_enti_e7
_enti_e8
_enti_e1
_enti_e9
_enti_e10
_enti_e4
_enti_e2
_enti_e3
_enti_e55
_enti_e53
_enti_e59
_enti_e56
_enti_e52
_enti_e51
_enti_e50
_enti_e54
_enti_e58
_enti_e61
_enti_e57
_enti_e62
_enti_e60
g2_fact_g2
g1_fact_g14
g1_fact_g1
g2_fact_g12
g2_fact_g13
p1_propro_p1
PMID: 17576036, 10099820
In its inactive state, GR resides in the cytoplasm as a part of a large multiprotein complex containing heat shock proteins (hsp90, hsp70), co-chaperones and immunofillins. Ligand binding induces a series of conformational changes in the receptor that result in rearrangement of this complex, exposure of the GR nuclear localization signal and rapid nuclear translocation.
c1 cso30:c:InputProcess connector
c2 cso30:c:InputProcess connector
c3 cso30:c:OutputProcess connector
p2_propro_p2
PMID: 17576036, 10099820
In its inactive state, GR resides in the cytoplasm as a part of a large multiprotein complex containing heat shock proteins (hsp90, hsp70), co-chaperones and immunofillins. Ligand binding induces a series of conformational changes in the receptor that result in rearrangement of this complex, exposure of the GR nuclear localization signal and rapid nuclear translocation.
c4 cso30:c:InputProcess connector
c5 cso30:c:OutputProcess connector
p3_propro_p3
PMID: 17576036
Simple GREs contain a specific DNA sequence to which GR binds as a sole regulator, typically as a homodimer.
PMID: 17576036, 17559307, 9582068
GREs have been proposed to serve as the second ‘allosteric ligand’ for the receptor.
c6 cso30:c:InputProcess connector
c7 cso30:c:InputProcess connector
c8 cso30:c:OutputProcess connector
p4_propro_p4
PMID: 17576036, 8455596, 2884660, 2038339
Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription.
c9 cso30:c:InputAssociation connector
c12 cso30:c:OutputProcess connector
p5_propro_p5
PMID: 17576036, 8455596, 2884660, 2038339
Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription.
c10 cso30:c:InputAssociation connector
c13 cso30:c:OutputProcess connector
p6_propro_p6
PMID: 17576036, 8455596, 2884660, 2038339
Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription.
c11 cso30:c:InputAssociation connector
c14 cso30:c:OutputProcess connector
p7_propro_p7
PMID: 17576036, 8455596, 2884660, 2038339
Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription.
c15 cso30:c:InputInhibitor connector
c17 cso30:c:InputAssociation connector
c20 cso30:c:OutputProcess connector
p8_propro_p8
PMID: 17576036, 8455596, 2884660, 2038339
Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription.
c16 cso30:c:InputInhibitor connector
c18 cso30:c:InputAssociation connector
c19 cso30:c:OutputProcess connector
p9_propro_p9
PMID: 17576036, 2169352, 10995388, 9388192
Tethering GREs do not contain bona fide DNA recognition sequence for GR, but rather a binding site for another transcription factor which recruits GR through protein:protein interactions. Binding to tethering GREs often requires neither GR DNA binding activity nor its dimerization. Several transcription factors, including AP1, NFkappaB, Stat3 and Stat5 can provide a “tether” for GR.
c23 cso30:c:InputProcess connector
c24 cso30:c:InputProcess connector
c25 cso30:c:OutputProcess connector
p10_propro_p10
PMID: 17576036, 2169352, 10995388, 9388192
Tethering GREs do not contain bona fide DNA recognition sequence for GR, but rather a binding site for another transcription factor which recruits GR through protein:protein interactions. Binding to tethering GREs often requires neither GR DNA binding activity nor its dimerization. Several transcription factors, including AP1, NFkappaB, Stat3 and Stat5 can provide a “tether” for GR.
