Autocatalytic phosphorylation of FGFR3c P250R mutant

Stable Identifier
R-HSA-2012073
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of FGFR3c P250R mutant dimer bound to FGF [plasma membrane]
Physical Entity
Activity
Disease
Name Identifier Synonyms
bone development disease 0080006
craniosynostosis 2340 Premature closure of cranial sutures
acrocephalosyndactylia 12960 Apert syndrome
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Reviewed
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