RM10_HUMAN
ID RM10_HUMAN Reviewed; 261 AA.
AC Q7Z7H8; A6NGJ4; Q96B80; Q96Q55;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=39S ribosomal protein L10, mitochondrial;
DE Short=L10mt;
DE Short=MRP-L10;
DE AltName: Full=39S ribosomal protein L8, mitochondrial;
DE Short=L8mt;
DE Short=MRP-L8;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL10m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL10; Synonyms=MRPL8, RPML8;
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] (ISOFORM 2).
RC TISSUE=Caudate nucleus;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-125.
RC TISSUE=Pancreas, and 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-261.
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=11551941; DOI=10.1074/jbc.m106510200;
RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA Moseley A., Spremulli L.L.;
RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:43958-43969(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] {ECO:0007744|PDB:3J7Y}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25278503; DOI=10.1126/science.1258026;
RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA Scheres S.H., Ramakrishnan V.;
RT "Structure of the large ribosomal subunit from human mitochondria.";
RL Science 346:718-722(2014).
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).
RN [11] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
RN [12]
RP VARIANT TRP-166.
RX PubMed=26443249;
RA Jazayeri R., Hu H., Fattahi Z., Musante L., Abedini S.S., Hosseini M.,
RA Wienker T.F., Ropers H.H., Najmabadi H., Kahrizi K.;
RT "Exome Sequencing and Linkage Analysis Identified Novel Candidate Genes in
RT Recessive Intellectual Disability Associated with Ataxia.";
RL Arch. Iran. Med. 18:670-682(2015).
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature
CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a
CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA
CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains
CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA
CC (mt-tRNA(Val)), which plays an integral structural role, and 52
CC different proteins. uL10m contributes a single cysteine residue to a
CC zinc-binding site with mL66. {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042,
CC ECO:0000305|PubMed:11551941}.
CC -!- INTERACTION:
CC Q7Z7H8; P35609: ACTN2; NbExp=3; IntAct=EBI-723524, EBI-77797;
CC Q7Z7H8; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-723524, EBI-10175124;
CC Q7Z7H8; Q53G59: KLHL12; NbExp=3; IntAct=EBI-723524, EBI-740929;
CC Q7Z7H8; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-723524, EBI-302345;
CC Q7Z7H8; Q04864: REL; NbExp=3; IntAct=EBI-723524, EBI-307352;
CC Q7Z7H8; P15884: TCF4; NbExp=3; IntAct=EBI-723524, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z7H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z7H8-2; Sequence=VSP_044481;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; AK127167; BAG54446.1; -; mRNA.
DR EMBL; AC003665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94796.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94798.1; -; Genomic_DNA.
DR EMBL; BC015904; AAH15904.1; -; mRNA.
DR EMBL; BC052601; AAH52601.1; -; mRNA.
DR EMBL; AB051618; BAB54946.1; -; Genomic_DNA.
DR CCDS; CCDS11516.1; -. [Q7Z7H8-1]
DR CCDS; CCDS11517.1; -. [Q7Z7H8-2]
DR RefSeq; NP_660298.2; NM_145255.3. [Q7Z7H8-1]
DR RefSeq; NP_683685.1; NM_148887.2. [Q7Z7H8-2]
DR PDB; 3J7Y; EM; 3.40 A; I=1-261.
DR PDB; 3J9M; EM; 3.50 A; I=1-261.
DR PDB; 5OOL; EM; 3.06 A; I=1-261.
DR PDB; 5OOM; EM; 3.03 A; I=1-261.
DR PDB; 6I9R; EM; 3.90 A; I=1-261.
DR PDB; 6NU2; EM; 3.90 A; I=30-197.
DR PDB; 6NU3; EM; 4.40 A; I=1-261.
DR PDB; 6VLZ; EM; 2.97 A; I=1-261.
DR PDB; 6VMI; EM; 2.96 A; I=1-261.
DR PDB; 6ZM5; EM; 2.89 A; I=1-261.
DR PDB; 6ZM6; EM; 2.59 A; I=1-261.