c22 cso30:c:InputProcess connector
c26 cso30:c:InputProcess connector
c27 cso30:c:OutputProcess connector
p11_propro_p11
PMID: 17576036, 2169352, 10995388, 9388192
Tethering GREs do not contain bona fide DNA recognition sequence for GR, but rather a binding site for another transcription factor which recruits GR through protein:protein interactions. Binding to tethering GREs often requires neither GR DNA binding activity nor its dimerization. Several transcription factors, including AP1, NFkappaB, Stat3 and Stat5 can provide a “tether” for GR.
c21 cso30:c:InputProcess connector
c28 cso30:c:InputProcess connector
c29 cso30:c:OutputProcess connector
p12_propro_p12
PMID: 17576036, 16751179, 15957004, 12215713
the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3.
c30 cso30:c:InputProcess connector
c31 cso30:c:InputProcess connector
c32 cso30:c:OutputProcess connector
p13_propro_p13
PMID: 17576036, 16751179, 15957004, 12215713
the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3.
c33 cso30:c:InputProcess connector
c34 cso30:c:InputProcess connector
c35 cso30:c:OutputProcess connector
p14_propro_p14
PMID: 17576036, 16751179, 15957004, 12215713
the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3.
PMID: 17576036
GR and IRF3 hinder each other's binding to GRIP1 in vitro suggesting that interacting surfaces may partially overlap precluding GR and IRF3 from binding GRIP1 at the same time.
c36 cso30:c:InputProcess connector
c37 cso30:c:InputProcess connector
c290 cso30:c:InputInhibitor connector
c38 cso30:c:OutputProcess connector
p15_propro_p15
PMID: 17576036, 16751179, 15957004, 12215713
the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3.
c39 cso30:c:InputProcess connector
c40 cso30:c:InputProcess connector
c41 cso30:c:OutputProcess connector
p16_propro_p16
PMID: 17576036, 14966289, 14690606, 15988012
Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57.
c42 cso30:c:InputProcess connector
c43 cso30:c:InputProcess connector
c50 cso30:c:OutputProcess connector
p17_propro_p17
PMID: 17576036, 14966289, 14690606, 15988012
Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57.
c44 cso30:c:InputProcess connector
c45 cso30:c:InputProcess connector
c51 cso30:c:OutputProcess connector
p18_propro_p18
PMID: 17576036, 14966289, 14690606, 15988012
Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57.
c46 cso30:c:InputProcess connector
c47 cso30:c:InputProcess connector
c52 cso30:c:OutputProcess connector
p19_propro_p19
PMID: 17576036, 14966289, 14690606, 15988012
Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57.
c48 cso30:c:InputProcess connector
c49 cso30:c:InputProcess connector
c53 cso30:c:OutputProcess connector
p20_propro_p20
PMID: 17576036, 9430642, 11997499, 15731352
The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively.
c54 cso30:c:InputProcess connector
c337 cso30:c:InputProcess connector
c56 cso30:c:OutputProcess connector
p21_propro_p21
PMID: 17576036, 9430642, 11997499, 15731352
The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively.
c65 cso30:c:InputProcess connector
c73 cso30:c:InputProcess connector
c57 cso30:c:OutputProcess connector
p22_propro_p22
PMID: 17576036, 9430642, 11997499, 15731352
The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively.
c66 cso30:c:InputProcess connector
c74 cso30:c:InputProcess connector
c58 cso30:c:OutputProcess connector
p23_propro_p23
PMID: 17576036, 9430642, 11997499, 15731352
The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively.
c67 cso30:c:InputProcess connector
c76 cso30:c:InputProcess connector
c59 cso30:c:OutputProcess connector
p24_propro_p24
c68 cso30:c:InputProcess connector
c77 cso30:c:InputProcess connector
c60 cso30:c:OutputProcess connector
p25_propro_p25
PMID: 17576036, 10817756, 15767262, 15169882
Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs.
c69 cso30:c:InputProcess connector
c78 cso30:c:InputProcess connector
c61 cso30:c:OutputProcess connector
p26_propro_p26
PMID: 17576036, 10817756, 15767262, 15169882
Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs.
