NUP2
Gene Ontology Biological Process
- NLS-bearing protein import into nucleus [IGI, IMP]
- chromatin silencing at silent mating-type cassette [IMP]
- mRNA export from nucleus in response to heat stress [IMP]
- maintenance of chromatin silencing at telomere [IMP]
- poly(A)+ mRNA export from nucleus [IMP]
- posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery [IMP]
- protein export from nucleus [IGI, IMP, IPI]
- protein import into nucleus, substrate release [IDA]
- protein targeting to nuclear inner membrane [IMP]
- transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
NSP1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Exportin-1 functions as an adaptor for transcription factor-mediated docking of chromatin at the nuclear pore complex.
Nuclear pore proteins (nucleoporins [Nups]) physically interact with hundreds of chromosomal sites, impacting transcription. In yeast, transcription factors mediate interactions between Nups and enhancers and promoters. To define the molecular basis of this mechanism, we exploited a separation-of-function mutation in the Gcn4 transcription factor that blocks its interaction with the nuclear pore complex (NPC). This mutation reduces the interaction of ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NUP2 NSP1 | 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 | 3384947 | |
| NSP1 NUP2 | 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 | - | |
| NSP1 NUP2 | Synthetic Lethality 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. | Low | - | BioGRID | 158387 |
Curated By
- BioGRID