RM39_HUMAN
ID RM39_HUMAN Reviewed; 338 AA.
AC Q9NYK5; C9JYA5; Q32Q74; Q5QTR3; Q96Q65; Q9BSQ7; Q9BZV6; Q9NX44;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=39S ribosomal protein L39, mitochondrial;
DE Short=L39mt;
DE Short=MRP-L39;
DE AltName: Full=39S ribosomal protein L5, mitochondrial;
DE Short=L5mt;
DE Short=MRP-L5;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL39 {ECO:0000303|PubMed:25278503};
GN Name=MRPL39; Synonyms=C21orf92, MRPL5, RPML5; ORFNames=MSTP003, PRED22;
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] (ISOFORM 1), AND VARIANT PRO-31.
RA Choi D.K., Taylor T.D., Hattori M., Sakaki Y.;
RT "Construction of a transcript map in the LL56-APP region of chromosome
RT 21q21.1-21.2.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-31.
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 GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-31.
RC TISSUE=Muscle;
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 [MRNA] OF 5-338 (ISOFORM 1), AND VARIANT PRO-31.
RC TISSUE=Heart;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., Liu S.,
RA Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-338 (ISOFORM 2).
RC TISSUE=Heart;
RX PubMed=11167009; DOI=10.1016/s0378-1119(00)00504-7;
RA Spirina O., Bykhovskaya Y., Kajava A.V., O'Brien T.W., Nierlich D.P.,
RA Mougey E.B., Sylvester J.E., Graack H.-R., Wittmann-Liebold B.,
RA Fischel-Ghodsian N.;
RT "Heart-specific splice-variant of a human mitochondrial ribosomal protein
RT (mRNA processing; tissue specific splicing).";
RL Gene 261:229-234(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-183.
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 [8]
RP IDENTIFICATION.
RX PubMed=10593885; DOI=10.1074/jbc.274.51.36043;
RA O'Brien T.W., Fiesler S.E., Denslow N.D., Thiede B., Wittmann-Liebold B.,
RA Mougey E.B., Sylvester J.E., Graack H.R.;
RT "Mammalian mitochondrial ribosomal proteins (2). Amino acid sequencing,
RT characterization, and identification of corresponding gene sequences.";
RL J. Biol. Chem. 274:36043-36051(1999).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND IDENTIFICATION BY MASS
RP 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 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 [12] {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 [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).
RN [14] {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: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=Q9NYK5-1; Sequence=Displayed;
CC Name=2; Synonyms=MRP-L5V1;
CC IsoId=Q9NYK5-2; Sequence=VSP_005718;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2 is
CC heart-specific.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL39 family. {ECO:0000305}.
CC -!- CAUTION: Ref.1 indicates C21orf8 as a synonym for this orf, this is
CC incorrect, C21orf8 is already assigned to another chromosome 21 region.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF44696.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ13505.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91177.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF239727; AAF44696.1; ALT_INIT; mRNA.
DR EMBL; AK000458; BAA91177.1; ALT_FRAME; mRNA.
DR EMBL; AP000223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004896; AAH04896.2; -; mRNA.
DR EMBL; BC107719; AAI07720.1; -; mRNA.
DR EMBL; AF109357; AAQ13505.1; ALT_INIT; mRNA.
DR EMBL; AF270511; AAK12856.1; -; mRNA.
DR EMBL; AB051346; BAB54936.1; -; Genomic_DNA.
DR CCDS; CCDS13573.1; -. [Q9NYK5-1]
DR CCDS; CCDS33522.1; -. [Q9NYK5-2]
DR RefSeq; NP_059142.2; NM_017446.3. [Q9NYK5-1]
DR RefSeq; NP_542984.2; NM_080794.3. [Q9NYK5-2]
DR RefSeq; XP_006724089.1; XM_006724026.3. [Q9NYK5-2]
DR PDB; 3J7Y; EM; 3.40 A; 7=1-338.
DR PDB; 3J9M; EM; 3.50 A; 7=1-338.
DR PDB; 5OOL; EM; 3.06 A; 7=1-338.
DR PDB; 5OOM; EM; 3.03 A; 7=1-338.
