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Contents

   



(Top)
 


1 Interactions  





2 References  





3 Further reading  














FER (gene)






فارسی
Srpskohrvatski / српскохрватски
Татарча / tatarça
Українська
 

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From Wikipedia, the free encyclopedia
 


FER
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFER, FerT, PPP1R74, Pe1Fe10, Pe1Fe13, Pe1Fe3, Pe1Fe6, TYK3, p94-Fer, FER tyrosine kinase
External IDsOMIM: 176942; MGI: 105917; HomoloGene: 74300; GeneCards: FER; OMA:FER - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 MbChr 17: 64.17 – 64.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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[edit]

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

References[edit]

  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ a b "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. 434 (3). NETHERLANDS: 339–45. doi:10.1016/S0014-5793(98)01003-5. ISSN 0014-5793. PMID 9742951. S2CID 24338520.
  • ^ 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. 273 (36). UNITED STATES: 23542–8. doi:10.1074/jbc.273.36.23542. ISSN 0021-9258. PMID 9722593.
  • Further reading[edit]

  • 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.

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    This page was last edited on 17 October 2022, at 09:45 (UTC).

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