IRF1
Gene Ontology Biological Process
- apoptotic process [IDA]
- blood coagulation [TAS]
- cell cycle arrest [IDA]
- cellular response to interferon-beta [IDA]
- cellular response to mechanical stimulus [IEP]
- cytokine-mediated signaling pathway [TAS]
- defense response to virus [IDA]
- interferon-gamma-mediated signaling pathway [ISS, TAS]
- negative regulation of cell proliferation [TAS]
- negative regulation of regulatory T cell differentiation [ISS]
- negative regulation of transcription, DNA-templated [IMP]
- positive regulation of interferon-beta production [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of transcription, DNA-templated [IDA, IMP]
- positive regulation of type I interferon production [ISS]
- regulation of CD8-positive, alpha-beta T cell proliferation [ISS]
- regulation of MyD88-dependent toll-like receptor signaling pathway [ISS]
- regulation of adaptive immune response [TAS]
- regulation of cell cycle [TAS]
- regulation of innate immune response [TAS]
- transcription from RNA polymerase II promoter [TAS]
- type I interferon signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
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
A multiprotein binding interface in an intrinsically disordered region of the tumor suppressor protein interferon regulatory factor-1.
The interferon-regulated transcription factor and tumor suppressor protein IRF-1 is predicted to be largely disordered outside of the DNA-binding domain. One of the advantages of intrinsically disordered protein domains is thought to be their ability to take part in multiple, specific but low affinity protein interactions; however, relatively few IRF-1-interacting proteins have been described. The recent identification of a functional ... [more]
Throughput
- Low Throughput
Related interactions
Curated By
- BioGRID