RM27_HUMAN
ID RM27_HUMAN Reviewed; 148 AA.
AC Q9P0M9; B2RE14;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=39S ribosomal protein L27, mitochondrial;
DE Short=L27mt;
DE Short=MRP-L27;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL27m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL27; ORFNames=HSPC250;
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], 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].
RC TISSUE=Umbilical cord blood;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 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 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 [8] {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 [9] {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 [10] {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 Q9P0M9; Q13643: FHL3; NbExp=6; IntAct=EBI-5325236, EBI-741101;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069,
CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family.
CC {ECO:0000305}.
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DR EMBL; AB049647; BAB40852.1; -; mRNA.
DR EMBL; AF151084; AAF36170.1; -; mRNA.
DR EMBL; AK315758; BAG38111.1; -; mRNA.
DR EMBL; CH471109; EAW94623.1; -; Genomic_DNA.
DR EMBL; BC001066; AAH01066.1; -; mRNA.
DR EMBL; BC021986; AAH21986.1; -; mRNA.
DR CCDS; CCDS11564.1; -.
DR RefSeq; NP_057588.1; NM_016504.2.
DR PDB; 3IY9; EM; 14.10 A; O=31-99.
DR PDB; 3J7Y; EM; 3.40 A; W=1-148.
DR PDB; 3J9M; EM; 3.50 A; W=1-148.
DR PDB; 5OOL; EM; 3.06 A; W=1-148.
DR PDB; 5OOM; EM; 3.03 A; W=1-148.
DR PDB; 6I9R; EM; 3.90 A; W=1-148.
DR PDB; 6NU2; EM; 3.90 A; W=34-148.
DR PDB; 6NU3; EM; 4.40 A; W=1-148.
DR PDB; 6VLZ; EM; 2.97 A; W=1-148.
DR PDB; 6VMI; EM; 2.96 A; W=1-148.
DR PDB; 6ZM5; EM; 2.89 A; W=1-148.
DR PDB; 6ZM6; EM; 2.59 A; W=1-148.
DR PDB; 6ZS9; EM; 4.00 A; XW=1-148.
DR PDB; 6ZSA; EM; 4.00 A; XW=1-148.
DR PDB; 6ZSB; EM; 4.50 A; XW=1-148.
DR PDB; 6ZSC; EM; 3.50 A; XW=1-148.
DR PDB; 6ZSD; EM; 3.70 A; XW=1-148.
DR PDB; 6ZSE; EM; 5.00 A; XW=1-148.
DR PDB; 6ZSG; EM; 4.00 A; XW=1-148.
DR PDB; 7A5F; EM; 4.40 A; W3=1-148.
DR PDB; 7A5G; EM; 4.33 A; W3=1-148.
DR PDB; 7A5H; EM; 3.30 A; W=1-148.
DR PDB; 7A5I; EM; 3.70 A; W3=1-148.
DR PDB; 7A5J; EM; 3.10 A; W=1-148.
DR PDB; 7A5K; EM; 3.70 A; W3=1-148.
DR PDB; 7L08; EM; 3.49 A; W=1-148.
DR PDB; 7L20; EM; 3.15 A; W=1-148.
DR PDB; 7O9K; EM; 3.10 A; W=1-148.
DR PDB; 7O9M; EM; 2.50 A; W=1-148.
DR PDB; 7ODR; EM; 2.90 A; W=1-148.
DR PDB; 7ODS; EM; 3.10 A; W=1-148.
DR PDB; 7ODT; EM; 3.10 A; W=1-148.
DR PDB; 7OF0; EM; 2.20 A; W=1-148.
DR PDB; 7OF2; EM; 2.70 A; W=1-148.
DR PDB; 7OF3; EM; 2.70 A; W=1-148.
DR PDB; 7OF4; EM; 2.70 A; W=1-148.
DR PDB; 7OF5; EM; 2.90 A; W=1-148.
DR PDB; 7OF6; EM; 2.60 A; W=1-148.
DR PDB; 7OF7; EM; 2.50 A; W=1-148.
DR PDB; 7OG4; EM; 3.80 A; XW=1-148.
DR PDB; 7OI6; EM; 5.70 A; W=1-148.
DR PDB; 7OI7; EM; 3.50 A; W=1-148.
DR PDB; 7OI8; EM; 3.50 A; W=1-148.
DR PDB; 7OI9; EM; 3.30 A; W=1-148.
