ID RT30_HUMAN Reviewed; 439 AA. AC Q9NP92; Q96I91; Q96Q19; Q9H0P8; Q9NSF9; Q9NZ76; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=Large ribosomal subunit protein mL65 {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein S30, mitochondrial; DE Short=MRP-S30; DE Short=S30mt; DE AltName: Full=Large ribosomal subunit protein mS30 {ECO:0000303|PubMed:27023846}; DE AltName: Full=Programmed cell death protein 9; GN Name=MRPS30; Synonyms=PDCD9; ORFNames=BM-047; 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:CAB90810.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT SER-33. RX PubMed=10640817; DOI=10.1159/000015397; RA Carim-Todd L., Sumoy L., Nadal M., Estivill X., Escarceller M.; RT "Cloning, expression, and mapping of PDCD9, the human homolog of Gallus RT gallus pro-apoptotic protein p52."; RL Cytogenet. Cell Genet. 87:85-88(1999). RN [2] {ECO:0000312|EMBL:CAB90810.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-33. RG The European IMAGE consortium; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-33. RC TISSUE=Kidney; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Teratocarcinoma; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-439. RC TISSUE=Bone marrow; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 275-284. 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] {ECO:0000305} 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 [9] 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 [10] 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 [11] RP NOMENCLATURE. RX PubMed=27023846; DOI=10.1146/annurev-biochem-060815-014343; RA Greber B.J., Ban N.; RT "Structure and function of the mitochondrial ribosome."; RL Annu. Rev. Biochem. 85:103-132(2016). RN [12] RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), 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] RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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. mL65 forms a heterodimer with mL37. CC {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279123, CC ECO:0000269|PubMed:28892042}. CC -!- TISSUE SPECIFICITY: Heart, skeletal muscle, kidney and liver. Lower CC expression in placenta and peripheral blood leukocytes. CC {ECO:0000269|PubMed:10640817, ECO:0000269|PubMed:11279123}. CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein CC mL65 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF67634.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF67634.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF146192; AAF65227.1; -; mRNA. DR EMBL; AL355715; CAB90810.1; -; mRNA. DR EMBL; AL355716; CAB90811.1; -; mRNA. DR EMBL; AL136706; CAB66641.1; -; mRNA. DR EMBL; AK074777; BAC11202.1; -; mRNA. DR EMBL; BC007735; AAH07735.1; -; mRNA. DR EMBL; AF217523; AAF67634.1; ALT_SEQ; mRNA. DR EMBL; AB061211; BAB54961.1; -; Genomic_DNA. DR CCDS; CCDS3951.1; -. DR RefSeq; NP_057724.2; NM_016640.3. DR PDB; 3J7Y; EM; 3.40 A; s=1-439. DR PDB; 3J9M; EM; 3.50 A; s=1-439. DR PDB; 5OOL; EM; 3.06 A; s=1-439. DR PDB; 5OOM; EM; 3.03 A; s=1-439. DR PDB; 6I9R; EM; 3.90 A; s=1-439. DR PDB; 6NU2; EM; 3.90 A; s=41-430. DR PDB; 6NU3; EM; 4.40 A; s=1-439. DR PDB; 6VLZ; EM; 2.97 A; s=1-439. DR PDB; 6VMI; EM; 2.96 A; s=1-439. DR PDB; 6ZM5; EM; 2.89 A; s=1-439. DR PDB; 6ZM6; EM; 2.59 A; s=1-439. DR PDB; 6ZS9; EM; 4.00 A; s=1-439. DR PDB; 6ZSA; EM; 4.00 A; s=1-439. DR PDB; 6ZSB; EM; 4.50 A; s=1-439. DR PDB; 6ZSC; EM; 3.50 A; s=1-439. DR PDB; 6ZSD; EM; 3.70 A; s=1-439. DR PDB; 6ZSE; EM; 5.00 A; s=1-439. DR PDB; 6ZSG; EM; 4.00 A; s=1-439. DR PDB; 7A5F; EM; 4.40 A; s3/t3=1-439. DR