ID RT25_HUMAN Reviewed; 173 AA. AC P82663; B4DFJ5; B4DQG6; Q9H7P5; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 183. DE RecName: Full=Small ribosomal subunit protein mS25 {ECO:0000303|PubMed:25838379}; DE AltName: Full=28S ribosomal protein S25, mitochondrial; DE Short=MRP-S25; DE Short=S25mt; GN Name=MRPS25; Synonyms=RPMS25; 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] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain cortex; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Spleen; RX PubMed=11214971; DOI=10.1093/dnares/7.6.357; RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.; RT "Characterization of long cDNA clones from human adult spleen."; RL DNA Res. 7:357-366(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 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 [6] 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 [7] 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 [8] 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). RN [9] RP VARIANT COXPD50 LEU-72, INVOLVEMENT IN COXPD50, AND CHARACTERIZATION OF RP VARIANT COXPD50 LEU-72. RX PubMed=31039582; DOI=10.1093/hmg/ddz093; RA Bugiardini E., Mitchell A.L., Rosa I.D., Horning-Do H.T., Pitmann A.M., RA Poole O.V., Holton J.L., Shah S., Woodward C., Hargreaves I., Quinlivan R., RA Amunts A., Wiesner R.J., Houlden H., Holt I.J., Hanna M.G., RA Pitceathly R.D.S., Spinazzola A.; RT "MRPS25 mutations impair mitochondrial translation and cause RT encephalomyopathy."; RL Hum. Mol. Genet. 28:2711-2719(2019). 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. {ECO:0000269|PubMed:25838379}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P82663-1; Sequence=Displayed; CC Name=2; CC IsoId=P82663-2; Sequence=VSP_056423; CC Name=3; CC IsoId=P82663-3; Sequence=VSP_056422, VSP_056424; CC -!- DISEASE: Combined oxidative phosphorylation deficiency 50 (COXPD50) CC [MIM:619025]: An autosomal recessive, mitochondrial encephalomyopathy CC characterized by intrauterine growth retardation, poor overall growth, CC delayed psychomotor development, hypotonia, muscle weakness, CC progressive loss of ambulation, and mitochondrial oxidative CC phosphorylation deficiency in patient tissues. Brain imaging shows CC partial agenesis of the corpus callosum. {ECO:0000269|PubMed:31039582}. CC Note=The disease may be caused by variants affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein CC mS25 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15723.1; Type=Erroneous initiation; Evidence={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; AK024702; BAB14968.1; -; mRNA. DR EMBL; AK024433; BAB15723.1; ALT_INIT; mRNA. DR EMBL; AK294123; BAG57456.1; -; mRNA. DR EMBL; AK298791; BAG60928.1; -; mRNA. DR EMBL; AC090954; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003590; AAH03590.1; -; mRNA. DR CCDS; CCDS2622.1; -. [P82663-1] DR RefSeq; NP_071942.1; NM_022497.4. [P82663-1] DR PDB; 3J9M; EM; 3.50 A; AT=1-173. DR PDB; 6NU2; EM; 3.90 A; AT=2-163. DR PDB; 6NU3; EM; 4.40 A; AT=1-173. DR PDB; 6RW4; EM; 2.97 A; T=1-173. DR PDB; 6RW5; EM; 3.14 A; T=1-173. DR PDB; 6VLZ; EM; 2.97 A; AT=1-173. DR PDB; 6VMI; EM; 2.96 A; AT=1-173. DR PDB; 6ZM5; EM; 2.89 A; AT=1-173. DR PDB; 6ZM6; EM; 2.59 A; AT=1-173. DR PDB; 6ZS9; EM; 4.00 A; AT=1-173. DR PDB; 6ZSA; EM; 4.00 A; AT=1-173. DR PDB; 6ZSB; EM; 4.50 A; AT=1-173. DR PDB; 6ZSC; EM; 3.50 A; AT=1-173. DR PDB; 6ZSD; EM; 3.70 A; AT=1-173. DR