FER (gene)

From Wikipedia, the free encyclopedia

Fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94)

Identifiers

FER; TYK3

External IDs

OMIM: 176942 MGI: 105917 HomoloGene: 74300

Gene ontology
Molecular Function:	• nucleotide binding • protein-tyrosine kinase activity • protein binding • ATP binding • transferase activity
Cellular Component:	• nucleus
Biological Process:	• chemotaxis • cell adhesion • intracellular signaling cascade • protein amino acid autophosphorylation

Orthologs

Human

Mouse

Refseq

NM_005246 (mRNA)
NP_005237 (protein)

NM_001037997 (mRNA)
NP_001033086 (protein)

Location

Chr 5: 108.11 - 108.56 Mb

Chr 17: 63.58 - 63.82 Mb

Pubmed search

[1]

[2]

Fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94), also known as FER, is a human 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]

[edit] References

^ ^a ^b Entrez Gene: FER fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94).

[edit] 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 10998246.