CRKL
Gene Ontology Biological Process
Gene Ontology Molecular Function
INPP5D
Gene Ontology Biological Process
- T cell receptor signaling pathway [TAS]
- blood coagulation [TAS]
- inositol phosphate metabolic process [TAS]
- leukocyte migration [TAS]
- phosphate-containing compound metabolic process [TAS]
- phosphatidylinositol biosynthetic process [TAS]
- phospholipid metabolic process [TAS]
- signal transduction [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
CrkL is recruited through its SH2 domain to the erythropoietin receptor and plays a role in Lyn-mediated receptor signaling.
The erythropoietin (Epo) receptor transduces its signals by activating physically associated tyrosine kinases, mainly Jak2 and Lyn, and thereby inducing tyrosine phosphorylation of various substrates including the Epo receptor (EpoR) itself. We previously demonstrated that, in Epo-stimulated cells, an adapter protein, CrkL, becomes tyrosine-phosphorylated, physically associates with Shc, SHP-2, and Cbl, and plays a role in activation of the Ras/Erk ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
CRKL INPP5D | Affinity Capture-Western 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. | Low | - | BioGRID | - |
Curated By
- BioGRID