DR PDB; 6ZS9; EM; 4.00 A; XI=1-261.
DR PDB; 6ZSA; EM; 4.00 A; XI=1-261.
DR PDB; 6ZSB; EM; 4.50 A; XI=1-261.
DR PDB; 6ZSC; EM; 3.50 A; XI=1-261.
DR PDB; 6ZSD; EM; 3.70 A; XI=1-261.
DR PDB; 6ZSE; EM; 5.00 A; XI=1-261.
DR PDB; 6ZSG; EM; 4.00 A; XI=1-261.
DR PDB; 7A5F; EM; 4.40 A; I3=1-261.
DR PDB; 7A5G; EM; 4.33 A; I3=1-261.
DR PDB; 7A5H; EM; 3.30 A; I=1-261.
DR PDB; 7A5I; EM; 3.70 A; I3=1-261.
DR PDB; 7A5J; EM; 3.10 A; I=1-261.
DR PDB; 7A5K; EM; 3.70 A; I3=1-261.
DR PDB; 7L08; EM; 3.49 A; I=1-261.
DR PDB; 7L20; EM; 3.15 A; I=1-261.
DR PDB; 7O9K; EM; 3.10 A; I=1-261.
DR PDB; 7O9M; EM; 2.50 A; I=1-261.
DR PDB; 7ODR; EM; 2.90 A; I=1-261.
DR PDB; 7ODS; EM; 3.10 A; I=1-261.
DR PDB; 7ODT; EM; 3.10 A; I=1-261.
DR PDB; 7OF0; EM; 2.20 A; I=1-261.
DR PDB; 7OF2; EM; 2.70 A; I=1-261.
DR PDB; 7OF3; EM; 2.70 A; I=1-261.
DR PDB; 7OF4; EM; 2.70 A; I=1-261.
DR PDB; 7OF5; EM; 2.90 A; I=1-261.
DR PDB; 7OF6; EM; 2.60 A; I=1-261.
DR PDB; 7OF7; EM; 2.50 A; I=1-261.
DR PDB; 7OG4; EM; 3.80 A; XI=1-261.
DR PDB; 7OI6; EM; 5.70 A; I=1-261.
DR PDB; 7OI7; EM; 3.50 A; I=1-261.
DR PDB; 7OI8; EM; 3.50 A; I=1-261.
DR PDB; 7OI9; EM; 3.30 A; I=1-261.
DR PDB; 7OIA; EM; 3.20 A; I=1-261.
DR PDB; 7OIB; EM; 3.30 A; I=1-261.
DR PDB; 7OIC; EM; 3.10 A; I=1-261.
DR PDB; 7OID; EM; 3.70 A; I=1-261.
DR PDB; 7OIE; EM; 3.50 A; I=1-261.
DR PDB; 7PD3; EM; 3.40 A; G=1-261.
DR PDBsum; 3J7Y; -.
DR PDBsum; 3J9M; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6I9R; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
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; 7A5H; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF6; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OG4; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIA; -.
DR PDBsum; 7OIB; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR AlphaFoldDB; Q7Z7H8; -.
DR SMR; Q7Z7H8; -.
DR BioGRID; 125910; 179.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q7Z7H8; -.
DR DIP; DIP-59717N; -.
DR IntAct; Q7Z7H8; 83.
DR MINT; Q7Z7H8; -.
DR STRING; 9606.ENSP00000290208; -.
DR iPTMnet; Q7Z7H8; -.
DR PhosphoSitePlus; Q7Z7H8; -.
DR SwissPalm; Q7Z7H8; -.
DR BioMuta; MRPL10; -.
DR DMDM; 215274216; -.
DR EPD; Q7Z7H8; -.
DR jPOST; Q7Z7H8; -.
DR MassIVE; Q7Z7H8; -.
DR MaxQB; Q7Z7H8; -.
DR PaxDb; Q7Z7H8; -.
DR PeptideAtlas; Q7Z7H8; -.
DR PRIDE; Q7Z7H8; -.
DR ProteomicsDB; 1131; -.
