protein
| receptor-regulated SMAD specific for the BMP pathway (MADH1 and MADH5) |
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XPO1 (CRM1)dependent nuclear export |
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interacts with PDLIM7 |
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interacting wtith TGFBR1 through SMAD7 and inducing receptor degradation |
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targets osteogenic SMADs, SMAD1/5, for ubiquitin-mediated proteasomal degradation |
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interacting with SMURF2 but SMURF1 failed to induce degradation of SMURF2 |
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interacting with ARHGEF9 (induces proteasomal degradation of ARHGEFG9 in cells) |
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interacting with Talin head |
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interacts with and targets ING2 for poly-ubiquitination and proteasomal degradation |
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interacts with and targets KLF2 for poly-ubiquitination and proteasomal degradation specifically in lung cancer |
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inhibited the transcriptional activity of KLF2 to control its target genes, WEE1 and SELL |
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WFS1 is a specific degradation substrate of SMURF1 (interacts with WFS1 at the ER and promotes the ubiquitination and proteasomal degradation of WFS1) |
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FBXL15 targets SMURF1 for ubiquitination and proteasomal degradation |
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interacting with RHOA (C2 domain of SMURF1 is necessary and sufficient for binding RHOA, and therefore is crucial for targeting RhHOA for ubiquitination) |
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CDH1 promotes the E3 ligase activity of SMURF1 |
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SMURF1 interacted with STAT1 through the WW domains of SMURF1 and the PY motif in STAT1 and catalyzed K48-linked polyubiquitination of STAT1 |
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PLEKHO1 is an activator of the SMURF1 ubiquitin ligase acting to promote the ubiquitylation of SMAD5 and MAP2K1 |
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PLEKHO1 mediates the SMURF1-PSMC5 interaction and delivers the ubiquitylated substrates to the proteasome |
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USP9X interacts with SMURF1 and stabilizes SMURF1 through deubiquitination |
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SMURF1 interaction with EFNB1 prevents the association with SMURF2 and precludes EFNB1 from ubiquitination and degradation, since it is a substantially weaker substrate for SMURF1 |
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growth-suppressive role of PLEKHO1 was dependent on the downregulation of the cell cycle-regulated oncogene SMURF1 |
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FGFR3 facilitates BMPR1A to degradation through SMURF1-mediated ubiquitination pathway |
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dual role of SMURF1 C2 domain, recruiting SMURF1 to membrane for accessing Axin and mediating its interaction with Axin, and SMURF1-mediated Axin ubiquitination is subjected to the regulation of cell cycle |
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physically SMURF1 interacts with NEDD8 and UBE2M, forms a NEDD8-thioester intermediate, then catalyses its own neddylation on multiple lysine residues, and NEDD8 is critical for the activation of SMURF1 ubiquitin ligase in tumorigenesis |
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TRIB2 associated-BTRC, RFWD2 and SMURF1 reduced TCF4/CTNNB1 expression, and these effects could be enhanced by TRIB2 |
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interacts with and targets SMURF1 for poly-ubiquitination and proteasomal degradation |
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E3 ligase SMURF1 regulates USP5 protein stability and USP5-mediated TNF production through the ubiquitin proteasome pathway |
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disruption of PKHD1 function results in dysregulated trafficking of both ubiquitin E3 ligases, SMURF1 and SMURF2 |
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SMURF1, an E3 ubiquitin ligase, targets LHX9 for ubiquitin-mediated proteasome degradation, thereby negatively modulating its function |