RT25_HUMAN
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 03-AUG-2022, entry version 175.
DE RecName: Full=28S ribosomal protein S25, mitochondrial;
DE Short=MRP-S25;
DE Short=S25mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS25 {ECO:0000303|PubMed:25838379};
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};
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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 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; P82663; -.
DR SMR; P82663; -.
DR BioGRID; 122180; 258.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P82663; -.
DR IntAct; P82663; 56.
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; P82663; -.
DR PeptideAtlas; P82663; -.
DR PRIDE; P82663; -.
DR ProteomicsDB; 4046; -.
DR ProteomicsDB; 4871; -.
DR ProteomicsDB; 57710; -. [P82663-1]
DR TopDownProteomics; P82663-1; -. [P82663-1]
DR Antibodypedia; 26653; 265 antibodies from 28 providers.
DR DNASU; 64432; -.
DR Ensembl; ENST00000253686.7; ENSP00000253686.2; ENSG00000131368.8. [P82663-1]
DR Ensembl; ENST00000444840.6; ENSP00000407733.2; ENSG00000131368.8. [P82663-3]
DR Ensembl; ENST00000449354.6; ENSP00000390882.2; ENSG00000131368.8. [P82663-2]
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 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; QIMLFRN; -.
DR OrthoDB; 1438394at2759; -.
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; 409 hits in 1095 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 181 other tissues.
DR ExpressionAtlas; P82663; baseline and differential.
DR Genevisible; P82663; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IC: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; IC:ComplexPortal.
DR InterPro; IPR040049; MRPS25.
DR InterPro; IPR007741; Ribosome/NADH_DH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13274; PTHR13274; 1.
DR Pfam; PF05047; L51_S25_CI-B8; 1.
DR SMART; SM00916; L51_S25_CI-B8; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
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="28S ribosomal protein S25, mitochondrial"
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"
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
