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

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 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
Cross References
Mondo
Authored
Rothfels, K  (2012-02-10)
Reviewed
Ezzat, S  (2012-05-15)
Created
Rothfels, K  (2011-11-22)
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