Autocatalytic phosphorylation of FGFR1c P252X mutant dimers

Stable Identifier
R-HSA-2023455
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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FGFR1 gain-of-function mutations at P252 that result in increased binding affinity to ligand are presumed to be phosphorylated on the same sites as the wild-type receptor, although this has not been demonstrated (Ibrahimi, 2004a).

Literature References
PubMed ID Title Journal Year
14613973 Proline to arginine mutations in FGF receptors 1 and 3 result in Pfeiffer and Muenke craniosynostosis syndromes through enhancement of FGF binding affinity

Ibrahimi, OA, Zhang, F, Eliseenkova, AV, Linhardt, RJ, Mohammadi, M

Hum Mol Genet 2004
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of FGFR1c P252X mutant dimers bound to FGFs [plasma membrane]
Physical Entity
Activity
Normal reaction
Disease
Name Identifier Synonyms
bone development disease 0080006
cancer 162 malignant tumor, malignant neoplasm, primary cancer
Authored
Reviewed
Created