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   27-MAR-2024, entry version 181.
DE   RecName: Full=Small ribosomal subunit protein bS1m {ECO:0000303|PubMed:25838379};
DE   AltName: 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   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   PDB; 7P2E; EM; 2.40 A; W=1-187.
DR   PDB; 7PNX; EM; 2.76 A; W=1-187.
DR   PDB; 7PNY; EM; 3.06 A; W=1-187.
DR   PDB; 7PNZ; EM; 3.09 A; W=1-187.
DR   PDB; 7PO0; EM; 2.90 A; W=1-187.
DR   PDB; 7PO1; EM; 2.92 A; W=1-187.
DR   PDB; 7PO2; EM; 3.09 A; W=1-187.
DR   PDB; 7PO3; EM; 2.92 A; W=1-187.
DR   PDB; 7QI4; EM; 2.21 A; AW=1-187.
DR   PDB; 7QI5; EM; 2.63 A; AW=1-187.
DR   PDB; 7QI6; EM; 2.98 A; AW=1-187.
DR   PDB; 8ANY; EM; 2.85 A; AW=1-187.
DR   PDB; 8CSP; EM; 2.66 A; W=1-187.
DR   PDB; 8CSQ; EM; 2.54 A; W=1-187.
DR   PDB; 8CSR; EM; 2.54 A; W=1-187.
DR   PDB; 8CSS; EM; 2.36 A; W=1-187.
DR   PDB; 8CST; EM; 2.85 A; W=1-187.
DR   PDB; 8CSU; EM; 3.03 A; W=1-187.
DR   PDB; 8OIR; EM; 3.10 A; AW=1-187.
DR   PDB; 8OIS; EM; 3.00 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   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; Q9Y2Q9; -.
DR   EMDB; EMD-11278; -.
DR   EMDB; EMD-11279; -.
DR   EMDB; EMD-11390; -.
DR   EMDB; EMD-11392; -.
DR   EMDB; EMD-11393; -.
DR   EMDB; EMD-11394; -.
DR   EMDB; EMD-11395; -.
DR   EMDB; EMD-11397; -.
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-26966; -.
DR   EMDB; EMD-26967; -.
DR   EMDB; EMD-26968; -.
DR   EMDB; EMD-26969; -.
DR   EMDB; EMD-26970; -.
DR   EMDB; EMD-26971; -.
DR   SMR; Q9Y2Q9; -.
DR   BioGRID; 118784; 231.
DR   ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR   CORUM; Q9Y2Q9; -.
DR   IntAct; Q9Y2Q9; 54.
DR   MINT; Q9Y2Q9; -.
DR   STRING; 9606.ENSP00000276585; -.
DR   iPTMnet; Q9Y2Q9; -.
DR   MetOSite; Q9Y2Q9; -.
DR   PhosphoSitePlus; Q9Y2Q9; -.
DR   SwissPalm; Q9Y2Q9; -.
DR   BioMuta; MRPS28; -.
DR   DMDM; 22001973; -.
DR   EPD; Q9Y2Q9; -.
DR   jPOST; Q9Y2Q9; -.
DR   MassIVE; Q9Y2Q9; -.
DR   MaxQB; Q9Y2Q9; -.
DR   PaxDb; 9606-ENSP00000276585; -.
DR   PeptideAtlas; Q9Y2Q9; -.
DR   ProteomicsDB; 85872; -.
DR   Pumba; Q9Y2Q9; -.
DR   TopDownProteomics; Q9Y2Q9; -.
DR   Antibodypedia; 12414; 124 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   AGR; HGNC:14513; -.
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; CSRPTRN; -.
DR   OrthoDB; 2881116at2759; -.
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; 324 hits in 1166 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 102 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2Q9; baseline and differential.
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_bS1m.
DR   PANTHER; PTHR13447:SF2; 28S RIBOSOMAL PROTEIN S28, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13447; MITOCHONDRIAL 28S RIBOSOMAL PROTEIN S28; 1.
DR   Pfam; PF10246; MRP-S35; 1.
DR   Genevisible; Q9Y2Q9; HS.
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="Small ribosomal subunit protein bS1m"
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                   dbSNP:rs1808705345)"
FT                   /evidence="ECO:0000269|PubMed:30566640"
FT                   /id="VAR_084507"
FT   HELIX           80..85
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           88..92
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          98..108
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          111..115
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          139..148
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:8CSS"
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
//