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

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

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
Cross References
Mondo
Authored
Rothfels, K  (2012-02-10)
Reviewed
Ezzat, S  (2012-05-15)
Created
Rothfels, K  (2011-12-08)
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