ARAF (Serine/threonine-protein kinase A-Raf) is a protein kinase, an enzyme that switches other proteins on by adding phosphate groups. The public catalogues list it as a drug target, an oncogene driver and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Lung cancer, Colorectal cancer, Langerhans cell histiocytosis and 4 more.
Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signalling cascade. Phosphorylates PFKFB2.
CIViC holds 10 clinical evidence items and 1 assertion across 8 variants, naming Sorafenib, Cobimetinib, Vemurafenib and Cetuximab and others. Open Targets scores its association with cancer at 0.66 (direct and indirect evidence; datatypes clinical 0.17, affected pathway 0.88, literature 0.94, genetic association 0.00, somatic mutation 0.46, animal model 0.43). IntOGen calls it a driver in 3 cohorts (3 activating, 0 loss-of-function), covering Cholangiocarcinoma, Lung Adenocarcinoma, Small Cell Lung Cancer.
In plain words · ARAF (Serine/threonine-protein kinase A-Raf) is a protein kinase, an enzyme that switches other proteins on by adding phosphate groups. The public catalogues list it as a drug target, an oncogene driver and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Lung cancer, Colorectal cancer, Langerhans cell histiocytosis and 4 more.
ARAF (Serine/threonine-protein kinase A-Raf) is a protein kinase, an enzyme that switches other proteins on by adding phosphate groups. The public catalogues list it as a drug target, an oncogene driver and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Lung cancer, Colorectal cancer, Langerhans cell histiocytosis and 4 more.
Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signalling cascade.
No product in this corpus aims at ARAF yet. Kinases are switched on by binding ATP inside the cell, so most drugs are small molecules shaped to plug that ATP pocket.
Tumour-specific alteration: the catalogues call it an oncogene driver (IntOGen cohort analysis finds it activated more often than chance); what a medicine would aim at or exploit is the altered form or its loss, absent from normal cells; no corpus medicine is aimed at it yet. HPA ARAF: RNA low tissue specificity; high antibody staining in 10 normal tissues; highest cancer staining cervical cancer (3 of 12 high). Distribution: 5 cancer families in the corpus carry a prevalence row, label threshold or catalogue link for it (Lung cancer (all types), Colorectal cancer, Langerhans cell histiocytosis (LCH), Erdheim-Chester disease, Rosai-Dorfman disease and other histiocytic neoplasms, Biliary tract cancer (all types)); Open Targets associates it with 0 specific cancer types at or above 0.5. (Rule 6 of scripts/fetch-target-specificity.ts.)
Sources: UniProt P10398; CIViC gene ARAF; IntOGen ARAF; Human Protein Atlas ARAF tissue; Open Targets ENSG00000078061 associations
First described 1986. Earliest sequence paper UniProt cites for the protein: Mark G.E. et al, Proc. Natl. Acad. Sci. U.S.A, 1986, "Pks, a raf-related sequence in humans". Source.
Sources: HGNC HGNC:646 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P10398 (protein name, function text, keywords and locations (REST API)); CIViC gene ARAF (10 evidence items, 1 assertions, 8 variants; diseases: Lung Non-small Cell Carcinoma, Lung Cancer, Colorectal Cancer, Langerhans-cell Histiocytosis, Erdheim-Chester Disease (GraphQL API, CC0)); Open Targets ENSG00000078061 (association with cancer (MONDO_0004992) 0.66; (GraphQL API, CC0)); IntOGen ARAF (driver in 3 cohorts (Act 3, LoF 0); Compendium_Cancer_Genes.tsv release 20240920, CC0 1.0)
Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signalling cascade. Phosphorylates PFKFB2. Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation. Locus Xp11.3 (HGNC).
RNA: low tissue specificity, detected in all normal tissues.
Medium: Adrenal gland, Bone marrow, Breast, Bronchus, Cervix, Colon, Endometrium, Epididymis.
Medium only: breast cancer, endometrial cancer, glioma, head and neck cancer.
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"ARAF" OR ABSTRACT:"ARAF" OR TITLE:"A-Raf proto-oncogene, serine/threonine kinase" OR ABSTRACT:"A-Raf proto-oncogene, serine/threonine kinase" OR TITLE:"Serine/threonine-protein kinase A-Raf" OR ABSTRACT:"Serine/threonine-protein kinase A-Raf" OR TITLE:"A-Raf" OR ABSTRACT:"A-Raf" OR TITLE:"ARAF1" OR ABSTRACT:"ARAF1") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about ARAF, not a curated reading list.
Shares Erdheim-Chester disease, Colorectal cancer, Non-small-cell lung cancer.
Shares Langerhans cell histiocytosis (LCH), Erdheim-Chester disease.
Shares Langerhans cell histiocytosis (LCH), Erdheim-Chester disease.
Shares Langerhans cell histiocytosis (LCH), Erdheim-Chester disease, Biliary tract cancer (cholangiocarcinoma), Lung cancer (all types).
Shares Langerhans cell histiocytosis (LCH), Erdheim-Chester disease.
Shares Langerhans cell histiocytosis (LCH), Erdheim-Chester disease, Colorectal cancer.