| + |
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 |
| + |
CTDSP2 | up-regulates activity 
dephosphorylation
|
SMAD3 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248293 |
Ser204 |
NHSMDAGsPNLSPNP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17035229 |
Dephosphorylation of Smad2/3 Linkers by SCP2 and SCP3|MAPK-mediated linker phosphorylation appears to have a dual role in Smad2/3 regulation. Mitogens and hyperactive Ras result in extracellular signal-regulated kinase (ERK)-mediated phosphorylation of Smad3 at Ser-204, Ser-208, and Thr-179 and of Smad2 at Ser-245/250/255 and Thr-220. Mutation of these sites increases the ability of Smad3 to activate target genes, suggesting that MAPK phosphorylation of Smad3 is inhibitory (11, 12). However, in contrast, ERK-dependent phosphorylation of Smad2 at Thr-8 enhances its transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248294 |
Ser208 |
DAGSPNLsPNPMSPA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17035229 |
Dephosphorylation of Smad2/3 Linkers by SCP2 and SCP3|MAPK-mediated linker phosphorylation appears to have a dual role in Smad2/3 regulation. Mitogens and hyperactive Ras result in extracellular signal-regulated kinase (ERK)-mediated phosphorylation of Smad3 at Ser-204, Ser-208, and Thr-179 and of Smad2 at Ser-245/250/255 and Thr-220. Mutation of these sites increases the ability of Smad3 to activate target genes, suggesting that MAPK phosphorylation of Smad3 is inhibitory (11, 12). However, in contrast, ERK-dependent phosphorylation of Smad2 at Thr-8 enhances its transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248295 |
Ser213 |
NLSPNPMsPAHNNLD |
Homo sapiens |
|
| pmid |
sentence |
| 17035229 |
Dephosphorylation of Smad2/3 Linkers by SCP2 and SCP3|MAPK-mediated linker phosphorylation appears to have a dual role in Smad2/3 regulation. Mitogens and hyperactive Ras result in extracellular signal-regulated kinase (ERK)-mediated phosphorylation of Smad3 at Ser-204, Ser-208, and Thr-179 and of Smad2 at Ser-245/250/255 and Thr-220. Mutation of these sites increases the ability of Smad3 to activate target genes, suggesting that MAPK phosphorylation of Smad3 is inhibitory (11, 12). However, in contrast, ERK-dependent phosphorylation of Smad2 at Thr-8 enhances its transcriptional activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CTDSP2 | down-regulates activity
dephosphorylation
|
SMAD2 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248297 |
Ser245 |
NQSMDTGsPAELSPT |
Homo sapiens |
|
| pmid |
sentence |
| 17035229 |
Dephosphorylation of Smad2/3 Linkers by SCP2 and SCP3|MAPK-mediated linker phosphorylation appears to have a dual role in Smad2/3 regulation. Mitogens and hyperactive Ras result in extracellular signal-regulated kinase (ERK)-mediated phosphorylation of Smad3 at Ser-204, Ser-208, and Thr-179 and of Smad2 at Ser-245/250/255 and Thr-220. Mutation of these sites increases the ability of Smad3 to activate target genes, suggesting that MAPK phosphorylation of Smad3 is inhibitory (11, 12). However, in contrast, ERK-dependent phosphorylation of Smad2 at Thr-8 enhances its transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248298 |
Ser250 |
TGSPAELsPTTLSPV |
Homo sapiens |
|
| pmid |
sentence |
| 17035229 |
Dephosphorylation of Smad2/3 Linkers by SCP2 and SCP3|MAPK-mediated linker phosphorylation appears to have a dual role in Smad2/3 regulation. Mitogens and hyperactive Ras result in extracellular signal-regulated kinase (ERK)-mediated phosphorylation of Smad3 at Ser-204, Ser-208, and Thr-179 and of Smad2 at Ser-245/250/255 and Thr-220. Mutation of these sites increases the ability of Smad3 to activate target genes, suggesting that MAPK phosphorylation of Smad3 is inhibitory (11, 12). However, in contrast, ERK-dependent phosphorylation of Smad2 at Thr-8 enhances its transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248299 |
Ser255 |
ELSPTTLsPVNHSLD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17035229 |
Dephosphorylation of Smad2/3 Linkers by SCP2 and SCP3|MAPK-mediated linker phosphorylation appears to have a dual role in Smad2/3 regulation. Mitogens and hyperactive Ras result in extracellular signal-regulated kinase (ERK)-mediated phosphorylation of Smad3 at Ser-204, Ser-208, and Thr-179 and of Smad2 at Ser-245/250/255 and Thr-220. Mutation of these sites increases the ability of Smad3 to activate target genes, suggesting that MAPK phosphorylation of Smad3 is inhibitory (11, 12). However, in contrast, ERK-dependent phosphorylation of Smad2 at Thr-8 enhances its transcriptional activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248296 |
Thr220 |
QSNYIPEtPPPGYIS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17035229 |
Dephosphorylation of Smad2/3 Linkers by SCP2 and SCP3|MAPK-mediated linker phosphorylation appears to have a dual role in Smad2/3 regulation. Mitogens and hyperactive Ras result in extracellular signal-regulated kinase (ERK)-mediated phosphorylation of Smad3 at Ser-204, Ser-208, and Thr-179 and of Smad2 at Ser-245/250/255 and Thr-220. Mutation of these sites increases the ability of Smad3 to activate target genes, suggesting that MAPK phosphorylation of Smad3 is inhibitory (11, 12). However, in contrast, ERK-dependent phosphorylation of Smad2 at Thr-8 enhances its transcriptional activity |
|
| Publications: |
4 |
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 |
3.0
CTDSP2
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