c70 cso30:c:InputProcess connector
c79 cso30:c:InputProcess connector
c62 cso30:c:OutputProcess connector
p27_propro_p27
PMID: 17576036, 10817756, 15767262, 15169882
Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs.
c71 cso30:c:InputProcess connector
c82 cso30:c:InputProcess connector
c63 cso30:c:OutputProcess connector
p28_propro_p28
PMID: 17576036, 10817756, 15767262, 15169882
Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs.
c72 cso30:c:InputProcess connector
c75 cso30:c:InputProcess connector
c64 cso30:c:OutputProcess connector
p29_propro_p29
PMID: 17576036, 10817756, 15767262, 15169882
Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs.
c80 cso30:c:InputProcess connector
c83 cso30:c:InputProcess connector
c81 cso30:c:OutputProcess connector
p30_propro_p30
PMID: 17576036, 10817756, 15767262, 15169882
Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs.
c84 cso30:c:InputProcess connector
c85 cso30:c:InputProcess connector
c86 cso30:c:OutputProcess connector
p31_propro_p31
PMID: 17576036, 10817756, 15767262, 15169882
Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs.
c87 cso30:c:InputProcess connector
c89 cso30:c:InputProcess connector
c88 cso30:c:OutputProcess connector
p32_propro_p32
PMID: 17576036
Ligand-dependent homo- or heterodimerization of TLRs brings two TIR domains in close proximity allowing for the recruitment of additional adaptor molecules.
c90 cso30:c:InputProcess connector
c91 cso30:c:InputProcess connector
c92 cso30:c:OutputProcess connector
p33_propro_p33
PMID: 17576036
Ligand-dependent homo- or heterodimerization of TLRs brings two TIR domains in close proximity allowing for the recruitment of additional adaptor molecules.
c93 cso30:c:InputProcess connector
c94 cso30:c:OutputProcess connector
p34_propro_p34
PMID: 17576036
Upon interaction with PAMPs, TLRs recruit adaptor proteins MyD88 and TRIF/TICAM1, which transmit signal to downstream kinases as well as ubuiquitin ligases involved in degradation of inhibitors of NFkappaB.
PMID: 17576036
Two additional adaptor proteins, TIRAP and TRAM, likely facilitate the recruitment of MyD88 and TRIF to specific TLRs.
c95 cso30:c:InputProcess connector
c96 cso30:c:InputProcess connector
c97 cso30:c:InputProcess connector
c98 cso30:c:OutputProcess connector
p35_propro_p35
PMID: 17576036
Upon interaction with PAMPs, TLRs recruit adaptor proteins MyD88 and TRIF/TICAM1, which transmit signal to downstream kinases as well as ubuiquitin ligases involved in degradation of inhibitors of NFkappaB.
PMID: 17576036
Two additional adaptor proteins, TIRAP and TRAM, likely facilitate the recruitment of MyD88 and TRIF to specific TLRs.
c99 cso30:c:InputProcess connector
c100 cso30:c:InputProcess connector
c101 cso30:c:InputProcess connector
c108 cso30:c:OutputProcess connector
p36_propro_p36
PMID: 17576036
MyD88 contains two protein:protein interaction domains: the C-terminal TIR domain interacts with TIR domain of TLRs and IL-1R, while the N-terminal death domain binds the death domain-containing protein kinases, such as the IL-1R-associated kinase 4 (IRAK4), which phosphorylate another kinase, IRAK1.
c102 cso30:c:InputProcess connector
c103 cso30:c:InputProcess connector
c104 cso30:c:InputProcess connector
c105 cso30:c:OutputProcess connector
p37_propro_p37
PMID: 17576036
MyD88 contains two protein:protein interaction domains: the C-terminal TIR domain interacts with TIR domain of TLRs and IL-1R, while the N-terminal death domain binds the death domain-containing protein kinases, such as the IL-1R-associated kinase 4 (IRAK4), which phosphorylate another kinase, IRAK1.
c106 cso30:c:InputProcess connector
c107 cso30:c:OutputProcess connector
p38_propro_p38
PMID: 17576036
The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1.
