+ |
EP300 | up-regulates
acetylation
|
SMAD7 |
0.476 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-135469 |
Lys64 |
RAGCCLGkAVRGAKG |
Homo sapiens |
|
pmid |
sentence |
15831498 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95165 |
Lys64 |
RAGCCLGkAVRGAKG |
Homo sapiens |
|
pmid |
sentence |
12408818 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-135473 |
Lys70 |
GKAVRGAkGHHHPHP |
Homo sapiens |
|
pmid |
sentence |
15831498 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95169 |
Lys70 |
GKAVRGAkGHHHPHP |
Homo sapiens |
|
pmid |
sentence |
12408818 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS |
+ |
SIRT1 | down-regulates
deacetylation
|
SMAD7 |
0.452 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-150595 |
Lys64 |
RAGCCLGkAVRGAKG |
Homo sapiens |
|
pmid |
sentence |
17098745 |
Sirt1 reversed acetyl-transferase (p300)-mediated acetylation of two lysine residues (lys-64 and -70) on smad7. sirt1-mediated deacetylation of smad7 enhanced smad ubiquitination regulatory factor 1 (smurf1)-mediated ubiquitin proteasome degradation, which contributed to the low expression of smad7 in sirt1-overexpressing mesangial cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-150599 |
Lys70 |
GKAVRGAkGHHHPHP |
Homo sapiens |
|
pmid |
sentence |
17098745 |
Sirt1 reversed acetyl-transferase (p300)-mediated acetylation of two lysine residues (lys-64 and -70) on smad7. sirt1-mediated deacetylation of smad7 enhanced smad ubiquitination regulatory factor 1 (smurf1)-mediated ubiquitin proteasome degradation, which contributed to the low expression of smad7 in sirt1-overexpressing mesangial cells. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | form complex
binding
|
SMAD7/HDAC1/E2F-1 |
0.448 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199970 |
|
|
Homo sapiens |
|
pmid |
sentence |
23213415 |
Furthermore, smad7 caused hdac-1 bind to e2f-1 to form a ternary complex on chromosomal dna containing an e2f-binding motif and leading to repression in the activity of the e2f target genes |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMURF1 | down-regulates activity
ubiquitination
|
SMAD7 |
0.877 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97064 |
|
|
Homo sapiens |
|
pmid |
sentence |
12519765 |
Smad ubiquitin regulatory factor 1 (Smurf1), a HECT type E3 ubiquitin ligase, interacts with inhibitory Smad7 and induces translocation of Smad7 to the cytoplasm |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
WWP1 | up-regulates activity
relocalization, ubiquitination
|
SMAD7 |
0.72 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-126578 |
|
|
Homo sapiens |
|
pmid |
sentence |
15221015 |
We found that WWP1 inhibited transcriptional activities induced by TGF-beta. Similar to Smurfs, WWP1 associated with Smad7 and induced its nuclear export, and enhanced binding of Smad7 to TGF-beta type I receptor to cause ubiquitination and degradation of the receptor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227466 |
|
|
Homo sapiens |
|
pmid |
sentence |
15221015 |
Similar to Smurfs, WWP1 associated with Smad7 and induced its nuclear export, and enhanced binding of Smad7 to TGF-beta type I receptor to cause ubiquitination and degradation of the receptor. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | down-regulates
|
BMPR1B |
0.687 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236864 |
|
|
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 |
+ |
AXIN1 | down-regulates
binding
|
SMAD7 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145851 |
|
|
Homo sapiens |
|
pmid |
sentence |
16601693 |
Here, we show that axin activates tgf-beta signaling by forming a multimeric complex consisting of smad7 and ubiquitin e3 ligase arkadia. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GGCX | up-regulates quantity by expression
transcriptional regulation
|
SMAD7 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261233 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
31539109 |
GGCX can regulate osteoporosis via promoting the TGFβ/smad signaling pathway, facilitating BMSCs osteogenic differentiation, and inhibiting BMSCs adipogenic differentiation. The transfection of pcDNA-GGCX plasmid significantly promoted BMSC cell proliferation, increased calcified nodule formation, inhibited adipogenic differentiation, enhanced ALP activity, elevated RUNX2, and OPN mRNA expressions, and upregulated TGFβ1, Smad2, and Smad7 expressions (p < 0.05). |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
SMAD7 | down-regulates
|
ACVRL1 |
0.554 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-87673 |
