EGF receptor substrate eps15 acetyl - [Mus musculus]/[Homo sapiens] (Synonyms: Ac-Gln-Glu-Gln-Glu-Asp-Leu-Glu-Leu-Ala-Ile-Ala-Leu-Ser-Lys-Ser-Glu-Ile-Ser-Glu-Ala-OH ) |
رقم الكتالوجGP10030 |
EGF receptor substrate eps15 (Eps15) has been identified as a 142-kDa substrate of the EGF receptor1.
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Sample solution is provided at 25 µL, 10mM.
Sequence: AC-QEQEDLELAIALSKSEISEA-OH
Formula of EGF receptor substrate eps15 acetyl - [Mus musculus]/[Homo sapiens]:
C96H159N23O39
EGF receptor substrate eps15 (Eps15) has been identified as a 142-kDa substrate of the EGF receptor1. In quiescent cells Eps15 is associated to the EGF receptor, and upon EGF stimulation this association increases dramatically2. In addition, Eps15 has been shown to bind to both adaptor protein-2 and clathrin2, 3. Subcellular fractionation and immunolocalization studies have shown that Eps15 is present in clathrin-coated pits and vesicles but not in early endosomes2, 4. Eps15 shares homology with the yeast proteins End3p and Pan1p. Both proteins contain multiple Eps15 homology domains, a motif proposed to mediate proteinprotein interaction, and have been implicated in the endocytosis of the a-factor and lipids, respectively5, 6.
Eps15 can be directly phosphorylated in vitro by EGFR and is tyrosine phosphorylated at high stoichiometry in vivo following activation of the EGFR. Perturbation of Eps15 function affects cell proliferation. Overexpression of Eps15 can transform NIH 3T3 cells, albeit with low efficiency7.
Figure1.Structure of EGF receptor substrate eps15
Ref:
1. Fazioli, F., Minichiello, L., Matoskova, B., Wong, W. T., and Di Fiore, P. P. (1993) Mol. Cell. Biol. 13, 5814–5828
2. van Delft, S., Schumacher, C., Hage, W., Verkleij, A. J., and van Bergen en Henegouwen, P. M. P. (1997) J. Cell Biol. 136, 811–823
3. Benmerah, A., Gagnon, J., Be`gue, B., Me´garbane´, B., Dautry-Varsat, A., and Cerf-Bensussan, N. (1996) J. Cell Biol. 131, 1831–1838
4. Tebar, F., Sorkina, T., Sorkin, A., Ericsson, M., and Kirchhausen, T. (1996) J. Biol. Chem. 271, 28727–28730
5. Benedetti, H., Raths, S., Crausaz, F., and Riezman, H. (1994) Mol. Biol. Cell 5,1023–1037
6. Wendland, B., McCaffery, J. M., Xiao, Q., and Emr, S. D. (1996) J. Cell Biol. 135, 1485–1500
7. Fazioli, F., Minichiello, L., Matoskova, B., Wong, W. T. & Di Fiore, P. P. (1993) Mol. Cell. Biol. 13, 5814-5828.
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