ID   RT18B_HUMAN             Reviewed;         258 AA.
AC   Q9Y676; A6NDQ0; Q659G4; Q9BS27;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   05-FEB-2025, entry version 188.
DE   RecName: Full=Small ribosomal subunit protein mS40 {ECO:0000303|PubMed:27023846};
DE   AltName: Full=28S ribosomal protein S18-2, mitochondrial;
DE            Short=MRP-S18-2;
DE   AltName: Full=28S ribosomal protein S18b, mitochondrial;
DE            Short=MRP-S18-b;
DE            Short=Mrps18-b;
DE            Short=S18mt-b;
DE   AltName: Full=Small ribosomal subunit protein bS18b {ECO:0000303|PubMed:25838379};
DE   Flags: Precursor;
GN   Name=MRPS18B; Synonyms=C6orf14; ORFNames=HSPC183, PTD017;
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:AAF36103.1};
RN   [1] {ECO:0000312|EMBL:AAF36103.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary tumor;
RA   Zhang Q.H., Guan Z.Q., Dai M., Song H., Mao Y.F., Wu X.Y., Mao M., Fu G.,
RA   Luo M., Chen J.H., Hu R.;
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Peripheral blood leukocyte;
RX   PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA   Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA   Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA   Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA   Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA   Inoko H., Bahram S.;
RT   "Rapid evolution of major histocompatibility complex class I genes in
RT   primates generates new disease alleles in humans via hitchhiking
RT   diversity.";
RL   Genetics 173:1555-1570(2006).
RN   [5]
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   [6] {ECO:0000312|EMBL:AAF36103.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [8] {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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-49, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
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   [13]
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   [14] {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. mS40 has a zinc binding site.
CC       {ECO:0000269|PubMed:25838379}.
CC   -!- INTERACTION:
CC       Q9Y676; O95393: BMP10; NbExp=3; IntAct=EBI-750085, EBI-3922513;
CC       Q9Y676; P60033: CD81; NbExp=3; IntAct=EBI-750085, EBI-712921;
CC       Q9Y676; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-750085, EBI-11996768;
CC       Q9Y676; P24593: IGFBP5; NbExp=3; IntAct=EBI-750085, EBI-720480;
CC       Q9Y676; O43561-2: LAT; NbExp=3; IntAct=EBI-750085, EBI-8070286;
CC       Q9Y676; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-750085, EBI-2830349;
CC       Q9Y676; P30301: MIP; NbExp=3; IntAct=EBI-750085, EBI-8449636;
CC       Q9Y676; P82650: MRPS22; NbExp=5; IntAct=EBI-750085, EBI-1050752;
CC       Q9Y676; Q92552: MRPS27; NbExp=7; IntAct=EBI-750085, EBI-2211879;
CC       Q9Y676; P06400: RB1; NbExp=2; IntAct=EBI-750085, EBI-491274;
CC       Q9Y676; O75396: SEC22B; NbExp=3; IntAct=EBI-750085, EBI-1058865;
CC       Q9Y676; P78382: SLC35A1; NbExp=3; IntAct=EBI-750085, EBI-12870360;
CC       Q9Y676; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-750085, EBI-13075176;
CC       Q9Y676; Q6PL24: TMED8; NbExp=3; IntAct=EBI-750085, EBI-11603430;
CC       Q9Y676; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-750085, EBI-10171534;
CC       Q9Y676; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-750085, EBI-10694905;
CC       Q9Y676; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-750085, EBI-717441;
CC       Q9Y676; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-750085, EBI-11988865;
CC       Q9Y676; O95159: ZFPL1; NbExp=3; IntAct=EBI-750085, EBI-718439;
CC       Q9Y676; P03204: EBNA6; Xeno; NbExp=6; IntAct=EBI-750085, EBI-9255985;
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) binds
CC       to the same site as bacterial bS18, mS40 (bS18b, this protein) binds to
CC       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       Mitochondrion-specific ribosomal protein mS40 subfamily. {ECO:0000305}.
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; AF100761; AAD43025.1; -; mRNA.
DR   EMBL; AF151017; AAF36103.1; -; mRNA.
DR   EMBL; AL050361; CAH56415.1; -; mRNA.
DR   EMBL; AB110933; BAD13699.1; -; Genomic_DNA.
DR   EMBL; AB110934; BAD13700.1; -; Genomic_DNA.
DR   EMBL; AB202094; BAE78614.1; -; Genomic_DNA.
DR   EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL732442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX119957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX248507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR753328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03304.1; -; Genomic_DNA.
DR   EMBL; BC005373; AAH05373.1; -; mRNA.
DR   CCDS; CCDS4682.1; -.
DR   RefSeq; NP_054765.1; NM_014046.3.
DR   PDB; 3J9M; EM; 3.50 A; AO=1-258.
DR   PDB; 6NU2; EM; 3.90 A; AO=52-236.
DR   PDB; 6NU3; EM; 4.40 A; AO=52-236.
