RT07_HUMAN
ID RT07_HUMAN Reviewed; 242 AA.
AC Q9Y2R9; B2R9N5; Q53GD6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=28S ribosomal protein S7, mitochondrial;
DE Short=MRP-S7;
DE Short=S7mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS7m {ECO:0000303|PubMed:25838379};
DE AltName: Full=bMRP-27a;
DE Short=bMRP27a;
DE Flags: Precursor;
GN Name=MRPS7;
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], AND VARIANT VAL-2.
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], AND VARIANT VAL-2.
RC TISSUE=Skeletal muscle;
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 MRNA], AND VARIANT VAL-2.
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-2.
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION.
RX PubMed=10581179; DOI=10.1006/bbrc.1999.1785;
RA Koc E.C., Blackburn K., Burkhart W., Spremulli L.L.;
RT "Identification of a mammalian mitochondrial homolog of ribosomal protein
RT S7.";
RL Biochem. Biophys. Res. Commun. 266:141-146(1999).
RN [7]
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 [8]
RP IDENTIFICATION.
RX PubMed=11402041; DOI=10.1074/jbc.m103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-228, AND
RP IDENTIFICATION BY MASS 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 [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 FUNCTION, INVOLVEMENT IN COXPD34, VARIANT COXPD34 VAL-184, AND
RP CHARACTERIZATION OF VARIANT COXPD34 VAL-184.
RX PubMed=25556185; DOI=10.1093/hmg/ddu747;
RA Menezes M.J., Guo Y., Zhang J., Riley L.G., Cooper S.T., Thorburn D.R.,
RA Li J., Dong D., Li Z., Glessner J., Davis R.L., Sue C.M., Alexander S.I.,
RA Arbuckle S., Kirwan P., Keating B.J., Xu X., Hakonarson H.,
RA Christodoulou J.;
RT "Mutation in mitochondrial ribosomal protein S7 (MRPS7) causes congenital
RT sensorineural deafness, progressive hepatic and renal failure and lactic
RT acidemia.";
RL Hum. Mol. Genet. 24:2297-2307(2015).
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] {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), essential for mitochondrial protein synthesis (PubMed:25556185,
CC PubMed:25838379). Mature mammalian 55S mitochondrial ribosomes consist
CC of a small (28S) and a large (39S) subunit. The 28S small subunit
CC contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins.
CC The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of
CC mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an
CC integral structural role, and 52 different proteins (PubMed:25838379).
CC {ECO:0000269|PubMed:25556185, ECO:0000269|PubMed:25838379}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 34 (COXPD34)
CC [MIM:617872]: An autosomal recessive disorder caused by mitochondrial
CC dysfunction and combined respiratory chain deficiencies of complexes I,
CC III and IV. Clinical manifestations are variable and include congenital
CC sensorineural deafness, lactic acidemia, and progressive hepatic and
CC renal failure. {ECO:0000269|PubMed:25556185}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000305}.
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DR EMBL; AF077042; AAD27775.1; -; mRNA.
DR EMBL; AK222995; BAD96715.1; -; mRNA.
DR EMBL; AK313854; BAG36582.1; -; mRNA.
DR EMBL; AC022211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000241; AAH00241.1; -; mRNA.
DR CCDS; CCDS11718.1; -.
DR PIR; JC7165; JC7165.
DR RefSeq; NP_057055.2; NM_015971.3.
DR PDB; 3J9M; EM; 3.50 A; AF=1-242.
DR PDB; 6NU2; EM; 3.90 A; AF=35-242.
DR PDB; 6NU3; EM; 4.40 A; AF=1-242.
DR PDB; 6RW4; EM; 2.97 A; F=1-242.
DR PDB; 6RW5; EM; 3.14 A; F=1-242.
DR PDB; 6VLZ; EM; 2.97 A; AF=1-242.
DR PDB; 6VMI; EM; 2.96 A; AF=1-242.
DR PDB; 6ZM5; EM; 2.89 A; AF=1-242.
DR PDB; 6ZM6; EM; 2.59 A; AF=1-242.
DR PDB; 6ZS9; EM; 4.00 A; AF=1-242.
DR PDB; 6ZSA; EM; 4.00 A; AF=1-242.
DR PDB; 6ZSB; EM; 4.50 A; AF=1-242.
DR PDB; 6ZSC; EM; 3.50 A; AF=1-242.
DR PDB; 6ZSD; EM; 3.70 A; AF=1-242.
DR PDB; 6ZSE; EM; 5.00 A; AF=1-242.
DR PDB; 6ZSG; EM; 4.00 A; AF=1-242.
DR PDB; 7A5F; EM; 4.40 A; F6=1-242.
DR PDB; 7A5G; EM; 4.33 A; F6=1-242.
DR PDB; 7A5I; EM; 3.70 A; F6=1-242.
DR PDB; 7A5K; EM; 3.70 A; F6=1-242.