c109 cso30:c:InputProcess connector
c110 cso30:c:OutputProcess connector
c111 cso30:c:OutputProcess connector
p39_propro_p39
PMID: 17576036
The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1.
c112 cso30:c:InputProcess connector
c113 cso30:c:InputProcess connector
c114 cso30:c:OutputProcess connector
p40_propro_p40
PMID: 17576036
The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1.
c115 cso30:c:InputProcess connector
c116 cso30:c:OutputProcess connector
p41_propro_p41
PMID: 17576036
The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1.
c117 cso30:c:InputProcess connector
c118 cso30:c:InputProcess connector
c119 cso30:c:OutputProcess connector
p42_propro_p42
PMID: 17576036
The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1.
c120 cso30:c:InputProcess connector
c121 cso30:c:OutputProcess connector
p43_propro_p43
PMID: 17576036, 16186825, 16260493
Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways.
c122 cso30:c:InputAssociation connector
c123 cso30:c:InputProcess connector
c124 cso30:c:OutputProcess connector
p44_propro_p44
PMID: 17576036, 16186825, 16260493
Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways.
c125 cso30:c:InputAssociation connector
c126 cso30:c:InputProcess connector
c127 cso30:c:OutputProcess connector
p45_propro_p45
PMID: 17576036, 16186825, 16260493
Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways.
c128 cso30:c:InputProcess connector
c130 cso30:c:InputAssociation connector
c129 cso30:c:OutputProcess connector
p46_propro_p46
PMID: 17576036, 16186825, 16260493
Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways.
c132 cso30:c:InputProcess connector
c131 cso30:c:InputAssociation connector
c133 cso30:c:OutputProcess connector
p47_propro_p47
PMID: 17576036, 16186825, 16260493
Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways.
PMID: 17576036, 9407028, 9794429
glucocorticoids inhibit several TLR-activated protein kinases including JNK and p38 without altering their levels, suggesting that GR does not repress transcription of JNK or p38.
c135 cso30:c:InputProcess connector
c134 cso30:c:InputAssociation connector
c184 cso30:c:InputInhibitor connector
c136 cso30:c:OutputProcess connector
p48_propro_p48
PMID: 17576036, 16186825, 16260493
Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways.
PMID: 17576036, 9407028, 9794429
glucocorticoids inhibit several TLR-activated protein kinases including JNK and p38 without altering their levels, suggesting that GR does not repress transcription of JNK or p38.
c138 cso30:c:InputProcess connector
c137 cso30:c:InputAssociation connector
c185 cso30:c:InputInhibitor connector
c139 cso30:c:OutputProcess connector
p49_propro_p49
PMID: 17576036
The former activates transcription factor NFkappaB through the phosphorylation and degradation of its inhibitor, IkappaB, while the latter is involved in numerous stress-related pathways including activation of transcription factors from the AP1 family.
c140 cso30:c:InputProcess connector
c142 cso30:c:InputAssociation connector
c141 cso30:c:OutputProcess connector
p50_propro_p50
PMID: 17576036
The former activates transcription factor NFkappaB through the phosphorylation and degradation of its inhibitor, IkappaB, while the latter is involved in numerous stress-related pathways including activation of transcription factors from the AP1 family.
c143 cso30:c:InputProcess connector
c144 cso30:c:OutputProcess connector
c145 cso30:c:OutputProcess connector
p51_propro_p51
PMID: 17576036
The former activates transcription factor NFkappaB through the phosphorylation and degradation of its inhibitor, IkappaB, while the latter is involved in numerous stress-related pathways including activation of transcription factors from the AP1 family.
c147 cso30:c:InputProcess connector
c146 cso30:c:InputAssociation connector
c148 cso30:c:OutputProcess connector
p52_propro_p52
PMID: 17576036, 16720699
In TLR3, two positively charged patches (patch1 and patch2) were proposed to be involved in interaction with dsRNA as substitution of either of these patches with alanines abolishes TLR3 signaling.