DR PDB; 7OIA; EM; 3.20 A; W=1-148.
DR PDB; 7OIB; EM; 3.30 A; W=1-148.
DR PDB; 7OIC; EM; 3.10 A; W=1-148.
DR PDB; 7OID; EM; 3.70 A; W=1-148.
DR PDB; 7OIE; EM; 3.50 A; W=1-148.
DR PDB; 7PD3; EM; 3.40 A; W=1-148.
DR PDB; 7QH6; EM; 3.08 A; W=1-148.
DR PDBsum; 3IY9; -.
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; Q9P0M9; -.
DR SMR; Q9P0M9; -.
DR BioGRID; 119418; 196.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9P0M9; -.
DR IntAct; Q9P0M9; 44.
DR MINT; Q9P0M9; -.
DR STRING; 9606.ENSP00000225969; -.
DR iPTMnet; Q9P0M9; -.
DR PhosphoSitePlus; Q9P0M9; -.
DR BioMuta; MRPL27; -.
DR DMDM; 20139806; -.
DR EPD; Q9P0M9; -.
DR jPOST; Q9P0M9; -.
DR MassIVE; Q9P0M9; -.
DR MaxQB; Q9P0M9; -.
DR PaxDb; Q9P0M9; -.
DR PeptideAtlas; Q9P0M9; -.
DR PRIDE; Q9P0M9; -.
DR ProteomicsDB; 83581; -.
DR TopDownProteomics; Q9P0M9; -.
DR Antibodypedia; 18064; 91 antibodies from 21 providers.
DR DNASU; 51264; -.
DR Ensembl; ENST00000225969.9; ENSP00000225969.4; ENSG00000108826.16.
DR GeneID; 51264; -.
DR KEGG; hsa:51264; -.
DR MANE-Select; ENST00000225969.9; ENSP00000225969.4; NM_016504.3; NP_057588.1.
DR UCSC; uc002iqq.4; human.
DR CTD; 51264; -.
DR GeneCards; MRPL27; -.
DR HGNC; HGNC:14483; MRPL27.
DR HPA; ENSG00000108826; Low tissue specificity.
DR MIM; 611837; gene.
DR neXtProt; NX_Q9P0M9; -.
DR OpenTargets; ENSG00000108826; -.
DR PharmGKB; PA30957; -.
DR VEuPathDB; HostDB:ENSG00000108826; -.
DR eggNOG; KOG4600; Eukaryota.
DR GeneTree; ENSGT00390000014660; -.
DR InParanoid; Q9P0M9; -.
DR OMA; DGHYVSH; -.
DR OrthoDB; 1177118at2759; -.
DR PhylomeDB; Q9P0M9; -.
DR TreeFam; TF323523; -.
DR PathwayCommons; Q9P0M9; -.
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; Q9P0M9; -.
DR SIGNOR; Q9P0M9; -.
DR BioGRID-ORCS; 51264; 479 hits in 1083 CRISPR screens.
DR ChiTaRS; MRPL27; human.
DR GenomeRNAi; 51264; -.
DR Pharos; Q9P0M9; Tdark.
DR PRO; PR:Q9P0M9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9P0M9; protein.
DR Bgee; ENSG00000108826; Expressed in left ventricle myocardium and 183 other tissues.
DR ExpressionAtlas; Q9P0M9; baseline and differential.
DR Genevisible; Q9P0M9; 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; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR InterPro; IPR001684; Ribosomal_L27.
DR PANTHER; PTHR15893; PTHR15893; 1.
DR Pfam; PF01016; Ribosomal_L27; 1.
DR PRINTS; PR00063; RIBOSOMALL27.
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|UniProtKB:Q32PC3"
FT CHAIN 31..148
FT /note="39S ribosomal protein L27, mitochondrial"
FT /id="PRO_0000181229"
FT VARIANT 24
FT /note="T -> A (in dbSNP:rs17776919)"
FT /id="VAR_052023"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7OIB"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 89..103
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 148 AA; 16073 MW; 90945F471E80EFB6 CRC64;
MASVVLALRT RTAVTSLLSP TPATALAVRY ASKKSGGSSK NLGGKSSGRR QGIKKMEGHY
VHAGNIIATQ RHFRWHPGAH VGVGKNKCLY ALEEGIVRYT KEVYVPHPRN TEAVDLITRL
PKGAVLYKTF VHVVPAKPEG TFKLVAML
