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   27-MAR-2024, entry version 160.
DE   RecName: Full=Large ribosomal subunit protein uL14m {ECO:0000303|PubMed:25278503};
DE   AltName: 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   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; 7PO4; EM; 2.56 A; L=1-145.
DR   PDB; 7QH6; EM; 3.08 A; L=1-145.
DR   PDB; 7QH7; EM; 2.89 A; L=31-145.
DR   PDB; 7QI4; EM; 2.21 A; L=1-145.
DR   PDB; 7QI5; EM; 2.63 A; L=1-145.
DR   PDB; 7QI6; EM; 2.98 A; L=1-145.
DR   PDB; 8ANY; EM; 2.85 A; L=1-145.
DR   PDB; 8OIR; EM; 3.10 A; BS=1-145.
DR   PDB; 8OIT; EM; 2.90 A; BS=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; 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; Q6P1L8; -.
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; Q6P1L8; -.
DR   BioGRID; 122350; 127.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q6P1L8; -.
DR   IntAct; Q6P1L8; 39.
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; 9606-ENSP00000361084; -.
DR   PeptideAtlas; Q6P1L8; -.
DR   ProteomicsDB; 66848; -.
DR   Pumba; Q6P1L8; -.
DR   TopDownProteomics; Q6P1L8; -.
DR   Antibodypedia; 49263; 151 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   AGR; HGNC:14279; -.
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; 5310262at2759; -.
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; 376 hits in 1155 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 189 other cell types or tissues.
DR   ExpressionAtlas; Q6P1L8; baseline and differential.
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; NAS:ComplexPortal.
DR   Gene3D; 2.40.150.20; Ribosomal protein L14; 1.
DR   HAMAP; MF_01367; Ribosomal_uL14; 1.
DR   InterPro; IPR000218; Ribosomal_uL14.
DR   InterPro; IPR036853; Ribosomal_uL14_sf.
DR   PANTHER; PTHR21037; 39S RIBOSOMAL PROTEIN L14, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21037:SF3; 39S RIBOSOMAL PROTEIN L14, MITOCHONDRIAL; 1.
DR   Pfam; PF00238; Ribosomal_L14; 1.
DR   SMART; SM01374; Ribosomal_L14; 1.
DR   SUPFAM; SSF50193; Ribosomal protein L14; 1.
DR   Genevisible; Q6P1L8; HS.
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="Large ribosomal subunit protein uL14m"
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..121
FT                   /evidence="ECO:0007829|PDB:7QH6"
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
//