FER (gene)

FER
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KK6
Identifiers
Aliases	FER, FerT, PPP1R74, Pe1Fe10, Pe1Fe13, Pe1Fe3, Pe1Fe6, TYK3, p94-Fer, FER tyrosine kinase
External IDs	OMIM: 176942 MGI: 105917 HomoloGene: 74300 GeneCards: FER
Gene location (Human) Chr. Chromosome 5 (human) Band 5q21.3 Start 108,747,841 bp End 109,196,841 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 E1.1 Start 64,170,057 bp End 64,446,491 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon secondary oocyte sural nerve sperm corpus callosum internal globus pallidus lactiferous duct trigeminal ganglion parietal pleura ganglionic eminence Top expressed in spermatid otic placode spermatocyte saccule secondary oocyte esophagus placenta seminiferous tubule belly cord molar More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity epidermal growth factor receptor binding non-membrane spanning protein tyrosine kinase activity kinase activity protein phosphatase 1 binding protein binding protein tyrosine kinase activity ATP binding lipid binding Cellular component cytoplasm cell projection membrane microtubule cytoskeleton extrinsic component of cytoplasmic side of plasma membrane plasma membrane cell junction cell cortex actin cytoskeleton cytoskeleton nucleus lamellipodium cytosol Biological process regulation of protein phosphorylation regulation of lamellipodium assembly actin cytoskeleton reorganization diapedesis cell differentiation intracellular signal transduction positive regulation of actin filament polymerization extracellular matrix-cell signaling phosphorylation cytokine-mediated signaling pathway Kit signaling pathway positive regulation of cell migration regulation of epidermal growth factor receptor signaling pathway response to platelet-derived growth factor cellular response to macrophage colony-stimulating factor stimulus cell-cell adhesion mediated by cadherin cellular response to reactive oxygen species chemotaxis protein phosphorylation Fc-epsilon receptor signaling pathway interleukin-6-mediated signaling pathway response to lipopolysaccharide cell adhesion positive regulation of NF-kappaB transcription factor activity positive regulation of cell population proliferation insulin receptor signaling pathway via phosphatidylinositol 3-kinase cellular response to insulin stimulus mitotic cell cycle peptidyl-tyrosine autophosphorylation negative regulation of mast cell activation involved in immune response protein autophosphorylation peptidyl-tyrosine phosphorylation substrate adhesion-dependent cell spreading regulation of mast cell degranulation platelet-derived growth factor receptor signaling pathway cell population proliferation regulation of fibroblast migration innate immune response microtubule cytoskeleton organization signal transduction tyrosine phosphorylation of STAT protein regulation of cell population proliferation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2241 14158 Ensembl ENSG00000151422 ENSMUSG00000000127 UniProt P16591 P70451 RefSeq (mRNA) NM_001308028 NM_001308031 NM_001308038 NM_005246 NM_001037997 NM_001286415 NM_008000 RefSeq (protein) NP_001294957 NP_001294960 NP_001294967 NP_005237 NP_001033086 NP_001273344 NP_032026 Location (UCSC) Chr 5: 108.75 – 109.2 Mb Chr 17: 64.17 – 64.45 Mb PubMed search
Wikidata
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Proto-oncogene tyrosine-protein kinase FER is an enzyme that in humans is encoded by the FER gene.

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.

Interactions

FER (gene) has been shown to interact with TMF1 and Cortactin.