c149 cso30:c:InputProcess connector
c150 cso30:c:InputProcess connector
c151 cso30:c:OutputProcess connector
p53_propro_p53
PMID: 17576036, 12471095
TLR3 is the only TLR which does not interact with MyD88 and utilizes another TIR-domain adaptor, TRIF.
c152 cso30:c:InputProcess connector
c55 cso30:c:InputProcess connector
c153 cso30:c:OutputProcess connector
p54_propro_p54
PMID: 17576036, 16822173, 12692549
The N-terminal domain of TRIF interacts with IRF3 and several kinases including IKK-related TBK1 and IKKepsilon.
c154 cso30:c:InputProcess connector
c155 cso30:c:InputProcess connector
c156 cso30:c:InputProcess connector
c157 cso30:c:InputProcess connector
c158 cso30:c:OutputProcess connector
p55_propro_p55
PMID: 17576036
TBK1/IKKepsilon phosphorylate IRF3 and possibly IRF7 leading to dimerization and nuclear translocation of these transcription factors.
c159 cso30:c:InputProcess connector
c309 cso30:c:InputAssociation connector
c160 cso30:c:OutputProcess connector
c161 cso30:c:OutputProcess connector
p56_propro_p56
PMID: 17576036
TBK1/IKKepsilon phosphorylate IRF3 and possibly IRF7 leading to dimerization and nuclear translocation of these transcription factors.
c162 cso30:c:InputProcess connector
c163 cso30:c:OutputProcess connector
p57_propro_p57
PMID: 17576036
TBK1/IKKepsilon phosphorylate IRF3 and possibly IRF7 leading to dimerization and nuclear translocation of these transcription factors.
c164 cso30:c:InputProcess connector
c165 cso30:c:OutputProcess connector
p58_propro_p58
PMID: 17576036
The C-terminal domain of TRIF interacts with protein kinase RIP1.
c166 cso30:c:InputProcess connector
c167 cso30:c:InputProcess connector
c168 cso30:c:OutputProcess connector
p59_propro_p59
PMID: 17576036, 17073741
Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs).
c175 cso30:c:InputProcess connector
c182 cso30:c:InputAssociation connector
c176 cso30:c:OutputProcess connector
p60_propro_p60
PMID: 17576036, 17073741
Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs).
c173 cso30:c:InputProcess connector
c181 cso30:c:InputAssociation connector
c174 cso30:c:OutputProcess connector
p61_propro_p61
PMID: 17576036, 17073741
Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs).
c171 cso30:c:InputProcess connector
c180 cso30:c:InputAssociation connector
c172 cso30:c:OutputProcess connector
p62_propro_p62
PMID: 17576036, 17073741
Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs).
c169 cso30:c:InputProcess connector
c179 cso30:c:InputAssociation connector
c170 cso30:c:OutputProcess connector
p63_propro_p63
PMID: 17576036, 17073741
Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs).
c177 cso30:c:InputProcess connector
c183 cso30:c:InputAssociation connector
c178 cso30:c:OutputProcess connector
p64_propro_p64
PMID: 17576036, 15032587
These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation.
c192 cso30:c:InputProcess connector
c193 cso30:c:InputProcess connector
c194 cso30:c:OutputProcess connector
p65_propro_p65
PMID: 17576036, 15032587
These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation.
c195 cso30:c:InputProcess connector
c196 cso30:c:InputProcess connector
c198 cso30:c:InputInhibitor connector
c197 cso30:c:OutputProcess connector
p66_propro_p66
PMID: 17576036, 16415872
Recently, SOCS1 was reported to also directly interfere with TLR 2 and 4 signaling by inducing rapid degradation of their TIR domain-containing adaptor TIRAP through ubiquitin-mediated proteolysis.
c191 cso30:c:InputProcess connector
c187 cso30:c:OutputProcess connector
p67_propro_p67
PMID: 17576036, 16415872
Recently, SOCS1 was reported to also directly interfere with TLR 2 and 4 signaling by inducing rapid degradation of their TIR domain-containing adaptor TIRAP through ubiquitin-mediated proteolysis.
