RT18B_HUMAN
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 03-AUG-2022, entry version 175.
DE RecName: Full=28S ribosomal protein S18b, mitochondrial;
DE Short=MRP-S18-b;
DE Short=Mrps18-b;
DE Short=S18mt-b;
DE AltName: Full=28S ribosomal protein S18-2, mitochondrial;
DE Short=MRP-S18-2;
DE AltName: Full=Mitochondrial small ribosomal subunit protein bS18b {ECO:0000303|PubMed:25838379};
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS40 {ECO:0000303|PubMed:27023846};
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; Q92552: MRPS27; NbExp=3; 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}.
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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 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; Q9Y676; -.
DR SMR; Q9Y676; -.
DR BioGRID; 118797; 275.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q9Y676; -.
DR DIP; DIP-29894N; -.
DR IntAct; Q9Y676; 86.
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 EPD; Q9Y676; -.
DR jPOST; Q9Y676; -.
DR MassIVE; Q9Y676; -.
DR MaxQB; Q9Y676; -.
DR PaxDb; Q9Y676; -.
DR PeptideAtlas; Q9Y676; -.
DR PRIDE; Q9Y676; -.
DR ProteomicsDB; 86614; -.
DR Antibodypedia; 26399; 85 antibodies from 21 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 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; PWEYLET; -.
DR OrthoDB; 1023024at2759; -.
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; 313 hits in 1085 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 98 other tissues.
DR ExpressionAtlas; Q9Y676; baseline and differential.
DR Genevisible; Q9Y676; HS.
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 Gene3D; 4.10.640.10; -; 1.
DR InterPro; IPR040054; MRPS18B.
DR InterPro; IPR001648; Ribosomal_S18.
DR InterPro; IPR036870; Ribosomal_S18_sf.
DR PANTHER; PTHR13329; PTHR13329; 1.
DR Pfam; PF01084; Ribosomal_S18; 1.
DR SUPFAM; SSF46911; SSF46911; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P82918"
FT CHAIN 36..258
FT /note="28S ribosomal protein S18b, mitochondrial"
FT /id="PRO_0000030627"
FT REGION 214..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..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"
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
