NME1
Gene Ontology Biological Process
- DNA catabolic process [IDA]
- negative regulation of cell proliferation [TAS]
- nucleobase-containing small molecule interconversion [TAS]
- nucleobase-containing small molecule metabolic process [TAS]
- positive regulation of DNA binding [IDA]
- positive regulation of epithelial cell proliferation [IMP]
- regulation of apoptotic process [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
NME1
Gene Ontology Biological Process
- DNA catabolic process [IDA]
- negative regulation of cell proliferation [TAS]
- nucleobase-containing small molecule interconversion [TAS]
- nucleobase-containing small molecule metabolic process [TAS]
- positive regulation of DNA binding [IDA]
- positive regulation of epithelial cell proliferation [IMP]
- regulation of apoptotic process [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
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).
Publication
Cell fixation improves performance of in situ crosslinking mass spectrometry while preserving cellular ultrastructure.
Crosslinking mass spectrometry (XL-MS) has the potential to map the interactome of the cell with high resolution and depth of coverage. However, current in vivo XL-MS methods are hampered by crosslinkers that demonstrate low cell permeability and require long reaction times. Consequently, interactome sampling is not high and long incubation times can distort the cell, bringing into question the validity ... [more]
Throughput
- High Throughput
Additional Notes
- High confidence protein interaction in A549 cells from a 1X PhoX crosslinking experiment at 5% FDR
- High confidence protein interaction in A549 cells from a 3X PhoX crosslinking experiment at 5% FDR
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NME1 NME1 | 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 | - | |
| NME1 NME1 | 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 | - | |
| NME1 NME1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 697091 | |
| NME1 NME1 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 275791 | |
| NME1 NME1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | 2745783 | |
| NME1 NME1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - | |
| NME1 NME1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - | |
| NME1 NME1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - |
Curated By
- BioGRID