FER (gene)

Proto-oncogene tyrosine-protein kinase FER is an enzyme that in humans is encoded by the FER gene.[5]

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)[1] Band 5q21.3 Start 108,747,841 bp[1] End 109,196,841 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 E1.1 Start 63,863,062 bp[2] End 64,139,496 bp[2]
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 • GO:0001948 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 • cell membrane • cell junction • cell cortex • actin cytoskeleton • nuclear chromatin • cytoskeleton • cell nucleus • lamellipodium • cytosol Biological process • regulation of protein phosphorylation • regulation of lamellipodium assembly • actin cytoskeleton reorganization • Leukocyte extravasation • cell differentiation • GO:0007243 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 proliferation • insulin receptor signaling pathway via phosphatidylinositol 3-kinase • cellular response to insulin stimulus • GO:0007067 mitotic cell cycle • peptidyl-tyrosine autophosphorylation • negative regulation of mast cell activation involved in immune response • autophosphorylation • peptidyl-tyrosine phosphorylation • substrate adhesion-dependent cell spreading • regulation of mast cell degranulation • platelet-derived growth factor receptor signaling pathway • cellular proliferation • regulation of fibroblast migration • innate immune system • microtubule cytoskeleton organization • signal transduction • tyrosine phosphorylation of STAT protein • regulation of cell 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: 63.86 – 64.14 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

Interactions

FER (gene) has been shown to interact with TMF1[6] and Cortactin.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000151422 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000127 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: FER fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94)".
6. 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.
7. 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.
• 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. 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. 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. 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.
• 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. 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. 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.
• 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.