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. S2CID 22927394.
• Nishisho I, Nakamura Y, Miyoshi Y, et al. (1991). "Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients". Science. 253 (5020): 665–9. Bibcode:1991Sci...253..665N. doi:10.1126/science.1651563. PMID 1651563.
• Warrington JA, Hall LV, Hinton LM, et al. (1992). "Radiation hybrid map of 13 loci on the long arm of chromosome 5". Genomics. 11 (3): 701–8. doi:10.1016/0888-7543(91)90078-S. PMID 1663488.
• Hao QL, Ferris DK, White G, et al. (1991). "Nuclear and cytoplasmic location of the FER tyrosine kinase". Mol. Cell. Biol. 11 (2): 1180–3. doi:10.1128/mcb.11.2.1180. PMC 359807. PMID 1990274.
• Krolewski JJ, Lee R, Eddy R, et al. (1990). "Identification and chromosomal mapping of new human tyrosine kinase genes". Oncogene. 5 (3): 277–82. PMID 2156206.
• Morris C, Heisterkamp N, Hao QL, et al. (1990). "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. doi:10.1159/000132929. PMID 2209086.
• Pawson T, Letwin K, Lee T, et al. (1990). "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. doi:10.1128/mcb.9.12.5722. PMC 363745. PMID 2685575.
• Hao QL, Heisterkamp N, Groffen J (1989). "Isolation and sequence analysis of a novel human tyrosine kinase gene". Mol. Cell. Biol. 9 (4): 1587–93. doi:10.1128/mcb.9.4.1587. PMC 362575. PMID 2725517.
• Brunati AM, Pinna LA (1988). "Characterization of four tyrosine protein kinases from the particulate fraction of rat spleen". Eur. J. Biochem. 172 (2): 451–7. doi:10.1111/j.1432-1033.1988.tb13909.x. PMID 3350007.
• Meggio F, Brunati AM, Pinna LA (1987). "Polycation-dependent, Ca2+-antagonized phosphorylation of calmodulin by casein kinase-2 and a spleen tyrosine protein kinase". FEBS Lett. 215 (2): 241–6. doi:10.1016/0014-5793(87)80154-0. PMID 3472906. S2CID 2801487.
• Kim L, Wong TW (1995). "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. doi:10.1128/mcb.15.8.4553. PMC 230695. PMID 7623846.
• Lee ST, Strunk KM, Spritz RA (1993). "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes". Oncogene. 8 (12): 3403–10. PMID 8247543.
• Kim L, Wong TW (1998). "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. doi:10.1074/jbc.273.36.23542. PMID 9722593.
• Rosato R, Veltmaat JM, Groffen J, Heisterkamp N (1998). "Involvement of the tyrosine kinase fer in cell adhesion". Mol. Cell. Biol. 18 (10): 5762–70. doi:10.1128/mcb.18.10.5762. PMC 109162. PMID 9742093.
• Schwartz Y, Ben-Dor I, Navon A, et al. (1998). "Tyrosine phosphorylation of the TATA element modulatory factor by the FER nuclear tyrosine kinases". FEBS Lett. 434 (3): 339–45. doi:10.1016/S0014-5793(98)01003-5. PMID 9742951. S2CID 24338520.
• Huang C, Liu J, Haudenschild CC, Zhan X (1998). "The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells". J. Biol. Chem. 273 (40): 25770–6. doi:10.1074/jbc.273.40.25770. PMID 9748248.
• Corti C, Leclerc L'Hostis E, Quadroni M, et al. (1999). "Tyrosine phosphorylation modulates the interaction of calmodulin with its target proteins". Eur. J. Biochem. 262 (3): 790–802. doi:10.1046/j.1432-1327.1999.00441.x. PMID 10411641.
• Priel-Halachmi S, Ben-Dor I, Shpungin S, et al. (2000). "FER kinase activation of Stat3 is determined by the N-terminal sequence". J. Biol. Chem. 275 (37): 28902–10. doi:10.1074/jbc.M003402200. PMID 10878010.
• Kapus A, Di Ciano C, Sun J, et al. (2000). "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. doi:10.1074/jbc.M003172200. PMID 10921917.
• Orlovsky K, Ben-Dor I, Priel-Halachmi S, et al. (2000). "N-terminal sequences direct the autophosphorylation states of the FER tyrosine kinases in vivo". Biochemistry. 39 (36): 11084–91. doi:10.1021/bi0005153. PMID 10998246.