c186 cso30:c:InputProcess connector
c188 cso30:c:InputAssociation connector
c189 cso30:c:OutputProcess connector
p69_propro_p69
PMID: 17576036, 15032587
These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation.
c199 cso30:c:InputProcess connector
c204 cso30:c:InputAssociation connector
c200 cso30:c:OutputProcess connector
c201 cso30:c:OutputProcess connector
p70_propro_p70
PMID: 17576036, 15032587
These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation.
c202 cso30:c:InputProcess connector
c203 cso30:c:OutputProcess connector
p68_propro_p68
PMID: 17576036, 11259387, 12054511, 16293608
Interestingly, SOCS1 mRNA is induced by glucocorticoids in several cell lines of hematopoietic origin and in acute lymphoblastic leukemia (ALL) patients.
c190 cso30:c:InputAssociation connector
c205 cso30:c:OutputProcess connector
p71_propro_p71
PMID: 17576036, 11468175, 9430225, 17208592
Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X.
PMID: 17576036, 11028557, 11160251, 11867630
Transcription of the TLR2 gene in response to TLR agonists is activated by NFkappaB and could therefore be expected to be glucocorticoid-sensitive.
PMID: 17576036
In HeLa cervical carcinoma cells, the basal TLR2 expression is low but is induced upon exposure to lipoprotein from the Gram-negative bacterium Haemophilus influenzae and further potentiated by glucocorticoids.
PMID: 17576036,16765091
in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block.
c206 cso30:c:InputAssociation connector
c208 cso30:c:InputInhibitor connector
c235 cso30:c:InputAssociation connector
c207 cso30:c:OutputProcess connector
p72_propro_p72
PMID: 17576036, 11468175, 9430225, 17208592
Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X.
c209 cso30:c:InputInhibitor connector
c210 cso30:c:OutputProcess connector
p73_propro_p73
PMID: 17576036, 11468175, 11397794
GILZ was reported to physically interact with several effectors of TLR signaling, most notably Fos, Jun and p65/RelA.
PMID: 17576036, 17169985, 11397794, 12391160
Interestingly, GILZ homodimerization through the leucine zipper domain is required for its interaction with NFkappaB, but not AP1 or Raf-1, suggesting that GILZ interaction surfaces are partner-specific.
c211 cso30:c:InputProcess connector
c213 cso30:c:InputProcess connector
c212 cso30:c:OutputProcess connector
p74_propro_p74
PMID: 17576036, 12391160
In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2.
c215 cso30:c:InputProcess connector
c216 cso30:c:OutputProcess connector
p75_propro_p75
PMID: 17576036, 12391160
In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2.
c214 cso30:c:InputProcess connector
c217 cso30:c:InputProcess connector
c218 cso30:c:OutputProcess connector
p76_propro_p76
PMID: 17576036, 12391160
In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2.
c219 cso30:c:InputAssociation connector
c222 cso30:c:InputProcess connector
c283 cso30:c:InputInhibitor connector
c223 cso30:c:OutputProcess connector
p77_propro_p77
PMID: 17576036, 12391160
In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2.
c220 cso30:c:InputProcess connector
c224 cso30:c:InputAssociation connector
c316 cso30:c:InputInhibitor connector
c221 cso30:c:OutputProcess connector
p78_propro_p78
PMID: 17576036, 11468175, 11397794
GILZ was reported to physically interact with several effectors of TLR signaling, most notably Fos, Jun and p65/RelA.
c225 cso30:c:InputProcess connector
c229 cso30:c:InputProcess connector
c227 cso30:c:OutputProcess connector
p79_propro_p79
PMID: 17576036, 11468175, 11397794
GILZ was reported to physically interact with several effectors of TLR signaling, most notably Fos, Jun and p65/RelA.
c226 cso30:c:InputProcess connector
c230 cso30:c:InputProcess connector
c228 cso30:c:OutputProcess connector
p80_propro_p80
PMID: 17576036, 17169985, 11397794, 12391160
Interestingly, GILZ homodimerization through the leucine zipper domain is required for its interaction with NFkappaB, but not AP1 or Raf-1, suggesting that GILZ interaction surfaces are partner-specific.
