+ |
TGFBR2 | up-regulates activity
phosphorylation
|
TGFBR1 |
0.71 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246728 |
Ser172 |
SLDRPFIsEGTTLKD |
Homo sapiens |
|
pmid |
sentence |
8576253 |
Recent studies have revealed that upon TGF-beta binding several serine and threonine residues in the GS domain of TGF-beta type I receptor (T beta R-I) are phosphorylated by TGF-beta type II receptor (T beta R-II) and that the phosphorylation of GS domain is essential for TGF-beta signalingThese observations indicate that serine 172 and threonine 176 of T beta R-I are dispensable for extracellular matrix protein production but essential to the growth inhibition by TGF-beta |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255961 |
Thr176 |
PFISEGTtLKDLIYD |
in vitro |
|
pmid |
sentence |
8576253 |
From our present data, it is not easy to deduce the mechanistic significance of serine 172 and threonine 176 of TβR-I in TGF-β signaling. Although it was reported that TGF-β-induced phosphorylation of these residues was not detected in vivo(22), it is still possible that TβR-II may phosphorylate these residues as minor phosphorylation site(s). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246732 |
Thr176 |
PFISEGTtLKDLIYD |
Homo sapiens |
|
pmid |
sentence |
8576253 |
Recent studies have revealed that upon TGF-beta binding several serine and threonine residues in the GS domain of TGF-beta type I receptor (T beta R-I) are phosphorylated by TGF-beta type II receptor (T beta R-II) and that the phosphorylation of GS domain is essential for TGF-beta signalingThese observations indicate that serine 172 and threonine 176 of T beta R-I are dispensable for extracellular matrix protein production but essential to the growth inhibition by TGF-beta |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255962 |
Thr200 |
LPLLVQRtIARTIVL |
in vitro |
|
pmid |
sentence |
8576253 |
From our present data, it is not easy to deduce the mechanistic significance of serine 172 and threonine 176 of TβR-I in TGF-β signaling. Although it was reported that TGF-β-induced phosphorylation of these residues was not detected in vivo(22), it is still possible that TβR-II may phosphorylate these residues as minor phosphorylation site(s). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-32744 |
Thr200 |
LPLLVQRtIARTIVL |
Neovison vison |
|
pmid |
sentence |
7774578 |
The tgf-beta type ii receptor (t beta r-ii) is a transmembrane serine/threonine kinase that, upon ligand binding, recruits and phosphorylates a second transmembrane kinase, t beta r-i, as a requirement for signal transduction. In contrast to the relatively innocuous nature of single site mutations in the ttsgsgsg sequence, mutation of thr200 or 204 to valine causes marked losses in ligand-induced phosphorylation and signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-32748 |
Thr204 |
VQRTIARtIVLQESI |
Neovison vison |
|
pmid |
sentence |
7774578 |
The TGF-beta type II receptor (T beta R-II) is a transmembrane serine/threonine kinase that, upon ligand binding, recruits and phosphorylates a second transmembrane kinase, T beta R-I, as a requirement for signal transduction. In contrast to the relatively innocuous nature of single site mutations in the ttsgsgsg sequence, mutation of thr200 or 204 to valine causes marked losses in ligand-induced phosphorylation and signaling. |
|
Publications: |
6 |
Organism: |
Homo Sapiens, In Vitro, Neovison Vison |
Pathways: | COVID-19 Causal Network, Fibrosis, Hepatocellular Tumor, Multiple sclerosis, Pancreatic ductal adenocarcinoma (PDA), SARS-CoV FIBROSIS, Thyroid cancer, TGF-beta Signaling, TGFb in cancer |
+ |
TGFBR2 | up-regulates activity
phosphorylation
|
USP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273604 |
Ser207 |
ENYGRKGsASQVPSQ |
in vitro |
|
pmid |
sentence |
29490279 |
Here, we report the role of USP2a in promoting metastasis by facilitating TGF-β-triggered signaling. USP2a interacts with TGFBR1 and TGFBR2 upon TGF-β stimulation and removes K33-linked polyubiquitin chains from Lys502 of TGFBR1, promoting the recruitment of SMAD2/3. Simultaneously, TGFBR2 phosphorylates Ser207/Ser225 of USP2a, leading to the disassociation of SMAD2/3 from TGFBR1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273603 |
