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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": []} RPS0A Gene Ontology | SGD

Gene Ontology Help

RPS0A / YGR214W Gene Ontology

GO Annotations consist of four mandatory components: a gene product, a term from one of the three Gene Ontology (GO) controlled vocabularies (Molecular Function, Biological Process, and Cellular Component), a reference, and an evidence code. SGD has manually curated and high-throughput GO Annotations, both derived from the literature, as well as computational, or predicted, annotations.


Summary
Subunit of the cytosolic small ribosomal subunit; involved in rRNA processing and export from the nucleus, assembly of the small ribosomal subunit, and translation
GO Slim Terms

The yeast GO Slim terms are higher level terms that best represent the major S. cerevisiae biological processes, functions, and cellular components. The GO Slim terms listed here are the broader parent terms for the specific terms to which this gene product is annotated, and thus represent the more general processes, functions, and components in which it is involved.

structural constituent of ribosome, structural molecule activity, biosynthetic process, cellular component assembly, cytoplasmic translation, nuclear transport, nucleocytoplasmic transport, protein-RNA complex assembly, protein-containing complex assembly, rRNA processing, ribosomal subunit export from nucleus, translation, transport, organelle, 90S preribosome, cytoplasmic stress granule, cytosolic small ribosomal subunit, intracellular membraneless organelle, preribosome, ribonucleoprotein complex, small ribosomal subunit

Manually Curated

Manually curated GO annotations reflect our best understanding of the basic molecular function, biological process, and cellular component for this gene product. Manually curated annotations are assigned by SGD curators based on published papers when available, or by curatorial statements if necessary. Curators periodically review all manually curated GO annotations for accuracy and completeness.


Biological Process

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Molecular Function

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Cellular Component

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

High-throughput

GO annotations from high-throughput experiments are based on a variety of large scale high-throughput experiments, including genome-wide experiments. Many of these annotations are made based on GO annotations (or mappings to GO annotations) assigned by the authors, rather than SGD curators. While SGD curators read these publications and often work closely with authors to incorporate the information, each individual annotation may not necessarily be reviewed by a curator. GO annotations from high-throughput experiments will be assigned only when this type of data is available, and thus may not be assigned to terms from all three controlled vocabularies of the Gene Ontology.


Biological Process

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Molecular Function

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Cellular Component

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Computational

Computational GO Annotations are predictions. These annotations are NOT reviewed by a curator. Currently, all computational GO annotations for S. cerevisiae are assigned by an external source (for example, the Gene Ontology Annotation (GOA) project of the European Bioinformatics Institute (EBI)).


Biological Process

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Molecular Function

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Cellular Component

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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

Shared Annotations

This diagram displays manually curated and high-throughput GO terms (green squares) that are shared between the given gene (yellow circle) and other genes (gray circles) based on the number of GO terms shared (adjustable using the slider at the bottom).


Reset

Click on a gene or Biological Process GO term name to go to its specific page within SGD; drag any of the gene or GO term name objects around within the visualization for easier viewing; click “Reset” to automatically redraw the diagram; filter the genes that share GO Biological Process terms with the given gene by the number of terms they share by clicking anywhere on the slider bar or dragging the tab to the desired filter number.


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