_enti_e7
_enti_e8
_enti_e1
_enti_e9
_enti_e10
_enti_e4
_enti_e3
_enti_e2
_enti_e55
_enti_e53
_enti_e59
_enti_e54
_enti_e52
_enti_e51
_enti_e56
_enti_e50
_enti_e58
_enti_e57
_enti_e61
_enti_e62
_enti_e60
g2_fact_g2
g1_fact_g1
g2_fact_g12
g2_fact_g13
g1_fact_g14
p1_propro_p1
PMID: 10611754, 9759503, 9393997, 9561843
Receptor complexes are heterotetrameric, consisting of two ‘type II' receptors (7585 kDa), which bind ligand, and two signal transducing ‘type I' receptors (5060 kDa) which, in most instances, cannot bind ligand directly and thus are considered to act downstream of the type II receptor.
PMID: 10611754
Signals from all three isoforms of TGF-beta appear to be mediated by a single type II receptor called TBR-II and one type I receptor referred to either as TBR-I or ALK-5 (activin receptor-like kinase).
c1 cso30:c:InputProcess connector
c2 cso30:c:InputProcess connector
c5 cso30:c:OutputProcess connector
p2_propro_p2
PMID: 10611754
The assembly of the heteromeric complex is initiated by ligand binding and stabilized by interactions between the cytoplasmic domains of the type II and type I receptors.
PMID: 10611754
Signals from all three isoforms of TGF-beta appear to be mediated by a single type II receptor called TBR-II and one type I receptor referred to either as TBR-I or ALK-5 (activin receptor-like kinase).
c3 cso30:c:InputProcess connector
c6 cso30:c:InputProcess connector
c4 cso30:c:OutputProcess connector
p3_propro_p3
PMID: 10611754, 10187774
Another type I receptor, ALK-1, expressed on endothelial cells and mutated in the autosomal dominant disorder hereditary hemorrhagic telangiectasia (HHT), can also complex with ligand-bound TBR-II, but its role in signaling is presently not understood.
c8 cso30:c:InputProcess connector
c7 cso30:c:InputProcess connector
c9 cso30:c:OutputProcess connector
p4_propro_p4
PMID: 10611754
Signals from all three isoforms of TGF-beta appear to be mediated by a single type II receptor called TBR-II and one type I receptor referred to either as TBR-I or ALK-5 (activin receptor-like kinase).
c11 cso30:c:InputProcess connector
c10 cso30:c:InputProcess connector
c12 cso30:c:OutputProcess connector
p5_propro_p5
PMID: 10611754
Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.
c15 cso30:c:InputProcess connector
c26 cso30:c:InputProcess connector
c14 cso30:c:OutputProcess connector
p6_propro_p6
PMID: 10611754
Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.
c16 cso30:c:InputProcess connector
c17 cso30:c:InputProcess connector
c18 cso30:c:OutputProcess connector
p7_propro_p7
PMID: 10611754
Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.
c19 cso30:c:InputProcess connector
c23 cso30:c:InputProcess connector
c20 cso30:c:OutputProcess connector
p8_propro_p8
PMID: 10611754
Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.
c21 cso30:c:InputProcess connector
c24 cso30:c:InputProcess connector
c22 cso30:c:OutputProcess connector
p9_propro_p9
PMID: 10611754
Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.
c25 cso30:c:InputProcess connector
c29 cso30:c:InputProcess connector
c27 cso30:c:OutputProcess connector
p10_propro_p10
PMID: 10611754
Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.
c13 cso30:c:InputProcess connector
c30 cso30:c:InputProcess connector
c28 cso30:c:OutputProcess connector
p11_propro_p11
PMID: 10611754
Unlike betaglycan, endoglin binds TGF-beta1 and TGF-beta3 selectively.
c31 cso30:c:InputProcess connector
c32 cso30:c:InputProcess connector
c35 cso30:c:OutputProcess connector
p12_propro_p12
PMID: 10611754
Unlike betaglycan, endoglin binds TGF-beta1 and TGF-beta3 selectively.
