SRC
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- Ras protein signal transduction [TAS]
- T cell costimulation [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- bone resorption [IBA, ISS]
- cell adhesion [IBA]
- cellular response to peptide hormone stimulus [IBA]
- cellular response to progesterone stimulus [ISS]
- central nervous system development [IBA]
- epidermal growth factor receptor signaling pathway [IBA, TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [IBA, TAS]
- integrin-mediated signaling pathway [IMP]
- intracellular estrogen receptor signaling pathway [IBA]
- intracellular signal transduction [IDA]
- leukocyte migration [TAS]
- membrane organization [TAS]
- negative regulation of anoikis [IMP]
- negative regulation of apoptotic process [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- negative regulation of extrinsic apoptotic signaling pathway [IMP]
- negative regulation of focal adhesion assembly [ISS]
- negative regulation of intrinsic apoptotic signaling pathway [IMP]
- negative regulation of mitochondrial depolarization [IMP]
- negative regulation of protein homooligomerization [IMP]
- neurotrophin TRK receptor signaling pathway [TAS]
- osteoclast development [IBA]
- peptidyl-tyrosine autophosphorylation [IBA]
- peptidyl-tyrosine phosphorylation [IDA]
- platelet activation [TAS]
- platelet-derived growth factor receptor signaling pathway [IBA]
- positive regulation of integrin activation [TAS]
- positive regulation of protein kinase B signaling [IMP]
- progesterone receptor signaling pathway [IBA, ISS]
- protein autophosphorylation [IDA]
- regulation of bone resorption [TAS]
- regulation of caveolin-mediated endocytosis [IMP]
- regulation of cell cycle [IBA]
- regulation of cell proliferation [IBA]
- regulation of cell-cell adhesion [IMP]
- regulation of early endosome to late endosome transport [IMP]
- regulation of epithelial cell migration [IMP]
- regulation of podosome assembly [IBA]
- regulation of vascular permeability [TAS]
- response to interleukin-1 [IMP]
- signal complex assembly [TAS]
- signal transduction [TAS]
- stress fiber assembly [IMP]
- transforming growth factor beta receptor signaling pathway [IMP]
Gene Ontology Molecular Function- SH2 domain binding [IPI]
- SH3/SH2 adaptor activity [TAS]
- enzyme binding [IPI]
- ephrin receptor binding [IPI]
- growth factor receptor binding [IPI]
- heme binding [IDA]
- hormone receptor binding [IBA]
- integrin binding [TAS]
- ion channel binding [IPI]
- kinase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IBA, TAS]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA, TAS]
- protein tyrosine kinase activity [EXP, IDA, TAS]
- receptor binding [IPI]
- scaffold protein binding [IPI]
- SH2 domain binding [IPI]
- SH3/SH2 adaptor activity [TAS]
- enzyme binding [IPI]
- ephrin receptor binding [IPI]
- growth factor receptor binding [IPI]
- heme binding [IDA]
- hormone receptor binding [IBA]
- integrin binding [TAS]
- ion channel binding [IPI]
- kinase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IBA, TAS]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA, TAS]
- protein tyrosine kinase activity [EXP, IDA, TAS]
- receptor binding [IPI]
- scaffold protein binding [IPI]
Gene Ontology Cellular Component
TMPO
Gene Ontology Molecular Function
Biochemical Activity (Phosphorylation)
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.
Publication
Tyrosine phosphorylation of nuclear-membrane protein emerin by Src, Abl and other kinases.
X-linked recessive Emery-Dreifuss muscular dystrophy (EDMD) is caused by loss of emerin, a nuclear-membrane protein with roles in nuclear architecture, gene regulation and signaling. Phosphoproteomic studies have identified 13 sites of tyrosine phosphorylation in emerin. We validated one study, confirming that emerin is hyper-tyrosine-phosphorylated in Her2-overexpressing cells. We discovered that non-receptor tyrosine kinases Src and Abl each phosphorylate emerin and ... [more]
Throughput
- Low Throughput
Additional Notes
- Hit isoform P42167-1
Curated By
- BioGRID