DR PDB; 7L08; EM; 3.49 A; AF=1-242.
DR PDB; 7OG4; EM; 3.80 A; AF=1-242.
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; Q9Y2R9; -.
DR SMR; Q9Y2R9; -.
DR BioGRID; 119271; 344.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q9Y2R9; -.
DR IntAct; Q9Y2R9; 89.
DR MINT; Q9Y2R9; -.
DR STRING; 9606.ENSP00000245539; -.
DR ChEMBL; CHEMBL4295986; -.
DR GlyGen; Q9Y2R9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2R9; -.
DR MetOSite; Q9Y2R9; -.
DR PhosphoSitePlus; Q9Y2R9; -.
DR SwissPalm; Q9Y2R9; -.
DR BioMuta; MRPS7; -.
DR DMDM; 296452884; -.
DR EPD; Q9Y2R9; -.
DR jPOST; Q9Y2R9; -.
DR MassIVE; Q9Y2R9; -.
DR MaxQB; Q9Y2R9; -.
DR PaxDb; Q9Y2R9; -.
DR PeptideAtlas; Q9Y2R9; -.
DR PRIDE; Q9Y2R9; -.
DR ProteomicsDB; 85881; -.
DR TopDownProteomics; Q9Y2R9; -.
DR Antibodypedia; 19534; 136 antibodies from 20 providers.
DR DNASU; 51081; -.
DR Ensembl; ENST00000245539.11; ENSP00000245539.6; ENSG00000125445.11.
DR GeneID; 51081; -.
DR KEGG; hsa:51081; -.
DR MANE-Select; ENST00000245539.11; ENSP00000245539.6; NM_015971.4; NP_057055.2.
DR UCSC; uc002jnm.5; human.
DR CTD; 51081; -.
DR DisGeNET; 51081; -.
DR GeneCards; MRPS7; -.
DR HGNC; HGNC:14499; MRPS7.
DR HPA; ENSG00000125445; Low tissue specificity.
DR MalaCards; MRPS7; -.
DR MIM; 611974; gene.
DR MIM; 617872; phenotype.
DR neXtProt; NX_Q9Y2R9; -.
DR OpenTargets; ENSG00000125445; -.
DR Orphanet; 457223; Syndromic sensorineural deafness due to combined oxidative phosphorylation defect.
DR PharmGKB; PA31026; -.
DR VEuPathDB; HostDB:ENSG00000125445; -.
DR eggNOG; KOG3291; Eukaryota.
DR GeneTree; ENSGT00390000014620; -.
DR HOGENOM; CLU_072226_0_1_1; -.
DR InParanoid; Q9Y2R9; -.
DR OMA; PWTPRVF; -.
DR OrthoDB; 1212658at2759; -.
DR PhylomeDB; Q9Y2R9; -.
DR TreeFam; TF105978; -.
DR PathwayCommons; Q9Y2R9; -.
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; Q9Y2R9; -.
DR SIGNOR; Q9Y2R9; -.
DR BioGRID-ORCS; 51081; 327 hits in 1085 CRISPR screens.
DR ChiTaRS; MRPS7; human.
DR GeneWiki; MRPS7; -.
DR GenomeRNAi; 51081; -.
DR Pharos; Q9Y2R9; Tbio.
DR PRO; PR:Q9Y2R9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y2R9; protein.
DR Bgee; ENSG00000125445; Expressed in gastrocnemius and 200 other tissues.
DR ExpressionAtlas; Q9Y2R9; baseline and differential.
DR Genevisible; Q9Y2R9; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 1.10.455.10; -; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Mitochondrion;
KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..242
FT /note="28S ribosomal protein S7, mitochondrial"
FT /id="PRO_0000273056"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 2
FT /note="A -> V (in dbSNP:rs8075276)"
FT /evidence="ECO:0000269|PubMed:11042152,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_030076"
FT VARIANT 184
FT /note="M -> V (in COXPD34; results in decreased
FT mitochondrial protein synthesis and reduced levels of
FT respiratory complexes; MRPS7 mRNA and protein levels are
FT reduced; dbSNP:rs115047866)"
FT /evidence="ECO:0000269|PubMed:25556185"
FT /id="VAR_080411"
FT CONFLICT 223
FT /note="K -> S (in Ref. 3; BAD96715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 242 AA; 28134 MW; 945BC3E948B41CCA CRC64;
MAAPAVKVAR GWSGLALGVR RAVLQLPGLT QVRWSRYSPE FKDPLIDKEY YRKPVEELTE
EEKYVRELKK TQLIKAAPAG KTSSVFEDPV ISKFTNMMMI GGNKVLARSL MIQTLEAVKR
KQFEKYHAAS AEEQATIERN PYTIFHQALK NCEPMIGLVP ILKGGRFYQV PVPLPDRRRR
FLAMKWMITE CRDKKHQRTL MPEKLSHKLL EAFHNQGPVI KRKHDLHKMA EANRALAHYR
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