NPM1
Gene Ontology Biological Process
- DNA repair [ISO]
- cell aging [ISO]
- cell growth [IDA]
- cell volume homeostasis [IDA, IMP]
- centrosome cycle [ISO]
- negative regulation of apoptotic process [ISO]
- negative regulation of cell proliferation [ISO]
- negative regulation of centrosome duplication [ISO]
- negative regulation of mRNA splicing, via spliceosome [IDA]
- negative regulation of protein kinase activity by regulation of protein phosphorylation [ISO]
- nucleocytoplasmic transport [IDA, ISO]
- nucleosome assembly [ISO]
- positive regulation of DNA metabolic process [ISO]
- positive regulation of DNA replication [ISO]
- positive regulation of NF-kappaB transcription factor activity [ISO]
- positive regulation of catalytic activity [ISO]
- positive regulation of cell proliferation [IDA, IMP]
- positive regulation of cellular biosynthetic process [IDA, IMP]
- positive regulation of centrosome duplication [IGI]
- positive regulation of protein kinase activity [IDA]
- positive regulation of translation [ISO]
- protein destabilization [IMP]
- protein homooligomerization [ISO]
- protein localization [IMP, ISO]
- protein oligomerization [ISO]
- rRNA export from nucleus [IDA, IMP]
- regulation of DNA damage response, signal transduction by p53 class mediator [IGI]
- regulation of cell cycle [IMP]
- regulation of centriole replication [ISO]
- regulation of centrosome duplication [IMP]
- regulation of eIF2 alpha phosphorylation by dsRNA [ISO]
- regulation of endodeoxyribonuclease activity [ISO]
- regulation of endoribonuclease activity [ISO]
- regulation of neuron apoptotic process [ISO]
- response to stress [ISO]
- ribosomal large subunit biogenesis [IDA, IMP]
- ribosomal large subunit export from nucleus [IMP]
- ribosomal small subunit biogenesis [IDA, IMP]
- ribosomal small subunit export from nucleus [IDA]
Gene Ontology Molecular Function- DNA binding [ISO]
- NF-kappaB binding [ISO]
- RNA binding [IDA, ISO]
- Tat protein binding [ISO]
- enzyme binding [ISO]
- histone binding [ISO]
- phosphatidylinositol-3,4,5-trisphosphate binding [ISO]
- poly(A) RNA binding [ISO]
- protein binding [IPI]
- protein heterodimerization activity [ISO]
- protein homodimerization activity [ISO]
- protein kinase binding [ISO]
- protein kinase inhibitor activity [ISO]
- rRNA binding [IDA]
- ribosomal large subunit binding [ISO]
- ribosomal small subunit binding [ISO]
- transcription coactivator activity [ISO]
- unfolded protein binding [ISO]
- DNA binding [ISO]
- NF-kappaB binding [ISO]
- RNA binding [IDA, ISO]
- Tat protein binding [ISO]
- enzyme binding [ISO]
- histone binding [ISO]
- phosphatidylinositol-3,4,5-trisphosphate binding [ISO]
- poly(A) RNA binding [ISO]
- protein binding [IPI]
- protein heterodimerization activity [ISO]
- protein homodimerization activity [ISO]
- protein kinase binding [ISO]
- protein kinase inhibitor activity [ISO]
- rRNA binding [IDA]
- ribosomal large subunit binding [ISO]
- ribosomal small subunit binding [ISO]
- transcription coactivator activity [ISO]
- unfolded protein binding [ISO]
Gene Ontology Cellular Component
- cell [IMP]
- centrosome [IDA, ISO]
- cytoplasm [IDA, ISO]
- cytosol [IDA]
- focal adhesion [ISO]
- granular component [IDA]
- intracellular [IMP]
- large ribosomal subunit [IDA]
- membrane [ISO]
- nuclear speck [IDA]
- nucleolus [IDA, ISO]
- nucleoplasm [IDA, ISO]
- nucleus [IDA, ISO]
- ribonucleoprotein complex [ISO]
- small ribosomal subunit [IDA]
- spindle pole centrosome [ISO]
RPL5
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
Nucleophosmin serves as a rate-limiting nuclear export chaperone for the Mammalian ribosome.
Nucleophosmin (NPM) (B23) is an essential protein in mouse development and cell growth; however, it has been assigned numerous roles in very diverse cellular processes. Here, we present a unified mechanism for NPM's role in cell growth; NPM directs the nuclear export of both 40S and 60S ribosomal subunits. NPM interacts with rRNA and large and small ribosomal subunit proteins ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NPM1 RPL5 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| RPL5 NPM1 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| RPL5 NPM1 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 0.688 | BioGRID | 2664270 |
Curated By
- BioGRID