RM11_HUMAN
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 03-AUG-2022, entry version 194.
DE RecName: Full=39S ribosomal protein L11, mitochondrial;
DE Short=L11mt;
DE Short=MRP-L11;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL11m {ECO:0000303|PubMed:25278503};
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 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 AlphaFoldDB; Q9Y3B7; -.
DR SMR; Q9Y3B7; -.
DR BioGRID; 122369; 392.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9Y3B7; -.
DR IntAct; Q9Y3B7; 95.
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; Q9Y3B7; -.
DR PeptideAtlas; Q9Y3B7; -.
DR PRIDE; Q9Y3B7; -.
DR ProteomicsDB; 1491; -.
DR ProteomicsDB; 86004; -. [Q9Y3B7-1]
DR ProteomicsDB; 86005; -. [Q9Y3B7-2]
DR TopDownProteomics; Q9Y3B7-1; -. [Q9Y3B7-1]
DR TopDownProteomics; Q9Y3B7-2; -. [Q9Y3B7-2]
DR Antibodypedia; 30159; 318 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 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; 1346532at2759; -.
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; 157 hits in 1079 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 167 other tissues.
DR ExpressionAtlas; Q9Y3B7; baseline and differential.
DR Genevisible; Q9Y3B7; HS.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
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: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; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR TIGRFAMs; TIGR01632; L11_bact; 1.
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="39S ribosomal protein L11, mitochondrial"
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
