ID RM41_HUMAN Reviewed; 137 AA. AC Q8IXM3; Q96Q49; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 161. DE RecName: Full=Large ribosomal subunit protein mL41 {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L41, mitochondrial; DE Short=L41mt; DE Short=MRP-L41; DE AltName: Full=Bcl-2-interacting mitochondrial ribosomal protein L41; DE AltName: Full=Cell proliferation-inducing gene 3 protein; DE AltName: Full=MRP-L27 homolog; DE Flags: Precursor; GN Name=MRPL41; Synonyms=BMRP, MRPL27, RPML27; ORFNames=PIG3; 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]. RA Kim J.W.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-135. 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 [5] RP IDENTIFICATION. 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 [6] RP INTERACTION WITH BCL2, AND TISSUE SPECIFICITY. RX PubMed=15547950; DOI=10.1002/jcb.20292; RA Chintharlapalli S.R., Jasti M., Malladi S., Parsa K.V.L., Ballestero R.P., RA Gonzalez-Garcia M.; RT "BMRP is a Bcl-2 binding protein that induces apoptosis."; RL J. Cell. Biochem. 94:611-626(2005). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16024796; DOI=10.1128/mcb.25.15.6603-6616.2005; RA Yoo Y.A., Kim M.J., Park J.K., Chung Y.M., Lee J.H., Chi S.-G., Kim J.S., RA Yoo Y.D.; RT "Mitochondrial ribosomal protein L41 suppresses cell growth in association RT with p53 and p27Kip1."; RL Mol. Cell. Biol. 25:6603-6616(2005). RN [8] RP FUNCTION. RX PubMed=16256947; DOI=10.1016/j.bbrc.2005.10.064; RA Kim M.J., Yoo Y.A., Kim H.J., Kang S., Kim Y.G., Kim J.S., Yoo Y.D.; RT "Mitochondrial ribosomal protein L41 mediates serum starvation-induced RT cell-cycle arrest through an increase of p21(WAF1/CIP1)."; RL Biochem. Biophys. Res. Commun. 338:1179-1184(2005). RN [9] 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 [10] 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 [11] {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 [12] {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 [13] {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). RN [14] {ECO:0007744|PDB:7QH6, ECO:0007744|PDB:7QH7} RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) IN COMPLEX WITH MTLSU, AND RP SUBUNIT. RX PubMed=35177605; DOI=10.1038/s41467-022-28503-5; RA Rebelo-Guiomar P., Pellegrino S., Dent K.C., Sas-Chen A., RA Miller-Fleming L., Garone C., Van Haute L., Rogan J.F., Dinan A., RA Firth A.E., Andrews B., Whitworth A.J., Schwartz S., Warren A.J., RA Minczuk M.; RT "A late-stage assembly checkpoint of the human mitochondrial ribosome large RT subunit."; RL Nat. Commun. 13:929-929(2022). CC -!