ABL1
Gene Ontology Biological Process
- B cell proliferation [IMP]
- B cell proliferation involved in immune response [IGI, IMP]
- B cell receptor signaling pathway [IMP]
- B-1 B cell homeostasis [IMP]
- Bergmann glial cell differentiation [IGI]
- DNA damage induced protein phosphorylation [ISO]
- actin cytoskeleton organization [IDA]
- actin filament branching [IMP]
- activated T cell proliferation [IMP]
- alpha-beta T cell differentiation [IGI]
- cell migration [IBA]
- cellular response to DNA damage stimulus [ISO]
- cellular response to lipopolysaccharide [IMP]
- cerebellum morphogenesis [IGI]
- collateral sprouting [IMP]
- epidermal growth factor receptor signaling pathway [IGI]
- innate immune response [IBA]
- microspike assembly [IDA]
- negative regulation of BMP signaling pathway [IMP]
- negative regulation of ERK1 and ERK2 cascade [IMP]
- negative regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- negative regulation of cell-cell adhesion [IGI]
- negative regulation of cellular senescence [IGI]
- negative regulation of endothelial cell apoptotic process [IGI]
- negative regulation of mitotic cell cycle [IDA, IGI]
- negative regulation of phospholipase C activity [ISO]
- negative regulation of protein serine/threonine kinase activity [ISO]
- negative regulation of ubiquitin-protein transferase activity [ISO]
- neuromuscular process controlling balance [IGI]
- peptidyl-tyrosine autophosphorylation [IBA]
- peptidyl-tyrosine phosphorylation [IDA, IGI, ISO]
- phagocytosis [IGI, IMP]
- platelet-derived growth factor receptor signaling pathway [IDA, IMP]
- positive regulation of ERK1 and ERK2 cascade [IMP]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IGI]
- positive regulation of Wnt signaling pathway, planar cell polarity pathway [IGI]
- positive regulation of apoptotic process [IMP, ISO]
- positive regulation of cytosolic calcium ion concentration [ISO]
- positive regulation of interferon-gamma secretion [IGI]
- positive regulation of interleukin-2 secretion [IGI]
- positive regulation of mitotic cell cycle [IGI]
- positive regulation of neuron death [IMP]
- positive regulation of osteoblast proliferation [IMP]
- positive regulation of oxidoreductase activity [ISO]
- positive regulation of peptidyl-tyrosine phosphorylation [ISO]
- positive regulation of release of sequestered calcium ion into cytosol [IGI]
- regulation of actin cytoskeleton organization [IGI]
- regulation of cell cycle [IDA]
- regulation of cellular senescence [IGI]
- regulation of extracellular matrix organization [IGI]
- regulation of response to DNA damage stimulus [ISO]
- response to oxidative stress [IMP, ISO]
- signal transduction in response to DNA damage [IBA, ISO]
- spleen development [IMP]
- substrate adhesion-dependent cell spreading [IDA]
- thymus development [IMP]
- transitional one stage B cell differentiation [IMP]
Gene Ontology Molecular Function- ATP binding [IDA, ISO]
- SH3 domain binding [ISO]
- actin filament binding [IDA]
- delta-catenin binding [ISO]
- kinase activity [IDA]
- magnesium ion binding [IDA, ISO]
- manganese ion binding [IDA, ISO]
- mitogen-activated protein kinase binding [ISO]
- non-membrane spanning protein tyrosine kinase activity [IBA, ISO]
- proline-rich region binding [ISO]
- protein C-terminus binding [ISO]
- protein binding [IPI]
- protein domain specific binding [IPI]
- protein kinase activity [IDA, ISO]
- protein kinase binding [ISO]
- protein tyrosine kinase activity [IDA, IGI, IMP, ISO]
- receptor binding [IBA]
- syntaxin binding [ISO]
- ATP binding [IDA, ISO]
- SH3 domain binding [ISO]
- actin filament binding [IDA]
- delta-catenin binding [ISO]
- kinase activity [IDA]
- magnesium ion binding [IDA, ISO]
- manganese ion binding [IDA, ISO]
- mitogen-activated protein kinase binding [ISO]
- non-membrane spanning protein tyrosine kinase activity [IBA, ISO]
- proline-rich region binding [ISO]
- protein C-terminus binding [ISO]
- protein binding [IPI]
- protein domain specific binding [IPI]
- protein kinase activity [IDA, ISO]
- protein kinase binding [ISO]
- protein tyrosine kinase activity [IDA, IGI, IMP, ISO]
- receptor binding [IBA]
- syntaxin binding [ISO]
Gene Ontology Cellular Component
- actin cytoskeleton [IDA]
- cell leading edge [IDA]
- cytoplasm [IDA, ISO]
- cytosol [ISA, ISO]
- endoplasmic reticulum [ISO]
- extrinsic component of cytoplasmic side of plasma membrane [IBA]
- growth cone [ISO]
- mitochondrion [ISO]
- neuron projection [ISO]
- neuronal cell body [ISO]
- nucleolus [ISO]
- nucleoplasm [ISO]
- nucleus [IDA, ISO]
- perinuclear region of cytoplasm [ISO]
- ruffle [ISO]
- synapse [ISO]
RIN1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Protein binding and signaling properties of RIN1 suggest a unique effector function.
Human RIN1 was first characterized as a RAS binding protein based on the properties of its carboxyl-terminal domain. We now show that full-length RIN1 interacts with activated RAS in mammalian cells and defines a minimum region of 434 aa required for efficient RAS binding. RIN1 interacts with the "effector domain" of RAS and employs some RAS determinants that are common ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ABL1 RIN1 | Reconstituted Complex 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. | Low | - | BioGRID | - |
Curated By
- BioGRID