Autocatalytic phosphorylation of FGFR1c P252X mutant dimers

Stable Identifier
R-HSA-2023455
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane, cytosol
ReviewStatus
5/5
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Autocatalytic phosphorylation of FGFR1c P252X mutant dimers
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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

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

Hum Mol Genet 2004
Participants
Input
Output
Participates
as an event of
Catalyst Activity

protein tyrosine kinase activity of FGFR1c P252X mutant dimers bound to FGFs [plasma membrane]

Physical Entity
FGFR1c P252X mutant dimers bound to FGFs [plasma membrane] (Homo sapiens)
Activity
protein tyrosine kinase activity (GO:0004713)
Normal reaction
Autocatalytic phosphorylation of FGFR1c (Homo sapiens)
Functional status

Gain of function of FGFR1c P252X mutant dimers bound to FGFs [plasma membrane]

Normal Entity
Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
bone development disease DOID:0080006
Authored
Rothfels, K  (2012-02-10)
Reviewed
Ezzat, S  (2012-05-15)
Created
Rothfels, K  (2011-12-08)
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