c33 cso30:c:InputProcess connector
c34 cso30:c:InputProcess connector
c36 cso30:c:OutputProcess connector
p13_propro_p13
PMID: 10611754
This model for receptor activation involves potentiation of the kinase activity of the type I receptor by phosphorylation of several residues in a glycine-serine-rich juxtamembrane domain (GS domain) by the type II receptor kinase.
c37 cso30:c:InputProcess connector
c38 cso30:c:OutputProcess connector
p14_propro_p14
PMID: 10611754
receptor-activated Smads bind to and are phosphorylated on two C-terminal serine residues in their MH2 domain by the type I receptor kinase.
c39 cso30:c:InputProcess connector
c40 cso30:c:InputProcess connector
c41 cso30:c:OutputProcess connector
p15_propro_p15
PMID: 10611754
receptor-activated Smads bind to and are phosphorylated on two C-terminal serine residues in their MH2 domain by the type I receptor kinase.
c42 cso30:c:InputProcess connector
c43 cso30:c:OutputProcess connector
p16_propro_p16
PMID: 10611754
the phosphorylated, pathway-specific Smads then hetero-oligomerize in the cytoplasm with the common mediator, Smad4.
c46 cso30:c:InputProcess connector
c47 cso30:c:InputProcess connector
c49 cso30:c:OutputProcess connector
p17_propro_p17
PMID: 10611754
the phosphorylated, pathway-specific Smads then hetero-oligomerize in the cytoplasm with the common mediator, Smad4.
c44 cso30:c:InputProcess connector
c48 cso30:c:OutputProcess connector
c45 cso30:c:OutputProcess connector
p18_propro_p18
PMID: 10611754
the heteromeric Smad4-containing complex is then translocated to the nucleus where it mediates transcriptional activation of the target gene.
c50 cso30:c:InputProcess connector
c51 cso30:c:OutputProcess connector
p19_propro_p19
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
PMID: 10611754
The FYVE domain of SARA is predicted to interact with phosphosphotidyl inositol-3-phosphate in the cell membrane while an adjacent Smad binding domain recruits Smad2/3 from the cytoplasmic reservoir; the C-terminal domain anchors the Smad-SARA complex to the receptor complex.
c53 cso30:c:InputProcess connector
c52 cso30:c:InputProcess connector
c125 cso30:c:InputProcess connector
c54 cso30:c:OutputProcess connector
p20_propro_p20
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
PMID: 10611754
The FYVE domain of SARA is predicted to interact with phosphosphotidyl inositol-3-phosphate in the cell membrane while an adjacent Smad binding domain recruits Smad2/3 from the cytoplasmic reservoir; the C-terminal domain anchors the Smad-SARA complex to the receptor complex.
c55 cso30:c:InputProcess connector
c56 cso30:c:InputProcess connector
c126 cso30:c:InputProcess connector
c67 cso30:c:OutputProcess connector
p21_propro_p21
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c57 cso30:c:InputProcess connector
c58 cso30:c:OutputProcess connector
p22_propro_p22
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c59 cso30:c:InputProcess connector
c61 cso30:c:OutputProcess connector
c127 cso30:c:OutputProcess connector
p23_propro_p23
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c62 cso30:c:InputProcess connector
c63 cso30:c:InputProcess connector
c64 cso30:c:OutputProcess connector
p24_propro_p24
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
PMID: 10611754
Examples are the activating phosphorylation and nuclear translocation of Smad2 following treatment of cells with HGF [54] or activation of the SAPK/JNK pathway.
