PEAK1
Domain
The dimerization region encompasses helices both from the N- and C-terminal of the protein kinase domain.
Function
Probable catalytically inactive kinase. Scaffolding protein that regulates the cytoskeleton to control cell spreading and migration by modulating focal adhesion dynamics (PubMed:20534451, PubMed:23105102, PubMed:35687021). Acts as a scaffold for mediating EGFR signaling (PubMed:23846654).
Post-translational modifications
Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation (PubMed:20534451). Phosphorylation at Tyr-665 by a Src family kinase controls subcellular localization to focal adhesion and focal adhesion dynamics (PubMed:20534451). Phosphorylation at Tyr-1188 is essential for binding to SHC1 (PubMed:23846654). Phosphorylation at Tyr-635 promotes interaction with tensin TNS3 (PubMed:35687021).
Sequence Similarities
Belongs to the protein kinase superfamily.
Cellular localization
- Cytoplasm
- Cytoskeleton
- Cell junction
- Focal adhesion
- Colocalizes with F-actin in serum-rich medium (PubMed:20534451). Actin colocalization is reduced during serum starvation (PubMed:20534451).
Alternative names
KIAA2002, PEAK1, Inactive tyrosine-protein kinase PEAK1, Pseudopodium-enriched atypical kinase 1, Sugen kinase 269, Tyrosine-protein kinase SgK269