PDB; 7A5G; EM; 4.33 A; s3/t3=1-439. DR PDB; 7A5H; EM; 3.30 A; s=1-439. DR PDB; 7A5I; EM; 3.70 A; s3=1-439. DR PDB; 7A5J; EM; 3.10 A; s=1-439. DR PDB; 7A5K; EM; 3.70 A; s3=1-439. DR PDB; 7L08; EM; 3.49 A; s=1-439. DR PDB; 7L20; EM; 3.15 A; s=1-439. DR PDB; 7O9K; EM; 3.10 A; s=1-439. DR PDB; 7O9M; EM; 2.50 A; s=1-439. DR PDB; 7ODR; EM; 2.90 A; s=1-439. DR PDB; 7ODS; EM; 3.10 A; s=1-439. DR PDB; 7ODT; EM; 3.10 A; s=1-439. DR PDB; 7OF0; EM; 2.20 A; s=1-439. DR PDB; 7OF2; EM; 2.70 A; s=1-439. DR PDB; 7OF3; EM; 2.70 A; s=1-439. DR PDB; 7OF4; EM; 2.70 A; s=1-439. DR PDB; 7OF5; EM; 2.90 A; s=1-439. DR PDB; 7OF6; EM; 2.60 A; s=1-439. DR PDB; 7OF7; EM; 2.50 A; s=1-439. DR PDB; 7OG4; EM; 3.80 A; s=1-439. DR PDB; 7OI6; EM; 5.70 A; s=1-439. DR PDB; 7OI7; EM; 3.50 A; s=1-439. DR PDB; 7OI8; EM; 3.50 A; s=1-439. DR PDB; 7OI9; EM; 3.30 A; s=1-439. DR PDB; 7OIA; EM; 3.20 A; s=1-439. DR PDB; 7OIB; EM; 3.30 A; s=1-439. DR PDB; 7OIC; EM; 3.10 A; s=1-439. DR PDB; 7OID; EM; 3.70 A; s=1-439. DR PDB; 7OIE; EM; 3.50 A; s=1-439. DR PDB; 7PD3; EM; 3.40 A; s=1-439. DR PDB; 7PO4; EM; 2.56 A; s=1-439. DR PDB; 7QH6; EM; 3.08 A; s=1-439. DR PDB; 7QH7; EM; 2.89 A; s=41-430. DR PDB; 7QI4; EM; 2.21 A; s=1-439. DR PDB; 7QI5; EM; 2.63 A; s=1-439. DR PDB; 7QI6; EM; 2.98 A; s=1-439. DR PDB; 8ANY; EM; 2.85 A; s=1-439. DR PDB; 8OIR; EM; 3.10 A; Bi=1-439. DR PDB; 8OIT; EM; 2.90 A; Bi=1-439. 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; 7PO4; -. DR PDBsum; 7QH6; -. DR PDBsum; 7QH7; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q9NP92; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. 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-11643; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11645; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12763; -. DR EMDB; EMD-12764; -. DR EMDB; EMD-12845; -. DR EMDB; EMD-12846; -. DR EMDB; EMD-12847; -. DR EMDB; EMD-12865; -. DR EMDB; EMD-12867; -. DR EMDB; EMD-12868; -. DR EMDB; EMD-12869; -. DR EMDB; EMD-12870; -. DR EMDB; EMD-12871; -. DR EMDB; EMD-12872; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-12919; -. DR EMDB; EMD-12920; -. DR EMDB; EMD-12921; -. DR EMDB; EMD-12922; -. DR EMDB; EMD-12923; -. DR EMDB; EMD-12924; -. DR EMDB; EMD-12925; -. DR EMDB; EMD-12926; -. DR EMDB; EMD-12927; -. DR EMDB; EMD-13329; -. DR EMDB; EMD-13562; -. DR EMDB; EMD-13965; -. DR EMDB; EMD-13967; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16899; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-23121; -. DR EMDB; EMD-3842; -. DR EMDB; EMD-3843; -. DR EMDB; EMD-4434; -. DR SMR; Q9NP92; -. DR BioGRID; 116091; 222. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q9NP92; -. DR IntAct; Q9NP92; 85. DR MINT; Q9NP92; -. DR STRING; 9606.ENSP00000424328; -. DR GlyGen; Q9NP92; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NP92; -. DR PhosphoSitePlus; Q9NP92; -. DR SwissPalm; Q9NP92; -. DR BioMuta; MRPS30; -. DR DMDM; 116242771; -. DR EPD; Q9NP92; -. DR jPOST; Q9NP92; -. DR MassIVE; Q9NP92; -. DR MaxQB; Q9NP92; -. DR PaxDb; 9606-ENSP00000424328; -. DR PeptideAtlas; Q9NP92; -. DR ProteomicsDB; 81936; -. DR Pumba; Q9NP92; -. DR Antibodypedia; 10864; 164 antibodies from 22 providers. DR DNASU; 10884; -. DR Ensembl; ENST00000507110.6; ENSP00000424328.1; ENSG00000112996.11. DR GeneID; 10884; -. DR KEGG; hsa:10884; -. DR MANE-Select; ENST00000507110.6; ENSP00000424328.1; NM_016640.4; NP_057724.2. DR UCSC; uc003joh.4; human. DR AGR; HGNC:8769; -. DR CTD; 10884; -. DR DisGeNET; 10884; -. DR GeneCards; MRPS30; -. DR HGNC; HGNC:8769; MRPS30. DR HPA; ENSG00000112996; Low tissue specificity. DR MIM; 611991; gene. DR neXtProt; NX_Q9NP92; -. DR OpenTargets; ENSG00000112996; -. DR PharmGKB; PA31018; -. DR VEuPathDB; HostDB:ENSG00000112996; -. DR eggNOG; KOG4461; Eukaryota. DR GeneTree; ENSGT00390000001442; -. DR HOGENOM; CLU_049608_0_0_1; -. DR InParanoid; Q9NP92; -. DR OMA; ITDGHFF; -. DR OrthoDB; 2899382at2759; -. DR PhylomeDB; Q9NP92; -. DR TreeFam; TF320686; -. DR PathwayCommons; Q9NP92; -. 