RT28_HUMAN
ID RT28_HUMAN Reviewed; 187 AA.
AC Q9Y2Q9; B2RDZ7; Q96Q21;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=28S ribosomal protein S28, mitochondrial;
DE Short=MRP-S28;
DE Short=S28mt;
DE AltName: Full=28S ribosomal protein S35, mitochondrial;
DE Short=MRP-S35;
DE Short=S35mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein bS1m {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=MRPS28; Synonyms=MRPS35; ORFNames=HSPC007;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-71.
RX PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA Watanabe K., Tanaka T.;
RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes to
RT the chromosomes and implications for human disorders.";
RL Genomics 77:65-70(2001).
RN [6]
RP IDENTIFICATION.
RX PubMed=10938081; DOI=10.1074/jbc.m003596200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Koc H., Spremulli L.L.;
RT "A proteomics approach to the identification of mammalian mitochondrial
RT small subunit ribosomal proteins.";
RL J. Biol. Chem. 275:32585-32591(2000).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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].
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 [10]
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 [11]
RP INVOLVEMENT IN COXPD47, FUNCTION, VARIANT COXPD47 ARG-119, AND
RP CHARACTERIZATION OF VARIANT COXPD47 ARG-119.
RX PubMed=30566640; DOI=10.1093/hmg/ddy441;
RA Pulman J., Ruzzenente B., Bianchi L., Rio M., Boddaert N., Munnich A.,
RA Roetig A., Metodiev M.D.;
RT "Mutations in the MRPS28 gene encoding the small mitoribosomal subunit
RT protein bS1m in a patient with intrauterine growth retardation,
RT craniofacial dysmorphism and multisystemic involvement.";
RL Hum. Mol. Genet. 28:1445-1462(2019).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
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) (PubMed:30566640). Mature mammalian 55S mitochondrial ribosomes
CC consist of a small (28S) and a large (39S) subunit. The 28S small
CC subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different
CC proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a
CC copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays
CC an integral structural role, and 52 different proteins.
CC {ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:30566640}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 47 (COXPD47)
CC [MIM:618958]: An autosomal recessive, multisystemic, mitochondrial
CC disorder characterized by intrauterine growth retardation, swallowing
CC difficulties with failure to thrive, hypoglycemia, dehydration, and
CC hepatomegaly. Additional features include global developmental delay
CC with impaired intellectual development and absent speech, microcephaly,
CC facial dysmorphism, cataract, sensorineural deafness, skeletal
CC features, and cryptorchidism. Laboratory studies show metabolic
CC acidosis, increased serum lactate, and variably impaired activity of
CC mitochondrial respiratory complexes I, III, IV, and V in different
CC tissues. {ECO:0000269|PubMed:30566640}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; AF070663; AAD20969.1; -; mRNA.
DR EMBL; AK315739; BAG38094.1; -; mRNA.
DR EMBL; CH471068; EAW87069.1; -; Genomic_DNA.
DR EMBL; BC010150; AAH10150.1; -; mRNA.
DR EMBL; AB061209; BAB54959.1; -; Genomic_DNA.
DR CCDS; CCDS6226.1; -.
DR RefSeq; NP_054737.1; NM_014018.2.
DR PDB; 3J9M; EM; 3.50 A; AW=1-187.
DR PDB; 6NU2; EM; 3.90 A; AW=77-173.
DR PDB; 6NU3; EM; 4.40 A; AW=1-187.
DR PDB; 6RW4; EM; 2.97 A; W=1-187.
DR PDB; 6RW5; EM; 3.14 A; W=1-187.
DR PDB; 6VLZ; EM; 2.97 A; AW=1-187.
DR PDB; 6VMI; EM; 2.96 A; AW=1-187.
DR PDB; 6ZM5; EM; 2.89 A; AW=1-187.
DR PDB; 6ZM6; EM; 2.59 A; AW=1-187.
DR PDB; 6ZS9; EM; 4.00 A; AW=1-187.
DR PDB; 6ZSA; EM; 4.00 A; AW=1-187.
DR PDB; 6ZSB; EM; 4.50 A; AW=1-187.
DR PDB; 6ZSC; EM; 3.50 A; AW=1-187.
DR PDB; 6ZSD; EM; 3.70 A; AW=1-187.
DR PDB; 6ZSE; EM; 5.00 A; AW=1-187.
DR PDB; 6ZSG; EM; 4.00 A; AW=1-187.
DR PDB; 7A5F; EM; 4.40 A; W6=1-187.
DR PDB; 7A5G; EM; 4.33 A; W6=1-187.
DR PDB; 7A5I; EM; 3.70 A; W6=1-187.
DR PDB; 7A5K; EM; 3.70 A; W6=1-187.
