POU2F1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
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
Role of SUMO activating enzyme in cancer stem cell maintenance and self-renewal.
Cancer stem cells (CSCs) have key roles in treatment resistance, tumour metastasis and relapse. Using colorectal cancer (CC) cell lines, patient-derived xenograft (PDX) tissues and patient tissues, here we report that CC CSCs, which resist chemoradiation, have higher SUMO activating enzyme (E1) and global SUMOylation levels than non-CSCs. Knockdown of SUMO E1 or SUMO conjugating enzyme (E2) inhibits CC CSC ... [more]
Quantitative Score
- 2.41 [Custom Score]
Throughput
- High Throughput
Additional Notes
- Oct1 was affinity purified and associated proteins were identified by mass spectrometry. The method of scoring used was not indicated, but scoring was presumably performed by the Proteome Discoverer 1.4 software. Higher scores presumably indicate higher confidence in the interaction.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TNF POU2F1 | 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