c65 cso30:c:InputProcess connector
c178 cso30:c:InputAssociation connector
c66 cso30:c:OutputProcess connector
p25_propro_p25
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c71 cso30:c:InputProcess connector
c72 cso30:c:OutputProcess connector
c69 cso30:c:OutputProcess connector
p26_propro_p26
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c68 cso30:c:InputProcess connector
c70 cso30:c:OutputProcess connector
p27_propro_p27
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c73 cso30:c:InputProcess connector
c74 cso30:c:InputProcess connector
c75 cso30:c:OutputProcess connector
p28_propro_p28
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c76 cso30:c:InputProcess connector
c77 cso30:c:OutputProcess connector
p29_propro_p29
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c87 cso30:c:InputProcess connector
c109 cso30:c:InputProcess connector
c89 cso30:c:OutputProcess connector
p30_propro_p30
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c86 cso30:c:InputProcess connector
c108 cso30:c:InputProcess connector
c88 cso30:c:OutputProcess connector
p31_propro_p31
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c78 cso30:c:InputProcess connector
c79 cso30:c:InputProcess connector
c80 cso30:c:OutputProcess connector
p32_propro_p32
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c81 cso30:c:InputProcess connector
c82 cso30:c:InputProcess connector
c83 cso30:c:OutputProcess connector
p33_propro_p33
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c84 cso30:c:InputProcess connector
c85 cso30:c:InputProcess connector
c90 cso30:c:OutputProcess connector
p34_propro_p34
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c93 cso30:c:InputProcess connector
c94 cso30:c:OutputProcess connector
p35_propro_p35
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c95 cso30:c:InputProcess connector
c96 cso30:c:OutputProcess connector
c113 cso30:c:OutputProcess connector
p36_propro_p36
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c97 cso30:c:InputProcess connector
c98 cso30:c:InputProcess connector
c99 cso30:c:OutputProcess connector
p37_propro_p37
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c100 cso30:c:InputProcess connector
c101 cso30:c:InputProcess connector
c102 cso30:c:OutputProcess connector
p38_propro_p38
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c103 cso30:c:InputProcess connector
c104 cso30:c:InputProcess connector
c107 cso30:c:OutputProcess connector
p39_propro_p39
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c105 cso30:c:InputProcess connector
c106 cso30:c:OutputProcess connector
p40_propro_p40
PMID: 10611754, 9311995, 8752209
Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.
c91 cso30:c:InputProcess connector
c92 cso30:c:OutputProcess connector
p41_propro_p41
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c114 cso30:c:InputProcess connector
c111 cso30:c:OutputProcess connector
p42_propro_p42
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c110 cso30:c:InputProcess connector
c112 cso30:c:OutputProcess connector
p43_propro_p43
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
c115 cso30:c:InputProcess connector
c116 cso30:c:InputProcess connector
c117 cso30:c:OutputProcess connector
p44_propro_p44
PMID: 10611754, 9788633
Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.
PMID: 10611754
Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.
c118 cso30:c:InputProcess connector
c171 cso30:c:InputInhibitor connector
c174 cso30:c:InputInhibitor connector
c119 cso30:c:OutputProcess connector
p45_propro_p45
PMID: 10611754, 9214508, 9670020
Determination of the tertiary structure of the C-terminal domain of Smad4 shows that it associates as a homotrimer [25], and data now suggest that hetero-oligomeric Smads are also trimeric.
c120 cso30:c:InputProcess connector
c121 cso30:c:OutputProcess connector
p46_propro_p46
PMID: 19611754
he FYVE domain of SARA is predicted to interact with phosphosphotidyl inositol-3-phosphate in the cell membrane while an adjacent Smad binding domain recruits Smad2/3 from the cytoplasmic reservoir.
c122 cso30:c:InputProcess connector
c123 cso30:c:InputProcess connector
c124 cso30:c:OutputProcess connector
p47_propro_p47
PMID: 10611754
The mRNAs for Smad6 and Smad7 are rapidly induced by treatment of cells with TGF-beta suggesting that anti-Smads are direct effectors of a ligand-induced signal to suppress a response.
c128 cso30:c:InputAssociation connector
c130 cso30:c:OutputProcess connector
p48_propro_p48
PMID: 10611754
The mRNAs for Smad6 and Smad7 are rapidly induced by treatment of cells with TGF-beta suggesting that anti-Smads are direct effectors of a ligand-induced signal to suppress a response.
