| + |
MAPK1 | down-regulates 
phosphorylation
|
SMAD1 |
0.59 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52674 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161593 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161686 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52678 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161597 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161605 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161694 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52691 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1 |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
CTDSP1 | down-regulates activity
dephosphorylation
|
SMAD1 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248798 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248799 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248800 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248801 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CTDSPL | down-regulates activity
dephosphorylation
|
SMAD1 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248313 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248314 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248315 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248316 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CTDSP2 | down-regulates activity
dephosphorylation
|
SMAD1 |
0.477 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248300 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248301 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248302 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248303 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 17085434 |
Smad proteins transduce bone morphogenetic protein (BMP) and transforming growth factor-beta (TGFbeta) signals upon phosphorylation of their C-terminal SXS motif by receptor kinases.|Phosphatases that dephosphorylate the linker region are therefore likely to play an integral part in the regulation of Smad activity. We reported previously that small C-terminal domain phosphatases 1, 2, and 3 (SCP1-3) dephosphorylate Smad1 C-terminal tail, thereby attenuating BMP signaling. |The linker region of Smad1 consists of four MAPK phosphorylation sites (Ser-187, Ser-195, Ser-206, and Ser-214) |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CDK9 | down-regulates
phosphorylation
|
SMAD1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161565 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161569 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161658 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161666 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161577 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
CDK8 | down-regulates
phosphorylation
|
SMAD1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189129 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161626 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189133 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161634 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189141 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
CKM complex | down-regulates quantity by destabilization
phosphorylation
|
SMAD1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273145 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273140 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273152 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273144 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273143 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273148 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
SMAD1 |
0.59 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161601 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52687 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK9 | down-regulates quantity by destabilization
phosphorylation
|
SMAD1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161573 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK8 | down-regulates quantity by destabilization
phosphorylation
|
SMAD1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189137 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates 
phosphorylation
|
SMAD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197533 |
Ser239 |
DPMTQDGsQPMDTNM |
Homo sapiens |
|
| pmid |
sentence |
| 22588298 |
On genotoxic stress, atm phosphorylates bmps-activated smad1 in the nucleus on s239, which disrupts smad1 interaction with protein phosphatase ppm1a, leading to enhanced activation and upregulation of smad1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates
phosphorylation
|
SMAD1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52662 |
Ser462 |
GSPHNPIsSVS |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
The c terminus of smad1, which is phosphorylated directly by the bmp type i receptor at the ssvs sequence in contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52666 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
The c terminus of smad1, which is phosphorylated directly by the bmp type i receptor at the ssvs sequence in contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52670 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9335504 |
The c terminus of smad1, which is phosphorylated directly by the bmp type i receptor at the ssvs sequence in contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187190 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates
phosphorylation
|
SMAD1 |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-210084 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249649 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187181 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
BMPR1A/1B/2 | up-regulates activity
phosphorylation
|
SMAD1 |
0.652 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217985 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that BMP receptors phosphorylate and activate Smad1 directly. Phosphorylation of Smad1 in vivo involves serines in the carboxy-terminal motif SSXS. These residues are phosphorylated directly by a BMP type I receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217989 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that BMP receptors phosphorylate and activate Smad1 directly. Phosphorylation of Smad1 in vivo involves serines in the carboxy-terminal motif SSXS. These residues are phosphorylated directly by a BMP type I receptor in vitro |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Epithelium |
