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Details on Person Upon phosphorylation of the R-SMAD (SMAD2/3), the conformati...
| Class:Id | Summation:176005 |
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| _displayName | Upon phosphorylation of the R-SMAD (SMAD2/3), the conformati... |
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| _timestamp | 2013-06-05 15:43:40 |
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| created | [InstanceEdit:176006] Jassal, B, 2006-02-28 10:02:50 |
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| literatureReference | [LiteratureReference:177257] MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling
[LiteratureReference:175954] TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4
[LiteratureReference:177255] Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling
[LiteratureReference:208376] Structural basis of heteromeric smad protein assembly in TGF-beta signaling |
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| modified | [InstanceEdit:176037] Jassal, B, 2006-03-01 09:45:45
[InstanceEdit:202635] Jassal, B, 2007-11-07 13:11:04
[InstanceEdit:1530045] Orlic-Milacic, Marija, 2011-08-25
[InstanceEdit:2197781] Orlic-Milacic, M, 2012-04-15
[InstanceEdit:2199156] Orlic-Milacic, M, 2012-04-16
[InstanceEdit:3656493] Orlic-Milacic, M, 2013-06-05 |
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| text | Upon phosphorylation of the R-SMAD (SMAD2/3), the conformation of the C-terminal (MH2) domain of the R-SMAD changes, lowering its affinity for the type I receptor and ZFYVE9 (SARA). As a result, the phosphorylated R-SMAD dissociates from the activated receptor complex (TGFBR). |
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| (summation) | [Reaction:170850] Phosphorylated SMAD2/3 dissociates from TGFBR [Homo sapiens]
[Reaction:201453] Phospho-R-Smad1/5/8 dissociates from the receptor complex [Homo sapiens]
[Reaction:9846190] GOCAM Phosphorylated SMAD2/3 dissociates from TGFBR [Homo sapiens] |
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