c129 cso30:c:InputAssociation connector
c131 cso30:c:OutputProcess connector
p49_propro_p49
PMID: 10611754
the MH2 domain of Smad2 interacts with the C-terminal domain (Smad-interaction domain, SID) of FAST-1 directly, while the binding of Smad4 is assumed to be dependent on its association with activated Smad2 and possibly also on its ability to stabilize the DNA complex through its MH1 domain.
c60 cso30:c:InputProcess connector
c133 cso30:c:InputProcess connector
c132 cso30:c:OutputProcess connector
p50_propro_p50
PMID: 10611754, 9732876
Smad3 can interact directly with c-Jun and c-Fos through its MH1 and MH2 domains, respectively leading to the suggestion that AP-1 DNA binding sites can be activated either by direct binding of Smad3 and Smad4 to the DNA element itself or by interaction of the heteromeric Smad3/Smad4 complex and the AP-1 transcription factor complex, in such a manner as to provide additional stability to the complex.
c134 cso30:c:InputProcess connector
c135 cso30:c:InputProcess connector
c136 cso30:c:OutputProcess connector
p51_propro_p51
PMID: 10611754, 9732876
Smad3 can interact directly with c-Jun and c-Fos through its MH1 and MH2 domains, respectively leading to the suggestion that AP-1 DNA binding sites can be activated either by direct binding of Smad3 and Smad4 to the DNA element itself or by interaction of the heteromeric Smad3/Smad4 complex and the AP-1 transcription factor complex, in such a manner as to provide additional stability to the complex.
c137 cso30:c:InputProcess connector
c138 cso30:c:InputProcess connector
c139 cso30:c:OutputProcess connector
p52_propro_p52
PMID: 10611754
These proteins have now been shown to also interact with Smad proteins in the regulation of transcription.
PMID: 10611754, 9689110
The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.
c140 cso30:c:InputProcess connector
c144 cso30:c:InputProcess connector
c155 cso30:c:InputInhibitor connector
c148 cso30:c:OutputProcess connector
p53_propro_p53
PMID: 10611754, 9679060, 9865696
Depending on the system and the cell type, ligand-activated Smad1, Smad2, and Smad3, as well as Smad4 have all been shown to be capable of binding to CBP/p300.
PMID: 10611754, 9689110
The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.
c141 cso30:c:InputProcess connector
c145 cso30:c:InputProcess connector
c156 cso30:c:InputInhibitor connector
c149 cso30:c:OutputProcess connector
p54_propro_p54
PMID: 10611754, 9679060, 9865696
Depending on the system and the cell type, ligand-activated Smad1, Smad2, and Smad3, as well as Smad4 have all been shown to be capable of binding to CBP/p300.
PMID: 10611754, 9689110
The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.
c142 cso30:c:InputProcess connector
c146 cso30:c:InputProcess connector
c157 cso30:c:InputInhibitor connector
c150 cso30:c:OutputProcess connector
p55_propro_p55
PMID: 10611754, 9679060, 9865696
Depending on the system and the cell type, ligand-activated Smad1, Smad2, and Smad3, as well as Smad4 have all been shown to be capable of binding to CBP/p300.
PMID: 10611754, 9689110
The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.
c143 cso30:c:InputProcess connector
c147 cso30:c:InputProcess connector
c158 cso30:c:InputInhibitor connector
c151 cso30:c:OutputProcess connector
p56_propro_p56
PMID: 10611754, 9689110
The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.
c152 cso30:c:InputProcess connector
c153 cso30:c:InputProcess connector
c154 cso30:c:OutputProcess connector
p57_propro_p57
PMID: 10611754
Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.
c159 cso30:c:InputProcess connector
c160 cso30:c:InputProcess connector
c161 cso30:c:OutputProcess connector
p60_propro_p60
PMID: 10611754
Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.
