ID   RM11_HUMAN              Reviewed;         192 AA.
AC   Q9Y3B7; A6NLT0; A8K219; Q32P46; Q96Q73;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 202.
DE   RecName: Full=Large ribosomal subunit protein uL11m {ECO:0000303|PubMed:25278503};
DE   AltName: Full=39S ribosomal protein L11, mitochondrial;
DE            Short=L11mt;
DE            Short=MRP-L11;
DE   Flags: Precursor;
GN   Name=MRPL11; ORFNames=CGI-113;
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 SUBCELLULAR LOCATION.
RX   PubMed=11279069; DOI=10.1074/jbc.m100432200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Structural compensation for the deficit of rRNA with proteins in the
RT   mammalian mitochondrial ribosome. Systematic analysis of protein components
RT   of the large ribosomal subunit from mammalian mitochondria.";
RL   J. Biol. Chem. 276:21724-21736(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Subthalamic nucleus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Duodenum, Lymph, and Melanoma;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-141 (ISOFORMS 1/2).
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 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   [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   -!- 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   -!- INTERACTION:
CC       Q9Y3B7; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-5453723, EBI-11522760;
CC       Q9Y3B7; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-5453723, EBI-1383687;
CC       Q9Y3B7; Q13554: CAMK2B; NbExp=3; IntAct=EBI-5453723, EBI-1058722;
CC       Q9Y3B7; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-5453723, EBI-11523526;
CC       Q9Y3B7; Q13557: CAMK2D; NbExp=5; IntAct=EBI-5453723, EBI-351018;
CC       Q9Y3B7; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-5453723, EBI-12020154;
CC       Q9Y3B7; P0C7W6: CCDC172; NbExp=3; IntAct=EBI-5453723, EBI-2548868;
CC       Q9Y3B7; A1L4K1: FSD2; NbExp=6; IntAct=EBI-5453723, EBI-5661036;
CC       Q9Y3B7; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-5453723, EBI-5916454;
CC       Q9Y3B7; V9HW27: HEL-S-101; NbExp=3; IntAct=EBI-5453723, EBI-10178933;
CC       Q9Y3B7; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-5453723, EBI-2549423;
CC       Q9Y3B7; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-5453723, EBI-10172004;
CC       Q9Y3B7; Q96N16: JAKMIP1; NbExp=3; IntAct=EBI-5453723, EBI-2680803;
CC       Q9Y3B7; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-5453723, EBI-752007;
CC       Q9Y3B7; Q6A162: KRT40; NbExp=3; IntAct=EBI-5453723, EBI-10171697;
CC       Q9Y3B7; Q6P161: MRPL54; NbExp=3; IntAct=EBI-5453723, EBI-7825248;
CC       Q9Y3B7; Q5JR59-3: MTUS2; NbExp=5; IntAct=EBI-5453723, EBI-11522433;
CC       Q9Y3B7; Q13371: PDCL; NbExp=3; IntAct=EBI-5453723, EBI-5772890;
CC       Q9Y3B7; Q8ND90: PNMA1; NbExp=6; IntAct=EBI-5453723, EBI-302345;
CC       Q9Y3B7; Q7RTY1: SLC16A9; NbExp=3; IntAct=EBI-5453723, EBI-10232636;
CC       Q9Y3B7; P32856-2: STX2; NbExp=3; IntAct=EBI-5453723, EBI-11956649;
CC       Q9Y3B7; Q86VP1: TAX1BP1; NbExp=6; IntAct=EBI-5453723, EBI-529518;
CC       Q9Y3B7; Q12800: TFCP2; NbExp=3; IntAct=EBI-5453723, EBI-717422;
CC       Q9Y3B7; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-5453723, EBI-1105213;
CC       Q9Y3B7; Q9NVV9: THAP1; NbExp=4; IntAct=EBI-5453723, EBI-741515;
CC       Q9Y3B7; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-5453723, EBI-2799833;
CC       Q9Y3B7; O43829: ZBTB14; NbExp=3; IntAct=EBI-5453723, EBI-10176632;
CC       Q9Y3B7; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-5453723, EBI-2515601;
CC       Q9Y3B7; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-5453723, EBI-742740;
CC       Q9Y3B7; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-5453723, EBI-11962468;
CC       Q9Y3B7; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-5453723, EBI-11035148;
CC       Q9Y3B7; PRO_0000038596 [P04591]: gag; Xeno; NbExp=3; IntAct=EBI-5453723, EBI-6179727;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069,
CC       ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC       ECO:0000269|PubMed:28892042}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Y3B7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y3B7-2; Sequence=VSP_041077;
CC       Name=3;
CC         IsoId=Q9Y3B7-3; Sequence=VSP_045237;
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC       {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; AB049638; BAB40843.1; -; mRNA.
