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	MGI: 105917 HomoloGene: 74300 GeneCards: FER
Gene location (Human)
Chr.	Chromosome 5 (human)[1]
End	109,196,841 bp[1]
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)[2]
End	64,139,494 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; • 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; • nuclear chromatin; • cytoskeleton; • cell nucleus; • lamellipodium; • cytosol;
Biological process	• regulation of protein phosphorylation; • regulation of lamellipodium assembly; • actin cytoskeleton reorganization; • Leukocyte extravasation; • 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 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 proliferation; • regulation of fibroblast migration; • innate immune response; • microtubule cytoskeleton organization; • signal transduction; • tyrosine phosphorylation of STAT protein; • regulation of cell proliferation;
	Sources:Amigo / QuickGO
Orthologs
	2241
	14158
	ENSG00000151422
	ENSMUSG00000000127
	P16591
	P70451
	NM_001308028; NM_001308031; NM_001308038; NM_005246
	NM_001037997; NM_001286415; NM_008000
	NP_001294957; NP_001294960; NP_001294967; NP_005237
	NP_001033086; NP_001273344; NP_032026
	Wikidata
View/Edit Human	View/Edit Mouse

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

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 2 3 GRCh38: Ensembl release 89: ENSG00000151422 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000127 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "Entrez Gene: FER fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94)".
↑ 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.

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000151422 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000127 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[entrez-5] 1 2 "Entrez Gene: FER fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94)".

[pmid9742951-6] 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.

[pmid9722593-7] 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.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

FER (gene)

Interactions

References

Further reading