See More

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": []}; RPS0A Homology | SGD

AboutBlogDownloadExploreHelpGet Data

RPS0A / YGR214W Homology

Standard Name
RPS0A 1
Systematic Name
YGR214W
SGD ID
SGD:S000003446
Aliases
NAB1 1 , NAB1A 1 , YST1 3 , S0A 17 , S2 6 , uS2 18
Feature Type
ORF , Verified
Description
Ribosomal 40S subunit protein S0A; required for maturation of 18S rRNA along with Rps0Bp; deletion of either RPS0 gene reduces growth rate, deletion of both genes is lethal; homologous to human ribosomal protein SA and bacterial S2; RPS0A has a paralog, RPS0B, that arose from the whole genome duplication; 2 3 4 5 6
Name Description
Ribosomal Protein of the Small subunit 1
Paralog
RPS0B 5
Comparative Info

Homologs

Homology calls are sourced from the Alliance of Genome Resources. Many aspects of data integration presented at the Alliance require a common set of orthology relationships among genes for the organisms represented, including human. The Alliance provides the results of all methods that have been benchmarked by the Quest for Orthologs Consortium (QfO). The homolog inferences from the different methods have been integrated using the DRSC Integrative Ortholog Prediction Tool (DIOPT), which integrates a number of existing methods including those used by the Alliance: Ensembl Compara, HGNC, Hieranoid, InParanoid, OMA, OrthoFinder, OrthoInspector, PANTHER, PhylomeDB, Roundup, TreeFam, and ZFIN.

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.

Species Gene ID Gene name Source

Functional Complementation

Information about cross-species functional complementation between yeast and other species, curated by SGD and the Princeton Protein Orthology Database (P-POD).

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 Species Gene ID Strain background Direction Details Source Reference

Fungal Homologs

Fungal Homology calls are sourced from AllianceMine, which compiles fungal homology calls from FungiDB, CGD, Panther, PomBase, TreeFam, HomoloGene, and SGD.

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.

Species Gene ID Gene name Description Source

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

S288C only

BLASTN | BLASTP | Design Primers | Restriction Fragment Map | Restriction Fragment Sizes | Six-Frame Translation

S288C vs. other species

BLASTN vs. fungi | BLASTP at NCBI | BLASTP vs. fungi

S288C vs. other strains

Strain Alignment | Variant Viewer

© Stanford University, Stanford, CA 94305.