- FUNCTION: Component of the mitochondrial ribosome large subunit CC (PubMed:25278503, PubMed:25838379, PubMed:28892042, PubMed:35177605). CC Also involved in apoptosis and cell cycle (PubMed:16024796, CC PubMed:16256947). Enhances p53/TP53 stability, thereby contributing to CC p53/TP53-induced apoptosis in response to growth-inhibitory condition. CC Enhances p53/TP53 translocation to the mitochondria. Has the ability to CC arrest the cell cycle at the G1 phase, possibly by stabilizing the CC CDKN1A and CDKN1B (p27Kip1) proteins (PubMed:16024796). CC {ECO:0000269|PubMed:16024796, ECO:0000269|PubMed:16256947, CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042, ECO:0000269|PubMed:35177605}. CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt- CC LSU). Mature mammalian 55S mitochondrial ribosomes consist of a small CC (28S) and a large (39S) subunit. The 28S small subunit contains a 12S CC ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large CC subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial CC valine transfer RNA (mt-tRNA(Val)), which plays an integral structural CC role, and 52 different proteins (PubMed:11551941, PubMed:25278503, CC PubMed:25838379). Interacts with BCL2 (PubMed:15547950). CC {ECO:0000269|PubMed:15547950, ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000305|PubMed:11551941}. CC -!- INTERACTION: CC Q8IXM3; Q6PL24: TMED8; NbExp=3; IntAct=EBI-912501, EBI-11603430; CC Q8IXM3; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-912501, EBI-5661333; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16024796, CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042}. CC -!- TISSUE SPECIFICITY: Present in kidney, liver, thymus and testis, and at CC lower level in brain and spleen (at protein level). CC {ECO:0000269|PubMed:15547950}. CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein CC mL41 family. {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; AY232291; AAP69986.1; -; mRNA. DR EMBL; AL365502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC040035; AAH40035.1; -; mRNA. DR EMBL; AB051625; BAB54952.1; -; Genomic_DNA. DR CCDS; CCDS7046.1; -. DR RefSeq; NP_115866.1; NM_032477.3. DR PDB; 3J7Y; EM; 3.40 A; 9=1-137. DR PDB; 3J9M; EM; 3.50 A; 9=1-137. DR PDB; 5OOL; EM; 3.06 A; 9=1-137. DR PDB; 5OOM; EM; 3.03 A; 9=1-137. DR PDB; 6I9R; EM; 3.90 A; 9=1-137. DR PDB; 6NU2; EM; 3.90 A; 9=15-137. DR PDB; 6NU3; EM; 4.40 A; 9=1-137. DR PDB; 6VLZ; EM; 2.97 A; 9=1-137. DR PDB; 6VMI; EM; 2.96 A; 9=1-137. DR PDB; 6ZM5; EM; 2.89 A; 9=1-137. DR PDB; 6ZM6; EM; 2.59 A; 9=1-137. DR PDB; 6ZS9; EM; 4.00 A; 9=1-137. DR PDB; 6ZSA; EM; 4.00 A; 9=1-137. DR PDB; 6ZSB; EM; 4.50 A; 9=1-137. DR PDB; 6ZSC; EM; 3.50 A; 9=1-137. DR PDB; 6ZSD; EM; 3.70 A; 9=1-137. DR PDB; 6ZSE; EM; 5.00 A; 9=1-137. DR PDB; 6ZSG; EM; 4.00 A; 9=1-137. DR PDB; 7A5F; EM; 4.40 A; 93=1-137. DR PDB; 7A5G; EM; 4.33 A; 93=1-137. DR PDB; 7A5H; EM; 3.30 A; 9=1-137. DR PDB; 7A5I; EM; 3.70 A; 93=1-137. DR PDB; 7A5J; EM; 3.10 A; 9=1-137. DR PDB; 7A5K; EM; 3.70 A; 93=1-137. DR PDB; 7L08; EM; 3.49 A; 9=1-137. DR PDB; 7L20; EM; 3.15 A; 9=1-137. DR PDB; 7O9K; EM; 3.10 A; 9=1-137. DR PDB; 7O9M; EM; 2.50 A; 9=1-137. DR PDB; 7ODR; EM; 2.90 A; 9=1-137. DR PDB; 7ODS; EM; 3.10 A; 9=1-137. DR PDB; 7ODT; EM; 3.10 A; 9=1-137. DR PDB; 7OF0; EM; 2.20 A; 9=1-137. DR PDB; 7OF2; EM; 2.70 A; 9=1-137. DR PDB; 