NPM1
Gene Ontology Biological Process
- CENP-A containing nucleosome assembly [TAS]
- DNA repair [IDA]
- cell aging [IMP, ISS]
- centrosome cycle [IMP, ISS]
- intracellular protein transport [TAS]
- negative regulation of apoptotic process [IDA, NAS]
- negative regulation of cell proliferation [IMP, ISS]
- negative regulation of centrosome duplication [IMP]
- negative regulation of protein kinase activity by regulation of protein phosphorylation [IDA]
- nucleocytoplasmic transport [IDA, TAS]
- nucleosome assembly [IDA, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of translation [IDA]
- protein localization [IDA]
- protein oligomerization [IDA]
- regulation of centriole replication [IMP]
- regulation of eIF2 alpha phosphorylation by dsRNA [IDA]
- regulation of endodeoxyribonuclease activity [IDA]
- regulation of endoribonuclease activity [IDA]
- response to stress [IMP]
- ribosome assembly [TAS]
- signal transduction [NAS]
- viral process [TAS]
Gene Ontology Molecular Function- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
Gene Ontology Cellular Component
PARP1
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular response to insulin stimulus [IDA]
- double-strand break repair [IMP]
- gene expression [TAS]
- macrophage differentiation [TAS]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- protein ADP-ribosylation [IDA]
- protein poly-ADP-ribosylation [IDA]
- transcription from RNA polymerase II promoter [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription, DNA-templated [TAS]
- transforming growth factor beta receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing.
The ubiquitin-like SUMO system functions by a cyclic process of modification and demodification, and recent data suggest that the nucleolus is a site of sumoylation-desumoylation cycles. For example, the tumour suppressor ARF stimulates sumoylation of nucleolar proteins. Here, we show that the nucleolar SUMO-specific protease SENP3 is associated with nucleophosmin (NPM1), a crucial factor in ribosome biogenesis. SENP3 catalyses desumoylation ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NPM1 PARP1 | 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 | - | BioGRID | 3435349 | |
| NPM1 PARP1 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3681075 | |
| PARP1 NPM1 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | 5.09 | BioGRID | 2998627 |
Curated By
- BioGRID