DR   PDB; 6RW4; EM; 2.97 A; O=1-258.
DR   PDB; 6RW5; EM; 3.14 A; O=1-258.
DR   PDB; 6VLZ; EM; 2.97 A; AO=1-258.
DR   PDB; 6VMI; EM; 2.96 A; AO=1-258.
DR   PDB; 6ZM5; EM; 2.89 A; AO=1-258.
DR   PDB; 6ZM6; EM; 2.59 A; AO=1-258.
DR   PDB; 6ZS9; EM; 4.00 A; AO=1-258.
DR   PDB; 6ZSA; EM; 4.00 A; AO=1-258.
DR   PDB; 6ZSB; EM; 4.50 A; AO=1-258.
DR   PDB; 6ZSC; EM; 3.50 A; AO=1-258.
DR   PDB; 6ZSD; EM; 3.70 A; AO=1-258.
DR   PDB; 6ZSE; EM; 5.00 A; AO=1-236.
DR   PDB; 6ZSG; EM; 4.00 A; AO=1-258.
DR   PDB; 7A5F; EM; 4.40 A; O6=1-258.
DR   PDB; 7A5G; EM; 4.33 A; O6=1-258.
DR   PDB; 7A5I; EM; 3.70 A; O6=1-258.
DR   PDB; 7A5K; EM; 3.70 A; O6=1-258.
DR   PDB; 7L08; EM; 3.49 A; AO=1-258.
DR   PDB; 7OG4; EM; 3.80 A; AO=1-258.
DR   PDB; 7P2E; EM; 2.40 A; O=1-258.
DR   PDB; 7PNX; EM; 2.76 A; O=1-258.
DR   PDB; 7PNY; EM; 3.06 A; O=1-258.
DR   PDB; 7PNZ; EM; 3.09 A; O=1-258.
DR   PDB; 7PO0; EM; 2.90 A; O=1-258.
DR   PDB; 7PO1; EM; 2.92 A; O=1-258.
DR   PDB; 7PO2; EM; 3.09 A; O=1-258.
DR   PDB; 7PO3; EM; 2.92 A; O=1-258.
DR   PDB; 7QI4; EM; 2.21 A; AO=1-258.
DR   PDB; 7QI5; EM; 2.63 A; AO=1-258.
DR   PDB; 7QI6; EM; 2.98 A; AO=1-258.
DR   PDB; 8ANY; EM; 2.85 A; AO=1-258.
DR   PDB; 8CSP; EM; 2.66 A; O=1-258.
DR   PDB; 8CSQ; EM; 2.54 A; O=1-258.
DR   PDB; 8CSR; EM; 2.54 A; O=1-258.
DR   PDB; 8CSS; EM; 2.36 A; O=1-258.
DR   PDB; 8CST; EM; 2.85 A; O=1-258.
DR   PDB; 8CSU; EM; 3.03 A; O=1-258.
DR   PDB; 8K2A; EM; 2.90 A; SS=1-258.
DR   PDB; 8OIR; EM; 3.10 A; AO=1-258.
DR   PDB; 8OIS; EM; 3.00 A; AO=1-258.
DR   PDB; 8QRK; EM; 6.69 A; O=1-258.
DR   PDB; 8QRL; EM; 3.34 A; O=1-258.
DR   PDB; 8QRM; EM; 3.05 A; O=1-258.
DR   PDB; 8QRN; EM; 2.98 A; O=1-258.
DR   PDB; 8XT0; EM; 3.20 A; SS=1-258.
DR   PDB; 8XT2; EM; 3.30 A; SS=1-258.
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; 8K2A; -.
DR   PDBsum; 8OIR; -.
DR   PDBsum; 8OIS; -.
DR   PDBsum; 8QRK; -.
DR   PDBsum; 8QRL; -.
DR   PDBsum; 8QRM; -.
DR   PDBsum; 8QRN; -.
DR   PDBsum; 8XT0; -.
DR   PDBsum; 8XT2; -.
DR   AlphaFoldDB; Q9Y676; -.
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   EMDB; EMD-36836; -.
DR   EMDB; EMD-38632; -.
DR   EMDB; EMD-38634; -.
DR   SMR; Q9Y676; -.
DR   BioGRID; 118797; 322.
DR   ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR   CORUM; Q9Y676; -.
DR   DIP; DIP-29894N; -.
DR   IntAct; Q9Y676; 170.
DR   MINT; Q9Y676; -.
DR   STRING; 9606.ENSP00000259873; -.
DR   GlyGen; Q9Y676; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y676; -.
DR   PhosphoSitePlus; Q9Y676; -.
DR   SwissPalm; Q9Y676; -.
DR   BioMuta; MRPS18B; -.
DR   DMDM; 24212203; -.
DR   jPOST; Q9Y676; -.
DR   MassIVE; Q9Y676; -.
DR   PaxDb; 9606-ENSP00000259873; -.
DR   PeptideAtlas; Q9Y676; -.
DR   ProteomicsDB; 86614; -.
