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RALA — RALBP1

Pathways - manually collected, often from reviews:

• BioCarta ras signaling pathway: RALA → RALBP1 (modification, activates)
• KEGG Pathways in cancer: RALA/RALB → RALBP1 (protein-protein, activation)
• KEGG Pancreatic cancer: RALA/RALB → RALBP1 (protein-protein, activation)
• WikiPathways RalA downstream regulated genes: RALA → RALBP1 (activation)

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind_translation Interaction: RALA — RALBP1 (affinity chromatography technology) Ryu et al., Oncogene 2005*
• IRef Bind_translation Interaction: RALA — RALBP1 (two hybrid) Jullien-Flores et al., J Biol Chem 1995*
• IRef Bind_translation Interaction: RALA — RALBP1 (affinity chromatography technology) Jullien-Flores et al., J Biol Chem 1995*
• IRef Bind_translation Interaction: RALA — RALBP1 (affinity chromatography technology) Frankel et al., EMBO J 2005*
• IRef Bind_translation Interaction: RALA — RALBP1 (two hybrid) Frankel et al., EMBO J 2005*
• IRef Biogrid Interaction: RALA — RALBP1 (direct interaction, pull down) Ikeda et al., J Biol Chem 1998*
• IRef Biogrid Interaction: RALA — RALBP1 (direct interaction, two hybrid) Moskalenko et al., J Biol Chem 2003
• IRef Biogrid Interaction: RALA — RALBP1 (direct interaction, two hybrid) Jullien-Flores et al., J Biol Chem 1995*
• IRef Biogrid Interaction: RALA — RALBP1 (direct interaction, pull down) Jullien-Flores et al., J Biol Chem 1995*
• IRef Biogrid Interaction: RALA — RALBP1 (direct interaction, two hybrid) Cantor et al., Mol Cell Biol 1995*
• IRef Ophid Interaction: RALA — RALBP1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Wu et al., Neoplasia (New York, N.Y.) 2010 (Bone Neoplasms...) : Furthermore, we show that the requirement for RalA expression for manifestation of this phenotype is not entirely dependent on a RalA-RalBP1 interaction
Martin et al., Cancer Res 2011 (Colorectal Neoplasms) : Despite their opposing activities, both RalA and RalB regulation of anchorage independent growth required interaction with RalBP1/RLIP76 and components of the exocyst complex
Matsubara et al., FEBS Lett 1997 : Although Ral bound to RalBP1 at a molar ratio of 1 : 1, the interaction of Ral with RalBP1 did not affect the GTPase activating activity of RalBP1 for Rac1 ... These results suggest that the post-translational modification of Ral is important for the subcellular localization of RalBP1 and that the interaction of Ral with RalBP1 is not essential for the activity of RalBP1 but plays a role in recruiting RalBP1 to the membrane where its substrates, Rac1 and CDC42, reside