Ser225 |
SRVPEIIsPTYRPIG |
in vitro |
|
pmid |
sentence |
29490279 |
Here, we report the role of USP2a in promoting metastasis by facilitating TGF-β-triggered signaling. USP2a interacts with TGFBR1 and TGFBR2 upon TGF-β stimulation and removes K33-linked polyubiquitin chains from Lys502 of TGFBR1, promoting the recruitment of SMAD2/3. Simultaneously, TGFBR2 phosphorylates Ser207/Ser225 of USP2a, leading to the disassociation of SMAD2/3 from TGFBR1. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
TGFBR2 | up-regulates activity
phosphorylation
|
TGFBR2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236087 |
Ser213 |
TRKLMEFsEHCAIIL |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
9155023 |
Here we show that TbetaRII kinase is regulated intricately by autophosphorylation on at least three serine residues. Ser213, in the membrane-proximal segment outside the kinase domain, undergoes intra-molecular autophosphorylation which is essential for the activation of TbetaRII kinase activity, activation of TbetaRI and TGF-beta-induced growth inhibition. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246743 |
Ser409 |
LRLDPTLsVDDLANS |
Homo sapiens |
HEP-3B Cell |
pmid |
sentence |
9155023 |
Ser213, in the membrane-proximal segment outside the kinase domain, undergoes intra-molecular autophosphorylation which is essential for the activation of TbetaRII kinase activity, activation of TbetaRI and TGF-beta-induced growth inhibition. In contrast, phosphorylation of Ser409 and Ser416, located in a segment corresponding to the substrate recognition T-loop region in a three-dimensional structural model of protein kinases, is enhanced by receptor dimerization and can occur via an intermolecular mechanism. Phosphorylation of Ser409 is essential for TbetaRII kinase signaling, while phosphorylation of Ser416 inhibits receptor function. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-48859 |
Tyr259 |
KGRFAEVyKAKLKQN |
in vitro |
|
pmid |
sentence |
9169454 |
Tryptic mapping and amino acid sequencing of in vitro autophosphorylated type ii receptor cytoplasmic domain allowed the localization of the sites of tyrosine phosphorylation to positions 259, 336, and 424. Replacement of all three tyrosines with phenylalanines strongly inhibited the kinase activity of the receptor, suggesting that tyrosine autophosphorylation may play an autoregulatory role for the kinase activity of this receptor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-48863 |
Tyr336 |
AKGNLQEyLTRHVIS |
in vitro |
|
pmid |
sentence |
9169454 |
Tryptic mapping and amino acid sequencing of in vitro autophosphorylated type ii receptor cytoplasmic domain allowed the localization of the sites of tyrosine phosphorylation to positions 259, 336, and 424. Replacement of all three tyrosines with phenylalanines strongly inhibited the kinase activity of the receptor, suggesting that tyrosine autophosphorylation may play an autoregulatory role for the kinase activity of this receptor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-48867 |
Tyr424 |
GQVGTARyMAPEVLE |
in vitro |
|
pmid |
sentence |
9169454 |
Tryptic mapping and amino acid sequencing of in vitro autophosphorylated type ii receptor cytoplasmic domain allowed the localization of the sites of tyrosine phosphorylation to positions 259, 336, and 424. Replacement of all three tyrosines with phenylalanines strongly inhibited the kinase activity of the receptor, suggesting that tyrosine autophosphorylation may play an autoregulatory role for the kinase activity of this receptor. |
|
Publications: |
5 |
Organism: |
Homo Sapiens, In Vitro |
Pathways: | COVID-19 Causal Network, Fibrosis, Hepatocellular Tumor, Multiple sclerosis, Pancreatic ductal adenocarcinoma (PDA), SARS-CoV FIBROSIS, Thyroid cancer, TGF-beta Signaling, TGFb in cancer |
+ |
TGFBR2 | up-regulates
phosphorylation
|
PARD6A |
0.443 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227484 |
Ser345 |
RGDGSGFsL |
Homo sapiens |
NMuMg Cell |
pmid |
sentence |
15761148 |