|
|
Homo sapiens |
|
pmid |
sentence |
12023024 |
Smad7, induced by alk1 activation, recruits pp1? To alk1 and thereby inhibits tgf-?/Alk1-induced smad1/5 phosphorylation in ecs. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Ovary |
+ |
SMAD7 | up-regulates activity
relocalization, binding
|
SMURF2 |
0.865 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227556 |
|
|
Homo sapiens |
|
pmid |
sentence |
21791611 |
One of the major mechanisms underlying the inhibitory effect of Smad7 on TGF-_ signaling operates through accelerating T_RI turnover by recruiting ubiquitin E3 ligases such as Smurf1 and Smurf2 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272937 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
11163210 |
Smad7 Recruits Smurf2 to the TGFβ Receptor Complex. Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7. Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168450 |
|
|
Homo sapiens |
|
pmid |
sentence |
19352540 |
Smad7 also recruits the HECT type of E3 ubiquitin ligases, Smurf1 and Smurf2. It binds to Smurfs in the nucleus and translocates into the cytoplasm in response to TGF-_ and recruits the ubiquitin ligases to the activated type I receptor ALK5/T_RI, leading to the degradation of the receptor through the proteasomal pathway. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104996 |
|
|
Homo sapiens |
|
pmid |
sentence |
11163210 |
Smurf2 is nuclear, but binding to smad7 induces export and recruitment to the activated tgf beta receptor, where it causes degradation of receptors and smad7 via proteasomal and lysosomal pathways. |
|
Publications: |
4 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
+ |
SMURF2 | down-regulates activity
ubiquitination
|
SMAD7 |
0.865 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178501 |
|
|
Homo sapiens |
|
pmid |
sentence |
18448069 |
The association of Smurf2 with Smad7 and its ubiquitination were inhibited by AIMP1, thereby protecting its autocatalytic degradation stimulated by Smad7. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMURF1 | down-regulates quantity by destabilization
polyubiquitination
|
SMAD7 |
0.877 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272941 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11278251 |
Here we show that Smurf1, an E3 ubiquitin ligase for bone morphogenetic protein-specific Smads, also interacts with Smad7 and induces Smad7 ubiquitination and translocation into the cytoplasm. In addition, Smurf1 associates with TbetaR-I via Smad7, with subsequent enhancement of turnover of TbetaR-I and Smad7. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
SMAD7 | down-regulates activity
binding
|
TGFBR1 |
0.781 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167163 |
|
|
Homo sapiens |
|
pmid |
sentence |
20663871 |
The inhibitory Smads (I-Smads), i.e. Smad6 and Smad7, are negative regulators of transforming growth factor-_ (TGF-_) family signaling. I-Smads inhibit TGF-_ family signaling principally through physical interaction with type I receptors (activin receptor-like kinases), so as to compete with receptor-regulated Smads (R-Smads) for activation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260438 |
|
|
Homo sapiens |
|
pmid |
sentence |
30017632 |
Smad7 inhibits both transforming growth factor β (TGF-β)- and BMP-induced Smad signaling. Smad7 can use both surfaces in its interaction with the ALK-2, -3, and -4 receptors, but only the basic groove is used in the interaction between Smad7 and the TGF-β type I receptor (TβRI, also known as ALK-5). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64088 |
|
|
Homo sapiens |
|
pmid |
sentence |
9892110 |
SMAD7 functions as an antagonist to TGFB by binding to the TBRI and thus inhibiting activation of SMAD2 and SMAD3. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS, TGF-beta Signaling |
+ |
UCHL5 | up-regulates
binding
|
SMAD7 |
0.649 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-138879 |
|
|
Homo sapiens |
|
pmid |
sentence |
16027725 |
Here, we report a novel interaction between smads and ubiquitin c-terminal hydrolase uch37, a deubiquitinating enzyme that could potentially reverse smurf-mediated ubiquitination. In gst pull down experiments, uch37 bound weakly to smad2 and smad3, and bound very strongly to smad7 in a region that is distinct from the -py- motif in smad7 that interacts with smurf ubiquitin ligases. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | up-regulates activity
relocalization
|
SMURF |
0.895 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253258 |
|
|
Homo sapiens |
|
pmid |
sentence |
19352540 |
