Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Manual transfer of experimentally-verified manual GO annotation data to homologous complexes by curator judgment of sequence, composition and function similarity
Combined Automated Annotation using Multiple IEA Methods.
Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing.
Large-scale mapping of human protein-protein interactions by mass spectrometry.
Defining the membrane proteome of NK cells.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
Structures of the human and Drosophila 80S ribosome.
Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.
Structure of the human 80S ribosome.
Structural snapshots of actively translating human ribosomes.
Expression of Muscle-Specific Ribosomal Protein L3-Like Impairs Myotube Growth.
Architecture of the human interactome defines protein communities and disease networks.
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
Structural snapshots of human pre-60S ribosomal particles before and after nuclear export.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances Muscle Function in Healthy and Dystrophic Mice.
A male germ-cell-specific ribosome controls male fertility.
A map of 75 human ribosomal protein genes.
Dissociation of L13a from the 60s ribosomal subunit
Nascent polypeptide:mRNA:ribosome complex binds signal recognition particle (SRP)
Synthesis of nascent polypeptide containing signal sequence
12S pre-rRNA is nucleolytically processed to yield 5.8S rRNA
eIF5B:GTP is hydrolyzed and released
The 60S subunit joins the translation initiation complex
Release of 40S and 60S subunits from the 80S ribosome
Formation of UPF1:eRF3 complex on mRNA with a premature termination codon and no Exon Junction Complex
p-4S-UPF1 recruits SMG5, SMG7, SMG6, PNRC2, DCP1A, and PP2A
UPF1 binds an mRNP with a termination codon preceding an Exon Junction Complex
SMG6 hydrolyzes mRNA with premature termination codon
SMG1 phosphorylates UPF1 (enhanced by Exon Junction Complex)
Deep research on RPL18A function
Comprehensive deep research on RPL18A from Perplexity
Comprehensive deep research on RPL18A from OpenAI
Falcon deep research report on RPL18A
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RPL18A (eL20) is a structural ribosomal protein of the cytosolic 60S large
ribosomal subunit; ribosomal proteins stabilize rRNA structure, contribute
to assembly, and support translation as part of the ribosome's structural framework.
"RPL18A/eL20 is a ribosomal protein of the **cytosolic 60S large ribosomal subunit**. Ribosomal proteins stabilize rRNA structure, contribute to assembly, and support translation by forming part of the ribosome’s structural framework."
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Eukaryotic ribosome assembly is a multi-compartment process beginning in the
nucleolus, continuing in the nucleoplasm, and completed after export to the
cytoplasm, providing the expected localization itinerary for RPL18A during assembly.
"Eukaryotic ribosome assembly is a multi-compartment process that **begins in the nucleolus**, continues in the **nucleoplasm**, and is completed after export to the **cytoplasm** for final maturation. This provides the expected cellular itinerary for all cytosolic ribosomal proteins (including RPL18A) during assembly, even when a specific RPL18A localization experiment is not available."
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The best-supported localization model combines transient nuclear/nucleolar
localization during biogenesis followed by predominantly cytoplasmic
localization as part of mature 60S/80S ribosomes engaged in translation.
"- **Transient nuclear/nucleolar localization during ribosome biogenesis**, followed by
- **Predominantly cytoplasmic localization as part of mature 60S/80S ribosomes engaged in translation**."
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eL20 (RPL18A) can interact with hepatitis C virus (HCV) IRES RNA, and adding
eL20 protein to in vitro translation extracts moderately stimulated HCV IRES
activity, supporting RNA interaction capability beyond a purely passive structural role.
"eL20 (RPL18A)** can **interact with hepatitis C virus (HCV) IRES RNA** and that adding eL20 protein to **in vitro translation extracts** **moderately stimulated HCV IRES activity**. This supports a capacity for RPL18A/eL20 to contribute to specialized modes of translation initiation involving structured RNAs, beyond a purely passive structural role."
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Orthology evidence (C. elegans rpl-20) shows a missense substitution in eL20
reduces biogenesis of the 60S subunit and 80S ribosomes, and a deletion allele
is homozygous early larval lethal, supporting an essential role for eL20 in
60S biogenesis and organismal viability.
"an amino-acid substitution in this protein is associated with **reduced biogenesis of the 60S subunit**, leading to **reduced 80S ribosomes**. The same paper reports that a deletion allele removing the coding region is **homozygous early larval lethal**, supporting an essential role for the eL20 family protein in organismal viability consistent with fundamental ribosome function."
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60S ribosomal protein deficiency exerts stronger growth-inhibitory effects than
40S RP deficiency and acts through p53 signaling, providing pathway context for
RPL18A perturbation in ribosomal/nucleolar stress responses.
"**60S RP deficiency** was reported to exert stronger growth-inhibitory effects than 40S RP deficiency and to act through **p53 signaling**"
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A 2023 Cell chemical-proteomics study identified a ROS-controlled cysteine site
(C22) in RPL18A among sites for ROS-controlled translation, suggesting possible
redox-linked post-translational modulation rather than a change to its core
ribosomal identity.
"RPL18A contained a ROS-controlled cysteine site (C22) identified among sites for ROS-controlled translation in the study’s integrated proteogenomic framework"