We demonstrate that Par6, a regulator of epithelial cell polarity and tight-junction assembly, interacts with TGFbeta receptors and is a substrate of the type II receptor, TbetaRII. [...] These data suggest that T_RII phosphorylates Par6 at its penultimate residue, Ser345. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200193 |
Ser345 |
RGDGSGFsL |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
23249950 |
Transforming growth factor ? (tgf-?) Has been shown to regulate cell plasticity through the phosphorylation of par6 on a conserved serine residue (s345) by the type ii tgf-? Receptor. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TGFBR2 | down-regulates activity
phosphorylation
|
TGFBR2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-48412 |
Ser416 |
SVDDLANsGQVGTAR |
Homo sapiens |
|
pmid |
sentence |
9155023 |
Tbetarii kinase is regulated intricately by autophosphorylation on at least three serine residues. Phosphorylation of ser416 inhibits receptor function. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246737 |
Ser416 |
SVDDLANsGQVGTAR |
Homo sapiens |
HEP-3B Cell |
pmid |
sentence |
9155023 |
Ser213, in the membrane-proximal segment outside the kinase domain, undergoes intra-molecular autophosphorylation which is essential for the activation of TbetaRII kinase activity, activation of TbetaRI and TGF-beta-induced growth inhibition. In contrast, phosphorylation of Ser409 and Ser416, located in a segment corresponding to the substrate recognition T-loop region in a three-dimensional structural model of protein kinases, is enhanced by receptor dimerization and can occur via an intermolecular mechanism. Phosphorylation of Ser409 is essential for TbetaRII kinase signaling, while phosphorylation of Ser416 inhibits receptor function. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, Hepatocellular Tumor, Multiple sclerosis, Pancreatic ductal adenocarcinoma (PDA), SARS-CoV FIBROSIS, Thyroid cancer, TGF-beta Signaling, TGFb in cancer |
+ |
SRC | up-regulates
phosphorylation
|
TGFBR2 |
0.285 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182963 |
Tyr284 |
KIFPYEEyASWKTEK |
Homo sapiens |
|
pmid |
sentence |
19114990 |
Tbetarii can also be phosphorylated by src, a non-rtk, on y284, which can serve as a docking site for the recruitment of grb2 and shc, thereby bridging tbetarii to mapk activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TGFBR2 | up-regulates
binding
|
PIK3R1 |
0.459 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227521 |
|
|
Homo sapiens |
Respiratory Smooth Muscle |
pmid |
sentence |
9435577 |
These studies revealed that PI 3-kinase is associated in vivo with both TGF-_ receptor subtypes and that TGF-_1 stimulation enhances PI 3-kinase activity associated with type I TGF-_ receptor in hASM cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TGFb | up-regulates activity
binding
|
TGFBR2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256179 |
|
|
Homo sapiens |
Macrophage |
pmid |
sentence |
22703233 |
TGFbeta signals are transmitted via a cell surface receptor complex consisting of the TGFbeta type I receptor (TbetaRI) and TGFbeta type II receptor (TbetaRII). To initiate signal transduction, TGFbeta binds to TbetaRII, which in turn recruits TbetaRI, leading to the formation of a tetrameric receptor complex. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256178 |
|
|
Homo sapiens |
|
pmid |
sentence |
22326956 |
TGF-beta signaling mediates a wide range of biological activities in development and disease. TGF-beta ligands signal through heterodimeric type I and type II receptors (TGF-beta receptor type I [TbetaRI, also known as ALK5 and TGFBR1] and TbetaRII) that are members of the serine/threonine kinase family. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, Hepatocellular Tumor, Multiple sclerosis, Pancreatic ductal adenocarcinoma (PDA), SARS-CoV FIBROSIS, Thyroid cancer, TGFb in cancer |
+ |
SMURF2 | down-regulates activity
ubiquitination
|
TGFBR2 |
0.577 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195681 |
|
|
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 |
+ |
TGFB1 | up-regulates activity
binding
|
TGFBR2 |
0.847 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236080 |
