Autocatalytic phosphorylation of FGFR3c P250R mutant

Stable Identifier
R-HSA-2012073
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Participates
Catalyst Activity

protein tyrosine kinase activity of FGFR3c P250R mutant dimer bound to FGF [plasma membrane]

Functional status

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

Disease Entity
Status
Disease
Name Identifier Synonyms
bone development disease DOID:0080006
craniosynostosis DOID:2340 Premature closure of cranial sutures
acrocephalosyndactylia DOID:12960 Apert syndrome
Authored
Reviewed
Created
Cite Us!