ID RT15_HUMAN Reviewed; 257 AA.
AC P82914; B2RD82; Q9H2K1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Small ribosomal subunit protein uS15m {ECO:0000303|PubMed:25838379};
DE AltName: Full=28S ribosomal protein S15, mitochondrial;
DE Short=MRP-S15;
DE Short=S15mt;
DE Flags: Precursor;
GN Name=MRPS15; Synonyms=RPMS15; ORFNames=DC37;
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 [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RT "Novel genes expressed in human dendritic cell.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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=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 [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=27184847; DOI=10.1016/j.celrep.2016.04.064;
RA Lee S.Y., Kang M.G., Park J.S., Lee G., Ting A.Y., Rhee H.W.;
RT "APEX Fingerprinting Reveals the Subcellular Localization of Proteins of
RT Interest.";
RL Cell Rep. 15:1837-1847(2016).
RN [10] {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). 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 (PubMed:25838379). Interacts with
CC METTL17 (By similarity). {ECO:0000250|UniProtKB:Q9DC71,
CC ECO:0000269|PubMed:25838379}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:27184847}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG44697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB049946; BAB40999.1; -; mRNA.
DR EMBL; AF265439; AAG44697.1; ALT_INIT; mRNA.
DR EMBL; AK315441; BAG37829.1; -; mRNA.
DR EMBL; CH471059; EAX07359.1; -; Genomic_DNA.
DR EMBL; BC031336; AAH31336.1; -; mRNA.
DR CCDS; CCDS411.1; -.
DR RefSeq; NP_112570.2; NM_031280.3.
DR PDB; 3J9M; EM; 3.50 A; AL=1-257.
DR PDB; 6NU2; EM; 3.90 A; AL=66-229.
DR PDB; 6NU3; EM; 4.40 A; AL=1-257.
DR PDB; 6RW4; EM; 2.97 A; L=1-257.
DR PDB; 6RW5; EM; 3.14 A; L=1-257.
DR PDB; 6VLZ; EM; 2.97 A; AL=1-257.
DR PDB; 6VMI; EM; 2.96 A; AL=1-257.
DR PDB; 6ZM5; EM; 2.89 A; AL=1-257.
DR PDB; 6ZM6; EM; 2.59 A; AL=1-257.
DR PDB; 6ZS9; EM; 4.00 A; AL=1-257.
DR PDB; 6ZSA; EM; 4.00 A; AL=1-257.
DR PDB; 6ZSB; EM; 4.50 A; AL=1-257.
DR PDB; 6ZSC; EM; 3.50 A; AL=1-257.
DR PDB; 6ZSD; EM; 3.70 A; AL=1-257.
DR PDB; 6ZSE; EM; 5.00 A; AL=1-257.
DR PDB; 6ZSG; EM; 4.00 A; AL=1-257.
DR PDB; 7A5F; EM; 4.40 A; L6=1-257.
DR PDB; 7A5G; EM; 4.33 A; L6=1-257.
DR PDB; 7A5I; EM; 3.70 A; L6=1-257.
DR PDB; 7A5K; EM; 3.70 A; L6=1-257.
DR PDB; 7L08; EM; 3.49 A; AL=1-257.
DR PDB; 7OG4; EM; 3.80 A; AL=1-257.
DR PDB; 7P2E; EM; 2.40 A; L=1-257.
DR PDB; 7PNX; EM; 2.76 A; L=1-257.
DR PDB; 7PNY; EM; 3.06 A; L=1-257.
DR PDB; 7PNZ; EM; 3.09 A; L=1-257.
DR PDB; 7PO0; EM; 2.90 A; L=1-257.
DR PDB; 7PO1; EM; 2.92 A; L=1-257.
DR PDB; 7PO2; EM; 3.09 A; L=1-257.
DR PDB; 7PO3; EM; 2.92 A; L=1-257.
DR PDB; 7QI4; EM; 2.21 A; AL=1-257.
DR PDB; 7QI5; EM; 2.63 A; AL=1-257.
DR PDB; 7QI6; EM; 2.98 A; AL=1-257.
DR PDB; 8ANY; EM; 2.85 A; AL=1-257.
DR PDB; 8CSP; EM; 2.66 A; L=1-257.
DR PDB; 8CSQ; EM; 2.54 A; L=1-257.
DR PDB; 8CSR; EM; 2.54 A; L=1-257.
DR PDB; 8CSS; EM; 2.36 A; L=1-257.
DR PDB; 8CST; EM; 2.85 A; L=1-257.
DR PDB; 8CSU; EM; 3.03 A; L=1-257.
DR PDB; 8OIR; EM; 3.10 A; AL=1-257.