|
|
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
1310899 |
A cdna encoding the tgf-beta type ii receptor protein has been isolated by an expression cloning strategy. The cloned cdna, when transfected into cos cells, leads to overexpression of an approximately 80 kd protein that specifically binds radioiodinated tgf-beta 1. Excess tgf-beta 1 competes for binding of radioiodinated tgf-beta 1 in a dose-dependent manner and is more effective than tgf-beta 2. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
Pathways: | COVID-19 Causal Network, Thyroid cancer, TGF-beta Signaling, TGFb in cancer |
+ |
SMURF2 | down-regulates quantity by destabilization
polyubiquitination
|
TGFBR2 |
0.577 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272939 |
|
|
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 |
+ |
DAXX | up-regulates
binding
|
TGFBR2 |
0.508 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109542 |
|
|
Homo sapiens |
B-lymphocyte, Lymphoma Cell |
pmid |
sentence |
11483955 |
Tgf-beta-induced apoptosis is mediated by the adapter protein daxx that facilitates jnk activation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TGFBR2 | up-regulates
phosphorylation
|
TGFBR1 |
0.71 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255032 |
|
|
Homo sapiens |
|
pmid |
sentence |
26194464 |
TGF-b ligands bind to TGF-b type II receptor (TbRII), which transphosphorylates and activates TGF-b type I receptor (TbRI). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, Hepatocellular Tumor, Multiple sclerosis, Pancreatic ductal adenocarcinoma (PDA), SARS-CoV FIBROSIS, Thyroid cancer, TGF-beta Signaling, TGFb in cancer |
+ |
HSP90AA1 | up-regulates
binding
|
TGFBR2 |
0.392 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179271 |
|
|
Homo sapiens |
|
pmid |
sentence |
18591668 |
The data in fig. 5 suggest that hsp90 specifically interacts with t?RI And t?RII In vitro and in vivo. Coupled with our data showing that loss of hsp90 function decreases t?R Levels and blocks tgf?-Induced smad2/3 activation and transcription, this result suggests that hsp90 controls tgf? Signaling as an essential component for stabilizing t?Rs. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TGFB2 | up-regulates
binding
|
TGFBR2 |
0.744 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-16690 |
|
|
Homo sapiens |
|
pmid |
sentence |
1310899 |
A cdna encoding the tgf-beta type ii receptor protein has been isolated by an expression cloning strategy. The cloned cdna, when transfected into cos cells, leads to overexpression of an approximately 80 kd protein that specifically binds radioiodinated tgf-beta 1. Excess tgf-beta 1 competes for binding of radioiodinated tgf-beta 1 in a dose-dependent manner and is more effective than tgf-beta 2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104795 |
|
|
Homo sapiens |
|
pmid |
sentence |
11157754 |
We show that tbetarii-b, an alternatively spliced variant of the tgf-beta type ii receptor, is a tgf-beta2 binding receptor, which mediates signalling via the smad pathway in the absence of any tgf-beta type iii receptor |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | TGF-beta Signaling |
+ |
SMURF1 | down-regulates activity
ubiquitination
|
TGFBR2 |
0.598 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195672 |
|
|
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 |
+ |
TGFB1 | up-regulates
binding
|
TGFBR2 |
0.847 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255030 |
|
|
Homo sapiens |
|
pmid |
sentence |
26194464 |
TGF-b ligands bind to TGF-b type II receptor (TbRII), which transphosphorylates and activates TGF-b type I receptor (TbRI). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Thyroid cancer, TGF-beta Signaling, TGFb in cancer |
+ |
TGFBR2 | up-regulates activity
binding
|
ZFYVE9 |
0.551 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-245093 |
|
|
Homo sapiens |
|
pmid |
sentence |
9865696 |
Sara functions to recruit smad2 to the tgfbeta receptor by controlling the subcellular localization of smad2 and by interacting with the tgfbeta receptor complex |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | TGF-beta Signaling |
