BAIT
XPO1
CRM1, emb, exp1
exportin 1
GO Process (12)
GO Function (3)
GO Component (11)
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- gene expression [TAS]
- intracellular transport of virus [TAS]
- mRNA metabolic process [TAS]
- mitotic cell cycle [TAS]
- negative regulation of transforming growth factor beta receptor signaling pathway [TAS]
- protein export from nucleus [IMP]
- ribosomal large subunit export from nucleus [IMP]
- ribosomal small subunit export from nucleus [IMP]
- transforming growth factor beta receptor signaling pathway [TAS]
- viral life cycle [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
ABL1
ABL, JTK7, bcr/abl, c-ABL, c-ABL1, p150, v-abl, RP11-83J21.1
ABL proto-oncogene 1, non-receptor tyrosine kinase
GO Process (40)
GO Function (16)
GO Component (9)
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
Homo sapiens
Protein-peptide
An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.
Publication
Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl.
The Bcr-Abl tyrosine kinase causes different forms of leukemia in humans. Depending on its position within the cell, Bcr-Abl differentially affects cellular growth. However, no structural and molecular details for the anticipated localization determinants are available. We present the NMR structure of the F-actin binding domain (FABD) of Bcr-Abl and its cellular counterpart c-Abl. The FABD forms a compact left-handed ... [more]
Mol. Cell Aug. 19, 2005; 19(4);461-73 [Pubmed: 16109371]
Throughput
- Low Throughput
Additional Notes
- Interaction only observed with c-abl NES peptide in isolation. Interaction not found to be functional in full domain context.
Related interactions
Curated By
- BioGRID