RT18A_HUMAN
ID RT18A_HUMAN Reviewed; 196 AA.
AC Q9NVS2; A6XND3; Q5QPA4;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=39S ribosomal protein S18a, mitochondrial;
DE Short=MRP-S18-a;
DE Short=Mrps18a;
DE Short=S18mt-a;
DE AltName: Full=39S ribosomal protein S18-3, mitochondrial;
DE Short=MRP-S18-3;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bS18a {ECO:0000303|PubMed:25278503};
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL66 {ECO:0000303|PubMed:27023846};
DE Flags: Precursor;
GN Name=MRPS18A;
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:BAA91675.1};
RN [1] {ECO:0000312|EMBL:BAB41005.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] {ECO:0000312|EMBL:BAA91675.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Yu Z., Zheng Z., Tang T., Fu Y.;
RT "A computer system platform used to predict novel genes.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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] {ECO:0000312|EMBL:BAA91675.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [7] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=11279123; DOI=10.1074/jbc.m100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome: identification
RT of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [8]
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 [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 NOMENCLATURE.
RX PubMed=27023846; DOI=10.1146/annurev-biochem-060815-014343;
RA Greber B.J., Ban N.;
RT "Structure and function of the mitochondrial ribosome.";
RL Annu. Rev. Biochem. 85:103-132(2016).
RN [11] {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 [12] {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 [13] {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. mL66 forms a zinc-binding site with uL10m.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NVS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVS2-2; Sequence=VSP_041245;
CC Name=3;
CC IsoId=Q9NVS2-3; Sequence=VSP_043496;
CC -!- MISCELLANEOUS: There are 3 mitochondrial isoforms of bS18 in mammalia,
CC localizing to 3 distinct sites in the mitoribosome. bS18m (bs18c) binds
CC to the same site as bacterial bS18, mS40 (bS18b) binds to a novel
CC location of the 28S small subunit, and mL66 (bS18a, this protein) binds
CC to the 39S large subunit. {ECO:0000305|PubMed:27023846}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.
CC Mitochondrion-specific ribosomal protein mL66 subfamily. {ECO:0000305}.
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DR EMBL; AB049952; BAB41005.1; -; mRNA.
DR EMBL; DQ884400; ABI63367.1; -; mRNA.
DR EMBL; AK001410; BAA91675.1; -; mRNA.
DR EMBL; AK300757; BAG62423.1; -; mRNA.
DR EMBL; AL136131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04225.1; -; Genomic_DNA.
DR EMBL; BC010364; AAH10364.1; -; mRNA.
DR CCDS; CCDS4906.1; -. [Q9NVS2-1]
DR CCDS; CCDS55006.1; -. [Q9NVS2-3]
DR RefSeq; NP_001180272.1; NM_001193343.1. [Q9NVS2-3]
DR RefSeq; NP_060605.1; NM_018135.3. [Q9NVS2-1]
DR RefSeq; XP_006715197.1; XM_006715134.2. [Q9NVS2-2]
DR PDB; 3J7Y; EM; 3.40 A; r=1-196.
DR PDB; 3J9M; EM; 3.50 A; r=1-196.
DR PDB; 5OOL; EM; 3.06 A; r=1-196.
DR PDB; 5OOM; EM; 3.03 A; r=1-196.
DR PDB; 6I9R; EM; 3.90 A; r=1-196.
DR PDB; 6NU2; EM; 3.90 A; r=35-196.
DR PDB; 6NU3; EM; 4.40 A; r=1-196.
DR PDB; 6VLZ; EM; 2.97 A; r=1-196.
DR PDB; 6VMI; EM; 2.96 A; r=1-196.
DR PDB; 6ZM5; EM; 2.89 A; r=1-196.
DR PDB; 6ZM6; EM; 2.59 A; r=1-196.
DR PDB; 6ZS9; EM; 4.00 A; r=1-196.
