RM49_HUMAN
ID RM49_HUMAN Reviewed; 166 AA.
AC Q13405; B2R4G6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=39S ribosomal protein L49, mitochondrial;
DE Short=L49mt;
DE Short=MRP-L49;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL49 {ECO:0000303|PubMed:25278503};
DE AltName: Full=Neighbor of FAU;
DE Short=NOF;
DE AltName: Full=Protein NOF1;
GN Name=MRPL49; Synonyms=C11orf4, NOF1; ORFNames=OK/SW-cl.67;
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].
RC TISSUE=Skeletal muscle;
RX PubMed=8786148; DOI=10.1006/geno.1996.0310;
RA Kas K., Lemahieu V., Meyen E., van de Ven W.J.M., Merregaert J.;
RT "Isolation, cDNA, and genomic structure of a conserved gene (NOF) at
RT chromosome 11q13 next to FAU and oriented in the opposite transcriptional
RT orientation.";
RL Genomics 34:433-436(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION, AND SUBUNIT.
RX PubMed=11551941; DOI=10.1074/jbc.m106510200;
RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA Moseley A., Spremulli L.L.;
RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:43958-43969(2001).
RN [7]
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 [8]
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 [9] {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 [10] {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 [11] {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 (PubMed:11551941, PubMed:25278503, PubMed:25838379).
CC Interacts with OXA1L (By similarity). {ECO:0000250|UniProtKB:Q5EA71,
CC ECO:0000269|PubMed:11551941, ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC Q13405; Q86V38: ATN1; NbExp=3; IntAct=EBI-5325200, EBI-11954292;
CC Q13405; P23560-2: BDNF; NbExp=3; IntAct=EBI-5325200, EBI-12275524;
CC Q13405; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-5325200, EBI-1055254;
CC Q13405; P16284: PECAM1; NbExp=3; IntAct=EBI-5325200, EBI-716404;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL49 family. {ECO:0000305}.
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DR EMBL; U39400; AAB18826.1; -; mRNA.
DR EMBL; AB062395; BAB93482.1; -; mRNA.
DR EMBL; AK311821; BAG34763.1; -; mRNA.
DR EMBL; CH471076; EAW74355.1; -; Genomic_DNA.
DR EMBL; BC004378; AAH04378.1; -; mRNA.
DR CCDS; CCDS8096.1; -.
DR PIR; G02237; G02237.
DR RefSeq; NP_004918.1; NM_004927.3.
DR PDB; 3J7Y; EM; 3.40 A; g=1-166.
DR PDB; 3J9M; EM; 3.50 A; g=1-166.
DR PDB; 5OOL; EM; 3.06 A; g=1-166.
DR PDB; 5OOM; EM; 3.03 A; g=1-166.
DR PDB; 6I9R; EM; 3.90 A; g=1-166.
DR PDB; 6NU2; EM; 3.90 A; g=38-166.
DR PDB; 6NU3; EM; 4.40 A; g=1-166.
DR PDB; 6VLZ; EM; 2.97 A; g=1-166.
DR PDB; 6VMI; EM; 2.96 A; g=1-166.
DR PDB; 6ZM5; EM; 2.89 A; g=1-166.
DR PDB; 6ZM6; EM; 2.59 A; g=1-166.
DR PDB; 6ZS9; EM; 4.00 A; g=1-166.
DR PDB; 6ZSA; EM; 4.00 A; g=1-166.
DR PDB; 6ZSB; EM; 4.50 A; g=1-166.
DR PDB; 6ZSC; EM; 3.50 A; g=1-166.
DR PDB; 6ZSD; EM; 3.70 A; g=1-166.
DR PDB; 6ZSE; EM; 5.00 A; g=1-166.
DR PDB; 6ZSG; EM; 4.00 A; g=1-166.
DR PDB; 7A5F; EM; 4.40 A; g3=1-166.
DR PDB; 7A5G; EM; 4.33 A; g3=1-166.
DR PDB; 7A5H; EM; 3.30 A; g=1-166.
DR PDB; 7A5I; EM; 3.70 A; g3=1-166.
DR PDB; 7A5J; EM; 3.10 A; g=1-166.
DR PDB; 7A5K; EM; 3.70 A; g3=1-166.
DR PDB; 7L08; EM; 3.49 A; g=1-166.
DR PDB; 7L20; EM; 3.15 A; g=1-166.
DR PDB; 7O9K; EM; 3.10 A; g=1-166.
DR PDB; 7O9M; EM; 2.50 A; g=1-166.
DR PDB; 7ODR; EM; 2.90 A; g=1-166.
DR PDB; 7ODS; EM; 3.10 A; g=1-166.
DR PDB; 7ODT; EM; 3.10 A; g=1-166.
DR PDB; 7OF0; EM; 2.20 A; g=1-166.
DR PDB; 7OF2; EM; 2.70 A; g=1-166.
