RM14_HUMAN
ID RM14_HUMAN Reviewed; 145 AA.
AC Q6P1L8; B2R575; Q96Q72;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=39S ribosomal protein L14, mitochondrial;
DE Short=L14mt;
DE Short=MRP-L14;
DE AltName: Full=39S ribosomal protein L32, mitochondrial;
DE Short=L32mt;
DE Short=MRP-L32;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL14m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL14; Synonyms=MRPL32, RPML32;
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].
RC TISSUE=Thymus;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 25-76, AND SUBCELLULAR LOCATION.
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 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MALSU1.
RX PubMed=22829778; DOI=10.1371/journal.pgen.1002815;
RA Hauser R., Pech M., Kijek J., Yamamoto H., Titz B., Naeve F.,
RA Tovchigrechko A., Yamamoto K., Szaflarski W., Takeuchi N., Stellberger T.,
RA Diefenbacher M.E., Nierhaus K.H., Uetz P.;
RT "RsfA (YbeB) proteins are conserved ribosomal silencing factors.";
RL PLoS Genet. 8:E1002815-E1002815(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
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 [10] {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 [11] {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 [12] {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 -!- FUNCTION: Forms part of 2 intersubunit bridges in the assembled
CC ribosome. Upon binding to MALSU1 intersubunit bridge formation is
CC blocked, preventing ribosome formation and repressing translation
CC (Probable). {ECO:0000305|PubMed:22829778}.
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:25278503, PubMed:25838379, PubMed:28892042). 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 (PubMed:25278503, PubMed:25838379). Interacts with
CC MALSU1 (PubMed:22829778). {ECO:0000269|PubMed:22829778,
CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11543634,
CC ECO:0000269|PubMed:22829778, ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000305}.
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DR EMBL; AK312086; BAG35022.1; -; mRNA.
DR EMBL; AL109615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04243.1; -; Genomic_DNA.
DR EMBL; BC065005; AAH65005.1; -; mRNA.
DR EMBL; AB051339; BAB54929.2; -; Genomic_DNA.
DR CCDS; CCDS34460.1; -.
DR RefSeq; NP_001305696.1; NM_001318767.1.
DR RefSeq; NP_001305697.1; NM_001318768.1.
DR RefSeq; NP_115487.2; NM_032111.3.
DR PDB; 3J7Y; EM; 3.40 A; L=1-145.
DR PDB; 3J9M; EM; 3.50 A; L=1-145.
DR PDB; 5OOL; EM; 3.06 A; L=1-145.
DR PDB; 5OOM; EM; 3.03 A; L=1-145.
DR PDB; 6I9R; EM; 3.90 A; L=1-145.
DR PDB; 6NU2; EM; 3.90 A; L=31-145.
DR PDB; 6NU3; EM; 4.40 A; L=1-145.
DR PDB; 6VLZ; EM; 2.97 A; L=1-145.
DR PDB; 6VMI; EM; 2.96 A; L=1-145.
DR PDB; 6ZM5; EM; 2.89 A; L=1-145.
DR PDB; 6ZM6; EM; 2.59 A; L=1-145.
DR PDB; 6ZS9; EM; 4.00 A; XL=1-145.
DR PDB; 6ZSA; EM; 4.00 A; XL=1-145.
DR PDB; 6ZSB; EM; 4.50 A; XL=1-145.
DR PDB; 6ZSC; EM; 3.50 A; XL=1-145.
DR PDB; 6ZSD; EM; 3.70 A; XL=1-145.
DR PDB; 6ZSE; EM; 5.00 A; XL=1-145.
DR PDB; 6ZSG; EM; 4.00 A; XL=1-145.
DR PDB; 7A5F; EM; 4.40 A; L3=1-145.
DR PDB; 7A5G; EM; 4.33 A; L3=1-145.
DR PDB; 7A5H; EM; 3.30 A; L=1-145.
DR PDB; 7A5I; EM; 3.70 A; L3=1-145.
DR PDB; 7A5J; EM; 3.10 A; L=1-145.
DR PDB; 7A5K; EM; 3.70 A; L3=1-145.
DR PDB; 7L08; EM; 3.49 A; L=1-145.
DR PDB; 7L20; EM; 3.15 A; L=1-145.
DR PDB; 7O9K; EM; 3.10 A; L=1-145.
DR PDB; 7O9M; EM; 2.50 A; L=1-145.
DR PDB; 7ODR; EM; 2.90 A; L=1-145.
DR PDB; 7ODS; EM; 3.10 A; L=1-145.
DR PDB; 7ODT; EM; 3.10 A; L=1-145.
DR PDB; 7OF0; EM; 2.20 A; L=1-145.
DR PDB; 7OF2; EM; 2.70 A; L=1-145.
DR PDB; 7OF3; EM; 2.70 A; L=1-145.
