ID RT18C_HUMAN Reviewed; 142 AA. AC Q9Y3D5; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 176. DE RecName: Full=Small ribosomal subunit protein bS18m {ECO:0000303|PubMed:25838379}; DE AltName: Full=28S ribosomal protein S18-1, mitochondrial; DE Short=MRP-S18-1; DE AltName: Full=28S ribosomal protein S18c, mitochondrial; DE Short=MRP-S18-c; DE Short=Mrps18-c; DE Short=S18mt-c; DE AltName: Full=Small ribosomal subunit protein bS18c {ECO:0000303|PubMed:25838379}; DE Flags: Precursor; GN Name=MRPS18C; ORFNames=CGI-134; 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]. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [3] {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 [4] 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 [5] 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 [6] 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 [7] {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). CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt- CC SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small CC (28S) and a large (39S) subunit. The 28S small subunit contains a 12S CC ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large CC subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial CC valine transfer RNA (mt-tRNA(Val)), which plays an integral structural CC role, and 52 different proteins. bS18m has a zinc binding site. CC {ECO:0000269|PubMed:25838379}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}. CC -!- MISCELLANEOUS: There are 3 mitochondrial isoforms of bS18 in mammalia, CC localizing to 3 distinct sites in the mitoribosome. bS18m (bs18c, this CC protein) binds to the same site as bacterial bS18, mS40 (bS18b) binds CC to a novel location of the 28S small subunit, and mL66 (bS18a) binds to CC the 39S large subunit. {ECO:0000305|PubMed:27023846}. CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family. CC {ECO:0000250|UniProtKB:P80382}. 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; AF151892; AAD34129.1; -; mRNA. DR EMBL; BC005186; AAH05186.1; -; mRNA. DR CCDS; CCDS3604.1; -. DR RefSeq; NP_001284698.1; NM_001297769.1. DR RefSeq; NP_001284699.1; NM_001297770.1. DR RefSeq; NP_057151.1; NM_016067.3. DR PDB; 3J9M; EM; 3.50 A; AP=1-142. DR PDB; 6NU2; EM; 3.90 A; AP=47-142. DR PDB; 6NU3; EM; 4.40 A; AP=1-142. DR PDB; 6RW4; EM; 2.97 A; P=1-142. DR PDB; 6RW5; EM; 3.14 A; P=1-142. DR PDB; 6VLZ; EM; 2.97 A; AP=1-142. DR PDB; 6VMI; EM; 2.96 A; AP=1-142. DR PDB; 6ZM5; EM; 2.89 A; AP=1-142. DR PDB; 6ZM6; EM; 2.59 A; AP=1-142. DR PDB; 6ZS9; EM; 4.00 A; AP=1-142. DR PDB; 6ZSA; EM; 4.00 A; AP=1-142. DR PDB; 6ZSB; EM; 4.50 A; AP=1-142. DR PDB; 6ZSC; EM; 3.50 A; AP=1-142. DR PDB; 6ZSD; EM; 3.70 A; AP=1-142. DR PDB; 6ZSE; EM; 5.00 A; AP=1-142. DR PDB; 6ZSG; EM; 4.00 A; AP=1-142. DR PDB; 7A5F; EM; 4.40 A; P6=1-142. DR PDB; 7A5G; EM; 4.33 A; P6=1-142. DR PDB; 7A5I; EM; 3.70 A; P6=1-142. DR PDB; 7A5K; EM; 3.70 A; P6=1-142. DR PDB; 7L08; EM; 3.49 A; AP=1-142. DR PDB; 7OG4; EM; 3.80 A; AP=1-142. DR PDB; 7P2E; EM; 2.40 A; P=1-142. DR PDB; 7PNX; EM; 2.76 A; P=1-142. DR PDB; 7PNY; EM; 3.06 A; P=1-142. DR PDB; 7PNZ; EM; 3.09 A; P=1-142. DR PDB; 7PO0; EM; 2.90 A; P=1-142. DR PDB; 7PO1; EM; 2.92 A; P=1-142. DR PDB; 7PO2; EM; 3.09 A; P=1-142. DR PDB; 7PO3; EM; 2.92 A; P=1-142. DR PDB; 7QI4; EM; 2.21 A; AP=1-142. DR PDB; 7QI5; EM; 2.63 A; AP=1-142. DR PDB; 7QI6; EM; 2.98 A; AP=1-142. DR PDB; 8ANY; EM; 2.85 A; AP=1-142. DR PDB; 8CSP; EM; 2.66 A; P=1-142. DR PDB; 8CSQ; EM; 2.54 A; P=1-142. DR PDB; 8CSR; EM; 2.54 A; P=1-142. DR PDB; 8CSS; EM; 2.36 A; P=1-142. DR PDB; 8CST; EM; 2.85 A; P=1-142. DR PDB; 8CSU; EM; 3.03 A; P=1-142. DR PDB; 8OIR; EM; 3.10 A; AP=1-142. DR PDB; 8OIS; EM; 3.00 A; AP=1-142. DR PDBsum; 3J9M; -. DR PDBsum; 6NU2; -. DR PDBsum; 6NU3; -. DR PDBsum; 6RW4; -. DR PDBsum; 6RW5; -. 