Source:http://www.reactome.org/biopax/48887BiochemicalReaction1855
| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
Authored: Rothfels, K, 2012-02-09,
Edited: Rothfels, K, 2012-05-16,
FGFR4 is highly expressed in rhabdomyosarcoma (RMS) tissue, and high levels of expression are correlated with lower survival. Sequencing of exons from 94 RMS tumors identified 14 missense variants, 6 of which were localized in the tyrosine kinase domain, and four of which were in two amino acids (N535K/D and V550E/L). Mutations at amino acid 535 are predicted to eliminate an inhibitory H-bond that restricts receptor autophosphorylation, and mutations at amino acid 550 are believed to alter the ATP-binding site. Functional studies on N535K and V550 show that they undergo autophosphorylation when transfected into a murine RMS lines and transformed NIH 3T3 cells, leading to a metastatic phenotype (Taylor, 2009).,
Reviewed: Ezzat, S, 2012-05-15
|
| biopax3:xref | |
| biopax3:dataSource | |
| biopax3:displayName |
Dimerization of FGFR4 mutants with enhanced kinase activity
|
| biopax3:left | |
| biopax3:participantStoichio... | |
| biopax3:right |