| Interacting proteins: Q9HB71 and Q8IUQ4 |
Pubmed |
SVM Score :0.0 |
| Previously , we discovered a novel pathway for p 53 induced beta catenin degradation through a ubiquitin E 3 ligase complex involving Siah 1 , SIP ( CacyBP ) , Skp 1 , and Ebi . ^^^ |
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| Interacting proteins: Q9HB71 and Q8IUQ4 |
Pubmed |
SVM Score :0.0 |
| Structural analysis of Siah 1 and its interactions with Siah interacting protein ( SIP ) . ^^^ |
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| Interacting proteins: Q9HB71 and Q8IUQ4 |
Pubmed |
SVM Score :0.0 |
| Siah interacting protein ( SIP ) was identified as a novel adaptor that physically links the E 3 ubiquitin ligase activity of Siah 1 with Skp 1 and Ebi F Box protein in the degradation of beta catenin , a transcriptional activator of TCF / LEF genes . ^^^ |
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| Interacting proteins: Q9HB71 and Q8IUQ4 |
Pubmed |
SVM Score :0.0 |
| Structural analysis of Siah 1 Siah interacting protein interactions and insights into the assembly of an E 3 ligase multiprotein complex . ^^^ The E 3 complex comprises , in addition to Siah 1 , Siah interacting protein ( SIP ) , the adaptor protein Skp 1 , and the F box protein Ebi . ^^^ Here we show that SIP engages Siah 1 by means of two elements , both of which are required for mediating beta catenin destruction in cells . ^^^ An N terminal dimerization domain of SIP sits across the saddle shaped upper surface of Siah 1 , with two extended legs packing against the sides of Siah 1 by means of a consensus PXAXVXP motif that is common to a family of Siah binding proteins . ^^^ The C terminal domain of SIP , which binds to Skp 1 , protrudes from the lower surface of Siah 1 , and we propose that this surface provides the scaffold for bringing substrate and the E 2 enzyme into apposition in the functional complex . . ^^^ |
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