DR PDB; 6I9R; EM; 3.90 A; 7=1-338.
DR PDB; 6NU2; EM; 3.90 A; 7=36-322.
DR PDB; 6NU3; EM; 4.40 A; 7=1-338.
DR PDB; 6VLZ; EM; 2.97 A; 7=1-338.
DR PDB; 6VMI; EM; 2.96 A; 7=1-338.
DR PDB; 6ZM5; EM; 2.89 A; 7=1-338.
DR PDB; 6ZM6; EM; 2.59 A; 7=1-338.
DR PDB; 6ZS9; EM; 4.00 A; 7=1-338.
DR PDB; 6ZSA; EM; 4.00 A; 7=1-338.
DR PDB; 6ZSB; EM; 4.50 A; 7=1-338.
DR PDB; 6ZSC; EM; 3.50 A; 7=1-338.
DR PDB; 6ZSD; EM; 3.70 A; 7=1-338.
DR PDB; 6ZSE; EM; 5.00 A; 7=1-338.
DR PDB; 6ZSG; EM; 4.00 A; 7=1-338.
DR PDB; 7A5F; EM; 4.40 A; 73=1-338.
DR PDB; 7A5G; EM; 4.33 A; 73=1-338.
DR PDB; 7A5H; EM; 3.30 A; 7=1-338.
DR PDB; 7A5I; EM; 3.70 A; 73=1-338.
DR PDB; 7A5J; EM; 3.10 A; 7=1-338.
DR PDB; 7A5K; EM; 3.70 A; 73=1-338.
DR PDB; 7L08; EM; 3.49 A; 7=1-338.
DR PDB; 7L20; EM; 3.15 A; 7=1-338.
DR PDB; 7O9K; EM; 3.10 A; 7=1-338.
DR PDB; 7O9M; EM; 2.50 A; 7=1-338.
DR PDB; 7ODR; EM; 2.90 A; 7=1-338.
DR PDB; 7ODS; EM; 3.10 A; 7=1-338.
DR PDB; 7ODT; EM; 3.10 A; 7=1-338.
DR PDB; 7OF0; EM; 2.20 A; 7=1-338.
DR PDB; 7OF2; EM; 2.70 A; 7=1-338.
DR PDB; 7OF3; EM; 2.70 A; 7=1-338.
DR PDB; 7OF4; EM; 2.70 A; 7=1-338.
DR PDB; 7OF5; EM; 2.90 A; 7=1-338.
DR PDB; 7OF6; EM; 2.60 A; 7=1-338.
DR PDB; 7OF7; EM; 2.50 A; 7=1-338.
DR PDB; 7OG4; EM; 3.80 A; 7=1-338.
DR PDB; 7OI6; EM; 5.70 A; 7=1-338.
DR PDB; 7OI7; EM; 3.50 A; 7=1-338.
DR PDB; 7OI8; EM; 3.50 A; 7=1-338.
DR PDB; 7OI9; EM; 3.30 A; 7=1-338.
DR PDB; 7OIA; EM; 3.20 A; 7=1-338.
DR PDB; 7OIB; EM; 3.30 A; 7=1-338.
DR PDB; 7OIC; EM; 3.10 A; 7=1-338.
DR PDB; 7OID; EM; 3.70 A; 7=1-338.
DR PDB; 7OIE; EM; 3.50 A; 7=1-338.
DR PDB; 7PD3; EM; 3.40 A; 7=1-338.
DR PDB; 7QH6; EM; 3.08 A; 7=1-338.
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; Q9NYK5; -.
DR SMR; Q9NYK5; -.
DR BioGRID; 119918; 203.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9NYK5; -.
DR IntAct; Q9NYK5; 87.
DR MINT; Q9NYK5; -.
DR STRING; 9606.ENSP00000305682; -.
DR iPTMnet; Q9NYK5; -.
DR PhosphoSitePlus; Q9NYK5; -.
DR SwissPalm; Q9NYK5; -.
DR BioMuta; MRPL39; -.
DR DMDM; 296452977; -.
DR EPD; Q9NYK5; -.
DR jPOST; Q9NYK5; -.