+ |
TGFBR2 | up-regulates activity
binding
|
PIK3R1 |
0.459 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-217830 |
|
|
Homo sapiens |
|
pmid |
sentence |
19114990 |
in immunoprecipitation esperiments, the TGF _ RII receptor was found to be constitutively associated with p85, the regulatory subunity of PI3K |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LY-2157299 | down-regulates
chemical inhibition
|
TGFBR2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-193778 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TGFBR2 | up-regulates activity
binding
|
PI3K |
0.421 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252731 |
|
|
Homo sapiens |
|
pmid |
sentence |
19114990 |
In immunoprecipitation esperiments, the TGF _ RII receptor was found to be constitutively associated with p85, the regulatory subunity of PI3K |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Hepatocellular Tumor, Pancreatic ductal adenocarcinoma (PDA) |
+ |
TGFB3 | up-regulates
binding
|
TGFBR2 |
0.861 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104798 |
|
|
Homo sapiens |
|
pmid |
sentence |
11157754 |
T?RII Is known to bind the isoforms tgf??1 And tgf??3. Binding of these ligands causes recruitment of the type i receptor (t?RI) into a signalling receptor complex followed by activation of t?RI Through transphosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EIF3I | up-regulates
binding
|
TGFBR2 |
0.33 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-60700 |
|
|
Homo sapiens |
|
pmid |
sentence |
9774674 |
Another receptor-associated protein is trip-1, which interacts with and is phosphorylated by tbrii and contains five wd-40 repeats. The association of wd-40 repeat proteins may then allow them to play a role in signaling by the serine/threonine kinase receptors. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMURF | down-regulates activity
ubiquitination
|
TGFBR2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253265 |
|
|
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 |
Pathways: | TGF-beta Signaling |
+ |
KLF14 | down-regulates quantity by repression
transcriptional regulation
|
TGFBR2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271696 |
|
|
|
|
pmid |
sentence |
19088080 |
Mechanistically, KLF14 represses the TGFbetaRII promoter via a co-repressor complex containing mSin3A and HDAC2. |
|
Publications: |
1 |
+ |
SP6 | down-regulates quantity by repression
transcriptional regulation
|
TGFBR2 |
0.313 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271695 |
|
|
|
|
pmid |
sentence |
19088080 |
Mechanistically, KLF14 represses the TGFbetaRII promoter via a co-repressor complex containing mSin3A and HDAC2. |
|
Publications: |
1 |
+ |
TGFBR2 | up-regulates
binding
|
PI3K |
0.421 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252732 |
|
|
Homo sapiens |
Respiratory Smooth Muscle |
pmid |
sentence |
9435577 |
These studies revealed that PI 3-kinase is associated in vivo with both TGF-_ receptor subtypes and that TGF-_1 stimulation enhances PI 3-kinase activity associated with type I TGF-_ receptor in hASM cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Hepatocellular Tumor, Pancreatic ductal adenocarcinoma (PDA) |
+ |
TGFBR2 | up-regulates
binding
|
PIK3R2 |
0.444 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227528 |
|
|
Homo sapiens |
|
pmid |
sentence |
9435577 |
These studies revealed that PI 3-kinase is associated in vivo with both TGF-_ receptor subtypes and that TGF-_1 stimulation enhances PI 3-kinase activity associated with type I TGF-_ receptor in hASM cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TGFBR2 | up-regulates activity
binding
|
VPS39 |
0.331 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261374 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
12941698 |
TLP interacts with TGF-β and activin receptors in vivo. Endogenous TLP associates with both active and kinase-deficient TGF-beta and activin type II receptors, but interacts with the common-mediator Smad4 only in the presence of TGF-beta/activin signaling. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |