FER (gene)

VALUE_ERROR (nil)

Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
Entrez| |

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Ensembl| |

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UniProt| |

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RefSeq (mRNA)| |

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RefSeq (protein)| |

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Location (UCSC)| n/a| n/a
PubMed search| n/a| n/a
Wikidata
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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[edit | edit source]

FER (gene) has been shown to interact with TMF1[2] and Cortactin.[3]

## References[edit | edit source]

1. ↑ 1.0 1.1 "Entrez Gene: FER fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94)".
2. ↑ 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.
3. ↑ 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[edit | edit source]

* 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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Protein kinases: tyrosine kinases (EC 2.7.10)

Receptor tyrosine kinases (EC 2.7.10.1)

| Growth factor receptors|

| EGF receptor family|

* EGFR
* ERBB2
* ERBB3
* ERBB4

|

Insulin receptor family|

* IGF1R
* INSR
* INSRR

PDGF receptor family|

* CSF1R
* FLT3
* KIT
* PDGFR (PDGFRA
* PDGFRB)

FGF receptor family|

* FGFR1
* FGFR2
* FGFR3
* FGFR4

VEGF receptors family|

* VEGFR1
* VEGFR2
* VEGFR3

HGF receptor family|

* MET
* RON

Trk receptor family|

* NTRK1
* NTRK2
* NTRK3

EPH receptor family|

* EPHA1
* EPHA2
* EPHA3
* EPHA4
* EPHA5
* EPHA6
* EPHA7
* EPHA8
* EPHB1
* EPHB2
* EPHB3
* EPHB4
* EPHB5
* EPHB6
* EPHX

LTK receptor family|

* LTK
* ALK

TIE receptor family|

* TIE
* TEK

ROR receptor family|

* ROR1
* ROR2

DDR receptor family|

* DDR1
* DDR2

PTK7 receptor family|

* PTK7

RYK receptor family|

* RYK

MuSK receptor family|

* MUSK

ROS receptor family|

* ROS1

AATYK receptor family|

* AATYK
* AATYK2

AXL receptor family|

* AXL
* MER
* TYRO3

RET receptor family|

* RET

uncategorised|

* STYK1

Non-receptor tyrosine kinases (EC 2.7.10.2)

| ABL family|

* ABL1
* ARG

|

ACK family|

* ACK1
* TNK1

CSK family|

* CSK
* MATK

FAK family|

* FAK
* PYK2

FES family|

* FES
* FER

FRK family|

* FRK
* BRK
* SRMS

JAK family|

* JAK1
* JAK2
* JAK3
* TYK2

SRC-A family|

* SRC
* FGR
* FYN
* YES1

SRC-B family|

* BLK
* HCK
* LCK
* LYN

TEC family|

* TEC
* BMX
* BTK
* ITK
* TXK

SYK family|

* SYK
* ZAP70

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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)

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