Autocatalytic phosphorylation of FGFR3c P250R mutant

Stable Identifier
R-HSA-2012073
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane, cytosol
ReviewStatus
5/5
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Autocatalytic phosphorylation of FGFR3c P250R mutant
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After high-affinity ligand binding, FGFR3 P250R is believed to undergo trans-autophosphorylation in a manner analogous to the wild-type receptor, although this remains to be experimentally validated (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 FGFR3c P250R mutant dimer bound to FGF [plasma membrane]

Physical Entity
FGFR3c P250R mutant dimer bound to FGF [plasma membrane] (Homo sapiens)
Activity
protein tyrosine kinase activity (GO:0004713)
Functional status

Gain of function of FGFR3c P250R mutant dimer bound to FGF [plasma membrane]

Disease Entity
Status
Disease
Name Identifier Synonyms
craniosynostosis DOID:2340 Premature closure of cranial sutures
bone development disease DOID:0080006
acrocephalosyndactylia DOID:12960 Apert syndrome
Authored
Rothfels, K  (2012-02-10)
Reviewed
Ezzat, S  (2012-05-15)
Created
Rothfels, K  (2011-11-22)
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