| + |
ACVR1 | up-regulates activity
phosphorylation
|
SMAD1 |
0.69 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247674 |
Ser463 |
SPHNPISsVS |
Mus musculus |
|
| pmid |
sentence |
| 9748228 |
Biochemical analysis revealed that constitutively active ALK2 associated with and phosphorylated Smad1 on the COOH-terminal SSXS motif, and also regulated Smad5 and Smad8 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251439 |
Ser465 |
HNPISSVs |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9748228 |
ALK2 receptor specifically interacts with and phosphorylates Smad1 protein. ALK2 Activates Smad1 and Induces BMP-specific Signals. Biochemical analysis revealed that constitutively active ALK2 associated with and phosphorylated Smad1 on the COOH-terminal SSXS motif |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Chlorocebus Aethiops |
| + |
BMPR1A/1B/2 | up-regulates
phosphorylation
|
SMAD1 |
0.652 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-210079 |
Ser463 |
SPHNPISsVS |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249648 |
Ser465 |
HNPISSVs |
Homo sapiens |
|
| pmid |
sentence |
| 9136927 |
Here, we report that bmp receptors phosphorylate and activate smad1 directly. Phosphorylation of smad1 in vivo involves serines in the carboxy-terminal motif ssxs. These residues are phosphorylated directly by a bmp type i receptor in vitro |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAP4K4 | down-regulates activity
phosphorylation
|
SMAD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276335 |
Thr322 |
SNVNRNStIENTRRH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21690388 |
Msn kinases directly phosphorylate α-helix 1 of Smad. we have identified Misshapen (Msn) and the mammalian orthologs TNIK, MINK1, and MAP4K4 as the kinases responsible for α-helix 1 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MINK1 | down-regulates activity
phosphorylation
|
SMAD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276336 |
Thr322 |
SNVNRNStIENTRRH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21690388 |
Msn kinases directly phosphorylate α-helix 1 of Smad. we have identified Misshapen (Msn) and the mammalian orthologs TNIK, MINK1, and MAP4K4 as the kinases responsible for α-helix 1 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNIK | down-regulates activity
phosphorylation
|
SMAD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276334 |
Thr322 |
SNVNRNStIENTRRH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21690388 |
Msn kinases directly phosphorylate α-helix 1 of Smad. we have identified Misshapen (Msn) and the mammalian orthologs TNIK, MINK1, and MAP4K4 as the kinases responsible for α-helix 1 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates activity
phosphorylation
|
SMAD1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255265 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTDSP2 | down-regulates
dephosphorylation
|
SMAD1 |
0.477 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148434 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16882717 |
In human cells, rnai-mediated depletion of scp1 and scp2 increases the extent and duration of smad1 phosphorylation in response to bmp, the transcriptional action of smad1, and the strength of endogenous bmp gene responses. The present identification of the scp family as smad c-terminal phosphatases sheds light on the events that attenuate smad signaling and reveals unexpected links to the essential phosphatases that control rna polymerase ii in eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD1 | up-regulates
binding
|
DVL1 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146131 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16621789 |
These results identify a potential mechanism whereby bmp-2 antagonizes wnt signaling in osteoblast progenitors by promoting an interaction between smad1 and dvl-1 that restricts beta-catenin activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination, ubiquitination
|
SMAD1 |
0.713 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272936 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11158580 |
Here, we report the identification of Smurf2, a new member of the Hect family of E3 ubiquitin ligases. Smurf2 selectively interacts with receptor-regulated Smads and preferentially targets Smad1 for ubiquitination and proteasome-mediated degradation. At higher expression levels, Smurf2 also decreases the protein levels of Smad2, but not Smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120647 |
|
|
Homo sapiens |
Osteoblast |
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| Tissue: |
Bone |
| + |
SMURF1 | down-regulates
ubiquitination
|
SMAD1 |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195660 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degradation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD1 | up-regulates
phosphorylation, binding
|
SMAD4 |
0.655 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168734 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20957627 |
Whereas alk5 signalling is mediated by phosphorylation of smad2 and smad3 proteins, alk1 signalling is mediated by smad1, smad5, and smad8. Activated smads form a complex with the common(co-Smad; Smad4 in mammals) and shuttle into the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172990 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21454478 |
Upon ligand binding, the specific heteromeric transmembrane serine/threonine kinase receptor complexes undergo phosphorylation/activation and subsequently phosphorylate the two ser residues in the c-terminal sxs motif of specific r-smads, smad1/5/8 for bmp pathway and smad2/3 for tgf-_/activin signaling. The activated r-smads then associate with co-smad, smad4. The heteromeric complexes translocate into the nucleus, where they bind to dna directly or indirectly to regulate the transcription of specific genes. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EP300 | up-regulates
binding
|
SMAD1 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195582 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Ski and snon also prevent smads from binding to the transcriptional coactivator p300/cbp |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95462 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12419246 |