DR MassIVE; Q9NYK5; -.
DR MaxQB; Q9NYK5; -.
DR PaxDb; Q9NYK5; -.
DR PeptideAtlas; Q9NYK5; -.
DR PRIDE; Q9NYK5; -.
DR ProteomicsDB; 83241; -. [Q9NYK5-1]
DR ProteomicsDB; 83242; -. [Q9NYK5-2]
DR Antibodypedia; 6007; 209 antibodies from 23 providers.
DR DNASU; 54148; -.
DR Ensembl; ENST00000307301.11; ENSP00000305682.7; ENSG00000154719.14. [Q9NYK5-2]
DR Ensembl; ENST00000352957.9; ENSP00000284967.7; ENSG00000154719.14. [Q9NYK5-1]
DR GeneID; 54148; -.
DR KEGG; hsa:54148; -.
DR MANE-Select; ENST00000352957.9; ENSP00000284967.7; NM_017446.4; NP_059142.3.
DR UCSC; uc002yln.4; human. [Q9NYK5-1]
DR CTD; 54148; -.
DR DisGeNET; 54148; -.
DR GeneCards; MRPL39; -.
DR HGNC; HGNC:14027; MRPL39.
DR HPA; ENSG00000154719; Low tissue specificity.
DR MIM; 611845; gene.
DR neXtProt; NX_Q9NYK5; -.
DR OpenTargets; ENSG00000154719; -.
DR PharmGKB; PA30970; -.
DR VEuPathDB; HostDB:ENSG00000154719; -.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000156271; -.
DR InParanoid; Q9NYK5; -.
DR OMA; HLKAHHT; -.
DR OrthoDB; 1202682at2759; -.
DR PhylomeDB; Q9NYK5; -.
DR TreeFam; TF300858; -.
DR PathwayCommons; Q9NYK5; -.
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; Q9NYK5; -.
DR SIGNOR; Q9NYK5; -.
DR BioGRID-ORCS; 54148; 465 hits in 1089 CRISPR screens.
DR ChiTaRS; MRPL39; human.
DR GeneWiki; MRPL39; -.
DR GenomeRNAi; 54148; -.
DR Pharos; Q9NYK5; Tbio.
DR PRO; PR:Q9NYK5; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9NYK5; protein.
DR Bgee; ENSG00000154719; Expressed in adrenal tissue and 190 other tissues.
DR ExpressionAtlas; Q9NYK5; baseline and differential.
DR Genevisible; Q9NYK5; 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:0005761; C:mitochondrial ribosome; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..338
FT /note="39S ribosomal protein L39, mitochondrial"
FT /id="PRO_0000087684"
FT DOMAIN 63..129
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 324..338
FT /note="VTEDQSKATEECTST -> TPFPILLLFTTQSFFTTSPESYLLHGTVSE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11167009"
FT /id="VSP_005718"
FT VARIANT 31
FT /note="S -> P (in dbSNP:rs3989369)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.5"
FT /id="VAR_052041"
FT CONFLICT 140
FT /note="K -> E (in Ref. 1; AAF44696 and 2; BAA91177)"
FT /evidence="ECO:0000305"
FT HELIX 37..58
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5OOM"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 247..259
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 275..285
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 338 AA; 38712 MW; BB0139678F72B63D CRC64;
MEALAMGSRA LRLWLVAPGG GIKWRFIATS SASQLSPTEL TEMRNDLFNK EKARQLSLTP
RTEKIEVKHV GKTDPGTVFV MNKNISTPYS CAMHLSEWYC RKSILALVDG QPWDMYKPLT
KSCEIKFLTF KDCDPGEVNK AYWRSCAMMM GCVIERAFKD EYMVNLVRAP EVPVISGAFC
YDVVLDSKLD EWMPTKENLR SFTKDAHALI YKDLPFETLE VEAKVALEIF QHSKYKVDFI
EEKASQNPER IVKLHRIGDF IDVSEGPLIP RTSICFQYEV SAVHNLQPTQ PSLIRRFQGV
SLPVHLRAHF TIWDKLLERS RKMVTEDQSK ATEECTST