7OF3; EM; 2.70 A; 9=1-137. DR PDB; 7OF4; EM; 2.70 A; 9=1-137. DR PDB; 7OF5; EM; 2.90 A; 9=1-137. DR PDB; 7OF6; EM; 2.60 A; 9=1-137. DR PDB; 7OF7; EM; 2.50 A; 9=1-137. DR PDB; 7OG4; EM; 3.80 A; 9=1-137. DR PDB; 7OI6; EM; 5.70 A; 9=1-137. DR PDB; 7OI7; EM; 3.50 A; 9=1-137. DR PDB; 7OI8; EM; 3.50 A; 9=1-137. DR PDB; 7OI9; EM; 3.30 A; 9=1-137. DR PDB; 7OIA; EM; 3.20 A; 9=1-137. DR PDB; 7OIB; EM; 3.30 A; 9=1-137. DR PDB; 7OIC; EM; 3.10 A; 9=1-137. DR PDB; 7OID; EM; 3.70 A; 9=1-137. DR PDB; 7OIE; EM; 3.50 A; 9=1-137. DR PDB; 7PD3; EM; 3.40 A; 9=1-137. DR PDB; 7PO4; EM; 2.56 A; 9=1-137. DR PDB; 7QH6; EM; 3.08 A; 9=1-137. DR PDB; 7QH7; EM; 2.89 A; 9=15-137. DR PDB; 7QI4; EM; 2.21 A; 9=1-137. DR PDB; 7QI5; EM; 2.63 A; 9=1-137. DR PDB; 7QI6; EM; 2.98 A; 9=1-137. DR PDB; 8ANY; EM; 2.85 A; 9=1-137. DR PDB; 8K2A; EM; 2.90 A; Lo=1-137. DR PDB; 8K2B; EM; 3.40 A; Lo=1-137. DR PDB; 8OIR; EM; 3.10 A; Bq=1-137. DR PDB; 8OIT; EM; 2.90 A; Bq=1-137. DR PDB; 8PK0; EM; 3.03 A; 9=1-137. DR PDB; 8QSJ; EM; 3.00 A; 9=1-137. DR PDB; 8QU5; EM; 2.42 A; 9=1-137. DR PDB; 8RRI; EM; 2.40 A; 9=1-137. DR PDB; 8XT0; EM; 3.20 A; Lo=1-137. DR PDB; 8XT1; EM; 3.10 A; Lo=1-137. DR PDB; 8XT2; EM; 3.30 A; Lo=1-137. DR PDB; 8XT3; EM; 3.10 A; Lo=1-137. DR PDB; 9CN3; EM; 2.62 A; 9=1-137. DR PDB; 9UWH; EM; 3.00 A; 9=1-137. DR AlphaFoldDB; Q8IXM3; -. 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-17719; -. DR EMDB; EMD-19460; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-23121; -. DR EMDB; EMD-36836; -. DR EMDB; EMD-36837; -. DR EMDB; EMD-3842; -. DR EMDB; EMD-3843; -. DR EMDB; EMD-38632; -. DR EMDB; EMD-38633; -. DR EMDB; EMD-38634; -. DR EMDB; EMD-38635; -. DR EMDB; EMD-4434; -. DR EMDB; EMD-45757; -. DR EMDB; EMD-64554; -. DR EMDB; EMD-70592; -. DR EMDB; EMD-71623; -. DR EMDB; EMD-71630; -. DR EMDB; EMD-71633; -. DR EMDB; EMD-71634; -. DR EMDB; EMD-71635; -. DR EMDB; EMD-71797; -. DR EMDB; EMD-71802; -. DR EMDB; EMD-71809; -. DR EMDB; EMD-71811; -. DR EMDB; EMD-71815; -. DR EMDB; EMD-71818; -. DR EMDB; EMD-71825; -. DR EMDB; EMD-71828; -. DR EMDB; EMD-71829; -. DR SMR; Q8IXM3; -. DR BioGRID; 122363; 222. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q8IXM3; -. DR FunCoup; Q8IXM3; 852. DR IntAct; Q8IXM3; 114. DR MINT; Q8IXM3; -. DR NDEx; MUSIC2-C5209-MRPL41; Osteosarcoma (U2OS) cell map - Mitochondrial large ribosomal subunit (32 proteins). DR STRING; 9606.ENSP00000360498; -. DR GlyGen; Q8IXM3; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8IXM3; -. DR PhosphoSitePlus; Q8IXM3; -. DR BioMuta; MRPL41; -. DR DMDM; 74750734; -. DR jPOST; Q8IXM3; -. DR MassIVE; Q8IXM3; -. DR PaxDb; 9606-ENSP00000360498; -. DR PeptideAtlas; Q8IXM3; -. DR ProteomicsDB; 71029; -. DR Pumba; Q8IXM3; -. DR TopDownProteomics; Q8IXM3; -. DR Antibodypedia; 19072; 153 antibodies from 25 providers. DR DNASU; 64975; -. DR Ensembl; ENST00000371443.6; ENSP00000360498.5; ENSG00000182154.8. DR GeneID; 64975; -. DR KEGG; hsa:64975; -. DR MANE-Select; ENST00000371443.6; ENSP00000360498.5; NM_032477.3; NP_115866.1. DR