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The early stages of ribosome assembly occur in conjunction with processing of the 35S pre-ribosomal RNA transcript into the mature 18S, 5.8S, and 25S rRNA molecules. The first three cleavages at A0, A1, and A2 (see diagram) are essential for production of the 18S rRNA and the 40S small ribosomal subunit, but mutations which interfere with these cleavages have little effect on production of the 60S large ribosomal subunit (7). These three early cleavages occur in a series of large U3-associated ribonucleoprotein complexes (5, 9) and require base pairing of the U3 snoRNA with sequences in the 5'-ETS and the 18S rRNA (11, 13).

Click on the following figure for more details about the rDNA repeat and cleavage sites within the rRNA transcript:

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About the 90S preribosome and SSU processome complexes

A number of U3-containing early ribosome assembly and rRNA processing complexes have been identified that contain the 35S pre-rRNA transcript and have overlapping but not identical protein compositions (5, 9). Both the 90S preribosome and the small subunit (SSU) processome complexes contain ribosomal proteins, primarily of the small subunit, and non-ribosomal proteins presumably involved in rRNA processing and assembly of the small 40S ribsomal subunit. While many proteins are found in both complexes, some are found in only one or the other (see lists below). It may be that the 90S preribosome and SSU processome complexes are both intermediates in a series of complexes leading to the assembly of the small ribosomal subunit (5), or it may be that the SSU processome lies on an alternate assembly pathway (9).

The 90S preribosome complex is described as corresponding to the earliest detectable rRNA processing and ribosome assembly complex (6). The 90S is itself assembled from a number of stable subcomplexes including the t-UTP subcomplex (Utp5p, Utp4p, Nan1p, Utp8p, Utp9p, Utp10p, and Utp15p), the Pwp2p/UTP-B subcomplex (Utp6p, Pwp2p, Utp18p, Utp21p, Utp13p, and Dip2p) which interacts directly with the 5'-ETS of the 35S pre-rRNA (12), the UTP-C subcomplex (Rrp7p, Utp22p, Ckb1p, Cka1p, Ckb2p, and Cka2p), and the Mpp10 subcomplex (Mpp10p, Imp3p, and Imp4p) (15). The t-UTP subcomplex is also found as part of the SSU processome complex, which is slightly smaller at 80S (8, 1). Depletion of any of the members of the t-UTP subcomplex results in decreased transcription of rDNA leading to decreased levels of the primary 35S rRNA transcript (16). In contrast, mutation or depletion of most other members of either the 90S preribosome or SSU processome complexes causes decreased 18S rRNA levels without affecting the levels of the 25S or 5.8S rRNAs.

Non-ribosomal protein components of the 90S preribosome and SSU processome

Subunits of both the 90S preribosome (6) and SSU processome (8, 1) include: Bud21p, Dip2p, Ecm16p, Emg1p, Imp3p, Imp4p, Krr1p, Mpp10p, Nan1p, Noc4p, Nop1p, Nop14p, Nop58p, Pwp2p, Rrp5p, Rrp9p, Nop56p, Sof1p, Utp4p, Utp6p, Utp7p, Utp8p, Utp9p, Utp10p, Utp13p, Utp15p, Utp18p, Utp20p, Utp21p, and Utp22p

Additional subunits of the 90S preribosome (6) include: Bfr2p, Bms1p, Cbf5p, Cms1p, Dbp8p, Dim1p, Enp1p, Enp2p, Has1p, Kre33p, Mrd1p, Nop9p (10), Pno1p, Prp43p, Rcl1p, Rok1p, Rrp12p, Scl1p, Slx9p (14), Tsr1p, and Utp30p

Additional subunits of the SSU processome (8, 1) include: Fcf1p, Utp23p, Sas10p, Snu13p, Utp5p, Utp11p, and Utp14p", "date_edited": "2008-07-17"}, "literature_overview": {"primary_count": 9, "additional_count": 15, "review_count": 11, "go_count": 5, "phenotype_count": 2, "disease_count": 0, "interaction_count": 61, "regulation_count": 3, "ptm_count": 10, "funComplement_count": 0, "htp_count": 11, "total_count": 106}, "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": 3, "target_count": 0}, "reference_mapping": {"536153": 1, "467126": 2, "639860": 3, "367227": 4, "487996": 5, "528372": 6, "592595": 7, "560820": 8, "487987": 9, "495094": 10, "577538": 11, "536381": 12, "545434": 13, "511975": 14, "501066": 15, "511344": 16}, "history": [{"category": "Name", "history_type": "LSP", "note": "Name: ENP2", "date_created": "2002-08-13", "references": [{"id": 536153, "display_name": "Bernstein KA, et al. (2004)", "citation": "Bernstein KA, et al. (2004) The small-subunit processome is a ribosome assembly intermediate. Eukaryot Cell 3(6):1619-26", "pubmed_id": 15590835, "link": "/reference/S000079989", "year": 2004, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1128/EC.3.6.1619-1626.2004"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC539036/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/15590835"}]}]}, {"category": "Sequence change", "history_type": "SEQUENCE", "note": "Sequence change: A single nucleotide substitution within the coding region of ENP2/YGR145W resulted in an altered protein sequence. The start, stop, and reading frame remain the same, but protein residue 678 is now Aspartic Acid rather than Glutamic Acid.

