RT18C_HUMAN
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 03-AUG-2022, entry version 167.
DE RecName: Full=28S ribosomal protein S18c, mitochondrial;
DE Short=MRP-S18-c;
DE Short=Mrps18-c;
DE Short=S18mt-c;
DE AltName: Full=28S ribosomal protein S18-1, mitochondrial;
DE Short=MRP-S18-1;
DE AltName: Full=Mitochondrial small ribosomal subunit protein bS18c {ECO:0000303|PubMed:25838379};
DE AltName: Full=Mitochondrial small ribosomal subunit protein bS18m {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}.
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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 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 AlphaFoldDB; Q9Y3D5; -.
DR SMR; Q9Y3D5; -.
DR BioGRID; 119229; 215.
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; Q9Y3D5; -.
DR PeptideAtlas; Q9Y3D5; -.
DR PRIDE; Q9Y3D5; -.
DR ProteomicsDB; 86021; -.
DR Antibodypedia; 56067; 115 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 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; GYHKDLD; -.
DR OrthoDB; 1592020at2759; -.
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; 284 hits in 1074 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 178 other tissues.
DR ExpressionAtlas; Q9Y3D5; baseline and differential.
DR Genevisible; Q9Y3D5; HS.
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; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 4.10.640.10; -; 1.
DR InterPro; IPR001648; Ribosomal_S18.
DR InterPro; IPR018275; Ribosomal_S18_CS.
DR InterPro; IPR036870; Ribosomal_S18_sf.
DR PANTHER; PTHR13479; PTHR13479; 1.
DR Pfam; PF01084; Ribosomal_S18; 1.
DR SUPFAM; SSF46911; SSF46911; 1.
DR TIGRFAMs; TIGR00165; S18; 1.
DR PROSITE; PS00057; RIBOSOMAL_S18; 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 ?..142
FT /note="28S ribosomal protein S18c, mitochondrial"
FT /id="PRO_0000030629"
SQ SEQUENCE 142 AA; 15850 MW; 375E0F8558492E63 CRC64;
MAAVVAVCGG LGRKKLTHLV TAAVSLTHPG THTVLWRRGC SQQVSSNEDL PISMENPYKE
PLKKCILCGK HVDYKNVQLL SQFVSPFTGC IYGRHITGLC GKKQKEITKA IKRAQIMGFM
PVTYKDPAYL KDPKVCNIRY RE
