Biology:FER (gene)
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Proto-oncogene tyrosine-protein kinase FER is an enzyme that in humans is encoded by the FER gene.[1]
Fer protein is a member of the FPS/FES family of nontransmembrane receptor tyrosine kinases. It regulates cell-cell adhesion and mediates signaling from the cell surface to the cytoskeleton via growth factor receptors.[1]
Interactions
FER (gene) has been shown to interact with TMF1[2] and Cortactin.[3]
References
- ↑ 1.0 1.1 "Entrez Gene: FER fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2241.
- ↑ Schwartz, Y; Ben-Dor I; Navon A; Motro B; Nir U (Sep 1998). "Tyrosine phosphorylation of the TATA element modulatory factor by the FER nuclear tyrosine kinases". FEBS Lett. (NETHERLANDS) 434 (3): 339–45. doi:10.1016/S0014-5793(98)01003-5. ISSN 0014-5793. PMID 9742951.
- ↑ Kim, L; Wong T W (Sep 1998). "Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER". J. Biol. Chem. (UNITED STATES) 273 (36): 23542–8. doi:10.1074/jbc.273.36.23542. ISSN 0021-9258. PMID 9722593.
Further reading
- Greer P (2002). "Closing in on the biological functions of Fps/Fes and Fer". Nat. Rev. Mol. Cell Biol. 3 (4): 278–89. doi:10.1038/nrm783. PMID 11994747.
- "Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients". Science 253 (5020): 665–9. 1991. doi:10.1126/science.1651563. PMID 1651563. Bibcode: 1991Sci...253..665N.
- "Radiation hybrid map of 13 loci on the long arm of chromosome 5". Genomics 11 (3): 701–8. 1992. doi:10.1016/0888-7543(91)90078-S. PMID 1663488.
- "Nuclear and cytoplasmic location of the FER tyrosine kinase". Mol. Cell. Biol. 11 (2): 1180–3. 1991. doi:10.1128/mcb.11.2.1180. PMID 1990274.
- "Identification and chromosomal mapping of new human tyrosine kinase genes". Oncogene 5 (3): 277–82. 1990. PMID 2156206.
- "The human tyrosine kinase gene (FER) maps to chromosome 5 and is deleted in myeloid leukemias with a del(5q)". Cytogenet. Cell Genet. 53 (4): 196–200. 1990. doi:10.1159/000132929. PMID 2209086.
- "The FER gene is evolutionarily conserved and encodes a widely expressed member of the FPS/FES protein-tyrosine kinase family". Mol. Cell. Biol. 9 (12): 5722–5. 1990. doi:10.1128/mcb.9.12.5722. PMID 2685575.
- "Isolation and sequence analysis of a novel human tyrosine kinase gene". Mol. Cell. Biol. 9 (4): 1587–93. 1989. doi:10.1128/mcb.9.4.1587. PMID 2725517.
- "Characterization of four tyrosine protein kinases from the particulate fraction of rat spleen". Eur. J. Biochem. 172 (2): 451–7. 1988. doi:10.1111/j.1432-1033.1988.tb13909.x. PMID 3350007.
- "Polycation-dependent, Ca2+-antagonized phosphorylation of calmodulin by casein kinase-2 and a spleen tyrosine protein kinase". FEBS Lett. 215 (2): 241–6. 1987. doi:10.1016/0014-5793(87)80154-0. PMID 3472906.
- "The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors". Mol. Cell. Biol. 15 (8): 4553–61. 1995. doi:10.1128/mcb.15.8.4553. PMID 7623846.
- "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes". Oncogene 8 (12): 3403–10. 1993. PMID 8247543.
- "Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER". J. Biol. Chem. 273 (36): 23542–8. 1998. doi:10.1074/jbc.273.36.23542. PMID 9722593.
- "Involvement of the tyrosine kinase fer in cell adhesion". Mol. Cell. Biol. 18 (10): 5762–70. 1998. doi:10.1128/mcb.18.10.5762. PMID 9742093.
- "Tyrosine phosphorylation of the TATA element modulatory factor by the FER nuclear tyrosine kinases". FEBS Lett. 434 (3): 339–45. 1998. doi:10.1016/S0014-5793(98)01003-5. PMID 9742951.
- "The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells". J. Biol. Chem. 273 (40): 25770–6. 1998. doi:10.1074/jbc.273.40.25770. PMID 9748248.
- "Tyrosine phosphorylation modulates the interaction of calmodulin with its target proteins". Eur. J. Biochem. 262 (3): 790–802. 1999. doi:10.1046/j.1432-1327.1999.00441.x. PMID 10411641.
- "FER kinase activation of Stat3 is determined by the N-terminal sequence". J. Biol. Chem. 275 (37): 28902–10. 2000. doi:10.1074/jbc.M003402200. PMID 10878010.
- "Cell volume-dependent phosphorylation of proteins of the cortical cytoskeleton and cell-cell contact sites. The role of Fyn and FER kinases". J. Biol. Chem. 275 (41): 32289–98. 2000. doi:10.1074/jbc.M003172200. PMID 10921917.
- "N-terminal sequences direct the autophosphorylation states of the FER tyrosine kinases in vivo". Biochemistry 39 (36): 11084–91. 2000. doi:10.1021/bi0005153. PMID 10998246.
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