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Ribosomes are highly conserved large ribonucleoprotein (RNP) particles, consisting in yeast of a large 60S subunit and a small 40S subunit, that perform protein synthesis. Yeast ribosomes contain one copy each of four ribosomal RNAs (5S, 5.8S, 18S, and 25S; produced in two separate transcripts encoded within the rDNA repeat present as hundreds of copies on Chromosome 12) and 79 different ribosomal proteins (r-proteins), which are encoded by 137 different genes scattered about the genome, 59 of which are duplicated (7, 6). The 60S subunit contains 46 proteins and three RNA molecules: 25S RNA of 3392 nt, hydrogen bonded to the 5.8S RNA of 158 nt and associated with the 5S RNA of 121 nt. The 40S subunit has a single 18S RNA of 1798 nt and 33 proteins (8, 6). All yeast ribosomal proteins have a mammalian homolog (1).

In a rapidly growing yeast cell, 60% of total transcription is devoted to ribosomal RNA, and 50% of RNA polymerase II transcription and 90% of mRNA splicing are devoted to the production of mRNAs for r-proteins. Coordinate regulation of the rRNA genes and 137 r-protein genes is affected by nutritional cues and a number of signal transduction pathways that can abruptly induce or silence the ribosomal genes, whose transcripts have naturally short lifetimes, leading to major implications for the expression of other genes as well (9, 10, 11). The expression of some r-protein genes is influenced by Abf1p (12), and most are directly induced by binding of Rap1p to their promoters, which excludes nucleosomes and recruits Fhl1p and Ifh1p to drive transcription (13).

