TNF
Gene Ontology Biological Process
- MAPK cascade [IMP]
- activation of MAPK activity [IDA]
- activation of MAPKKK activity [IDA]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- apoptotic process [TAS]
- apoptotic signaling pathway [TAS]
- cellular response to nicotine [IDA]
- cellular response to organic cyclic compound [IDA]
- chronic inflammatory response to antigenic stimulus [IMP]
- embryonic digestive tract development [IEP]
- extrinsic apoptotic signaling pathway [IDA]
- extrinsic apoptotic signaling pathway via death domain receptors [IDA, NAS]
- inflammatory response [IDA]
- leukocyte tethering or rolling [IDA]
- lipopolysaccharide-mediated signaling pathway [IDA]
- necroptotic signaling pathway [IDA]
- negative regulation of branching involved in lung morphogenesis [IDA]
- negative regulation of cytokine secretion involved in immune response [IDA]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [IDA]
- negative regulation of fat cell differentiation [NAS]
- negative regulation of gene expression [IDA]
- negative regulation of interleukin-6 production [IDA]
- negative regulation of lipid catabolic process [IDA]
- negative regulation of lipid storage [NAS]
- negative regulation of protein complex disassembly [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of viral genome replication [IDA]
- positive regulation of ERK1 and ERK2 cascade [NAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of JUN kinase activity [IDA]
- positive regulation of MAP kinase activity [IDA]
- positive regulation of NF-kappaB import into nucleus [IDA]
- positive regulation of NF-kappaB transcription factor activity [IDA]
- positive regulation of NFAT protein import into nucleus [IDA]
- positive regulation of apoptotic process [IDA]
- positive regulation of calcidiol 1-monooxygenase activity [IDA]
- positive regulation of chemokine (C-X-C motif) ligand 2 production [IDA]
- positive regulation of chemokine biosynthetic process [IDA]
- positive regulation of chemokine production [IDA]
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- positive regulation of cytokine production [IDA]
- positive regulation of cytokine secretion [IDA]
- positive regulation of fever generation [ISS]
- positive regulation of gene expression [IDA]
- positive regulation of heterotypic cell-cell adhesion [IDA]
- positive regulation of interleukin-8 biosynthetic process [IDA]
- positive regulation of membrane protein ectodomain proteolysis [IDA]
- positive regulation of mononuclear cell migration [NAS]
- positive regulation of nitric oxide biosynthetic process [IDA]
- positive regulation of osteoclast differentiation [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of podosome assembly [IDA]
- positive regulation of programmed cell death [IDA]
- positive regulation of protein complex assembly [IDA]
- positive regulation of protein complex disassembly [IDA]
- positive regulation of protein localization to cell surface [IDA]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of protein transport [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of smooth muscle cell proliferation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IGI]
- positive regulation of transcription, DNA-templated [IDA]
- positive regulation of vitamin D biosynthetic process [IDA]
- protein import into nucleus, translocation [IDA]
- protein kinase B signaling [IMP]
- receptor biosynthetic process [IDA]
- regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- regulation of insulin secretion [IDA]
- response to glucocorticoid [IDA]
- response to salt stress [TAS]
- response to virus [IDA]
- sequestering of triglyceride [IDA]
- transformed cell apoptotic process [IDA]
- tumor necrosis factor-mediated signaling pathway [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TNFRSF1B
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Tumor necrosis factor and lymphotoxin. Qualitative and quantitative differences in the mediation of early and late cellular response.
Tumor necrosis factor (TNF) is a 17-kDa protein produced by monocytes and a wide variety of other cell types in response to endotoxin and other cytokines. In contrast, lymphotoxin (LT) is a 25-kDa glycoprotein produced only by lymphocytes activated by mitogens. These two cytokines are 28% identical in their amino acid sequences. As they have common cell surface receptors, it ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TNFRSF1B TNF | 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 | - | |
| TNF TNFRSF1B | 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. | Low | - | BioGRID | - | |
| TNF TNFRSF1B | 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 | - | |
| TNFRSF1B TNF | 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 | 2399209 | |
| TNF TNFRSF1B | 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 | - | |
| TNF TNFRSF1B | 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 | - | |
| TNF TNFRSF1B | 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 | - | |
| TNFRSF1B TNF | 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 | - | |
| TNFRSF1B TNF | 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 | - | |
| TNFRSF1B TNF | 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 | - |
Curated By
- BioGRID