DR   EMBL; AF151871; AAD34108.1; -; mRNA.
DR   EMBL; AK290084; BAF82773.1; -; mRNA.
DR   EMBL; AP002748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74528.1; -; Genomic_DNA.
DR   EMBL; CH471076; EAW74529.1; -; Genomic_DNA.
DR   EMBL; CH471076; EAW74531.1; -; Genomic_DNA.
DR   EMBL; BC005002; AAH05002.1; -; mRNA.
DR   EMBL; BC108277; AAI08278.1; -; mRNA.
DR   EMBL; BM554886; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB051338; BAB54928.1; -; Genomic_DNA.
DR   CCDS; CCDS44655.1; -. [Q9Y3B7-2]
DR   CCDS; CCDS8139.1; -. [Q9Y3B7-1]
DR   CCDS; CCDS8140.1; -. [Q9Y3B7-3]
DR   RefSeq; NP_057134.1; NM_016050.4. [Q9Y3B7-1]
DR   RefSeq; NP_733934.1; NM_170738.3. [Q9Y3B7-2]
DR   RefSeq; NP_733935.1; NM_170739.3. [Q9Y3B7-3]
DR   PDB; 3J7Y; EM; 3.40 A; J=1-192.
DR   PDB; 3J9M; EM; 3.50 A; J=1-192.
DR   PDB; 5OOL; EM; 3.06 A; J=1-192.
DR   PDB; 5OOM; EM; 3.03 A; J=1-192.
DR   PDB; 6I9R; EM; 3.90 A; J=1-192.
DR   PDB; 6NU2; EM; 3.90 A; J=18-157.
DR   PDB; 6NU3; EM; 4.40 A; J=1-192.
DR   PDB; 6VLZ; EM; 2.97 A; J=1-192.
DR   PDB; 6VMI; EM; 2.96 A; J=1-192.
DR   PDB; 6ZM5; EM; 2.89 A; J=1-192.
DR   PDB; 6ZM6; EM; 2.59 A; J=1-192.
DR   PDB; 6ZS9; EM; 4.00 A; XJ=1-192.
DR   PDB; 6ZSA; EM; 4.00 A; XJ=1-192.
DR   PDB; 6ZSB; EM; 4.50 A; XJ=1-192.
DR   PDB; 6ZSC; EM; 3.50 A; XJ=1-192.
DR   PDB; 6ZSD; EM; 3.70 A; XJ=1-192.
DR   PDB; 6ZSE; EM; 5.00 A; XJ=1-192.
DR   PDB; 6ZSG; EM; 4.00 A; XJ=1-192.
DR   PDB; 7A5F; EM; 4.40 A; J3=1-192.
DR   PDB; 7A5G; EM; 4.33 A; J3=1-192.
DR   PDB; 7A5H; EM; 3.30 A; J=1-192.
DR   PDB; 7A5I; EM; 3.70 A; J3=1-192.
DR   PDB; 7A5J; EM; 3.10 A; J=1-192.
DR   PDB; 7A5K; EM; 3.70 A; J3=1-192.
DR   PDB; 7L08; EM; 3.49 A; J=1-192.
DR   PDB; 7L20; EM; 3.15 A; J=1-192.
DR   PDB; 7O9K; EM; 3.10 A; J=1-192.
DR   PDB; 7O9M; EM; 2.50 A; J=1-192.
DR   PDB; 7ODR; EM; 2.90 A; J=1-192.
DR   PDB; 7ODS; EM; 3.10 A; J=1-192.
DR   PDB; 7ODT; EM; 3.10 A; J=1-192.
DR   PDB; 7OF0; EM; 2.20 A; J=1-192.
DR   PDB; 7OF2; EM; 2.70 A; J=1-192.