UCSC; uc004cnh.5; human. DR AGR; HGNC:14492; -. DR ClinPGx; PA30973; -. DR CTD; 64975; -. DR DisGeNET; 64975; -. DR GeneCards; MRPL41; -. DR HGNC; HGNC:14492; MRPL41. DR HPA; ENSG00000182154; Tissue enhanced (heart). DR MIM; 611846; gene. DR OpenTargets; ENSG00000182154; -. DR VEuPathDB; HostDB:ENSG00000182154; -. DR eggNOG; KOG4756; Eukaryota. DR GeneTree; ENSGT00390000013158; -. DR HOGENOM; CLU_155983_0_0_1; -. DR InParanoid; Q8IXM3; -. DR OMA; DRMSAWT; -. DR OrthoDB; 408933at2759; -. DR PAN-GO; Q8IXM3; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q8IXM3; -. DR PathwayCommons; Q8IXM3; -. 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 Reactome; R-HSA-9937383; Mitochondrial ribosome-associated quality control. DR SignaLink; Q8IXM3; -. DR SIGNOR; Q8IXM3; -. DR Agora; ENSG00000182154; -. DR BioGRID-ORCS; 64975; 544 hits in 1167 CRISPR screens. DR ChiTaRS; MRPL41; human. DR EvolutionaryTrace; Q8IXM3; -. DR GeneWiki; Mitochondrial_ribosomal_protein_L41; -. DR GenomeRNAi; 64975; -. DR Pharos; Q8IXM3; Tbio. DR PRO; PR:Q8IXM3; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q8IXM3; protein. DR Bgee; ENSG00000182154; Expressed in apex of heart and 182 other cell types or tissues. 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:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; IDA:UniProtKB. DR InterPro; IPR019189; Ribosomal_mL41. DR PANTHER; PTHR21338:SF0; LARGE RIBOSOMAL SUBUNIT PROTEIN ML41; 1. DR PANTHER; PTHR21338; MITOCHONDRIAL RIBOSOMAL PROTEIN L41; 1. DR Pfam; PF09809; MRP-L27; 1. 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; 8K2A; -. DR PDBsum; 8K2B; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR PDBsum; 8PK0; -. DR PDBsum; 8QSJ; -. DR PDBsum; 8QU5; -. DR PDBsum; 8RRI; -. DR PDBsum; 8XT0; -. DR PDBsum; 8XT1; -. DR PDBsum; 8XT2; -. DR PDBsum; 8XT3; -. DR PDBsum; 9CN3; -. DR PDBsum; 9UWH; -. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Cell cycle; Mitochondrion; KW Proteomics identification; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Transit peptide. FT TRANSIT 1..13 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 14..137 FT /note="Large ribosomal subunit protein mL41" FT /id="PRO_0000273228" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:7QI4" FT TURN 23..25 FT /evidence="ECO:0007829|PDB:7OF7" FT HELIX 28..33 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:7A5H" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:6ZM6" FT HELIX 88..95 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 97..105 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:7PO4" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 123..128 FT /evidence="ECO:0007829|PDB:7O9M" FT TURN 130..133 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 137 AA; 15383 MW; 25A9F3105ABF1189 CRC64; MGVLAAAARC LVRGADRMSK WTSKRGPRSF RGRKGRGAKG IGFLTSGWRF VQIKEMVPEF VVPDLTGFKL KPYVSYLAPE SEETPLTAAQ LFSEAVAPAI EKDFKDGTFD PDNLEKYGFE PTQEGKLFQL YPRNFLR //