RM18_HUMAN
ID RM18_HUMAN Reviewed; 180 AA.
AC Q9H0U6; Q5TAP9; Q9NZW8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=39S ribosomal protein L18, mitochondrial;
DE Short=L18mt;
DE Short=MRP-L18;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL18m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL18; ORFNames=HSPC071;
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 {ECO:0000312|EMBL:CAB66568.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-6.
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 [3] {ECO:0000305, ECO:0000312|EMBL:CAB66568.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [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 FUNCTION, AND RNA-BINDING.
RX PubMed=21685364; DOI=10.1101/gad.624711;
RA Smirnov A., Entelis N., Martin R.P., Tarassov I.;
RT "Biological significance of 5S rRNA import into human mitochondria: role of
RT ribosomal protein MRP-L18.";
RL Genes Dev. 25:1289-1305(2011).
RN [9]
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 [10]
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 [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 -!- FUNCTION: Together with thiosulfate sulfurtransferase (TST), acts as a
CC mitochondrial import factor for the cytosolic 5S rRNA. The precursor
CC form shows RNA chaperone activity; is able to fold the 5S rRNA into an
CC import-competent conformation that is recognized by rhodanese (TST).
CC Both the cytoplasmic and mitochondrial forms are able to bind to the
CC helix IV-loop D in the gamma domain of the 5S rRNA.
CC {ECO:0000269|PubMed:21685364}.
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:28892042, PubMed:25278503). 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:25278503, ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC Q9H0U6; Q13571: LAPTM5; NbExp=3; IntAct=EBI-2560240, EBI-2865663;
CC Q9H0U6; Q96DV4: MRPL38; NbExp=4; IntAct=EBI-2560240, EBI-720441;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
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DR EMBL; AL136633; CAB66568.1; -; mRNA.
DR EMBL; AF161556; AAF29043.1; -; mRNA.
DR EMBL; CR533491; CAG38522.1; -; mRNA.
DR EMBL; AL139045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001623; AAH01623.1; -; mRNA.
DR CCDS; CCDS5270.1; -.
DR RefSeq; NP_001305746.1; NM_001318817.1.
DR RefSeq; NP_054880.2; NM_014161.4.
DR PDB; 3J7Y; EM; 3.40 A; P=1-180.
DR PDB; 5OOL; EM; 3.06 A; P=1-180.
DR PDB; 5OOM; EM; 3.03 A; P=1-180.
DR PDB; 6NU2; EM; 3.90 A; P=43-180.
DR PDB; 6NU3; EM; 4.40 A; P=1-180.
DR PDB; 6ZM5; EM; 2.89 A; P=1-180.
DR PDB; 6ZM6; EM; 2.59 A; P=1-180.
DR PDB; 6ZSA; EM; 4.00 A; XP=1-180.
DR PDB; 6ZSB; EM; 4.50 A; XP=1-180.
DR PDB; 6ZSC; EM; 3.50 A; XP=1-180.
DR PDB; 6ZSD; EM; 3.70 A; XP=1-180.
DR PDB; 6ZSE; EM; 5.00 A; XP=1-180.
DR PDB; 6ZSG; EM; 4.00 A; XP=1-180.
DR PDB; 7A5F; EM; 4.40 A; P3=1-180.
DR PDB; 7A5G; EM; 4.33 A; P3=1-180.
DR PDB; 7ODR; EM; 2.90 A; P=1-180.
DR PDB; 7ODS; EM; 3.10 A; P=1-180.
DR PDB; 7ODT; EM; 3.10 A; P=1-180.
DR PDB; 7OF0; EM; 2.20 A; P=1-180.
DR PDB; 7OF2; EM; 2.70 A; P=1-180.
DR PDB; 7OF3; EM; 2.70 A; P=1-180.
DR PDB; 7OF4; EM; 2.70 A; P=1-180.
DR PDB; 7OF5; EM; 2.90 A; P=1-180.
DR PDB; 7OF6; EM; 2.60 A; P=1-180.
DR PDB; 7OF7; EM; 2.50 A; P=1-180.
DR PDB; 7OG4; EM; 3.80 A; XP=1-180.
DR PDB; 7OI6; EM; 5.70 A; P=1-180.
DR PDB; 7OI7; EM; 3.50 A; P=1-180.
DR PDB; 7OI8; EM; 3.50 A; P=1-180.
DR PDB; 7OI9; EM; 3.30 A; P=1-180.
DR PDB; 7OIA; EM; 3.20 A; P=1-180.
DR PDB; 7OIB; EM; 3.30 A; P=1-180.