DR   PDB; 7OF3; EM; 2.70 A; J=1-192.
DR   PDB; 7OF4; EM; 2.70 A; J=1-192.
DR   PDB; 7OF5; EM; 2.90 A; J=1-192.
DR   PDB; 7OF6; EM; 2.60 A; J=1-192.
DR   PDB; 7OF7; EM; 2.50 A; J=1-192.
DR   PDB; 7OG4; EM; 3.80 A; XJ=1-192.
DR   PDB; 7OI6; EM; 5.70 A; J=1-192.
DR   PDB; 7OI7; EM; 3.50 A; J=1-192.
DR   PDB; 7OI8; EM; 3.50 A; J=1-192.
DR   PDB; 7OI9; EM; 3.30 A; J=1-192.
DR   PDB; 7OIA; EM; 3.20 A; J=1-192.
DR   PDB; 7OIB; EM; 3.30 A; J=1-192.
DR   PDB; 7OIC; EM; 3.10 A; J=1-192.
DR   PDB; 7OID; EM; 3.70 A; J=1-192.
DR   PDB; 7OIE; EM; 3.50 A; J=1-192.
DR   PDB; 7PD3; EM; 3.40 A; J=1-192.
DR   PDB; 7PO4; EM; 2.56 A; J=1-192.
DR   PDB; 7QI4; EM; 2.21 A; J=1-192.
DR   PDB; 7QI5; EM; 2.63 A; J=1-192.
DR   PDB; 7QI6; EM; 2.98 A; J=1-192.
DR   PDB; 8ANY; EM; 2.85 A; J=1-192.
DR   PDB; 8OIR; EM; 3.10 A; BQ=1-192.
DR   PDB; 8OIT; EM; 2.90 A; BQ=1-192.
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; 7QI4; -.
DR   PDBsum; 7QI5; -.
DR   PDBsum; 7QI6; -.
DR   PDBsum; 8ANY; -.
DR   PDBsum; 8OIR; -.
DR   PDBsum; 8OIT; -.
DR   AlphaFoldDB; Q9Y3B7; -.
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-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; Q9Y3B7; -.
DR   BioGRID; 122369; 410.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q9Y3B7; -.
DR   IntAct; Q9Y3B7; 100.
DR   MINT; Q9Y3B7; -.
DR   STRING; 9606.ENSP00000308897; -.
DR   GlyGen; Q9Y3B7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y3B7; -.
DR   PhosphoSitePlus; Q9Y3B7; -.
DR   SwissPalm; Q9Y3B7; -.
DR   BioMuta; MRPL11; -.
DR   DMDM; 22001931; -.
DR   EPD; Q9Y3B7; -.
DR   jPOST; Q9Y3B7; -.
DR   MassIVE; Q9Y3B7; -.
DR   MaxQB; Q9Y3B7; -.
DR   PaxDb; 9606-ENSP00000308897; -.
DR   PeptideAtlas; Q9Y3B7; -.
DR   ProteomicsDB; 1491; -.
DR   ProteomicsDB; 86004; -. [Q9Y3B7-1]
DR   ProteomicsDB; 86005; -. [Q9Y3B7-2]
DR   Pumba; Q9Y3B7; -.
DR   TopDownProteomics; Q9Y3B7-1; -. [Q9Y3B7-1]
DR   TopDownProteomics; Q9Y3B7-2; -. [Q9Y3B7-2]
DR   Antibodypedia; 30159; 364 antibodies from 30 providers.
DR   DNASU; 65003; -.
DR   Ensembl; ENST00000310999.11; ENSP00000308897.7; ENSG00000174547.13. [Q9Y3B7-1]
DR   Ensembl; ENST00000329819.4; ENSP00000329630.4; ENSG00000174547.13. [Q9Y3B7-3]
DR   Ensembl; ENST00000430466.6; ENSP00000415356.2; ENSG00000174547.13. [Q9Y3B7-2]
DR   GeneID; 65003; -.
DR   KEGG; hsa:65003; -.
DR   MANE-Select; ENST00000310999.11; ENSP00000308897.7; NM_016050.5; NP_057134.1.
DR   UCSC; uc001ohy.5; human. [Q9Y3B7-1]
DR   AGR; HGNC:14042; -.