DR PDB; 8OIS; EM; 3.00 A; AL=1-257.
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; P82914; -.
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; P82914; -.
DR BioGRID; 122358; 160.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P82914; -.
DR IntAct; P82914; 84.
DR MINT; P82914; -.
DR STRING; 9606.ENSP00000362208; -.
DR GlyGen; P82914; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P82914; -.
DR PhosphoSitePlus; P82914; -.
DR BioMuta; MRPS15; -.
DR DMDM; 13633907; -.
DR EPD; P82914; -.
DR jPOST; P82914; -.
DR MassIVE; P82914; -.
DR MaxQB; P82914; -.
DR PaxDb; 9606-ENSP00000362208; -.
DR PeptideAtlas; P82914; -.
DR ProteomicsDB; 57720; -.
DR Pumba; P82914; -.
DR TopDownProteomics; P82914; -.
DR Antibodypedia; 31697; 216 antibodies from 27 providers.
DR DNASU; 64960; -.
DR Ensembl; ENST00000373116.6; ENSP00000362208.5; ENSG00000116898.12.
DR GeneID; 64960; -.
DR KEGG; hsa:64960; -.
DR MANE-Select; ENST00000373116.6; ENSP00000362208.5; NM_031280.4; NP_112570.2.
DR UCSC; uc001cas.3; human.
DR AGR; HGNC:14504; -.
DR CTD; 64960; -.
DR GeneCards; MRPS15; -.
DR HGNC; HGNC:14504; MRPS15.
DR HPA; ENSG00000116898; Tissue enhanced (skeletal).
DR MIM; 611979; gene.
DR neXtProt; NX_P82914; -.
DR OpenTargets; ENSG00000116898; -.
DR PharmGKB; PA30999; -.
DR VEuPathDB; HostDB:ENSG00000116898; -.
DR eggNOG; KOG2815; Eukaryota.
DR GeneTree; ENSGT00390000001737; -.
DR HOGENOM; CLU_094627_0_0_1; -.
DR InParanoid; P82914; -.
DR OMA; FMKKIVA; -.
DR OrthoDB; 5357773at2759; -.
DR PhylomeDB; P82914; -.
DR TreeFam; TF319038; -.
DR PathwayCommons; P82914; -.
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; P82914; -.
DR SIGNOR; P82914; -.
DR BioGRID-ORCS; 64960; 101 hits in 1160 CRISPR screens.
DR ChiTaRS; MRPS15; human.
DR GenomeRNAi; 64960; -.
DR Pharos; P82914; Tdark.
DR PRO; PR:P82914; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P82914; Protein.
DR Bgee; ENSG00000116898; Expressed in biceps brachii and 203 other cell types or tissues.
DR Genevisible; P82914; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR HAMAP; MF_01343_B; Ribosomal_uS15_B; 1.
DR InterPro; IPR000589; Ribosomal_uS15.
DR InterPro; IPR005290; Ribosomal_uS15_bac-type.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR PANTHER; PTHR46685; 28S RIBOSOMAL PROTEIN S15, MITOCHONDRIAL; 1.
DR PANTHER; PTHR46685:SF1; 28S RIBOSOMAL PROTEIN S15, MITOCHONDRIAL; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SMART; SM01387; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 58..257
FT /note="Small ribosomal subunit protein uS15m"
FT /id="PRO_0000030614"
FT REGION 225..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 27..79
FT /note="GGGSAKFPFNQWGLQPRSLLLQAARGYVVRKPAQSRLDDDPPPSTLLKDYQN
FT V -> AVGAPSFLSTSGACSLEVSSSRPRADMSSGNQPSLGWMMTHLLLRCSKTTRMS
FT (in Ref. 2; AAG44697)"
FT /evidence="ECO:0000305"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:8CSS"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 125..145
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 150..173
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:8CSS"
FT HELIX 201..224
FT /evidence="ECO:0007829|PDB:8CSS"
SQ SEQUENCE 257 AA; 29842 MW; B2D951BC47B8FFEB CRC64;
MLRVAWRTLS LIRTRAVTQV LVPGLPGGGS AKFPFNQWGL QPRSLLLQAA RGYVVRKPAQ
SRLDDDPPPS TLLKDYQNVP GIEKVDDVVK RLLSLEMANK KEMLKIKQEQ FMKKIVANPE
DTRSLEARII ALSVKIRSYE EHLEKHRKDK AHKRYLLMSI DQRKKMLKNL RNTNYDVFEK
ICWGLGIEYT FPPLYYRRAH RRFVTKKALC IRVFQETQKL KKRRRALKAA AAAQKQAKRR
NPDSPAKAIP KTLKDSQ
//
