FER (gen)
Izvor: Wikipedija
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| Fer (fps/fes srodna) tirozinska kinaza | |||||||||||
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| Dostupne strukture | |||||||||||
| 2KK6 | |||||||||||
| Identifikatori | |||||||||||
| Simboli | FER; FerT; PPP1R74; Pe1Fe10; Pe1Fe13; Pe1Fe3; Pe1Fe6; TYK3 | ||||||||||
| Vanjski ID | OMIM: 176942 MGI: 105917 HomoloGene: 74300 GeneCards: FER Gene | ||||||||||
| EC broj | 2.7.10.2 | ||||||||||
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| Ortolozi | |||||||||||
| Vrsta | Čovek | Miš | |||||||||
| Entrez | 2241 | 14158 | |||||||||
| Ensembl | ENSG00000151422 | ENSMUSG00000000127 | |||||||||
| UniProt | P16591 | P70451 | |||||||||
| Ref. Sekv. (iRNK) | NM_005246 | NM_001037997 | |||||||||
| Ref. Sekv. (protein) | NP_005237 | NP_001033086 | |||||||||
| Lokacija (UCSC) | Chr 5: 108.08 - 108.53 Mb | Chr 17: 63.9 - 64.14 Mb | |||||||||
| PubMed pretraga | [1] | [2] | |||||||||
Proto-onkogena tirozinska proteinska kinaza FER je enzim koji je kod ljudi kodiran FER genom.[1]
Fer protein je član FPS/FES familije netransmembranskih receptorskih tirozinskih kinaza. On reguliše međućelijsku adheziju i posreduje signalizaciju sa ćelijske površine na citoskeleton putem receptora faktora rasta.[1]
FER (gen) formira interakcije sa TMF1[2] i kortaktinom.[3]
- ↑ 1,0 1,1 „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. 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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