c162 cso30:c:InputProcess connector
c163 cso30:c:InputProcess connector
c164 cso30:c:OutputProcess connector
p58_propro_p58
PMID: 10611754
Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.
c165 cso30:c:InputProcess connector
c168 cso30:c:InputAssociation connector
c172 cso30:c:InputAssociation connector
c170 cso30:c:OutputProcess connector
p59_propro_p59
PMID: 10611754
Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.
c166 cso30:c:InputProcess connector
c167 cso30:c:InputAssociation connector
c173 cso30:c:InputAssociation connector
c169 cso30:c:OutputProcess connector
p61_propro_p61
PMID: 10611754
Examples are the activating phosphorylation and nuclear translocation of Smad2 following treatment of cells with HGF [54] or activation of the SAPK/JNK pathway.
c175 cso30:c:InputProcess connector
c177 cso30:c:InputAssociation connector
c176 cso30:c:OutputProcess connector
p62_propro_p62
PMID: 10611754, 9712726, 10067896
Smad7 is also an important focal point of disparate signaling pathways as evidenced by its induction by EGF [35] and interferon.
c181 cso30:c:InputAssociation connector
c179 cso30:c:OutputProcess connector
p63_propro_p63
PMID: 10611754, 9712726, 10067896
Smad7 is also an important focal point of disparate signaling pathways as evidenced by its induction by EGF [35] and interferon.
c185 cso30:c:InputAssociation connector
c180 cso30:c:OutputProcess connector
p64_propro_p64
PMID: 10611754, 9712726, 10067896
Smad7 is also an important focal point of disparate signaling pathways as evidenced by its induction by EGF [35] and interferon.
c182 cso30:c:InputProcess connector
c184 cso30:c:InputProcess connector
c183 cso30:c:OutputProcess connector
p65_propro_p65
PMID: 10611754, 9707553
Another nuclear protein that strongly activates transcription without binding to DNA, MSG1, has been shown to interact functionally with the SAD domain in the middle linker region of Smad4 and to be required for activation of Smad4-dependent transcription in certain cells.
c186 cso30:c:InputProcess connector
c187 cso30:c:InputProcess connector
c188 cso30:c:OutputProcess connector
Smads_enti_MO000016824
Smads
Smad3_enti_MO000017450
Smad3
Smad4: Smad4_enti_MO000017458
Smad4: Smad4
Smad2_enti_MO000017658
Smad2
SARA_enti_MO000017659
SARA
Smad1_enti_MO000017762
Smad1
TGFbeta_enti_MO000016808
TGFbeta
TGFbeta: TBR2 (2): Tbr-1(2)_enti_e5
TGFbeta: TBR2 (2): Tbr-1(2)
TGFbeta: TBR2 (2)_enti_e11
TGFbeta: TBR2 (2)
Tbr-1_enti_MO000118339
Tbr-1
TBR2_enti_e6
TBR2
ALK-1 (2)_enti_MO000017720
ALK-1 (2)
TGFbeta: TBR2 (2): ALK-1(2)_enti_e12
TGFbeta: TBR2 (2): ALK-1(2)
ALK-5 (2)_enti_MO000017445
ALK-5 (2)
TGFbeta: TBR2 (2): ALK-5(2)_enti_e13
TGFbeta: TBR2 (2): ALK-5(2)
TGFbetaR-III (2)_enti_MO000017733
TGFbetaR-III (2)