DR PDB; 6ZSA; EM; 4.00 A; r=1-196.
DR PDB; 6ZSB; EM; 4.50 A; r=1-196.
DR PDB; 6ZSC; EM; 3.50 A; r=1-196.
DR PDB; 6ZSD; EM; 3.70 A; r=1-196.
DR PDB; 6ZSE; EM; 5.00 A; r=1-196.
DR PDB; 6ZSG; EM; 4.00 A; r=1-196.
DR PDB; 7A5F; EM; 4.40 A; r3=1-196.
DR PDB; 7A5G; EM; 4.33 A; r3=1-196.
DR PDB; 7A5H; EM; 3.30 A; r=1-196.
DR PDB; 7A5I; EM; 3.70 A; r3=1-196.
DR PDB; 7A5J; EM; 3.10 A; r=1-196.
DR PDB; 7A5K; EM; 3.70 A; r3=1-196.
DR PDB; 7L08; EM; 3.49 A; r=1-196.
DR PDB; 7L20; EM; 3.15 A; r=1-196.
DR PDB; 7O9K; EM; 3.10 A; r=1-196.
DR PDB; 7O9M; EM; 2.50 A; r=1-196.
DR PDB; 7ODR; EM; 2.90 A; r=1-196.
DR PDB; 7ODS; EM; 3.10 A; r=1-196.
DR PDB; 7ODT; EM; 3.10 A; r=1-196.
DR PDB; 7OF0; EM; 2.20 A; r=1-196.
DR PDB; 7OF2; EM; 2.70 A; r=1-196.
DR PDB; 7OF3; EM; 2.70 A; r=1-196.
DR PDB; 7OF4; EM; 2.70 A; r=1-196.
DR PDB; 7OF5; EM; 2.90 A; r=1-196.
DR PDB; 7OF6; EM; 2.60 A; r=1-196.
DR PDB; 7OF7; EM; 2.50 A; r=1-196.
DR PDB; 7OG4; EM; 3.80 A; r=1-196.
DR PDB; 7OI6; EM; 5.70 A; r=1-196.
DR PDB; 7OI7; EM; 3.50 A; r=1-196.
DR PDB; 7OI8; EM; 3.50 A; r=1-196.
DR PDB; 7OI9; EM; 3.30 A; r=1-196.
DR PDB; 7OIA; EM; 3.20 A; r=1-196.
DR PDB; 7OIB; EM; 3.30 A; r=1-196.
DR PDB; 7OIC; EM; 3.10 A; r=1-196.
DR PDB; 7OID; EM; 3.70 A; r=1-196.
DR PDB; 7OIE; EM; 3.50 A; r=1-196.
DR PDB; 7PD3; EM; 3.40 A; r=1-196.
DR PDB; 7QH6; EM; 3.08 A; r=1-196.
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; Q9NVS2; -.
DR SMR; Q9NVS2; -.
DR BioGRID; 120468; 144.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9NVS2; -.
DR IntAct; Q9NVS2; 33.
DR MINT; Q9NVS2; -.
DR STRING; 9606.ENSP00000361206; -.
DR GlyGen; Q9NVS2; 1 site, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; Q9NVS2; -.
DR SwissPalm; Q9NVS2; -.
DR BioMuta; MRPS18A; -.
DR DMDM; 24212201; -.
DR EPD; Q9NVS2; -.
DR jPOST; Q9NVS2; -.
DR MassIVE; Q9NVS2; -.
DR MaxQB; Q9NVS2; -.
DR PaxDb; Q9NVS2; -.
DR PeptideAtlas; Q9NVS2; -.
DR PRIDE; Q9NVS2; -.
DR ProteomicsDB; 82852; -. [Q9NVS2-1]
DR ProteomicsDB; 82853; -. [Q9NVS2-2]
DR ProteomicsDB; 82854; -. [Q9NVS2-3]
DR TopDownProteomics; Q9NVS2-1; -. [Q9NVS2-1]
DR TopDownProteomics; Q9NVS2-2; -. [Q9NVS2-2]
DR Antibodypedia; 30568; 102 antibodies from 22 providers.