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; Q9NP92; -. DR SIGNOR; Q9NP92; -. DR BioGRID-ORCS; 10884; 234 hits in 1159 CRISPR screens. DR ChiTaRS; MRPS30; human. DR GeneWiki; MRPS30; -. DR GenomeRNAi; 10884; -. DR Pharos; Q9NP92; Tbio. DR PRO; PR:Q9NP92; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9NP92; Protein. DR Bgee; ENSG00000112996; Expressed in adrenal tissue and 204 other cell types or tissues. 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:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR InterPro; IPR010793; Ribosomal_mL37/mL65. DR InterPro; IPR039982; Ribosomal_mL65. DR PANTHER; PTHR13014:SF3; 39S RIBOSOMAL PROTEIN S30, MITOCHONDRIAL; 1. DR PANTHER; PTHR13014; MITOCHONDRIAL 28S RIBOSOMAL PROTEIN S30/P52 PRO-APOTOTIC PROTEIN; 1. DR Pfam; PF07147; PDCD9; 1. DR Genevisible; Q9NP92; HS. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1..439 FT /note="Large ribosomal subunit protein mL65" FT /id="PRO_0000087720" FT VARIANT 33 FT /note="C -> S (in dbSNP:rs3747479)" FT /evidence="ECO:0000269|PubMed:10640817, FT ECO:0000269|PubMed:11230166, ECO:0000269|Ref.2" FT /id="VAR_028023" FT VARIANT 102 FT /note="A -> V (in dbSNP:rs35601455)" FT /id="VAR_052048" FT CONFLICT 82 FT /note="I -> V (in Ref. 3; CAB66641)" FT /evidence="ECO:0000305" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 56..72 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 76..84 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 102..110 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 141..154 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:7QH6" FT HELIX 168..188 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 206..216 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 221..224 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 226..235 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 238..245 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 268..272 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:7OIA" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 294..301 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 308..314 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 318..343 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:5OOM" FT STRAND 355..374 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 381..384 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 391..395 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 403..406 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 409..411 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 415..426 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 439 AA; 50365 MW; 2A22DB6170F6D04F CRC64; MAAARCWRPL LRGPRLSLHT AANAAATATE TTCQDVAATP VARYPPIVAS MTADSKAARL RRIERWQATV HAAESVDEKL RILTKMQFMK YMVYPQTFAL NADRWYQYFT KTVFLSGLPP PPAEPEPEPE PEPEPALDLA ALRAVACDCL LQEHFYLRRR RRVHRYEESE VISLPFLDQL VSTLVGLLSP HNPALAAAAL DYRCPVHFYW VRGEEIIPRG HRRGRIDDLR YQIDDKPNNQ IRISKQLAEF VPLDYSVPIE IPTIKCKPDK LPLFKRQYEN HIFVGSKTAD PCCYGHTQFH LLPDKLRRER LLRQNCADQI EVVFRANAIA SLFAWTGAQA MYQGFWSEAD VTRPFVSQAV ITDGKYFSFF CYQLNTLALT TQADQNNPRK NICWGTQSKP LYETIEDNDV KGFNDDVLLQ IVHFLLNRPK EEKSQLLEN //