Thus, Ski/SnoN represses TGFβ signaling by multiple mechanisms. In addition to recruitment of a transcriptional repressor complex and dissociation of the transcriptional coactivator p300/CBP from the Smads |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CBP/p300 | up-regulates
binding
|
SMAD1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217217 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12419246 |
Thus, Ski/SnoN represses TGFβ signaling by multiple mechanisms. In addition to recruitment of a transcriptional repressor complex and dissociation of the transcriptional coactivator p300/CBP from the Smads |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1A | up-regulates activity
phosphorylation
|
SMAD1 |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255263 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19620713 |
Two types of bmp-induced signaling pathways are known, the smad and p38 mapk pathways. In the former case, bmpr1 phosphorylates smad-1,-5,-8, which forms a complex with smad4 that translocates into the nucleus and regulates gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDP2 | down-regulates
dephosphorylation
|
SMAD1 |
0.245 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144909 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16510868 |
We show that the mammalian pdps are important in dephosphorylation of bmp-activated smad1 but not tgf-beta-activated smad2 or smad3. Thus, pdps specifically inactivate smads in the bmp/dpp pathway. [...] These observations suggest that pdp1 and pdp2 are important for dephosphorylation of smad1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YAP1 | up-regulates
binding
|
SMAD1 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201462 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23431053 |
Yap binds to the phosphorylated smad1 to activate gene transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF | down-regulates
ubiquitination
|
SMAD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270214 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMPR1B | up-regulates 
|
SMAD1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235622 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10564272 |
We found that both smad6 and smad7 inhibit the activation of smad1 and smad5 by bmpr-ia/alk-3 and bmpr-ib/alk-6, as well as that by alk-2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
STUB1 | down-regulates
ubiquitination
|
SMAD1 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172993 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21454478 |
In ad-dition, some proteins (e.g. Chip, carboxyl terminus of hsc70-interacting protein) inhibit the signaling activities of smad1/5 by recruiting smad1/5 from the functional r-/co-smad complex and further pro-moting the ubiquitination and degradation of smad1/5 in a chaperone-independent manner |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195687 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
In ad-dition, some proteins (e.g. Chip, carboxyl terminus of hsc70-interacting protein) inhibit the signaling activities of smad1/5 by recruiting smad1/5 from the functional r-/co-smad complex and further pro-moting the ubiquitination and degradation of smad1/5 in a chaperone-independent manner |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120731 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701756 |
These results suggest that chip can interact with the smad1/smad4 proteins and block bmp signal transduction through the ubiquitin-mediated degradation of smad proteins. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | down-regulates
phosphorylation
|
SMAD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270137 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10197981 |
Ras signaling was shown previously to induce the phosphorylation of the bmp mediator smad1 at four erk consensus sites in the linker domain (kretzschmar et al. 1997a). Phosphorylation of these four sites inhibits smad1 accumulation in the nucleus |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Lung, Breast |
| + |
SKIL | down-regulates
binding
|
SMAD1 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195636 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12419246 |
Ski also represses bmp signaling through interactions with smad4 and bmp-specific r-smads, smad1 or smad7 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates
phosphorylation
|
SMAD1 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66755 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10197981 |
Ras signaling was shown previously to induce the phosphorylation of the bmp mediator smad1 at four erk consensus sites in the linker domain (kretzschmar et al. 1997a). Phosphorylation of these four sites inhibits smad1 accumulation in the nucleus |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACVR1 | up-regulates
phosphorylation
|
SMAD1 |
0.69 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60174 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9748228 |
Bmp7 stimulated phosphorylation of endogenous smad1 and 5, formation of complexes with smad4 and induced the promoter for the homeobox gene, tlx2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD1 | up-regulates quantity
transcriptional regulation
|
GATA3 |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268938 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22219353 |
Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPM1A | down-regulates
dephosphorylation
|
SMAD1 |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149077 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16931515 |
In this study, we have found that ppm1a, a metal ion-dependent protein serine/threonine phosphatase, physically interacts with and dephosphorylates smad1 both in vitro and in vivo. considering the highly conserved nature of the sxs motif in all r-smads, we reasoned that ppm1a might also recognize the sxs motif in the bmp-activated smad1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | down-regulates
phosphorylation
|
SMAD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270005 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10197981 |
Ras signaling was shown previously to induce the phosphorylation of the bmp mediator smad1 at four erk consensus sites in the linker domain (kretzschmar et al. 1997a). Phosphorylation of these four sites inhibits smad1 accumulation in the nucleus |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Lung, Breast |
