Feline sarcoma oncogene

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FES proto-oncogene, tyrosine kinase
Protein FES PDB 1wqu.png
PDB rendering based on 1wqu.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols FES ; FPS
External IDs OMIM190030 MGI95514 HomoloGene37563 ChEMBL: 5455 GeneCards: FES Gene
EC number
RNA expression pattern
PBB GE FES 205418 at tn.png
More reference expression data
Species Human Mouse
Entrez 2242 14159
Ensembl ENSG00000182511 ENSMUSG00000053158
UniProt P07332 P16879
RefSeq (mRNA) NM_001143783 NM_010194
RefSeq (protein) NP_001137255 NP_034324
Location (UCSC) Chr 15:
90.88 – 90.9 Mb
Chr 7:
80.38 – 80.39 Mb
PubMed search [1] [2]

Tyrosine-protein kinase Fes/Fps also known as proto-oncogene c-Fes/Fps is an enzyme that in humans is encoded by the FES gene.[1][2] FES was originally cloned as a retroviral oncogene from feline (v-FES) and avian (v-FPS) sarcomas. This triggered the subsequent identification and cloning of the cellular FES (c-FES) genes (also referred to as FPS) in birds and mammals.[3]


This gene encodes the human cellular counterpart of a feline sarcoma retrovirus protein with transforming capabilities. The gene product has tyrosine-specific protein kinase activity and that activity is required for maintenance of cellular transformation. Its chromosomal location has linked it to a specific translocation event identified in patients with acute promyelocytic leukemia but it is also involved in normal hematopoiesis. A truncated transcript has been identified that is generated utilizing a start site in one of the far downstream exons but a protein product associated with this transcript has not been identified.[2]


Feline sarcoma oncogene has been shown to interact with BCAR1[4] and BCR gene.[5][6]


  1. ^ Bowden DW, Akots G, Rothschild CB (Aug 1991). "An insertion deletion polymorphism associated with C-FES". Nucleic Acids Research 19 (15): 4311. doi:10.1093/nar/19.15.4311. PMC 328602. PMID 1870997. 
  2. ^ a b "Entrez Gene: FES feline sarcoma oncogene". 
  3. ^ Craig AW (2012). "FES/FER kinase signaling in hematopoietic cells and leukemias". Frontiers in Bioscience 17: 861–75. doi:10.2741/3961. PMID 22201778. 
  4. ^ Jücker M, McKenna K, da Silva AJ, Rudd CE, Feldman RA (Jan 1997). "The Fes protein-tyrosine kinase phosphorylates a subset of macrophage proteins that are involved in cell adhesion and cell-cell signaling". The Journal of Biological Chemistry 272 (4): 2104–9. doi:10.1074/jbc.272.4.2104. PMID 8999909. 
  5. ^ Lionberger JM, Smithgall TE (Feb 2000). "The c-Fes protein-tyrosine kinase suppresses cytokine-independent outgrowth of myeloid leukemia cells induced by Bcr-Abl". Cancer Research 60 (4): 1097–103. PMID 10706130. 
  6. ^ Maru Y, Peters KL, Afar DE, Shibuya M, Witte ON, Smithgall TE (Feb 1995). "Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS". Molecular and Cellular Biology 15 (2): 835–42. PMC 231961. PMID 7529874. 

Further reading[edit]

  • Smithgall TE, Rogers JA, Peters KL, Li J, Briggs SD, Lionberger JM, Cheng H, Shibata A, Scholtz B, Schreiner S, Dunham N (1998). "The c-Fes family of protein-tyrosine kinases". Critical Reviews in Oncogenesis 9 (1): 43–62. doi:10.1615/critrevoncog.v9.i1.40. PMID 9754447. 
  • Jiang H, Harris MB, Rothman P (Jun 2000). "IL-4/IL-13 signaling beyond JAK/STAT". The Journal of Allergy and Clinical Immunology 105 (6 Pt 1): 1063–70. doi:10.1067/mai.2000.107604. PMID 10856136. 
  • Greer P (Apr 2002). "Closing in on the biological functions of Fps/Fes and Fer". Nature Reviews Molecular Cell Biology 3 (4): 278–89. doi:10.1038/nrm783. PMID 11994747.