Smad7 also recruits the HECT type of E3 ubiquitin ligases, Smurf1 and Smurf2. It binds to Smurfs in the nucleus and translocates into the cytoplasm in response to TGF-_ and recruits the ubiquitin ligases to the activated type I receptor ALK5/T_RI, leading to the degradation of the receptor through the proteasomal pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | TGF-beta Signaling |
+ |
HDAC3 | up-regulates
binding
|
SMAD7 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199967 |
|
|
Homo sapiens |
|
pmid |
sentence |
23213415 |
We show here that smad7 can form a complex with endogenous histone deacetylase proteins hdac-1 and hdac-3 in nih 3t3 mouse fibroblast cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | up-regulates
binding
|
STRAP |
0.593 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-76771 |
|
|
Homo sapiens |
|
pmid |
sentence |
10757800 |
Strap recruits smad7 to the activated type i receptor and forms a complex |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | down-regulates
|
MAP3K1 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-65572 |
|
|
Homo sapiens |
|
pmid |
sentence |
10085121 |
Overexpression of smad7 can inhibit the mekk-1-mediated stimulation of smad2 transcriptional activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network |
+ |
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 |
+ |
SMAD7 | up-regulates
|
CTNNB1 |
0.688 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133447 |
|
|
Homo sapiens |
Prostate Gland Cancer Cell |
pmid |
sentence |
15684397 |
In the current study, our data indicate that both smad7 and p38 map kinase positively contributed to the accumulation of -catenin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ITCH | down-regulates
ubiquitination
|
SMAD7 |
0.52 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137951 |
|
|
Homo sapiens |
|
pmid |
sentence |
15946939 |
We identified atrophin 1-interacting protein 4 (aip4) as an e3 ubiquitin ligase that specifically targets smad7 for ubiquitin-dependent degradation without affecting the turnover of the activated tbetari. Surprisingly, we found that despite the ability to degrade smad7, aip4 can inhibit tgf-beta signaling, presumably by enhancing the association of smad7 with the activated tbetari. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF111 | down-regulates
binding, ubiquitination
|
SMAD7 |
0.725 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-119663 |
|
|
Homo sapiens |
|
pmid |
sentence |
14657019 |
Arkadia physically interacts with inhibitory smad, smad7, and induces its poly-ubiquitination and degradation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-119666 |
|
|
Homo sapiens |
|
pmid |
sentence |
14657019 |
Axin is a scaffold protein in tgf-beta signaling that promotes degradation of smad7 by arkadia |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | up-regulates
binding
|
TAB2 |
0.55 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153917 |
|
|
Homo sapiens |
|
pmid |
sentence |
17384642 |
The formation of smad7-tab2 and smad7-tab3 complexes resulted in the suppression of tnf signaling |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination
|
SMAD7 |
0.865 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272940 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
11163210 |
Smad7 Recruits Smurf2 to the TGFβ Receptor Complex. Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7. Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
SMAD7 | up-regulates
binding
|
PPP1CA |
0.405 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145389 |
|
|
Homo sapiens |
|
pmid |
sentence |
16571110 |
Smad7, induced by alk1 activation, recruits pp1? To alk1 and thereby inhibits tgf-?/Alk1-induced smad1/5 phosphorylation in ecs |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | up-regulates
binding
|
PPP1R15A |
0.667 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-121280 |
|
|
Homo sapiens |
|
pmid |
sentence |
14718519 |
We found smad7 interacts with growth arrest and dna damage protein, gadd34, a regulatory subunit of the protein phosphatase 1 (pp1) holoenzyme, which subsequently recruits catalytic subunit of pp1 (pp1c) to dephosphorylate t?RI. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network |
+ |
ZNF165 | down-regulates quantity by repression
transcriptional regulation
|
SMAD7 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266093 |
|
|
Homo sapiens |
|
pmid |
sentence |
26567849 |
ZNF165 drives the unrestrained activation of transforming growth factor β (TGFβ) signalling by directly inactivating the expression of negative feedback pathway regulators, SMURF2, SMAD7 and PMEPA1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | down-regulates activity
