TPR
Gene Ontology Biological Process
- MAPK import into nucleus [IMP]
- RNA export from nucleus [IMP]
- RNA import into nucleus [IDA]
- carbohydrate metabolic process [TAS]
- cellular response to heat [IDA]
- cellular response to interferon-alpha [ISS]
- cytokine-mediated signaling pathway [TAS]
- glucose transport [TAS]
- hexose transport [TAS]
- mRNA export from nucleus in response to heat stress [IDA]
- mitotic cell cycle [TAS]
- mitotic nuclear envelope disassembly [TAS]
- mitotic spindle assembly checkpoint [IMP]
- negative regulation of RNA export from nucleus [IDA, IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- negative regulation of translational initiation [IMP]
- nuclear matrix organization [IMP]
- nuclear pore complex assembly [IMP]
- nuclear pore organization [IMP]
- positive regulation of heterochromatin assembly [IMP]
- positive regulation of intracellular protein transport [IMP]
- positive regulation of mitotic cell cycle spindle assembly checkpoint [IMP]
- positive regulation of protein export from nucleus [ISS]
- positive regulation of protein import into nucleus [IMP]
- protein export from nucleus [IMP]
- protein import into nucleus [IDA, IMP]
- regulation of glucose transport [TAS]
- regulation of mRNA export from nucleus [IMP]
- regulation of mitotic sister chromatid separation [IMP]
- regulation of protein export from nucleus [IMP]
- regulation of protein import into nucleus [IMP]
- regulation of protein stability [IMP]
- regulation of spindle assembly involved in mitosis [IMP]
- response to epidermal growth factor [IDA]
- small molecule metabolic process [TAS]
- transmembrane transport [TAS]
- viral process [TAS]
Gene Ontology Molecular Function- chromatin binding [IDA]
- dynein complex binding [IDA]
- heat shock protein binding [IDA]
- mRNA binding [IDA]
- mitogen-activated protein kinase binding [IDA]
- nucleocytoplasmic transporter activity [IDA]
- poly(A) RNA binding [IDA]
- protein anchor [IMP]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- transporter activity [IMP]
- tubulin binding [IDA]
- chromatin binding [IDA]
- dynein complex binding [IDA]
- heat shock protein binding [IDA]
- mRNA binding [IDA]
- mitogen-activated protein kinase binding [IDA]
- nucleocytoplasmic transporter activity [IDA]
- poly(A) RNA binding [IDA]
- protein anchor [IMP]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- transporter activity [IMP]
- tubulin binding [IDA]
Gene Ontology Cellular Component
NUP153
Gene Ontology Biological Process
- carbohydrate metabolic process [TAS]
- cytokine-mediated signaling pathway [TAS]
- glucose transport [TAS]
- hexose transport [TAS]
- mitotic cell cycle [TAS]
- mitotic nuclear envelope disassembly [TAS]
- negative regulation of RNA export from nucleus [IDA]
- nuclear pore complex assembly [IMP]
- regulation of glucose transport [TAS]
- small molecule metabolic process [TAS]
- transmembrane transport [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein-protein interactions in the human cell.
Significant recent advances in structural biology, particularly in the field of cryoelectron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to these approaches because of their low abundance, low stability, or-in the case of complexes-simply not having yet been analyzed. Here, we demonstrate the power of using cross-linking ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NUP153 TPR | 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 | 1447937 | |
| TPR NUP153 | 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 | - | |
| TPR NUP153 | 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 | 3437717 | |
| TPR NUP153 | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | Low | - | BioGRID | 2879430 | |
| TPR NUP153 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| TPR NUP153 | 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. | Low | - | BioGRID | - |
Curated By
- BioGRID