ADAM15
Gene Ontology Biological Process
- apoptotic process [IDA]
- cell-matrix adhesion [TAS]
- extracellular matrix disassembly [TAS]
- extracellular matrix organization [TAS]
- innate immune response [IDA]
- integrin-mediated signaling pathway [IMP]
- negative regulation of cell growth [IMP]
- negative regulation of cell migration [IMP]
- negative regulation of cell-matrix adhesion [IMP]
- negative regulation of receptor binding [IMP]
- protein kinase C signaling [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
LCK
Gene Ontology Biological Process
- B cell receptor signaling pathway [IBA]
- Fc-epsilon receptor signaling pathway [TAS]
- T cell costimulation [TAS]
- T cell differentiation [IMP, ISS]
- T cell receptor signaling pathway [TAS]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA, ISS]
- blood coagulation [TAS]
- cellular response to peptide hormone stimulus [IBA]
- cellular zinc ion homeostasis [IEP, ISS]
- dephosphorylation [IDA, ISS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- hemopoiesis [NAS]
- innate immune response [IBA, TAS]
- leukocyte migration [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- peptidyl-tyrosine autophosphorylation [IBA]
- phosphatidylinositol-mediated signaling [TAS]
- platelet activation [TAS]
- positive regulation of T cell activation [IDA, ISS]
- positive regulation of T cell receptor signaling pathway [NAS]
- positive regulation of intrinsic apoptotic signaling pathway [IMP, ISS]
- protein phosphorylation [IDA]
- regulation of cell proliferation [IBA]
- regulation of defense response to virus by virus [TAS]
- regulation of lymphocyte activation [NAS]
- release of sequestered calcium ion into cytosol [ISS]
- response to drug [IDA, ISS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IBA]
- viral process [TAS]
Gene Ontology Molecular Function- ATPase binding [IPI]
- CD4 receptor binding [IPI]
- CD8 receptor binding [IPI]
- SH2 domain binding [IPI, ISS]
- glycoprotein binding [IPI]
- identical protein binding [IPI]
- non-membrane spanning protein tyrosine kinase activity [IBA]
- phosphatidylinositol 3-kinase binding [IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- protein phosphatase binding [IPI]
- protein serine/threonine phosphatase activity [IDA, ISS]
- protein tyrosine kinase activity [EXP, IDA, ISS, TAS]
- ATPase binding [IPI]
- CD4 receptor binding [IPI]
- CD8 receptor binding [IPI]
- SH2 domain binding [IPI, ISS]
- glycoprotein binding [IPI]
- identical protein binding [IPI]
- non-membrane spanning protein tyrosine kinase activity [IBA]
- phosphatidylinositol 3-kinase binding [IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- protein phosphatase binding [IPI]
- protein serine/threonine phosphatase activity [IDA, ISS]
- protein tyrosine kinase activity [EXP, IDA, ISS, TAS]
Gene Ontology Cellular Component
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases.
The adamalysins (ADAMs) are transmembrane glycoproteins involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. Many ADAM cytoplasmic domains are proline-rich and have potential phosphorylation sites. We show here that the cytoplasmic domain of ADAM15, metargidin, can interact specifically with Src family protein-tyrosine kinases (PTKs) and the adaptor protein Grb2 in hematopoietic cells (Jurkat, THP-1, U937, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ADAM15 LCK | 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 | - | |
| ADAM15 LCK | 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