DR DNASU; 55168; -.
DR Ensembl; ENST00000372116.5; ENSP00000361188.1; ENSG00000096080.12. [Q9NVS2-3]
DR Ensembl; ENST00000372133.8; ENSP00000361206.3; ENSG00000096080.12. [Q9NVS2-1]
DR GeneID; 55168; -.
DR KEGG; hsa:55168; -.
DR MANE-Select; ENST00000372133.8; ENSP00000361206.3; NM_018135.4; NP_060605.1.
DR UCSC; uc003ovy.3; human. [Q9NVS2-1]
DR CTD; 55168; -.
DR DisGeNET; 55168; -.
DR GeneCards; MRPS18A; -.
DR HGNC; HGNC:14515; MRPS18A.
DR HPA; ENSG00000096080; Low tissue specificity.
DR MIM; 611981; gene.
DR neXtProt; NX_Q9NVS2; -.
DR OpenTargets; ENSG00000096080; -.
DR PharmGKB; PA31003; -.
DR VEuPathDB; HostDB:ENSG00000096080; -.
DR eggNOG; KOG3162; Eukaryota.
DR GeneTree; ENSGT00390000006493; -.
DR HOGENOM; CLU_107628_0_0_1; -.
DR InParanoid; Q9NVS2; -.
DR OMA; YKKGHRW; -.
DR OrthoDB; 1619493at2759; -.
DR PhylomeDB; Q9NVS2; -.
DR TreeFam; TF315738; -.
DR PathwayCommons; Q9NVS2; -.
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; Q9NVS2; -.
DR SIGNOR; Q9NVS2; -.
DR BioGRID-ORCS; 55168; 374 hits in 1090 CRISPR screens.
DR GeneWiki; MRPS18A; -.
DR GenomeRNAi; 55168; -.
DR Pharos; Q9NVS2; Tdark.
DR PRO; PR:Q9NVS2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NVS2; protein.
DR Bgee; ENSG00000096080; Expressed in gastrocnemius and 206 other tissues.
DR ExpressionAtlas; Q9NVS2; baseline and differential.
DR Genevisible; Q9NVS2; 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:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
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; NAS:UniProtKB.
DR Gene3D; 4.10.640.10; -; 1.
DR InterPro; IPR001648; Ribosomal_S18.
DR InterPro; IPR036870; Ribosomal_S18_sf.
DR PANTHER; PTHR13479; PTHR13479; 1.
DR Pfam; PF01084; Ribosomal_S18; 1.
DR SUPFAM; SSF46911; SSF46911; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..196
FT /note="39S ribosomal protein S18a, mitochondrial"
FT /id="PRO_0000030625"
FT VAR_SEQ 125
FT /note="A -> AGRRPWGPRGAEGCRHSLPTQLPHVSAPPGRKVDIRSVNYTHHPMPT
FT FPLPWAFPLAPSELQRELQRLSPLPRHS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041245"
FT VAR_SEQ 127..196
FT /note="LLPNHRPRLPEGVVPKSKPQLNRYLTRWAPGSVKPIYKKGPRWNRVRMPVGS
FT PLLRDNVCYSRTPWKLYH -> T (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043496"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7OIB"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 196 AA; 22184 MW; CC086B8FC27242D6 CRC64;
MAALKALVSG CGRLLRGLLA GPAATSWSRL PARGFREVVE TQEGKTTIIE GRITATPKES
PNPPNPSGQC PICRWNLKHK YNYDDVLLLS QFIRPHGGML PRKITGLCQE EHRKIEECVK
MAHRAGLLPN HRPRLPEGVV PKSKPQLNRY LTRWAPGSVK PIYKKGPRWN RVRMPVGSPL
LRDNVCYSRT PWKLYH