DR   CTD; 65003; -.
DR   DisGeNET; 65003; -.
DR   GeneCards; MRPL11; -.
DR   HGNC; HGNC:14042; MRPL11.
DR   HPA; ENSG00000174547; Low tissue specificity.
DR   MIM; 611826; gene.
DR   neXtProt; NX_Q9Y3B7; -.
DR   OpenTargets; ENSG00000174547; -.
DR   PharmGKB; PA30940; -.
DR   VEuPathDB; HostDB:ENSG00000174547; -.
DR   eggNOG; KOG3257; Eukaryota.
DR   GeneTree; ENSGT00390000003153; -.
DR   HOGENOM; CLU_074237_1_1_1; -.
DR   InParanoid; Q9Y3B7; -.
DR   OMA; CKQFNAK; -.
DR   OrthoDB; 166522at2759; -.
DR   PhylomeDB; Q9Y3B7; -.
DR   TreeFam; TF313471; -.
DR   PathwayCommons; Q9Y3B7; -.
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; Q9Y3B7; -.
DR   SIGNOR; Q9Y3B7; -.
DR   BioGRID-ORCS; 65003; 183 hits in 1162 CRISPR screens.
DR   ChiTaRS; MRPL11; human.
DR   GeneWiki; MRPL11; -.
DR   GenomeRNAi; 65003; -.
DR   Pharos; Q9Y3B7; Tbio.
DR   PRO; PR:Q9Y3B7; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9Y3B7; Protein.
DR   Bgee; ENSG00000174547; Expressed in mucosa of transverse colon and 169 other cell types or tissues.
DR   ExpressionAtlas; Q9Y3B7; 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:0005761; C:mitochondrial ribosome; NAS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd00349; Ribosomal_L11; 1.
DR   Gene3D; 1.10.10.250; Ribosomal protein L11, C-terminal domain; 1.
DR   Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1.
DR   HAMAP; MF_00736; Ribosomal_uL11; 1.
DR   InterPro; IPR000911; Ribosomal_uL11.
DR   InterPro; IPR006519; Ribosomal_uL11_bac-typ.
DR   InterPro; IPR020783; Ribosomal_uL11_C.
DR   InterPro; IPR036769; Ribosomal_uL11_C_sf.
DR   InterPro; IPR020784; Ribosomal_uL11_N.
DR   InterPro; IPR036796; Ribosomal_uL11_N_sf.
DR   NCBIfam; TIGR01632; L11_bact; 1.
DR   PANTHER; PTHR11661:SF19; 39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11661; 60S RIBOSOMAL PROTEIN L12; 1.
DR   Pfam; PF00298; Ribosomal_L11; 1.
DR   Pfam; PF03946; Ribosomal_L11_N; 1.
DR   SMART; SM00649; RL11; 1.
DR   SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1.
DR   SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1.
DR   Genevisible; Q9Y3B7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..192
FT                   /note="Large ribosomal subunit protein uL11m"
FT                   /id="PRO_0000030443"
FT   VAR_SEQ         16..41
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_041077"
FT   VAR_SEQ         158..192
FT                   /note="DLSSEELAAFQKERAIFLAAQKEADLAAQEEAAKK -> ERCSANVLRNGKI
FT                   SMKDPSGRSSV (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045237"
FT   CONFLICT        68
FT                   /note="T -> I (in Ref. 6; BM554886)"
FT                   /evidence="ECO:0000305"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           36..40
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           46..59
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:3J7Y"
FT   HELIX           88..94
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            123..126
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   HELIX           137..150
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   CONFLICT        Q9Y3B7-3:181
FT                   /note="V -> L (in Ref. 6; BM554886)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   192 AA;  20683 MW;  92506A20044BF278 CRC64;
     MSKLGRAARG LRKPEVGGVI RAIVRAGLAM PGPPLGPVLG QRGVSINQFC KEFNERTKDI
     KEGIPLPTKI LVKPDRTFEI KIGQPTVSYF LKAAAGIEKG ARQTGKEVAG LVTLKHVYEI
     ARIKAQDEAF ALQDVPLSSV VRSIIGSARS LGIRVVKDLS SEELAAFQKE RAIFLAAQKE
     ADLAAQEEAA KK
//