DR   Pumba; Q9Y676; -.
DR   Antibodypedia; 26399; 125 antibodies from 23 providers.
DR   DNASU; 28973; -.
DR   Ensembl; ENST00000259873.5; ENSP00000259873.4; ENSG00000204568.12.
DR   Ensembl; ENST00000327800.10; ENSP00000383438.3; ENSG00000203624.10.
DR   Ensembl; ENST00000412451.6; ENSP00000402718.2; ENSG00000223775.8.
DR   Ensembl; ENST00000426945.6; ENSP00000397790.2; ENSG00000229861.8.
DR   Ensembl; ENST00000430402.6; ENSP00000398494.2; ENSG00000233813.8.
DR   Ensembl; ENST00000451032.6; ENSP00000415703.2; ENSG00000226111.8.
DR   Ensembl; ENST00000454427.6; ENSP00000414972.2; ENSG00000227420.8.
DR   GeneID; 28973; -.
DR   KEGG; hsa:28973; -.
DR   MANE-Select; ENST00000259873.5; ENSP00000259873.4; NM_014046.4; NP_054765.1.
DR   UCSC; uc003nqo.3; human.
DR   AGR; HGNC:14516; -.
DR   CTD; 28973; -.
DR   DisGeNET; 28973; -.
DR   GeneCards; MRPS18B; -.
DR   HGNC; HGNC:14516; MRPS18B.
DR   HPA; ENSG00000204568; Low tissue specificity.
DR   MIM; 611982; gene.
DR   neXtProt; NX_Q9Y676; -.
DR   OpenTargets; ENSG00000204568; -.
DR   PharmGKB; PA31004; -.
DR   VEuPathDB; HostDB:ENSG00000204568; -.
DR   eggNOG; KOG4021; Eukaryota.
DR   GeneTree; ENSGT00390000010554; -.
DR   HOGENOM; CLU_089746_0_0_1; -.
DR   InParanoid; Q9Y676; -.
DR   OMA; RSAYGVQ; -.
DR   OrthoDB; 21463at2759; -.
DR   PhylomeDB; Q9Y676; -.
DR   TreeFam; TF315059; -.
DR   PathwayCommons; Q9Y676; -.
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; Q9Y676; -.
DR   SIGNOR; Q9Y676; -.
DR   BioGRID-ORCS; 28973; 335 hits in 1163 CRISPR screens.
DR   ChiTaRS; MRPS18B; human.
DR   GeneWiki; MRPS18B; -.
DR   GenomeRNAi; 28973; -.
DR   Pharos; Q9Y676; Tbio.
DR   PRO; PR:Q9Y676; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9Y676; protein.
DR   Bgee; ENSG00000204568; Expressed in gastrocnemius and 100 other cell types or tissues.
DR   ExpressionAtlas; Q9Y676; baseline and differential.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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   FunFam; 4.10.640.10:FF:000008; 28S ribosomal protein S18b, mitochondrial; 1.
DR   Gene3D; 4.10.640.10; Ribosomal protein S18; 1.
DR   InterPro; IPR040054; MRPS18B.
DR   InterPro; IPR001648; Ribosomal_bS18.
DR   InterPro; IPR036870; Ribosomal_bS18_sf.
DR   PANTHER; PTHR13329; MITOCHONDRIAL RIBOSOMAL PROTEIN S18B; 1.
DR   PANTHER; PTHR13329:SF2; SMALL RIBOSOMAL SUBUNIT PROTEIN MS40; 1.
DR   Pfam; PF01084; Ribosomal_S18; 1.
DR   SUPFAM; SSF46911; Ribosomal protein S18; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P82918"
FT   CHAIN           36..258
FT                   /note="Small ribosomal subunit protein mS40"
FT                   /id="PRO_0000030627"
FT   REGION          214..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..242
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         230
FT                   /note="P -> A (in dbSNP:rs34315095)"
FT                   /id="VAR_052056"
FT   CONFLICT        196
FT                   /note="G -> S (in Ref. 7; AAH05373)"
FT                   /evidence="ECO:0000305"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           55..59
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           62..68
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            73..76
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           120..124
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           137..140
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           144..159
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           191..195
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           210..219
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:8CSS"
SQ   SEQUENCE   258 AA;  29396 MW;  B4C83E5593796C5D CRC64;
     MAASVLNTVL RRLPMLSLFR GSHRVQVPLQ TLCTKAPSEE DSLSSVPISP YKDEPWKYLE
     SEEYQERYGS RPVWADYRRN HKGGVPPQRT RKTCIRRNKV VGNPCPICRD HKLHVDFRNV
     KLLEQFVCAH TGIIFYAPYT GVCVKQHKRL TQAIQKARDH GLLIYHIPQV EPRDLDFSTS
     HGAVSATPPA PTLVSGDPWY PWYNWKQPPE RELSRLRRLY QGHLQEESGP PPESMPKMPP
     RTPAEASSTG QTGPQSAL
//