\r\nNew    783751   ATTATAAATCCAGGCGTCATGATAATTCATCGGATGAAGAAGGTATTGACGAAAATGGTA  783810\r\n                ||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||\r\nOld    783756   ATTATAAATCCAGGCGTCATGATAATTCATCGGATGAAGAAGGTATTGAAGAAAATGGTA  783815\r\n", "date_created": "2011-02-03", "references": [{"id": 374815, "display_name": "Engel SR, et al. (2014)", "citation": "Engel SR, et al. (2014) The reference genome sequence of Saccharomyces cerevisiae: then and now. G3 (Bethesda) 4(3):389-98", "pubmed_id": 24374639, "link": "/reference/S000156273", "year": 2014, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1534/g3.113.008995"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962479/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/24374639"}]}]}], "complexes": [{"format_name": "CPX-1604", "display_name": "Small ribosomal subunit processome"}]},
        tabs: {"id": 1267112, "protein_tab": true, "interaction_tab": true, "summary_tab": true, "go_tab": true, "sequence_section": true, "expression_tab": true, "phenotype_tab": true, "literature_tab": true, "wiki_tab": false, "regulation_tab": true, "sequence_tab": true, "history_tab": true, "homology_tab": true, "disease_tab": false}
    };


	
	
	
    
    
	
    ENP2 | SGD
    
	
	
	









	
	

ENP2 / YGR145W Overview


Standard Name
ENP2 1
Systematic Name
YGR145W
SGD ID
SGD:S000003377
Feature Type
ORF , Verified
Description
Component of the SSU; required for pre-18S rRNA processing, biogenesis of the small ribosomal subunit; interacts with U3 snoRNA, Mpp10p and Bfr2p; contains WD repeats, and has homology to Spb1p 1 2 3 4
Name Description
Essential Nuclear Protein 1
Comparative Info
Sequence Details

Sequence

The S. cerevisiae Reference Genome sequence is derived from laboratory strain S288C. Download DNA or protein sequence, view genomic context and coordinates. Click "Sequence Details" to view all sequence information for this locus, including that for other strains.


Protein Details

Protein

Basic sequence-derived (length, molecular weight, isoelectric point) and experimentally-determined (median abundance, median absolute deviation) protein information. Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein.


Length (a.a.)
707
Mol. Weight (Da)
81729.0
Isoelectric Point
6.54
Median Abundance (molecules/cell)
6039 +/- 1890
Half-life (hr)
6.5

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 ENP2 alleles in SGD search

Gene Ontology Details

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. Click "Gene Ontology Details" to view all GO information and evidence for this locus as well as biological processes it shares with other genes.


Summary
Protein involved in maturation of 18S rRNA and ribosomal small subunit biogenesis; localizes to 90S preribosome, nucleolus, and small-subunit processome

View computational annotations

Molecular Function

Manually Curated

Cellular Component

Manually Curated

Complex

Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.


Phenotype Details

Phenotype

Phenotype annotations for a gene are curated single mutant phenotypes that require an observable (e.g., "cell shape"), a qualifier (e.g., "abnormal"), a mutant type (e.g., null), strain background, and a reference. In addition, annotations are classified as classical genetics or high-throughput (e.g., large scale survey, systematic mutation set). Whenever possible, allele information and additional details are provided. Click "Phenotype Details" to view all phenotype annotations and evidence for this locus as well as phenotypes it shares with other genes.


Interaction Details

Interaction

Interaction annotations are curated by BioGRID and include physical or genetic interactions observed between at least two genes. An interaction annotation is composed of the interaction type, name of the interactor, assay type (e.g., Two-Hybrid), annotation type (e.g., manual or high-throughput), and a reference, as well as other experimental details. Click "Interaction Details" to view all interaction annotations and evidence for this locus, including an interaction visualization.


229 total interactions for 181 unique genes

Physical Interactions

  • Affinity Capture-MS: 167
  • Affinity Capture-RNA: 9
  • Affinity Capture-Western: 5
  • Co-localization: 1
  • Proximity Label-MS: 2
  • Reconstituted Complex: 1
  • Two-hybrid: 5

Genetic Interactions

  • Negative Genetic: 33
  • Positive Genetic: 5
  • Synthetic Rescue: 1
Regulation Details

Regulation

The number of putative Regulators (genes that regulate it) and Targets (genes it regulates) for the given locus, based on experimental evidence. This evidence includes data generated through high-throughput techniques. Click "Regulation Details" to view all regulation annotations, shared GO enrichment among regulation Targets, and a regulator/target diagram for the locus.


Regulators
3
Targets
0
Expression Details

Expression

Expression data are derived from records contained in the Gene Expression Omnibus (GEO), and are first log2 transformed and normalized. Referenced datasets may contain one or more condition(s), and as a result there may be a greater number of conditions than datasets represented in a single clickable histogram bar. The histogram division at 0.0 separates the down-regulated (green) conditions and datasets from those that are up-regulated (red). Click "Expression Details" to view all expression annotations and details for this locus, including a visualization of genes that share a similar expression pattern.


Summary Paragraph

A summary of the locus, written by SGD Biocurators following a thorough review of the literature. Links to gene names and curated GO terms are included within the Summary Paragraphs.


Last Updated: 2008-07-17

Literature Details

Literature

All manually curated literature for the specified gene, organized into topics according to their relevance to the gene (Primary Literature, Additional Literature, or Review). Click "Literature Details" to view all literature information for this locus, including shared literature between genes.


Primary
9
Additional
15
Reviews
11

Resources


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