DR PDB; 7OF4; EM; 2.70 A; L=1-145.
DR PDB; 7OF5; EM; 2.90 A; L=1-145.
DR PDB; 7OF6; EM; 2.60 A; L=1-145.
DR PDB; 7OF7; EM; 2.50 A; L=1-145.
DR PDB; 7OG4; EM; 3.80 A; XL=1-145.
DR PDB; 7OI6; EM; 5.70 A; L=1-145.
DR PDB; 7OI7; EM; 3.50 A; L=1-145.
DR PDB; 7OI8; EM; 3.50 A; L=1-145.
DR PDB; 7OI9; EM; 3.30 A; L=1-145.
DR PDB; 7OIA; EM; 3.20 A; L=1-145.
DR PDB; 7OIB; EM; 3.30 A; L=1-145.
DR PDB; 7OIC; EM; 3.10 A; L=1-145.
DR PDB; 7OID; EM; 3.70 A; L=1-145.
DR PDB; 7OIE; EM; 3.50 A; L=1-145.
DR PDB; 7PD3; EM; 3.40 A; L=1-145.
DR PDB; 7QH6; EM; 3.08 A; L=1-145.
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; Q6P1L8; -.
DR SMR; Q6P1L8; -.
DR BioGRID; 122350; 109.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q6P1L8; -.
DR IntAct; Q6P1L8; 37.
DR MINT; Q6P1L8; -.
DR STRING; 9606.ENSP00000361084; -.
DR GlyGen; Q6P1L8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P1L8; -.
DR PhosphoSitePlus; Q6P1L8; -.
DR SwissPalm; Q6P1L8; -.
DR BioMuta; MRPL14; -.
DR DMDM; 74749064; -.
DR EPD; Q6P1L8; -.
DR jPOST; Q6P1L8; -.
DR MassIVE; Q6P1L8; -.
DR MaxQB; Q6P1L8; -.
DR PaxDb; Q6P1L8; -.
DR PeptideAtlas; Q6P1L8; -.
DR PRIDE; Q6P1L8; -.
DR ProteomicsDB; 66848; -.
DR TopDownProteomics; Q6P1L8; -.
DR Antibodypedia; 49263; 127 antibodies from 22 providers.
DR DNASU; 64928; -.
DR Ensembl; ENST00000372014.5; ENSP00000361084.3; ENSG00000180992.7.
DR GeneID; 64928; -.
DR KEGG; hsa:64928; -.
DR MANE-Select; ENST00000372014.5; ENSP00000361084.3; NM_032111.4; NP_115487.2.
DR UCSC; uc003owp.4; human.
DR CTD; 64928; -.
DR DisGeNET; 64928; -.
DR GeneCards; MRPL14; -.
DR HGNC; HGNC:14279; MRPL14.
DR HPA; ENSG00000180992; Tissue enhanced (skeletal).
DR MIM; 611827; gene.
DR neXtProt; NX_Q6P1L8; -.
DR OpenTargets; ENSG00000180992; -.
DR PharmGKB; PA30943; -.
DR VEuPathDB; HostDB:ENSG00000180992; -.
DR eggNOG; KOG3441; Eukaryota.
DR GeneTree; ENSGT00390000001121; -.
DR HOGENOM; CLU_128925_1_0_1; -.
DR InParanoid; Q6P1L8; -.
DR OMA; RCIHVYT; -.
DR OrthoDB; 1547267at2759; -.
DR PhylomeDB; Q6P1L8; -.
DR TreeFam; TF324586; -.
DR PathwayCommons; Q6P1L8; -.
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; Q6P1L8; -.
DR SIGNOR; Q6P1L8; -.
DR BioGRID-ORCS; 64928; 350 hits in 1077 CRISPR screens.
DR ChiTaRS; MRPL14; human.
DR GenomeRNAi; 64928; -.
DR Pharos; Q6P1L8; Tdark.
DR PRO; PR:Q6P1L8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6P1L8; protein.
DR Bgee; ENSG00000180992; Expressed in tibialis anterior and 187 other tissues.
DR ExpressionAtlas; Q6P1L8; baseline and differential.
DR Genevisible; Q6P1L8; 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: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:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 31..145
FT /note="39S ribosomal protein L14, mitochondrial"
FT /id="PRO_0000261134"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3J7Y"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:3J7Y"
SQ SEQUENCE 145 AA; 15948 MW; 841360D2E84071A4 CRC64;
MAFFTGLWGP FTCVSRVLSH HCFSTTGSLS AIQKMTRVRV VDNSALGNSP YHRAPRCIHV
YKKNGVGKVG DQILLAIKGQ KKKALIVGHC MPGPRMTPRF DSNNVVLIED NGNPVGTRIK
TPIPTSLRKR EGEYSKVLAI AQNFV
