NUP85
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
NUP120
Gene Ontology Biological Process
- double-strand break repair [IGI, IMP]
- mRNA export from nucleus [IMP]
- mRNA export from nucleus in response to heat stress [IMP]
- maintenance of chromatin silencing at telomere [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- nuclear pore distribution [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of transcription, DNA-templated [IDA, IGI]
- posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery [IMP]
- protein export from nucleus [IMP]
- protein import into nucleus [IMP]
- ribosomal large subunit export from nucleus [IMP]
- telomere tethering at nuclear periphery [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Synthetic Lethality
A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.
Publication
Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p.
In a screen for mutants defective in nucleocytoplasmic export of mRNA, we have identified a new component of the Saccharomyces cerevisiae nuclear pore complex (NPC). The RAT9/NUP85 (ribonucleic acid trafficking) gene encodes an 84.9-kDa protein that we have localized to NPCs by tagging the RAT9/NUP85 gene with the in vivo molecular marker Green Fluorescent Protein. In cells containing either the ... [more]
Throughput
- Low Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
NUP120 NUP85 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | Low | - | BioGRID | - | |
NUP85 NUP120 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | Low | - | BioGRID | - | |
NUP120 NUP85 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | - | BioGRID | - | |
NUP85 NUP120 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | - | BioGRID | - | |
NUP85 NUP120 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 6 | BioGRID | 3612192 | |
NUP120 NUP85 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | - | BioGRID | 3384863 | |
NUP85 NUP120 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | - | |
NUP120 NUP85 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
NUP85 NUP120 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
NUP85 NUP120 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | High | - | BioGRID | - | |
NUP85 NUP120 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - |
Curated By
- BioGRID