DR ProteomicsDB; 69551; -. [Q7Z7H8-1]
DR Antibodypedia; 17772; 177 antibodies from 25 providers.
DR DNASU; 124995; -.
DR Ensembl; ENST00000290208.11; ENSP00000290208.7; ENSG00000159111.13. [Q7Z7H8-2]
DR Ensembl; ENST00000351111.7; ENSP00000324100.4; ENSG00000159111.13. [Q7Z7H8-1]
DR Ensembl; ENST00000414011.1; ENSP00000395870.1; ENSG00000159111.13. [Q7Z7H8-2]
DR GeneID; 124995; -.
DR KEGG; hsa:124995; -.
DR MANE-Select; ENST00000351111.7; ENSP00000324100.4; NM_145255.4; NP_660298.2.
DR UCSC; uc002ily.4; human. [Q7Z7H8-1]
DR CTD; 124995; -.
DR GeneCards; MRPL10; -.
DR HGNC; HGNC:14055; MRPL10.
DR HPA; ENSG00000159111; Low tissue specificity.
DR MIM; 611825; gene.
DR neXtProt; NX_Q7Z7H8; -.
DR OpenTargets; ENSG00000159111; -.
DR PharmGKB; PA30939; -.
DR VEuPathDB; HostDB:ENSG00000159111; -.
DR eggNOG; KOG4241; Eukaryota.
DR GeneTree; ENSGT00390000000603; -.
DR HOGENOM; CLU_073093_0_0_1; -.
DR InParanoid; Q7Z7H8; -.
DR OMA; RENRMIA; -.
DR OrthoDB; 1484426at2759; -.
DR PhylomeDB; Q7Z7H8; -.
DR TreeFam; TF321349; -.
DR PathwayCommons; Q7Z7H8; -.
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; Q7Z7H8; -.
DR SIGNOR; Q7Z7H8; -.
DR BioGRID-ORCS; 124995; 580 hits in 1090 CRISPR screens.
DR ChiTaRS; MRPL10; human.
DR GeneWiki; MRPL10; -.
DR GenomeRNAi; 124995; -.
DR Pharos; Q7Z7H8; Tbio.
DR PRO; PR:Q7Z7H8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q7Z7H8; protein.
DR Bgee; ENSG00000159111; Expressed in apex of heart and 182 other tissues.
DR ExpressionAtlas; Q7Z7H8; baseline and differential.
DR Genevisible; Q7Z7H8; HS.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
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; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; ISS:UniProtKB.
DR CDD; cd05797; Ribosomal_L10; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR PANTHER; PTHR11560; PTHR11560; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 29..261
FT /note="39S ribosomal protein L10, mitochondrial"
FT /id="PRO_0000273075"
FT REGION 242..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..17
FT /note="MAAAVAGMLRGGLLPQA -> MISAHCNLHLPGSSDSPASASQVAGIT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044481"
FT VARIANT 125
FT /note="V -> I (in dbSNP:rs11538868)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030078"
FT VARIANT 166
FT /note="R -> W (found in a patient with intellectual
FT disability and ataxia; unknown pathological significance;
FT dbSNP:rs754258802)"
FT /evidence="ECO:0000269|PubMed:26443249"
FT /id="VAR_083398"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:7OIA"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3J7Y"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5OOM"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 261 AA; 29283 MW; CB4C2EBA74A29098 CRC64;
MAAAVAGMLR GGLLPQAGRL PTLQTVRYGS KAVTRHRRVM HFQRQKLMAV TEYIPPKPAI
HPSCLPSPPS PPQEEIGLIR LLRREIAAVF QDNRMIAVCQ NVALSAEDKL LMRHQLRKHK
ILMKVFPNQV LKPFLEDSKY QNLLPLFVGH NMLLVSEEPK VKEMVRILRT VPFLPLLGGC
IDDTILSRQG FINYSKLPSL PLVQGELVGG LTCLTAQTHS LLQHQPLQLT TLLDQYIREQ
REKDSVMSAN GKPDPDTVPD S