PDB; 6ZSE; EM; 5.00 A; AT=1-164. DR PDB; 6ZSG; EM; 4.00 A; AT=1-173. DR PDB; 7A5F; EM; 4.40 A; T6=1-173. DR PDB; 7A5G; EM; 4.33 A; T6=1-173. DR PDB; 7A5I; EM; 3.70 A; T6=1-173. DR PDB; 7A5K; EM; 3.70 A; T6=1-173. DR PDB; 7L08; EM; 3.49 A; AT=1-173. DR PDB; 7OG4; EM; 3.80 A; AT=1-173. DR PDB; 7P2E; EM; 2.40 A; T=1-173. DR PDB; 7PNX; EM; 2.76 A; T=1-173. DR PDB; 7PNY; EM; 3.06 A; T=1-173. DR PDB; 7PNZ; EM; 3.09 A; T=1-173. DR PDB; 7PO0; EM; 2.90 A; T=1-173. DR PDB; 7PO1; EM; 2.92 A; T=1-173. DR PDB; 7PO2; EM; 3.09 A; T=1-173. DR PDB; 7PO3; EM; 2.92 A; T=1-173. DR PDB; 7QI4; EM; 2.21 A; AT=1-173. DR PDB; 7QI5; EM; 2.63 A; AT=1-173. DR PDB; 7QI6; EM; 2.98 A; AT=1-173. DR PDB; 8ANY; EM; 2.85 A; AT=1-173. DR PDB; 8CSP; EM; 2.66 A; T=1-173. DR PDB; 8CSQ; EM; 2.54 A; T=1-173. DR PDB; 8CSR; EM; 2.54 A; T=1-173. DR PDB; 8CSS; EM; 2.36 A; T=1-173. DR PDB; 8CST; EM; 2.85 A; T=1-173. DR PDB; 8CSU; EM; 3.03 A; T=1-173. DR PDB; 8OIR; EM; 3.10 A; AT=1-173. DR PDB; 8OIS; EM; 3.00 A; AT=1-173. 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; P82663; -. 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 SMR; P82663; -. DR BioGRID; 122180; 275. DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit. DR CORUM; P82663; -. DR IntAct; P82663; 60. DR MINT; P82663; -. DR STRING; 9606.ENSP00000253686; -. DR GlyGen; P82663; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P82663; -. DR PhosphoSitePlus; P82663; -. DR SwissPalm; P82663; -. DR BioMuta; MRPS25; -. DR DMDM; 13633894; -. DR EPD; P82663; -. DR jPOST; P82663; -. DR MassIVE; P82663; -. DR MaxQB; P82663; -. DR PaxDb; 9606-ENSP00000253686; -. DR PeptideAtlas; P82663; -. DR ProteomicsDB; 4046; -. DR ProteomicsDB; 4871; -. DR ProteomicsDB; 57710; -. [P82663-1] DR Pumba; P82663; -. DR TopDownProteomics; P82663-1; -. [P82663-1] DR Antibodypedia; 26653; 284 antibodies from 28 providers. DR DNASU; 64432; -. DR Ensembl; ENST00000253686.7; ENSP00000253686.2; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000444840.6; ENSP00000407733.2; ENSG00000131368.9. [P82663-3] DR Ensembl; ENST00000449354.7; ENSP00000390882.2; ENSG00000131368.9. [P82663-2] DR Ensembl; ENST00000474866.3; ENSP00000511860.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000496484.3; ENSP00000511856.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695334.2; ENSP00000511812.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695376.1; ENSP00000511849.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695379.1; ENSP00000511852.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695380.2; ENSP00000511853.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695382.1; ENSP00000511855.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695386.1; ENSP00000511862.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695387.1; ENSP00000511863.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695391.1; ENSP00000511867.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695392.1; ENSP00000511868.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000695394.1; ENSP00000511870.