT 4
FT /note="A -> S (in dbSNP:rs1047911)"
FT /id="VAR_029475"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5OOM"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3J7Y"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 112 AA; 12107 MW; BFC43FF93A148C36 CRC64;
MAAALARLGL RPVKQVRVQF CPFEKNVEST RTFLQTVSSE KVRSTNLNCS VIADVRHDGS
EPCVDVLFGD GHRLIMRGAH LTALEMLTAF ASHIRARDAA GSGDKPGADT GR
