BAIT
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
PREY
PRDX1
MSP23, NKEF-A, NKEFA, PAG, PAGA, PAGB, PRX1, PRXI, TDPX2, RP11-291L19.4
peroxiredoxin 1
GO Process (3)
GO Function (4)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
FRET
An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.
Publication
Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case.
Protein-protein interactions are essential in most biological processes. Many proteomic approaches have succeeded in the identification of strong and obligatory interactions but the study of weak and transient protein-protein interactions is still a challenge. The aim of the present study was to test the ability of bimolecular fluorescence complementation to detect and discriminate in vivo weak intracellular protein interactions. As ... [more]
Proteomics Apr. 01, 2007; 7(7);1023-36 [Pubmed: 17352427]
Throughput
- Low Throughput
Curated By
- BioGRID