binding
|
SMAD3 |
0.596 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64085 |
|
|
Homo sapiens |
|
pmid |
sentence |
9892110 |
Smad6 and smad7, can prevent tgfb signaling by interacting either with the receptor or with smad2 and smad3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS, TGF-beta Signaling |
+ |
SMAD7 | up-regulates
binding
|
TAB3 |
0.391 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153920 |
|
|
Homo sapiens |
|
pmid |
sentence |
17384642 |
The formation of smad7-tab2 and smad7-tab3 complexes resulted in the suppression of tnf signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | down-regulates
|
Fibrosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260433 |
|
|
Homo sapiens |
|
pmid |
sentence |
30017632 |
Transforming growth factor-β1 (TGF-β1) is considered as a crucial mediator in tissue fibrosis and causes tissue scarring largely by activating its downstream small mother against decapentaplegic (Smad) signaling. Different TGF-β signalings play different roles in fibrogenesis. TGF-β1 directly activates Smad signaling which triggers pro-fibrotic gene overexpression. Excessive studies have demonstrated that dysregulation of TGF-β1/Smad pathway was an important pathogenic mechanism in tissue fibrosis. Smad2 and Smad3 are the two major downstream regulator that promote TGF-β1-mediated tissue fibrosis, while Smad7 serves as a negative feedback regulator of TGF-β1/Smad pathway thereby protects against TGF-β1-mediated fibrosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS, TGF-beta Signaling |
+ |
SMAD7 | up-regulates activity
binding, relocalization
|
SMURF1 |
0.877 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272942 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11278251 |
Here we show that Smurf1, an E3 ubiquitin ligase for bone morphogenetic protein-specific Smads, also interacts with Smad7 and induces Smad7 ubiquitination and translocation into the cytoplasm. In addition, Smurf1 associates with TbetaR-I via Smad7, with subsequent enhancement of turnover of TbetaR-I and Smad7. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-185131 |
|
|
Homo sapiens |
|
pmid |
sentence |
19352540 |
Smad7 also recruits the HECT type of E3 ubiquitin ligases, Smurf1 and Smurf2. It binds to Smurfs in the nucleus and translocates into the cytoplasm in response to TGF-_ and recruits the ubiquitin ligases to the activated type I receptor ALK5/T_RI, leading to the degradation of the receptor through the proteasomal pathway. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-175269 |
|
|
Homo sapiens |
|
pmid |
sentence |
21791611 |
One of the major mechanisms underlying the inhibitory effect of Smad7 on TGF-_ signaling operates through accelerating T_RI turnover by recruiting ubiquitin E3 ligases such as Smurf1 and Smurf2 |
|
Publications: |
3 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
+ |
SMURF | down-regulates activity
ubiquitination
|
SMAD7 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253260 |
|
|
Homo sapiens |
|
pmid |
sentence |
12519765 |
Smad ubiquitin regulatory factor 1 (Smurf1), a HECT type E3 ubiquitin ligase, interacts with inhibitory Smad7 and induces translocation of Smad7 to the cytoplasm |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | TGF-beta Signaling |
+ |
WWP1 | up-regulates
binding
|
SMAD7 |
0.72 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-126128 |
|
|
Homo sapiens |
|
pmid |
sentence |
15221015 |
Wwp1 associated with smad7 and induced its nuclear export, and enhanced binding of smad7 to tgf-beta type i receptor to cause ubiquitination and degradation of the receptor. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | down-regulates
binding
|
TAB1 |
0.561 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112645 |
|
|
Homo sapiens |
|
pmid |
sentence |
11737269 |
Smad6 interacts with tak1 and tab1, and smad7 with tab1. The interaction of i-smads with tak1 and/or tab1 implies that several mechanisms exist underlying the repression of the tak1-p38 kinase pathway by i-smads. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMAD7 | down-regulates quantity
transcriptional regulation
|
SMAD3 |
0.596 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260437 |
|
|
Homo sapiens |
|
pmid |
sentence |
30017632 |
The downstream molecules including mad2, smad3, smad4 and smad7 are involved in TGF-β1-induced EMT,while Smad7 blocks the smad3 expression |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS, TGF-beta Signaling |