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; 7A5I; -. DR PDBsum; 7A5K; -. DR PDBsum; 7L08; -. DR PDBsum; 7OG4; -. DR PDBsum; 7P2E; -. DR PDBsum; 7PNX; -. DR PDBsum; 7PNY; -. DR PDBsum; 7PNZ; -. DR PDBsum; 7PO0; -. DR PDBsum; 7PO1; -. DR PDBsum; 7PO2; -. DR PDBsum; 7PO3; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8CSP; -. DR PDBsum; 8CSQ; -. DR PDBsum; 8CSR; -. DR PDBsum; 8CSS; -. DR PDBsum; 8CST; -. DR PDBsum; 8CSU; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIS; -. DR AlphaFoldDB; Q9Y3D5; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. DR EMDB; EMD-10021; -. DR EMDB; EMD-10022; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11391; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-11641; -. DR EMDB; EMD-11642; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-13170; -. DR EMDB; EMD-13555; -. DR EMDB; EMD-13556; -. DR EMDB; EMD-13557; -. DR EMDB; EMD-13558; -. DR EMDB; EMD-13559; -. DR EMDB; EMD-13560; -. DR EMDB; EMD-13561; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16898; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-26966; -. DR EMDB; EMD-26967; -. DR EMDB; EMD-26968; -. DR EMDB; EMD-26969; -. DR EMDB; EMD-26970; -. DR EMDB; EMD-26971; -. DR SMR; Q9Y3D5; -. DR BioGRID; 119229; 221. DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit. DR CORUM; Q9Y3D5; -. DR IntAct; Q9Y3D5; 31. DR MINT; Q9Y3D5; -. DR STRING; 9606.ENSP00000295491; -. DR iPTMnet; Q9Y3D5; -. DR PhosphoSitePlus; Q9Y3D5; -. DR BioMuta; MRPS18C; -. DR DMDM; 24212202; -. DR EPD; Q9Y3D5; -. DR jPOST; Q9Y3D5; -. DR MassIVE; Q9Y3D5; -. DR MaxQB; Q9Y3D5; -. DR PaxDb; 9606-ENSP00000295491; -. DR PeptideAtlas; Q9Y3D5; -. DR ProteomicsDB; 86021; -. DR Pumba; Q9Y3D5; -. DR Antibodypedia; 56067; 142 antibodies from 21 providers. DR DNASU; 51023; -. DR Ensembl; ENST00000295491.9; ENSP00000295491.4; ENSG00000163319.11. DR GeneID; 51023; -. DR KEGG; hsa:51023; -. DR MANE-Select; ENST00000295491.9; ENSP00000295491.4; NM_016067.4; NP_057151.1. DR UCSC; uc003hor.5; human. DR AGR; HGNC:16633; -. DR CTD; 51023; -. DR DisGeNET; 51023; -. DR GeneCards; MRPS18C; -. DR HGNC; HGNC:16633; MRPS18C. DR HPA; ENSG00000163319; Low tissue specificity. DR MIM; 611983; gene. DR neXtProt; NX_Q9Y3D5; -. DR OpenTargets; ENSG00000163319; -. DR PharmGKB; PA31005; -. DR VEuPathDB; HostDB:ENSG00000163319; -. DR eggNOG; KOG3162; Eukaryota. DR GeneTree; ENSGT00390000003791; -. DR HOGENOM; CLU_139337_2_0_1; -. DR InParanoid; Q9Y3D5; -. DR OMA; AQQCLLM; -. DR OrthoDB; 2903133at2759; -. DR PhylomeDB; Q9Y3D5; -. DR TreeFam; TF315059; -. DR PathwayCommons; Q9Y3D5; -. 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; Q9Y3D5; -. DR SIGNOR; Q9Y3D5; -. DR BioGRID-ORCS; 51023; 312 hits in 1155 CRISPR screens. DR ChiTaRS; MRPS18C; human. DR GenomeRNAi; 51023; -. DR Pharos; Q9Y3D5; Tdark. DR PRO; PR:Q9Y3D5; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9Y3D5; Protein. DR Bgee; ENSG00000163319; Expressed in hindlimb stylopod muscle and 180 other cell types or tissues. DR ExpressionAtlas; Q9Y3D5; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 4.10.640.10; Ribosomal protein S18; 1. DR InterPro; IPR001648; Ribosomal_bS18. DR InterPro; IPR018275; Ribosomal_bS18_CS. DR InterPro; IPR036870; Ribosomal_bS18_sf. DR NCBIfam; TIGR00165; S18; 1. DR PANTHER; PTHR13479:SF57; 28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL; 1. DR PANTHER; PTHR13479; 30S RIBOSOMAL PROTEIN S18; 1. DR Pfam; PF01084; Ribosomal_S18; 1. DR SUPFAM; SSF46911; Ribosomal protein S18; 1. DR PROSITE; PS00057; RIBOSOMAL_S18; 1. DR Genevisible; Q9Y3D5; HS. 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 ?..142 FT /note="Small ribosomal subunit protein bS18m" FT /id="PRO_0000030629" FT TURN 66..69 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 94..97 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 101..116 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:8CSS" SQ SEQUENCE 142 AA; 15850 MW; 375E0F8558492E63 CRC64; MAAVVAVCGG LGRKKLTHLV TAAVSLTHPG THTVLWRRGC SQQVSSNEDL PISMENPYKE PLKKCILCGK HVDYKNVQLL SQFVSPFTGC IYGRHITGLC GKKQKEITKA IKRAQIMGFM PVTYKDPAYL KDPKVCNIRY RE //