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000698782.1; ENSP00000513929.1; ENSG00000131368.9. [P82663-1] DR Ensembl; ENST00000698783.1; ENSP00000513930.1; ENSG00000131368.9. [P82663-1] DR GeneID; 64432; -. DR KEGG; hsa:64432; -. DR MANE-Select; ENST00000253686.7; ENSP00000253686.2; NM_022497.5; NP_071942.1. DR UCSC; uc003bzl.4; human. [P82663-1] DR AGR; HGNC:14511; -. DR CTD; 64432; -. DR GeneCards; MRPS25; -. DR HGNC; HGNC:14511; MRPS25. DR HPA; ENSG00000131368; Low tissue specificity. DR MalaCards; MRPS25; -. DR MIM; 611987; gene. DR MIM; 619025; phenotype. DR neXtProt; NX_P82663; -. DR OpenTargets; ENSG00000131368; -. DR PharmGKB; PA31013; -. DR VEuPathDB; HostDB:ENSG00000131368; -. DR eggNOG; KOG4079; Eukaryota. DR GeneTree; ENSGT00640000091558; -. DR HOGENOM; CLU_094727_0_0_1; -. DR InParanoid; P82663; -. DR OMA; NYNTYGE; -. DR OrthoDB; 2901943at2759; -. DR PhylomeDB; P82663; -. DR TreeFam; TF300292; -. DR PathwayCommons; P82663; -. 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; P82663; -. DR SIGNOR; P82663; -. DR BioGRID-ORCS; 64432; 425 hits in 1177 CRISPR screens. DR ChiTaRS; MRPS25; human. DR GeneWiki; MRPS25; -. DR GenomeRNAi; 64432; -. DR Pharos; P82663; Tdark. DR PRO; PR:P82663; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P82663; Protein. DR Bgee; ENSG00000131368; Expressed in apex of heart and 183 other cell types or tissues. DR ExpressionAtlas; P82663; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; NAS:ComplexPortal. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR007741; Ribosomal_mL43/mS25/NADH_DH. DR InterPro; IPR040049; Ribosomal_mS25/mL61. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR13274:SF2; 28S RIBOSOMAL PROTEIN S25, MITOCHONDRIAL; 1. DR PANTHER; PTHR13274; MITOCHONDRIAL RIBOSOMAL PROTEIN S25; 1. DR Pfam; PF05047; L51_S25_CI-B8; 1. DR SMART; SM00916; L51_S25_CI-B8; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR Genevisible; P82663; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; Mitochondrion; KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1..173 FT /note="Small ribosomal subunit protein mS25" FT /id="PRO_0000087708" FT VAR_SEQ 81..129 FT /note="DSGEQVLVDVETKSNKEIMEHIRKILGKNEETLREEEEEKKQLSHPANF -> FT GKPSGKRRRRKSSFLTQPTSALESTACGSASVKWKGRCPAPAWCHYPRR (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056422" FT VAR_SEQ 111..173 FT /note="ETLREEEEEKKQLSHPANFGPRKYCLRECICEVEGQVPCPSLVPLPKEMRGK FT YKAALKADAQD -> HYLAAPSKPVSSAVVPVTQEAEAGGSLEPRRLRLE (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056423" FT VAR_SEQ 130..173 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056424" FT VARIANT 72 FT /note="P -> L (in COXPD50; severe reduction of MRPS25 FT protein levels resulting in destabilization of the entire FT small ribosomal subunit and a decrease of mitochondrial FT translation rate; causes oxidative phosphorylation defects FT in patient cells; dbSNP:rs1192432123)" FT /evidence="ECO:0000269|PubMed:31039582" FT /id="VAR_084766" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 8..11 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 13..17 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 27..34 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 42..50 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 52..58 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 62..73 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 95..106 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 110..123 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:8CSS" SQ SEQUENCE 173 AA; 20116 MW; 78BB282C1539FA4C CRC64; MPMKGRFPIR RTLQYLSQGN VVFKDSVKVM TVNYNTHGEL GEGARKFVFF NIPQIQYKNP WVQIMMFKNM TPSPFLRFYL DSGEQVLVDV ETKSNKEIME HIRKILGKNE ETLREEEEEK KQLSHPANFG PRKYCLRECI CEVEGQVPCP SLVPLPKEMR GKYKAALKAD AQD //