DR PDB; 7OIC; EM; 3.10 A; P=1-180.
DR PDB; 7OID; EM; 3.70 A; P=1-180.
DR PDB; 7OIE; EM; 3.50 A; P=1-180.
DR PDB; 7PD3; EM; 3.40 A; P=1-180.
DR PDB; 7QH6; EM; 3.08 A; P=1-180.
DR PDBsum; 3J7Y; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
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; 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; Q9H0U6; -.
DR SMR; Q9H0U6; -.
DR BioGRID; 118846; 208.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9H0U6; -.
DR DIP; DIP-56844N; -.
DR IntAct; Q9H0U6; 51.
DR MINT; Q9H0U6; -.
DR STRING; 9606.ENSP00000356001; -.
DR GlyGen; Q9H0U6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H0U6; -.
DR PhosphoSitePlus; Q9H0U6; -.
DR BioMuta; MRPL18; -.
DR DMDM; 41017797; -.
DR EPD; Q9H0U6; -.
DR jPOST; Q9H0U6; -.
DR MassIVE; Q9H0U6; -.
DR MaxQB; Q9H0U6; -.
DR PaxDb; Q9H0U6; -.
DR PeptideAtlas; Q9H0U6; -.
DR PRIDE; Q9H0U6; -.
DR ProteomicsDB; 80326; -.
DR TopDownProteomics; Q9H0U6; -.
DR Antibodypedia; 33462; 126 antibodies from 21 providers.
DR DNASU; 29074; -.
DR Ensembl; ENST00000367034.5; ENSP00000356001.4; ENSG00000112110.10.
DR GeneID; 29074; -.
DR KEGG; hsa:29074; -.
DR MANE-Select; ENST00000367034.5; ENSP00000356001.4; NM_014161.5; NP_054880.2.
DR UCSC; uc003qsw.5; human.
DR CTD; 29074; -.
DR DisGeNET; 29074; -.
DR GeneCards; MRPL18; -.
DR HGNC; HGNC:14477; MRPL18.
DR HPA; ENSG00000112110; Low tissue specificity.
DR MIM; 611831; gene.
DR neXtProt; NX_Q9H0U6; -.
DR OpenTargets; ENSG00000112110; -.
DR PharmGKB; PA30947; -.
DR VEuPathDB; HostDB:ENSG00000112110; -.
DR eggNOG; KOG3333; Eukaryota.
DR GeneTree; ENSGT00390000006394; -.
DR HOGENOM; CLU_108540_0_0_1; -.
DR InParanoid; Q9H0U6; -.
DR OMA; TSEWAIK; -.
DR OrthoDB; 1336080at2759; -.
DR PhylomeDB; Q9H0U6; -.
DR TreeFam; TF313292; -.
DR PathwayCommons; Q9H0U6; -.
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; Q9H0U6; -.
DR SIGNOR; Q9H0U6; -.
DR BioGRID-ORCS; 29074; 442 hits in 1089 CRISPR screens.
DR ChiTaRS; MRPL18; human.
DR GeneWiki; MRPL18; -.
DR GenomeRNAi; 29074; -.
DR Pharos; Q9H0U6; Tbio.
DR PRO; PR:Q9H0U6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H0U6; protein.
DR Bgee; ENSG00000112110; Expressed in oocyte and 201 other tissues.
DR Genevisible; Q9H0U6; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
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; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008097; F:5S rRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0035928; P:rRNA import into mitochondrion; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.420.80; -; 1.
DR InterPro; IPR005484; Ribosomal_L18.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR12899; PTHR12899; 1.
DR Pfam; PF00861; Ribosomal_L18p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; Transit peptide;
KW Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..180
FT /note="39S ribosomal protein L18, mitochondrial"
FT /id="PRO_0000030556"
FT VARIANT 6
FT /note="R -> Q (in dbSNP:rs1128670)"
FT /evidence="ECO:0000269|PubMed:11042152"
FT /id="VAR_024609"
FT CONFLICT 10
FT /note="Missing (in Ref. 2; AAF29043)"
FT /evidence="ECO:0000305"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:7OI7"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5OOL"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3J7Y"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 180 AA; 20577 MW; C0CAD23465FE93B4 CRC64;
MALRSRFWGL FSVCRNPGCR FAALSTSSEP AAKPEVDPVE NEAVAPEFTN RNPRNLELLS
VARKERGWRT VFPSREFWHR LRVIRTQHHV EALVEHQNGK VVVSASTREW AIKKHLYSTR
NVVACESIGR VLAQRCLEAG INFMVYQPTP WEAASDSMKR LQSAMTEGGV VLREPQRIYE