| + |
SMAD1 | up-regulates quantity by expression
transcriptional regulation
|
PPARG |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236227 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 12589053 |
Overexpression of smad6, a natural antagonist for smad1, blocked ppargamma expression and adipocytic differentiation induced by bmp2 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMAD1 | form complex 
binding
|
SMAD1/4 |
0.655 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103615 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9436979 |
Bone morphogenetic protein (BMP) receptors signal by phosphorylating Smad1, which then associates with Smad4; this complex moves into the nucleus and activates transcription. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255774 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8893010 |
Conversely, Smad1 and DPC4 formed a complex when the cells were stimulated with BMP4 but not with activin of TGF-beta. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
SMAD1 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272948 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14701756 |
CHIP mediates the ubiquitination of Smad1. we demonstrate that the coexpression of Smad1 and Smad4 with the CHIP protein results in the degradation of the Smad proteins through a ubiquitin-mediated process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTDSP1 | down-regulates
dephosphorylation
|
SMAD1 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148396 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16882717 |
In human cells, rnai-mediated depletion of scp1 and scp2 increases the extent and duration of smad1 phosphorylation in response to bmp, the transcriptional action of smad1, and the strength of endogenous bmp gene responses. The present identification of the scp family as smad c-terminal phosphatases sheds light on the events that attenuate smad signaling and reveals unexpected links to the essential phosphatases that control rna polymerase ii in eukaryotes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD1 | up-regulates
binding
|
RUNX2 |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195642 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smad1 interacts with runx2 on the promoter of target genes and controls osteoblast gene expression and differentiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD1 | up-regulates quantity
transcriptional regulation
|
SMAD6 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268935 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22219353 |
Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMAD1 | up-regulates
|
Differentiation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255259 |
|
|
Mus musculus |
Ovarian Serous Carcinoma Cell |
| pmid |
sentence |
| 23993924 |
Engagement of BMP4-mediated signaling in adult mouse ovary-derived OSCs cultured in vitro drives differentiation of these cells into IVD oocytes through Smad1/5/8 activation and transcriptional up-regulation of key meiosis-initiating genes. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMAD1 | up-regulates quantity
transcriptional regulation
|
HAND1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268936 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22219353 |
Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PDP1 | down-regulates
dephosphorylation
|
SMAD1 |
0.245 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144876 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16510868 |
We show that the mammalian pdps are important in dephosphorylation of bmp-activated smad1 but not tgf-beta-activated smad2 or smad3. Thus, pdps specifically inactivate smads in the bmp/dpp pathway. [...] These observations suggest that pdp1 and pdp2 are important for dephosphorylation of smad1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD7 | down-regulates 
|
SMAD1 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154390 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17438144 |
Smad7 repressed smad3/4-, smad2/4-, and smad1/4-enhanced reporter gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKI | down-regulates
binding
|
SMAD1 |
0.685 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195630 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12419246 |
Ski also represses bmp signaling through interactions with smad4 and bmp-specific r-smads, smad1 or smad5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD1 | up-regulates quantity
transcriptional regulation
|
GADD45G |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268937 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22219353 |
Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMAD1 | up-regulates quantity
transcriptional regulation
|
SATB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268934 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22219353 |
Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMP2 | up-regulates
|
SMAD1 |
0.64 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195561 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Neogenin, a transmembranous protein, was reported to regulate bmp receptor association with lipid raft, where bmp induces canonical smad1/5/8 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates
phosphorylation
|
SMAD1 |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159484 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18045539 |
Phosphorylation at the gsk3 sites represses the transcriptional activity of smad1 by enhancing proteasomal degradation of psmad1cter |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD6 | down-regulates
binding
|
SMAD1 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103621 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12857866 |
Smad6 also inhibits bmp signaling by forming a complex with smad1 and by interfering with complex formation between smad1 and smad4 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF2 | down-regulates
ubiquitination
|
SMAD1 |
0.713 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153417 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degra-dation of smads and receptors for tgf-beta and bmps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SMAD1
- 
- 