Gene interactions and pathways from curated databases and text-mining

◀ Back to ARAF

ARAF — MAP2K1

Pathways - manually collected, often from reviews:

  • OpenBEL Selventa BEL large corpus: MAP2K1 → ARAF (increases) Wu et al., J Biol Chem 1996*
    Evidence: Activation of the mitogen-activated protein kinase cascade is a critical event in mitogenic growth factor signal transduction. Mitogen-activated protein kinase is directly activated by a dual specific kinase. Activation of MEK1 requires the phosphorylation of serine residues 218 and 222. The a-Raf activated by serum stimulation induced activation of MEK1, which is determined by the coupled kinase activity, and immunoprecipitation and yeast-two hybrid analysis showed that MEK1 is direct substrate...
  • OpenBEL Selventa BEL large corpus: MAP2K1 → ARAF (directlyIncreases, ARAF Activity, MAP2K1 Activity) Channavajhala et al., J Biol Chem 2003*
    Evidence: hKSR-2 selectively inhibited the Cot-mediated activation of MEK by 60%. In contrast, hKSR-2 up-regulated the Rafmediated MEK activation by up to 70%.
  • OpenBEL Selventa BEL large corpus: MAP2K1 → ARAF (directlyIncreases, ARAF Activity, MAP2K1 Activity) Wu et al., J Biol Chem 1996*
    Evidence: When the immunoprecipitated A-Raf was tested in a coupled in vitro kinase assay, A-Raf activated the recombinant GST-MEK1 (Fig. 3A).
  • OpenBEL Selventa BEL large corpus: MAP2K1 → ARAF (directlyIncreases, ARAF Activity, MAP2K1 Activity)
    Evidence: 124 However, Ras-mediated recruitment of C-Raf to the cell membrane and Src activation are not the only steps involved in the activation of C-Raf. A-Raf, which is structurally similar to C-Raf, is activated in a similar manner; however, the pertinent structural and activational aspects of B-Raf differ from those of A-Raf and C-Raf. Although the structural domains and phosphorylation sites of Raf proteins differ, the greater degree of phosphorylated amino acids in B-Raf confers a 15- to 20- fold ...
  • OpenBEL Selventa BEL large corpus: MAP2K1 → ARAF (directlyIncreases, ARAF Activity, MAP2K1 Activity)
    Evidence: The Structure of Raf The structure of Raf consists of the following: (1) an amino terminus that contains the regulatory domain; (2) an activation loop; and (3) a carboxyl terminus that contains the kinase domain116-118 (Fig 4). All Raf kinases are composed of three conserved regions, CR1 (adjacent to the amino terminus), CR2, and CR3 (adjacent to the carboxyl terminus). The regulation of Raf kinase activity is a complex process involving phosphorylation of the regulatory and catalytic domains of...
  • KEGG Vascular smooth muscle contraction: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Natural killer cell mediated cytotoxicity: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Long-term potentiation: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Long-term depression: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Regulation of actin cytoskeleton: ARAF/BRAF/MOS/RAF1 → MAP2K1/MAP2K2 (protein-protein, phosphorylation)
  • KEGG Insulin signaling pathway: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Pathways in cancer: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Colorectal cancer: ARAF/BRAF/RAF1 → MAP2K1 (protein-protein, phosphorylation)
  • KEGG Renal cell carcinoma: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Pancreatic cancer: ARAF/BRAF/RAF1 → MAP2K1 (protein-protein, activation)
  • KEGG Endometrial cancer: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Glioma: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Glioma: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Prostate cancer: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Melanoma: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Bladder cancer: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Chronic myeloid leukemia: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Acute myeloid leukemia: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG Non-small cell lung cancer: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • KEGG ErbB signaling pathway: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2 (protein-protein, activation)
  • WikiPathways ESC Pluripotency Pathways: BRAF/RAF1/ARAF → MAP2K1/MAP2K3/SEPP1/MAP2K5/MAP2K6/MAP2K2 (activation)
  • WikiPathways ErbB Signaling Pathway: ARAF → MAP2K1 (activation)
  • WikiPathways Focal Adhesion: ARAF/BRAF/RAF1 → SEPP1/MAP2K5/MAP2K6/MAP2K2/MAP2K3/MAP2K1 (activation)
  • WikiPathways MAPK Cascade: RAF1/ARAF/BRAF → MAP2K1/MAP2K2 (activation)
  • WikiPathways Signaling Pathways in Glioblastoma: ARAF/BRAF/RAF1 → MAP2K1/MAP2K2/MAP2K3/MAP2K4/MAP2K5/MAP2K6/MAP2K7 (mim-stimulation)
  • WikiPathways Common Pathways Underlying Drug Addiction: RAF1/ARAF/ARAF → MAP2K1/MAP2K2 (activation)

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

Studies that report less than 10 interactions are marked with *