DR PDB; 7L08; EM; 3.49 A; AW=1-187.
DR PDB; 7OG4; EM; 3.80 A; AW=1-187.
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; Q9Y2Q9; -.
DR SMR; Q9Y2Q9; -.
DR BioGRID; 118784; 212.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q9Y2Q9; -.
DR IntAct; Q9Y2Q9; 47.
DR MINT; Q9Y2Q9; -.
DR STRING; 9606.ENSP00000276585; -.
DR iPTMnet; Q9Y2Q9; -.
DR MetOSite; Q9Y2Q9; -.
DR PhosphoSitePlus; Q9Y2Q9; -.
DR BioMuta; MRPS28; -.
DR DMDM; 22001973; -.
DR EPD; Q9Y2Q9; -.
DR jPOST; Q9Y2Q9; -.
DR MassIVE; Q9Y2Q9; -.
DR MaxQB; Q9Y2Q9; -.
DR PaxDb; Q9Y2Q9; -.
DR PeptideAtlas; Q9Y2Q9; -.
DR PRIDE; Q9Y2Q9; -.
DR ProteomicsDB; 85872; -.
DR TopDownProteomics; Q9Y2Q9; -.
DR Antibodypedia; 12414; 102 antibodies from 22 providers.
DR DNASU; 28957; -.
DR Ensembl; ENST00000276585.9; ENSP00000276585.4; ENSG00000147586.10.
DR GeneID; 28957; -.
DR KEGG; hsa:28957; -.
DR MANE-Select; ENST00000276585.9; ENSP00000276585.4; NM_014018.3; NP_054737.1.
DR UCSC; uc003ybp.4; human.
DR CTD; 28957; -.
DR DisGeNET; 28957; -.
DR GeneCards; MRPS28; -.
DR HGNC; HGNC:14513; MRPS28.
DR HPA; ENSG00000147586; Low tissue specificity.
DR MalaCards; MRPS28; -.
DR MIM; 611990; gene.
DR MIM; 618958; phenotype.
DR neXtProt; NX_Q9Y2Q9; -.
DR PharmGKB; PA31016; -.
DR VEuPathDB; HostDB:ENSG00000147586; -.
DR eggNOG; KOG4078; Eukaryota.
DR GeneTree; ENSGT00390000001057; -.
DR HOGENOM; CLU_109102_2_0_1; -.
DR InParanoid; Q9Y2Q9; -.
DR OMA; LPEDNQT; -.
DR OrthoDB; 1566742at2759; -.
DR PhylomeDB; Q9Y2Q9; -.
DR TreeFam; TF315097; -.
DR PathwayCommons; Q9Y2Q9; -.
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; Q9Y2Q9; -.
DR SIGNOR; Q9Y2Q9; -.
DR BioGRID-ORCS; 28957; 302 hits in 1087 CRISPR screens.
DR ChiTaRS; MRPS28; human.
DR GeneWiki; MRPS28; -.
DR GenomeRNAi; 28957; -.
DR Pharos; Q9Y2Q9; Tdark.
DR PRO; PR:Q9Y2Q9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y2Q9; protein.
DR Bgee; ENSG00000147586; Expressed in adrenal tissue and 100 other tissues.
DR ExpressionAtlas; Q9Y2Q9; baseline and differential.
DR Genevisible; Q9Y2Q9; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IMP:UniProtKB.
DR InterPro; IPR019375; Ribosomal_S28_mit.
DR PANTHER; PTHR13447; PTHR13447; 1.
DR Pfam; PF10246; MRP-S35; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Mitochondrion; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..71
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 72..187
FT /note="28S ribosomal protein S28, mitochondrial"
FT /id="PRO_0000087714"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CY16"
FT MOD_RES 133
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 103
FT /note="R -> W (in dbSNP:rs16919579)"
FT /id="VAR_052047"
FT VARIANT 119
FT /note="K -> R (in COXPD47; strong decrease in mitochondrial
FT translation and in oxidative phosphorylation biogenesis;
FT this phenotype could be reversed in patient's fibroblasts
FT by transfection with the wild-type protein)"
FT /evidence="ECO:0000269|PubMed:30566640"
FT /id="VAR_084507"
SQ SEQUENCE 187 AA; 20843 MW; 2ED0EA43552B9B54 CRC64;
MAALCRTRAV AAESHFLRVF LFFRPFRGVG TESGSESGSS NAKEPKTRAG GFASALERHS
ELLQKVEPLQ KGSPKNVESF ASMLRHSPLT QMGPAKDKLV IGRIFHIVEN DLYIDFGGKF
HCVCRRPEVD GEKYQKGTRV RLRLLDLELT SRFLGATTDT TVLEANAVLL GIQESKDSRS
KEEHHEK
