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Details on Person IL-3, IL-5 and GM-CSF all induce tyrosine phosphorylation of...

Class:IdSummation:909742
_displayNameIL-3, IL-5 and GM-CSF all induce tyrosine phosphorylation of...
_timestamp2010-07-14 16:24:17
created[InstanceEdit:909735] Jupe, S, 2010-07-07
literatureReference[LiteratureReference:909736] Formation of Shc-Grb2 complexes is necessary to induce neoplastic transformation by overexpression of Shc proteins
[LiteratureReference:909746] A novel pathway from phosphorylation of tyrosine residues 239/240 of Shc, contributing to suppress apoptosis by IL-3
modified[InstanceEdit:909752] Jupe, S, 2010-07-07
[InstanceEdit:912307] Jupe, S, 2010-07-08
[InstanceEdit:912323] Jupe, S, 2010-07-08
[InstanceEdit:912542] Jupe, S, 2010-07-09
[InstanceEdit:913398] Jupe, S, 2010-07-14
textIL-3, IL-5 and GM-CSF all induce tyrosine phosphorylation of Shc (Dorsch et al. 1994). Three sites are known to mediate specific downstream associations; tyrosine Y427 (Salcini et al. 1994) mediates the subsequent association of Shc with Grb2 (Salcini et al. 1994). The identity of the kinase is unknown. Y349 and Y350 phosphorylation is not required for Ras-MAPK signaling but are involved in IL-3-induced cell survival (Gotoh et al. 1996).
Residue numbering used here refers to Uniprot P29353 where the p66 isoform has been selected as the canonical form. Literature references given here refer to the p52 isoform which lacks the first 110 residues, so Y427 is referred to as Y317 in Salcini et al. 1994, Y349 and Y350 as Y239 and Y240 in Gotoh et al. 1996.
(summation)[Reaction:879925] SHC1 bound to the common beta chain becomes tyrosine phosphorylated [Homo sapiens]
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