ABL1
Gene Ontology Biological Process
- DNA damage induced protein phosphorylation [IDA]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- actin cytoskeleton organization [ISS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell cycle arrest [TAS]
- cell differentiation [IBA]
- cell migration [IBA]
- cellular protein modification process [NAS]
- cellular response to DNA damage stimulus [IDA]
- cellular response to dopamine [TAS]
- cellular response to oxidative stress [TAS]
- epidermal growth factor receptor signaling pathway [IBA]
- innate immune response [IBA, TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage [TAS]
- mismatch repair [TAS]
- mitochondrial depolarization [TAS]
- mitotic nuclear division [TAS]
- muscle cell differentiation [TAS]
- negative regulation of phospholipase C activity [IMP]
- negative regulation of protein serine/threonine kinase activity [IDA]
- negative regulation of ubiquitin-protein transferase activity [IDA, TAS]
- peptidyl-tyrosine autophosphorylation [IBA]
- peptidyl-tyrosine phosphorylation [IDA, TAS]
- platelet-derived growth factor receptor signaling pathway [IBA]
- positive regulation of apoptotic process [IDA]
- positive regulation of cytosolic calcium ion concentration [IMP]
- positive regulation of muscle cell differentiation [TAS]
- positive regulation of oxidoreductase activity [IDA]
- positive regulation of peptidyl-tyrosine phosphorylation [IDA]
- regulation of actin cytoskeleton reorganization [TAS]
- regulation of autophagy [TAS]
- regulation of cell adhesion [TAS]
- regulation of cell motility [TAS]
- regulation of cell proliferation [IBA]
- regulation of endocytosis [TAS]
- regulation of response to DNA damage stimulus [IDA]
- regulation of transcription, DNA-templated [TAS]
- response to oxidative stress [IGI]
- signal transduction in response to DNA damage [IDA]
Gene Ontology Molecular Function- ATP binding [IDA]
- DNA binding [NAS]
- SH3 domain binding [IPI]
- actin monomer binding [TAS]
- magnesium ion binding [IDA]
- manganese ion binding [IDA]
- mitogen-activated protein kinase binding [IPI]
- nicotinate-nucleotide adenylyltransferase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IDA]
- proline-rich region binding [IDA, IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
- receptor binding [IBA]
- syntaxin binding [IPI]
- ATP binding [IDA]
- DNA binding [NAS]
- SH3 domain binding [IPI]
- actin monomer binding [TAS]
- magnesium ion binding [IDA]
- manganese ion binding [IDA]
- mitogen-activated protein kinase binding [IPI]
- nicotinate-nucleotide adenylyltransferase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IDA]
- proline-rich region binding [IDA, IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
- receptor binding [IBA]
- syntaxin binding [IPI]
Gene Ontology Cellular Component
CAT
Gene Ontology Biological Process
- UV protection [IMP]
- hydrogen peroxide catabolic process [IDA]
- negative regulation of apoptotic process [IMP]
- nucleobase-containing small molecule metabolic process [TAS]
- osteoblast differentiation [IDA]
- protein homotetramerization [IDA]
- protein tetramerization [IDA]
- purine nucleobase metabolic process [TAS]
- purine nucleotide catabolic process [TAS]
- response to reactive oxygen species [IMP]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Catalase activity is regulated by c-Abl and Arg in the oxidative stress response.
The Abl family of mammalian non-receptor tyrosine kinases includes c-Abl and Arg. Recent studies have demonstrated that c-Abl and Arg are activated in the response of cells to oxidative stress. This work demonstrates that catalase, a major effector of the cellular defense against H2O2, interacts with c-Abl and Arg. The results show that H2O2 induced binding of c-Abl and Arg ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ABL1 CAT | 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 | - | |
| CAT ABL1 | 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 | - | |
| ABL1 CAT | 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 | 258623 |
Curated By
- BioGRID