Ribosome assembly is a complex process, with different steps occurring in different parts of the cell. Ribosomal protein genes are transcribed in the nucleus, and the mRNA is transported to the cytoplasm for translation. The newly synthesized r-proteins then enter the nucleus and associate in the nucleolus with the two rRNA transcripts, one of which is methylated and pseudouridylated (view sites of modifications), and then cleaved into three individual rRNAs (18S, 5.8S, and 25S) as part of the assembly process (7). Separate ribosomal subunits are then transported from the nucleolus to the cytoplasm where they assemble into mature ribosomes before functioning in translation (14, 15). Blockage of subunit assembly, such as due to inhibition of rRNA synthesis or processing, results in degradation of newly synthesized r-proteins (16, 15). (For more information on the early steps of rRNA processing and small ribosomal subunit assembly, see the summary paragraph for the U3 snoRNA, encoded by snR17A and snR17B.)", "date_edited": "2007-02-14"}, "literature_overview": {"primary_count": 18, "additional_count": 77, "review_count": 10, "go_count": 6, "phenotype_count": 1, "disease_count": 0, "interaction_count": 101, "regulation_count": 8, "ptm_count": 6, "funComplement_count": 0, "htp_count": 36, "total_count": 233}, "disease_overview": {"manual_disease_terms": [], "htp_disease_terms": [], "computational_annotation_count": 0, "date_last_reviewed": null}, "ecnumbers": [], "URS_ID": null, "main_strain": "S288C", "regulation_overview": {"regulator_count": 25, "target_count": 0}, "reference_mapping": {"556638": 1, "633510": 2, "631251": 3, "548623": 4, "526423": 5, "397935": 6, "592595": 7, "517471": 8, "631529": 9, "554134": 10, "585697": 11, "608664": 12, "518051": 13, "592541": 14, "508692": 15, "508689": 16, "592544": 17, "316136": 18}, "history": [{"category": "Name", "history_type": "LSP", "note": "Name: RPS0A", "date_created": "2000-05-19", "references": [{"id": 556638, "display_name": "Mager WH, et al. (1997)", "citation": "Mager WH, et al. (1997) A new nomenclature for the cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Nucleic Acids Res 25(24):4872-5", "pubmed_id": 9396790, "link": "/reference/S000071623", "year": 1997, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1093/nar/25.24.4872"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC147144/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9396790"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: S0A", "date_created": "2010-02-16", "references": [{"id": 592544, "display_name": "Planta RJ and Mager WH (1998)", "citation": "Planta RJ and Mager WH (1998) The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Yeast 14(5):471-7", "pubmed_id": 9559554, "link": "/reference/S000058461", "year": 1998, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1002/(SICI)1097-0061(19980330)14:5<471::AID-YEA241>3.0.CO;2-U"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9559554"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: NAB1", "date_created": "2010-02-16", "references": [{"id": 556638, "display_name": "Mager WH, et al. (1997)", "citation": "Mager WH, et al. (1997) A new nomenclature for the cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Nucleic Acids Res 25(24):4872-5", "pubmed_id": 9396790, "link": "/reference/S000071623", "year": 1997, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1093/nar/25.24.4872"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC147144/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9396790"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: NAB1A", "date_created": "2010-02-16", "references": [{"id": 556638, "display_name": "Mager WH, et al. (1997)", "citation": "Mager WH, et al. (1997) A new nomenclature for the cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Nucleic Acids Res 25(24):4872-5", "pubmed_id": 9396790, "link": "/reference/S000071623", "year": 1997, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1093/nar/25.24.4872"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC147144/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9396790"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: YST1", "date_created": "2010-02-16", "references": [{"id": 631251, "display_name": "Demianova M, et al. (1996)", "citation": "Demianova M, et al. (1996) Yeast proteins related to the p40/laminin receptor precursor are essential components of the 40 S ribosomal subunit. J Biol Chem 271(19):11383-91", "pubmed_id": 8626693, "link": "/reference/S000045335", "year": 1996, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1074/jbc.271.19.11383"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/8626693"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: uS2", "date_created": "2016-08-09", "references": [{"id": 316136, "display_name": "Ban N, et al. (2014)", "citation": "Ban N, et al. (2014) A new system for naming ribosomal proteins. Curr Opin Struct Biol 24:165-9", "pubmed_id": 24524803, "link": "/reference/S000182084", "year": 2014, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/j.sbi.2014.01.002"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4358319/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/24524803"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: S2", "date_created": "2012-09-15", "references": [{"id": 397935, "display_name": "Jenner L, et al. (2012)", "citation": "Jenner L, et al. (2012) Crystal structure of the 80S yeast ribosome. Curr Opin Struct Biol 22(6):759-67", "pubmed_id": 22884264, "link": "/reference/S000150523", "year": 2012, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/j.sbi.2012.07.013"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/22884264"}]}]}, {"category": "Mapping", "history_type": "SEQUENCE", "note": "Mapping: Edition 13: YST1 (RPS0A) is 97% identical to YST2 (RPS0B) at the amino acid level.", "date_created": "1996-09-21", "references": [{"id": 542519, "display_name": "Cherry JM, et al. (1996)", "citation": "Cherry JM, et al. (1996) \"Genetic and Physical Maps of Saccharomyces cerevisiae (Edition 13)\". Pp. 361-364 in 1996 Yeast Genetics and Molecular Biology Meeting Program and Abstracts. Bethesda, MD: The Genetics Society of America", "pubmed_id": null, "link": "/reference/S000076283", "year": 1996, "urls": []}]}, {"category": "Mapping", "history_type": "SEQUENCE", "note": "Mapping: Edition 13: This gene was previously called NAB1A and NAB1", "date_created": "1996-09-21", "references": [{"id": 542519, "display_name": "Cherry JM, et al. (1996)", "citation": "Cherry JM, et al. (1996) \"Genetic and Physical Maps of Saccharomyces cerevisiae (Edition 13)\". Pp. 361-364 in 1996 Yeast Genetics and Molecular Biology Meeting Program and Abstracts. Bethesda, MD: The Genetics Society of America", "pubmed_id": null, "link": "/reference/S000076283", "year": 1996, "urls": []}]}, {"category": "Nomenclature history", "history_type": "LSP", "note": "Nomenclature history: Both NPL3/YDR432W and RPS0A/YGR214W have been referred to as NAB1 in the literature.", "date_created": "2004-04-30", "references": []}], "complexes": []}; var domains_table_filename = "RPS0A_domains"; var alias_table_filename = "RPS0A_external_ids"; var domain_network_filename = "RPS0A_domain_network"; var properties_table_filename = "RPS0A_protein_properties"; var protein_experiment_table_filename = "RPS0A_experimental_data"; var protein_abundance_table_filename = "RPS0A_abundance_data"; var phosphorylation_table_filename = "RPS0A_phosphorylation"; var display_name = "RPS0A"; var format_name = "YGR214W"; var locus_id = "1285181"; function customize() { if (window.viewerInstance && viewerInstance.canvas) { viewerInstance.canvas.setBgColor({ r: 255, g: 255, b: 255 }); } } RPS0A Protein | SGD

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RPS0A / YGR214W Protein

Protein abundance data, domains, shared domains with other proteins, protein sequence retrieval for various strains, sequence-based physico-chemical properties, protein modification sites, and external identifiers for the protein.