DR PDB; 7OF3; EM; 2.70 A; g=1-166.
DR PDB; 7OF4; EM; 2.70 A; g=1-166.
DR PDB; 7OF5; EM; 2.90 A; g=1-166.
DR PDB; 7OF6; EM; 2.60 A; g=1-166.
DR PDB; 7OF7; EM; 2.50 A; g=1-166.
DR PDB; 7OG4; EM; 3.80 A; g=1-166.
DR PDB; 7OI6; EM; 5.70 A; g=1-166.
DR PDB; 7OI7; EM; 3.50 A; g=1-166.
DR PDB; 7OI8; EM; 3.50 A; g=1-166.
DR PDB; 7OI9; EM; 3.30 A; g=1-166.
DR PDB; 7OIA; EM; 3.20 A; g=1-166.
DR PDB; 7OIB; EM; 3.30 A; g=1-166.
DR PDB; 7OIC; EM; 3.10 A; g=1-166.
DR PDB; 7OID; EM; 3.70 A; g=1-166.
DR PDB; 7OIE; EM; 3.50 A; g=1-166.
DR PDB; 7PD3; EM; 3.40 A; g=1-166.
DR PDB; 7QH6; EM; 3.08 A; g=1-166.
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; Q13405; -.
DR SMR; Q13405; -.
DR BioGRID; 107199; 173.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q13405; -.
DR IntAct; Q13405; 57.
DR MINT; Q13405; -.
DR STRING; 9606.ENSP00000279242; -.
DR GlyGen; Q13405; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13405; -.
DR PhosphoSitePlus; Q13405; -.
DR BioMuta; MRPL49; -.
DR EPD; Q13405; -.
DR jPOST; Q13405; -.
DR MassIVE; Q13405; -.
DR MaxQB; Q13405; -.
DR PaxDb; Q13405; -.
DR PeptideAtlas; Q13405; -.
DR PRIDE; Q13405; -.
DR ProteomicsDB; 59387; -.
DR TopDownProteomics; Q13405; -.
DR Antibodypedia; 29687; 130 antibodies from 23 providers.
DR DNASU; 740; -.
DR Ensembl; ENST00000279242.7; ENSP00000279242.2; ENSG00000149792.9.
DR Ensembl; ENST00000526319.5; ENSP00000434190.1; ENSG00000149792.9.
DR GeneID; 740; -.
DR KEGG; hsa:740; -.
DR MANE-Select; ENST00000279242.7; ENSP00000279242.2; NM_004927.4; NP_004918.1.
DR UCSC; uc001oda.3; human.
DR CTD; 740; -.
DR DisGeNET; 740; -.
DR GeneCards; MRPL49; -.
DR HGNC; HGNC:1176; MRPL49.
DR HPA; ENSG00000149792; Low tissue specificity.
DR MIM; 606866; gene.
DR neXtProt; NX_Q13405; -.
DR OpenTargets; ENSG00000149792; -.
DR PharmGKB; PA30981; -.
DR VEuPathDB; HostDB:ENSG00000149792; -.
DR eggNOG; KOG4034; Eukaryota.
DR GeneTree; ENSGT00390000017253; -.
DR HOGENOM; CLU_085757_2_3_1; -.
DR InParanoid; Q13405; -.
DR OMA; NPPEWKY; -.
DR OrthoDB; 1534017at2759; -.
DR PhylomeDB; Q13405; -.
DR TreeFam; TF317750; -.
DR PathwayCommons; Q13405; -.
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; Q13405; -.
DR SIGNOR; Q13405; -.
DR BioGRID-ORCS; 740; 414 hits in 1083 CRISPR screens.
DR ChiTaRS; MRPL49; human.
DR GenomeRNAi; 740; -.
DR Pharos; Q13405; Tbio.
DR PRO; PR:Q13405; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13405; protein.
DR Bgee; ENSG00000149792; Expressed in right adrenal gland cortex and 203 other tissues.
DR ExpressionAtlas; Q13405; baseline and differential.
DR Genevisible; Q13405; 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:0005761; C:mitochondrial ribosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR007740; Ribosomal_L49/IMG2.
DR PANTHER; PTHR13477; PTHR13477; 1.
DR Pfam; PF05046; Img2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..166
FT /note="39S ribosomal protein L49, mitochondrial"
FT /id="PRO_0000207664"
FT REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 9
FT /note="T -> A (in dbSNP:rs17146691)"
FT /id="VAR_021991"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 166 AA; 19198 MW; 66AB18FDE25D92B4 CRC64;
MAATMFRATL RGWRTGVQRG CGLRLLSQTQ GPPDYPRFVE SVDEYQFVER LLPATRIPDP
PKHEHYPTPS GWQPPRDPPP NLPYFVRRSR MHNIPVYKDI THGNRQMTVI RKVEGDIWAL
QKDVEDFLSP LLGKTPVTQV NEVTGTLRIK GYFDQELKAW LLEKGF
