RL39_HUMAN
ID RL39_HUMAN Reviewed; 51 AA.
AC P62891; P02404; P39025; Q9BYF2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=60S ribosomal protein L39;
DE AltName: Full=Large ribosomal subunit protein eL39 {ECO:0000303|PubMed:24524803};
GN Name=RPL39;
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=Heart;
RX PubMed=8908372; DOI=10.1080/15216549600201203;
RA Tsui S.K.W., Lee S.M.Y., Fung K.P., Waye M.M.Y., Lee C.Y.;
RT "Primary structures and sequence analysis of human ribosomal proteins L39
RT and S27.";
RL Biochem. Mol. Biol. Int. 40:611-616(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Colon;
RX PubMed=8764829; DOI=10.1016/0167-4781(96)00106-6;
RA Otsuka S., Tanaka M., Saito S., Yoshimoto K., Itakura M.;
RT "Molecular cloning of a cDNA encoding human ribosomal protein L39.";
RL Biochim. Biophys. Acta 1308:119-121(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=11401437; DOI=10.1006/geno.2000.6470;
RA Uechi T., Tanaka T., Kenmochi N.;
RT "A complete map of the human ribosomal protein genes: assignment of 80
RT genes to the cytogenetic map and implications for human disorders.";
RL Genomics 72:223-230(2001).
RN [6]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [8] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: RNA-binding component of the large ribosomal subunit. The
CC ribosome is a large ribonucleoprotein complex responsible for the
CC synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000269|PubMed:8764829}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). Interacts with IMPACT (By similarity).
CC {ECO:0000250|UniProtKB:P62892, ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family.
CC {ECO:0000305}.
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DR EMBL; U57846; AAB02265.1; -; mRNA.
DR EMBL; D79205; BAA11465.1; -; mRNA.
DR EMBL; AB061835; BAB79473.1; -; Genomic_DNA.
DR EMBL; BC001019; AAH01019.1; -; mRNA.
DR EMBL; BC070205; AAH70205.1; -; mRNA.
DR EMBL; AB046411; BAB21257.1; -; Genomic_DNA.
DR CCDS; CCDS14586.1; -.
DR PIR; G02654; G02654.
DR RefSeq; NP_000991.1; NM_001000.3.
DR PDB; 4UG0; EM; -; Ll=1-51.
DR PDB; 4V6X; EM; 5.00 A; Cl=1-51.
DR PDB; 5AJ0; EM; 3.50 A; Al=1-51.
DR PDB; 5LKS; EM; 3.60 A; Ll=1-51.
DR PDB; 5T2C; EM; 3.60 A; f=1-51.
DR PDB; 6IP5; EM; 3.90 A; 2f=1-51.
DR PDB; 6IP6; EM; 4.50 A; 2f=1-51.
DR PDB; 6IP8; EM; 3.90 A; 2f=1-51.
DR PDB; 6LQM; EM; 3.09 A; P=1-51.
DR PDB; 6LSR; EM; 3.13 A; P=1-51.
DR PDB; 6LSS; EM; 3.23 A; P=1-51.
DR PDB; 6LU8; EM; 3.13 A; P=1-51.
DR PDB; 6OLE; EM; 3.10 A; m=2-51.
DR PDB; 6OLF; EM; 3.90 A; m=2-51.
DR PDB; 6OLG; EM; 3.40 A; Al=2-51.
DR PDB; 6OLI; EM; 3.50 A; m=2-51.
DR PDB; 6OLZ; EM; 3.90 A; Al=2-51.
DR PDB; 6OM0; EM; 3.10 A; m=2-51.
DR PDB; 6OM7; EM; 3.70 A; m=2-51.
DR PDB; 6QZP; EM; 2.90 A; Ll=2-51.
DR PDB; 6W6L; EM; 3.84 A; m=1-51.
DR PDB; 6XA1; EM; 2.80 A; Ll=2-51.
DR PDB; 6Y0G; EM; 3.20 A; Ll=1-51.
DR PDB; 6Y2L; EM; 3.00 A; Ll=1-51.
DR PDB; 6Y57; EM; 3.50 A; Ll=1-51.
DR PDB; 6Y6X; EM; 2.80 A; Ll=2-51.
