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
CCND2
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
Disruption of retinoblastoma protein function by coexpression of its C pocket fragment.
The growth suppression function of the retinoblastoma protein (RB) is mediated by its interaction with a variety of cellular proteins. RB contains at least two protein-binding pockets: the large A/B pocket, which interacts with E2F and the D-type cyclins, and the C pocket, which interacts with the nuclear c-Abl tyrosine kinase. The large A/B pocket and the C pocket are ... [more]
Throughput
- Low Throughput
Additional Notes
- DNA complex
Curated By
- BioGRID