TGFbeta3: TBR2 (2): TGFbetaR-III (2)_enti_e14
TGFbeta3: TBR2 (2): TGFbetaR-III (2)
TGFbeta2_enti_MO000013604
TGFbeta2
TGFbeta1: TBR2 (2)_enti_e15
TGFbeta1: TBR2 (2)
TGFbeta3_enti_MO000019248
TGFbeta3
TGFbeta1_enti_MO000017443
TGFbeta1
TGFbeta2: TBR2 (2)_enti_e16
TGFbeta2: TBR2 (2)
TGFbeta3: TBR2 (2)_enti_e17
TGFbeta3: TBR2 (2)
TGFbeta2: TBR2 (2): TGFbetaR-III (2)_enti_e18
TGFbeta2: TBR2 (2): TGFbetaR-III (2)
TGFbeta1: TBR2 (2): TGFbetaR-III (2)_enti_e19
TGFbeta1: TBR2 (2): TGFbetaR-III (2)
endoglin_enti_MO000004387
endoglin
TGFbeta1: TBR2 (2): endoglin_enti_e20
TGFbeta1: TBR2 (2): endoglin
TGFbeta3: TBR2 (2): endoglin_enti_e21
TGFbeta3: TBR2 (2): endoglin
TGFbeta: TBR2 (2): Tbr-1(2) {p}_enti_e23
TGFbeta: TBR2 (2): Tbr-1(2) {p}
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD_enti_e22
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD {p}_enti_e24
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD {p}
SMAD {p}_enti_e25
SMAD {p}
SMAD {p}: Smad4: Smad4_enti_e26
SMAD {p}: Smad4: Smad4
SMAD {p}: Smad4: Smad4 {nucleus}_enti_e27
SMAD {p}: Smad4: Smad4 {nucleus}
TGFbeta: TBR2 (2): Tbr-1(2) {p}: phosphosphotidyl inositol-3-phosphate: SARA: SMAD2_enti_e28
TGFbeta: TBR2 (2): Tbr-1(2) {p}: phosphosphotidyl inositol-3-phosphate: SARA: SMAD2
TGFbeta: TBR2 (2): Tbr-1(2) {p}: phosphosphotidyl inositol-3-phosphate: SARA: SMAD2 {p}_enti_e29
TGFbeta: TBR2 (2): Tbr-1(2) {p}: phosphosphotidyl inositol-3-phosphate: SARA: SMAD2 {p}
SMAD2 {p}: Smad4: Smad4_enti_e30
SMAD2 {p}: Smad4: Smad4
SMAD2 {p}_enti_e31
SMAD2 {p}
SMAD2 {p}: Smad4: Smad4 (nucleus)_enti_e32
SMAD2 {p}: Smad4: Smad4 (nucleus)
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD3_enti_e33
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD3
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD3 {p}_enti_e34
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD3 {p}
SMAD3 {p}_enti_e35
SMAD3 {p}
SMAD3 {p}: Smad4: Smad4_enti_e36
SMAD3 {p}: Smad4: Smad4
SMAD3 {p}: Smad4: Smad4(nucleus)_enti_e37
SMAD3 {p}: Smad4: Smad4(nucleus)
activin: Type II receptor (2): Type I activin recptor (2) {p}: SMAD2_enti_e38
activin: Type II receptor (2): Type I activin recptor (2) {p}: SMAD2
activin: Type II receptor (2): Type I activin recptor (2) {p}: SMAD3_enti_e39
activin: Type II receptor (2): Type I activin recptor (2) {p}: SMAD3
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD1_enti_e40
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD1
activin_enti_MO000016809
activin
Type II receptor (2)_enti_e41
Type II receptor (2)
activin: Type II receptor (2)_enti_e42
activin: Type II receptor (2)
Type I activin recptor (2)_enti_e43
Type I activin recptor (2)
activin: Type II receptor (2): Type I activin recptor (2)_enti_e44
activin: Type II receptor (2): Type I activin recptor (2)
