RM42_HUMAN
ID RM42_HUMAN Reviewed; 142 AA.
AC Q9Y6G3; Q6FID1; Q96Q48; Q9P0S1;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=39S ribosomal protein L42, mitochondrial {ECO:0000303|PubMed:11551941};
DE Short=L42mt;
DE Short=MRP-L42;
DE AltName: Full=39S ribosomal protein L31, mitochondrial {ECO:0000250|UniProtKB:P0C2B9};
DE Short=L31mt;
DE Short=MRP-L31;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL42 {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL42; Synonyms=MRPL31, MRPS32, RPML31; ORFNames=HSPC204, PTD007;
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 {ECO:0000312|EMBL:BAA91054.1};
RN [1] {ECO:0000312|EMBL:BAA91054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary tumor;
RA Mao Y.F., Peng Y., Dai M., Huang Q.H., Song H., Zhang Q.H., Mao M., Fu G.,
RA Luo M., Chen J.H., Hu R.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAA91054.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen J.H., Luo W.Q., Hu S.N., Li G.T., Jin J., Huang X.W., Zhou H.J.,
RA Yuan J.G., Qiang B.Q.;
RT "Isolating a new human cDNA.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4] {ECO:0000312|EMBL:CAB66594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6] {ECO:0000312|EMBL:BAA91054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:BAA91054.1}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-128.
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 [10] {ECO:0000305}
RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOME SMALL SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [11]
RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOME LARGE SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [12]
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 [13]
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 [14] {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 [15] {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 [16] {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).
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. {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279123,
CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL42 family. {ECO:0000305}.
CC -!- CAUTION: Has also been found in a preparation of mitochondrial small
CC ribosomal subunits. Was erroneously (PubMed:11279123, PubMed:11551941)
CC assigned to be MRP-S32. {ECO:0000305|PubMed:11279123,
CC ECO:0000305|PubMed:11551941}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36124.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF078860; AAD44492.1; -; mRNA.
DR EMBL; AF135160; AAF43784.1; -; mRNA.
DR EMBL; AF151038; AAF36124.1; ALT_FRAME; mRNA.
DR EMBL; AL136659; CAB66594.1; -; mRNA.
DR EMBL; AK000285; BAA91054.1; -; mRNA.
DR EMBL; CR533495; CAG38526.1; -; mRNA.
DR EMBL; CH471054; EAW97484.1; -; Genomic_DNA.
DR EMBL; BC040240; AAH40240.1; -; mRNA.
DR EMBL; AB051626; BAB54953.1; -; Genomic_DNA.
DR CCDS; CCDS9045.1; -.
DR RefSeq; NP_054769.1; NM_014050.3.
DR RefSeq; NP_751917.1; NM_172177.3.
DR PDB; 3J7Y; EM; 3.40 A; a=1-142.
DR PDB; 3J9M; EM; 3.50 A; a=1-142.
DR PDB; 5OOL; EM; 3.06 A; a=1-142.
DR PDB; 5OOM; EM; 3.03 A; a=1-142.
DR PDB; 6I9R; EM; 3.90 A; a=1-142.
DR PDB; 6NU2; EM; 3.90 A; a=35-142.
DR PDB; 6NU3; EM; 4.40 A; a=1-142.
DR PDB; 6VLZ; EM; 2.97 A; a=1-142.
DR PDB; 6VMI; EM; 2.96 A; a=1-142.
DR PDB; 6ZM5; EM; 2.89 A; a=1-142.
DR PDB; 6ZM6; EM; 2.59 A; a=1-142.
DR PDB; 6ZS9; EM; 4.00 A; a=1-142.
DR PDB; 6ZSA; EM; 4.00 A; a=1-142.
DR PDB; 6ZSB; EM; 4.50 A; a=1-142.
DR PDB; 6ZSC; EM; 3.50 A; a=1-142.
DR PDB; 6ZSD; EM; 3.70 A; a=1-142.
DR PDB; 6ZSE; EM; 5.00 A; a=1-142.
DR PDB; 6ZSG; EM; 4.00 A; a=1-142.
DR PDB; 7A5F; EM; 4.40 A; a3=1-142.
DR PDB; 7A5G; EM; 4.33 A; a3=1-142.
DR PDB; 7A5H; EM; 3.30 A; a=1-142.
DR PDB; 7A5I; EM; 3.70 A; a3=1-142.
DR PDB; 7A5J; EM; 3.10 A; a=1-142.
DR PDB; 7A5K; EM; 3.70 A; a3=1-142.
DR PDB; 7L08; EM; 3.49 A; a=1-142.
DR PDB; 7L20; EM; 3.15 A; a=1-142.
DR PDB; 7O9K; EM; 3.10 A; a=1-142.
DR PDB; 7O9M; EM; 2.50 A; a=1-142.
DR PDB; 7ODR; EM; 2.90 A; a=1-142.
DR PDB; 7ODS; EM; 3.10 A; a=1-142.
DR PDB; 7ODT; EM; 3.10 A; a=1-142.
DR PDB; 7OF0; EM; 2.20 A; a=1-142.
DR PDB; 7OF2; EM; 2.70 A; a=1-142.
