Signaling by BRAF and RAF1 fusions

Summary
Organism
Homo sapiens (human)
Reactome
R-HSA-6802952
PubChem
R-HSA-6802952
Description
  • In addition to the more prevalent point mutations, BRAF and RAF1 are also subject to activation as a result of translocation events that yield truncated or fusion products (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015). In general these events put the C-terminal kinase domain of BRAF or RAF1 downstream of an N-terminal sequence provided by a partner protein. This removes the N-terminal region of the RAF protein, relieving the autoinhibition imposed by this region of the protein. In addition, some but not all of the fusion partner proteins have been shown to contain coiled-coil or other dimerization domains. Taken together, the fusion proteins are thought to dimerize constitutively and activate downstream signaling (Jones et al, 2008; Lee et al, 2012; Hutchinson et al, 2013; Ciampi et al, 2005; Cin et al, 2011; Stransky et al, 2014).
Click on a node on the pathway to see its details. Glycoproteins are marked with a glycoprotein icon in their name.
Displaying all 3 entries
GlyCosmos Lectin UniProt ID Lectin Name Pathway Viewer
GL_005388 P02671 Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain] view
GL_005389 P02675 Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain] view
GL_005390 P02679 Fibrinogen gamma chain view

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GlyCosmos is a member of the GlySpace Alliance together with GlyGen and Glycomics@ExPASy.

Acknowledgements

Supported by JST NBDC Grant Number JPMJND2204

Partly supported by NIH Common Fund Grant #1U01GM125267-01


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Last updated: April 6, 2026