BMP2_enti_MO000017729
BMP2
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD1 {p}_enti_e45
TGFbeta: TBR2 (2): Tbr-1(2) {p}: SMAD1 {p}
SMAD1 {p}_enti_e46
SMAD1 {p}
BMP2: Type II receptor (2)_enti_e47
BMP2: Type II receptor (2)
Type I receptor (2)_enti_e48
Type I receptor (2)
BMP2: Type II receptor (2): Type I receptor (2) {p} : SMAD1_enti_e63
BMP2: Type II receptor (2): Type I receptor (2) {p} : SMAD1
BMP2: Type II receptor (2): Type I receptor (2) {p}_enti_e64
BMP2: Type II receptor (2): Type I receptor (2) {p}
activin: Type II receptor (2): Type I activin recptor (2) {p}_enti_e65
activin: Type II receptor (2): Type I activin recptor (2) {p}
BMP2: Type II receptor (2): Type I receptor (2) {p} : SMAD1 {p}_enti_e66
BMP2: Type II receptor (2): Type I receptor (2) {p} : SMAD1 {p}
SMAD1 {p}: Smad4: Smad4_enti_e67
SMAD1 {p}: Smad4: Smad4
SMAD1 {p}: Smad4: Smad4 (nucleus)_enti_e68
SMAD1 {p}: Smad4: Smad4 (nucleus)
Smad4_enti_e69
Smad4
phosphosphotidyl inositol-3-phosphate_enti_e70
phosphosphotidyl inositol-3-phosphate
phosphosphotidyl inositol-3-phosphate: SARA_enti_e71
phosphosphotidyl inositol-3-phosphate: SARA
TGFbeta: TBR2 (2): Tbr-1(2) {p}: phosphosphotidyl inositol-3-phosphate: SARA_enti_e72
TGFbeta: TBR2 (2): Tbr-1(2) {p}: phosphosphotidyl inositol-3-phosphate: SARA
SMAD6_enti_G010667
SMAD6
SMAD7_enti_G010646
SMAD7
SMAD2 {p}: Smad4: Smad4 (nuclus): FAST1_enti_e73
SMAD2 {p}: Smad4: Smad4 (nuclus): FAST1
FAST1_enti_e74
FAST1
c-Jun_enti_MO000000049
c-Jun
SMAD3 {p}: Smad4: Smad4(nucleus): c-Jun_enti_e75
SMAD3 {p}: Smad4: Smad4(nucleus): c-Jun
c-Fos_enti_MO000000279
c-Fos
SMAD3 {p}: Smad4: Smad4(nucleus): c-Fos_enti_e76
SMAD3 {p}: Smad4: Smad4(nucleus): c-Fos
CBP:p300_enti_e77
CBP:p300
CBP: p300: SMAD1 {p}: Smad4: Smad4 (nucleus)_enti_e78
CBP: p300: SMAD1 {p}: Smad4: Smad4 (nucleus)
CBP: p300: SMAD3 {p}: Smad4: Smad4(nucleus)_enti_e79
CBP: p300: SMAD3 {p}: Smad4: Smad4(nucleus)
CBP: p300: SMAD2 {p}: Smad4: Smad4 (nucleus)_enti_e80
CBP: p300: SMAD2 {p}: Smad4: Smad4 (nucleus)
CBP: p300: SMAD {p}: Smad4: Smad4 {nucleus}_enti_e81
CBP: p300: SMAD {p}: Smad4: Smad4 {nucleus}
E1A_enti_MO000018970
E1A
CBP: p300: E1A_enti_e82
CBP: p300: E1A
BMP2: Type II receptor (2): Type I receptor (2)_enti_e49
BMP2: Type II receptor (2): Type I receptor (2)
EGF_enti_MO000000071
EGF
EGFR_enti_MO000000108
EGFR
EGF: EGFR_enti_e83
EGF: EGFR
HGF_enti_MO000017768
HGF
HGF receptor_enti_e86
HGF receptor
HGF: HGF receptor_enti_e87
HGF: HGF receptor
MAPKs_enti_MO000000077
MAPKs
IFNgamma_enti_MO000016665
IFNgamma
IFN gamma: IFNgamma receptor_enti_e84
IFN gamma: IFNgamma receptor
IFNgamma receptor_enti_e85
IFNgamma receptor
MSG1_enti_e88
MSG1
SMAD {p}: Smad4: Smad4 {nucleus}: MSG1_enti_e89
SMAD {p}: Smad4: Smad4 {nucleus}: MSG1