DR PDB; 6Z6L; EM; 3.00 A; Ll=1-51.
DR PDB; 6Z6M; EM; 3.10 A; Ll=1-51.
DR PDB; 6Z6N; EM; 2.90 A; Ll=1-51.
DR PDB; 6ZM7; EM; 2.70 A; Ll=1-51.
DR PDB; 6ZME; EM; 3.00 A; Ll=1-51.
DR PDB; 6ZMI; EM; 2.60 A; Ll=1-51.
DR PDB; 6ZMO; EM; 3.10 A; Ll=1-51.
DR PDB; 7BHP; EM; 3.30 A; Ll=1-51.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P62891; -.
DR SMR; P62891; -.
DR BioGRID; 112089; 73.
DR CORUM; P62891; -.
DR IntAct; P62891; 37.
DR MINT; P62891; -.
DR STRING; 9606.ENSP00000355315; -.
DR GlyGen; P62891; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62891; -.
DR PhosphoSitePlus; P62891; -.
DR BioMuta; RPL39; -.
DR DMDM; 51702812; -.
DR EPD; P62891; -.
DR jPOST; P62891; -.
DR MassIVE; P62891; -.
DR MaxQB; P62891; -.
DR PaxDb; P62891; -.
DR PeptideAtlas; P62891; -.
DR PRIDE; P62891; -.
DR ProteomicsDB; 57446; -.
DR TopDownProteomics; P62891; -.
DR Antibodypedia; 29833; 160 antibodies from 26 providers.
DR DNASU; 6170; -.
DR Ensembl; ENST00000361575.4; ENSP00000355315.3; ENSG00000198918.8.
DR GeneID; 6170; -.
DR KEGG; hsa:6170; -.
DR MANE-Select; ENST00000361575.4; ENSP00000355315.3; NM_001000.4; NP_000991.1.
DR UCSC; uc004erx.3; human.
DR CTD; 6170; -.
DR DisGeNET; 6170; -.
DR GeneCards; RPL39; -.
DR HGNC; HGNC:10350; RPL39.
DR HPA; ENSG00000198918; Low tissue specificity.
DR MIM; 300899; gene.
DR neXtProt; NX_P62891; -.
DR OpenTargets; ENSG00000198918; -.
DR PharmGKB; PA34743; -.
DR VEuPathDB; HostDB:ENSG00000198918; -.
DR eggNOG; KOG0002; Eukaryota.
DR GeneTree; ENSGT00390000014814; -.
DR HOGENOM; CLU_181948_3_0_1; -.
DR InParanoid; P62891; -.
DR OMA; MKRRHWR; -.
DR OrthoDB; 1618745at2759; -.
DR PhylomeDB; P62891; -.
DR TreeFam; TF300223; -.
DR PathwayCommons; P62891; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62891; -.
DR SIGNOR; P62891; -.
DR BioGRID-ORCS; 6170; 28 hits in 208 CRISPR screens.
DR ChiTaRS; RPL39; human.
DR GeneWiki; RPL39; -.
DR GenomeRNAi; 6170; -.
DR Pharos; P62891; Tbio.
DR PRO; PR:P62891; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P62891; protein.
DR Bgee; ENSG00000198918; Expressed in ganglionic eminence and 97 other tissues.
DR Genevisible; P62891; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:UniProtKB.
DR Gene3D; 1.10.1620.10; -; 1.
DR HAMAP; MF_00629; Ribosomal_L39e; 1.
DR InterPro; IPR000077; Ribosomal_L39.
DR InterPro; IPR020083; Ribosomal_L39_CS.
DR InterPro; IPR023626; Ribosomal_L39e_dom_sf.
DR Pfam; PF00832; Ribosomal_L39; 1.
DR SUPFAM; SSF48662; SSF48662; 1.
DR PROSITE; PS00051; RIBOSOMAL_L39E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..51
FT /note="60S ribosomal protein L39"
FT /id="PRO_0000127024"
SQ SEQUENCE 51 AA; 6407 MW; 2023CA8590C7752C CRC64;
MSSHKTFRIK RFLAKKQKQN RPIPQWIRMK TGNKIRYNSK RRHWRRTKLG L
