ArticleProtein science : a publication of the Protein Society1993
Identification of tyrosines 154 and 307 in the extracellular domain and 653 and 766 in the intracellular domain as phosphorylation sites in the heparin-binding fibroblast growth factor receptor tyrosine kinase (flg).
Article in Protein science : a publication of the Protein Society, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Structure, activation and dysregulation of fibroblast growth factor receptor kinases: perspectives for clinical targeting.Biochemical Society transactions · 2018Review
- Fibroblast growth factors, old kids on the new block.Seminars in cell & developmental biology · 2016Review
- Enhanced detection of multiply phosphorylated peptides and identification of their sites of modification.Analytical chemistry · 2013Article
- Novel phosphotyrosine targets of FGFR2IIIb signaling.Cellular signalling · 2009Article
- Fibroblast growth factor receptor 1 (FGFR1) tyrosine phosphorylation regulates binding of FGFR substrate 2alpha (FRS2alpha) but not FRS2 to the receptor.Molecular endocrinology (Baltimore, Md.) · 2008Article
- Direct and reversed amino acid sequence pattern analysis: structural reasons for activity of reversed sequence sites and results of kinase site mutagenesis.The Biochemical journal · 2000Article
- Down-regulation of a novel form of fibroblast growth factor receptor 1 in human breast cancer.British journal of cancer · 1997Article
- Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction.Molecular and cellular biology · 1996Article
- Identification of phosphorylation sites in phosphopeptides by positive and negative mode electrospray ionization-tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 1996Article
- bFGF and aFGF induce membrane ruffling in breast cancer cells but not in normal breast epithelial cells: FGFR-4 involvement.The Biochemical journal · 1995Article
- Mass spectrometric characterization of a series of adenosylated peptides acting as bisubstrate analogs of protein kinases.Journal of the American Society for Mass Spectrometry · 1994Article
- Selective detection of phosphopeptides in complex mixtures by electrospray liquid chromatography/mass spectrometry.Journal of the American Society for Mass Spectrometry · 1993Article
- Control of fibroblast growth factor receptor kinase signal transduction by heterodimerization of combinatorial splice variants.Molecular and cellular biology · 1993Article
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7 authors.
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Abstract
Four tyrosine residues have been identified as phosphorylation sites in the tyrosine kinase isoform of the heparin-binding fibroblast growth factor receptor flg (FGF-R1). Baculoviral-insect cell-derived recombinant FGF-R1 was phosphorylated and fragmented with trypsin while immobilized on heparin-agarose beads. Phosphotyrosine peptides were purified by chromatography on immobilized anti-phosphotyrosine antibody and analyzed by Edman degradation and electrospray tandem mass spectrometry. Tyrosine residue 653, which is in a homologous spatial position to major autophosphorylation sites in the catalytic domain of the src and insulin receptor kinases, is the major intracellular FGF-R1 phosphorylation site. Residue 766 in the COOH-terminus outside the kinase domain is a secondary site. Tyrosine residues 154 and 307, which are in the extracellular domain of transmembrane receptor isoforms and are in an unusual sequence context for tyrosine phosphorylation, were also phosphorylated.
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