Aliases
NAB1 1 , NAB1A 1 , YST1 3 , S0A 17 , S2 6 , uS2 18
Protein Product
40S ribosomal protein uS2 RPS0A
Feature Type
ORF , Verified
Paralog
RPS0B 5

AlphaFold Protein Structure

AlphaFold, developed by DeepMind, is an AI program that accurately predicts protein structures from amino acid sequences, enabling visualization of protein conformations. The predicted structures can be accessed through the Protein Data Bank (PDB) and AlphaFold Protein Structure Database.

Model Confidence

Very high
Confident
Low
Very low

Experimental Data

Contains experimentally-derived protein half-life data obtained using stable isotope labeling by amino acids (SILAC) coupled with mass spectrometry. This section also contains protein abundance data for both untreated and treated cells obtained from over 20 studies. These data have been normalized and converted to a common unit of molecules per cell.

Protein Half Life

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Gene Experiment Result Reference

Protein Abundance

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Gene Abundance (molecules/cell) Media Treatment Treatment time Fold Change Visualization Strain background Original Reference Reference

Domains and Classification - S288C

Collection of computationally identified domains and motifs, as determined by InterProScan analysis; includes protein coordinates for the domain, a domain Description, a Source and corresponding accession ID, and the number of S. cerevisiae genes that share the same domain.

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Gene Protein Coordinates Accession ID Description Source No. of Genes with Domain

Domain Locations

Visual representation of the locations of the domains within the protein, as listed in the Domains and Classification table. Each row displays the domain(s) derived from a different Source, with domains color-coded according to this Source.

Scroll over a domain to view its exact coordinates and its Description.

Shared Domains

This diagram displays domains (colored squares) shared between the given protein (yellow circle) and other proteins (gray circles); the domains are color-coded according to their source, as displayed in the Domain Locations table, above.

Reset

Click on a gene or domain name to go to its specific page within SGD; drag any of the gene or domain objects around within the visualization for easier viewing; click “Reset” to automatically redraw the diagram.

Alleles

Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.

View all RPS0A alleles in SGD search

Sequence

Protein sequence for the given gene in S288C and other strains, when available. Use the pull-down menu under "Strain" to select the sequence for a specific strain. The displayed sequence can be downloaded in FASTA format as a .txt file. Amino acids displayed in blue represent modification sites. More detailed evidence for these modification sites is presented in the Post-translational Modifications table, located just below the protein sequence.

* Blue amino acids indicate modification sites. More information below.

Post-translational Modifications -

Modification sites for the protein in the selected strain, based on the presence of a residue in the specific strain, as inferred from experimental evidence.

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Site Modification Modifier Reference

Sequence-Based Physico-chemical Properties - S288C

Calculated protein properties, including amino acid composition, length, coding region calculations, and atomic composition.

Amino Acid Composition

Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.

Amino Acid Frequency Percentage

Physical Details

Length (a.a):
Molecular Weight (Da):
Isoelectric Point (pl):
Formula:
Aliphatic Index:
Instability Index:

Coding Region Translation Calculations

Codon Bias:
Codon Adaptation Index:
Frequence of Optimal Codons:
Hydropathicity of Protein:
Aromaticity Score:

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines:
NO Cys residues appear as half cystines:

Atomic Composition

Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.

Atom Frequency Percentage

Data not found or not available for 

External Identifiers

List of external identifiers for the protein from various database sources.

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

External ID Source

Resources

Homologs

AGD | AnalogYeast | AspGD | BLASTP at NCBI | CGD | FungiDB | PhylomeDB | PomBase | PomBase | YGOB | YOGY

Protein Databases

AlphaFold Protein Structure | GPMDB | ModelArchive | Pfam domains | SUPERFAMILY | TopologYeast | UniProtKB

Localization

CYCLoPs | dHITS | LoQAtE | YeastGFP | YeastRC Public Images | YeastRGB | YPL+

Post-translational Modifications

PhosphoGRID | PhosphoPep

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