DR PDB; 7OF3; EM; 2.70 A; a=1-142.
DR PDB; 7OF4; EM; 2.70 A; a=1-142.
DR PDB; 7OF5; EM; 2.90 A; a=1-142.
DR PDB; 7OF6; EM; 2.60 A; a=1-142.
DR PDB; 7OF7; EM; 2.50 A; a=1-142.
DR PDB; 7OG4; EM; 3.80 A; a=1-142.
DR PDB; 7OI6; EM; 5.70 A; a=1-142.
DR PDB; 7OI7; EM; 3.50 A; a=1-142.
DR PDB; 7OI8; EM; 3.50 A; a=1-142.
DR PDB; 7OI9; EM; 3.30 A; a=1-142.
DR PDB; 7OIA; EM; 3.20 A; a=1-142.
DR PDB; 7OIB; EM; 3.30 A; a=1-142.
DR PDB; 7OIC; EM; 3.10 A; a=1-142.
DR PDB; 7OID; EM; 3.70 A; a=1-142.
DR PDB; 7OIE; EM; 3.50 A; a=1-142.
DR PDB; 7PD3; EM; 3.40 A; a=1-142.
DR PDB; 7QH6; EM; 3.08 A; a=1-142.
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 PDBsum; 7QH6; -.
DR AlphaFoldDB; Q9Y6G3; -.
DR SMR; Q9Y6G3; -.
DR BioGRID; 118800; 258.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9Y6G3; -.
DR IntAct; Q9Y6G3; 62.
DR STRING; 9606.ENSP00000449884; -.
DR iPTMnet; Q9Y6G3; -.
DR PhosphoSitePlus; Q9Y6G3; -.
DR BioMuta; MRPL42; -.
DR DMDM; 24212391; -.
DR EPD; Q9Y6G3; -.
DR jPOST; Q9Y6G3; -.
DR MassIVE; Q9Y6G3; -.
DR MaxQB; Q9Y6G3; -.
DR PaxDb; Q9Y6G3; -.
DR PeptideAtlas; Q9Y6G3; -.
DR PRIDE; Q9Y6G3; -.
DR ProteomicsDB; 86675; -.
DR TopDownProteomics; Q9Y6G3; -.
DR Antibodypedia; 30057; 214 antibodies from 21 providers.
DR DNASU; 28977; -.
DR Ensembl; ENST00000549561.6; ENSP00000449392.1; ENSG00000198015.14.
DR Ensembl; ENST00000549982.6; ENSP00000449884.1; ENSG00000198015.14.
DR Ensembl; ENST00000552217.6; ENSP00000447547.1; ENSG00000198015.14.
DR GeneID; 28977; -.
DR KEGG; hsa:28977; -.
DR MANE-Select; ENST00000549982.6; ENSP00000449884.1; NM_014050.4; NP_054769.1.
DR UCSC; uc001tcr.4; human.
DR CTD; 28977; -.
DR DisGeNET; 28977; -.
DR GeneCards; MRPL42; -.
DR HGNC; HGNC:14493; MRPL42.
DR HPA; ENSG00000198015; Low tissue specificity.
DR MIM; 611847; gene.
DR neXtProt; NX_Q9Y6G3; -.
DR OpenTargets; ENSG00000198015; -.
DR PharmGKB; PA30974; -.
DR VEuPathDB; HostDB:ENSG00000198015; -.
DR eggNOG; KOG4106; Eukaryota.
DR GeneTree; ENSGT00390000010491; -.
DR InParanoid; Q9Y6G3; -.
DR OMA; MQLTHTT; -.
DR OrthoDB; 1604174at2759; -.
DR PhylomeDB; Q9Y6G3; -.
DR TreeFam; TF324368; -.
DR PathwayCommons; Q9Y6G3; -.
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; Q9Y6G3; -.
DR SIGNOR; Q9Y6G3; -.
DR BioGRID-ORCS; 28977; 138 hits in 1086 CRISPR screens.
DR ChiTaRS; MRPL42; human.
DR GeneWiki; Mitochondrial_ribosomal_protein_L42; -.
DR GenomeRNAi; 28977; -.
DR Pharos; Q9Y6G3; Tbio.
DR PRO; PR:Q9Y6G3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y6G3; protein.
DR Bgee; ENSG00000198015; Expressed in adrenal tissue and 205 other tissues.
DR ExpressionAtlas; Q9Y6G3; baseline and differential.
DR Genevisible; Q9Y6G3; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR InterPro; IPR019346; MRPL42.
DR PANTHER; PTHR13450; PTHR13450; 1.
DR Pfam; PF10210; MRP-S32; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P0C2B9"
FT CHAIN 33..142
FT /note="39S ribosomal protein L42, mitochondrial"
FT /id="PRO_0000087724"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 142 AA; 16661 MW; AED9ECFA653F870A CRC64;
MAVAAVKWVM SKRTILKHLF PVQNGALYCV CHKSTYSPLP DDYNCNVELA LTSDGRTIVC
YHPSVDIPYE HTKPIPRPDP VHNNEETHDQ VLKTRLEEKV EHLEEGPMIE QLSKMFFTTK
HRWYPHGRYH RCRKNLNPPK DR