c231 cso30:c:InputProcess connector
c232 cso30:c:OutputProcess connector
p81_propro_p81
PMID: 17576036, 11259387, 9430225, 12393603
GILZ is dramatically induced by glucocorticoids in a wide range of cell types, and this induction requires the GR dimer interface and DNA binding, suggesting that GILZ is a direct transcriptional target for the receptor.
c233 cso30:c:InputAssociation connector
c234 cso30:c:OutputProcess connector
p82_propro_p82
PMID: 17576036, 12356755
ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists.
c236 cso30:c:InputProcess connector
c237 cso30:c:InputProcess connector
c238 cso30:c:OutputProcess connector
p83_propro_p83
PMID: 17576036, 12356755
ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists.
c239 cso30:c:InputAssociation connector
c240 cso30:c:OutputProcess connector
p84_propro_p84
PMID: 17576036, 12356755
ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1beta in response to TLR2 agonists.
PMID: 17576036,16765091
in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block.
c247 cso30:c:InputAssociation connector
c255 cso30:c:InputInhibitor connector
c244 cso30:c:OutputProcess connector
p85_propro_p85
PMID: 17576036, 12356755
ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists.
c243 cso30:c:InputAssociation connector
c245 cso30:c:OutputProcess connector
p86_propro_p86
PMID: 17576036, 12356755
ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists.
c242 cso30:c:InputAssociation connector
c246 cso30:c:OutputProcess connector
p87_propro_p87
c241 cso30:c:InputAssociation connector
c248 cso30:c:OutputProcess connector
p88_propro_p88
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c249 cso30:c:InputAssociation connector
c250 cso30:c:OutputProcess connector
p89_propro_p89
PMID: 17576036,16765091
in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block.
c252 cso30:c:InputInhibitor connector
c251 cso30:c:OutputProcess connector
p90_propro_p90
PMID: 17576036,16765091
in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block.
c253 cso30:c:InputAssociation connector
c254 cso30:c:OutputProcess connector
p91_propro_p91
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c259 cso30:c:InputAssociation connector
c263 cso30:c:InputAssociation connector
c265 cso30:c:OutputProcess connector
p92_propro_p92
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c258 cso30:c:InputAssociation connector
c264 cso30:c:InputAssociation connector
c266 cso30:c:OutputProcess connector
p93_propro_p93
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c257 cso30:c:InputAssociation connector
c274 cso30:c:InputAssociation connector
c267 cso30:c:OutputProcess connector
p94_propro_p94
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c260 cso30:c:InputProcess connector
c261 cso30:c:InputProcess connector
c262 cso30:c:OutputProcess connector
p95_propro_p95
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c272 cso30:c:InputAssociation connector
c273 cso30:c:InputAssociation connector
c268 cso30:c:OutputProcess connector
p96_propro_p96
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c269 cso30:c:InputProcess connector
c270 cso30:c:InputProcess connector
c271 cso30:c:OutputProcess connector
p97_propro_p97
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c277 cso30:c:InputAssociation connector
c280 cso30:c:InputAssociation connector
c275 cso30:c:OutputProcess connector
p98_propro_p98
PMID: 17576036, 15242847
Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid.
c278 cso30:c:InputAssociation connector
c279 cso30:c:InputAssociation connector
c276 cso30:c:OutputProcess connector
p100_propro_p100
PMID: 17576036, 16932750
This phosphorylation is required for nuclear translocation of IRF3 as well as binding of CBP/p300, the best known IRF3 coactivators.
c284 cso30:c:InputProcess connector
c285 cso30:c:InputProcess connector
c286 cso30:c:OutputProcess connector
p101_propro_p101
PMID: 17576036
GR and IRF3 hinder each other's binding to GRIP1 in vitro suggesting that interacting surfaces may partially overlap precluding GR and IRF3 from binding GRIP1 at the same time.
PMID: 17576036
both GRIP1 and IRF3 are conventional interacting partners for CBP/p300, their interaction with each other is CBP-independent.
c287 cso30:c:InputProcess connector
c288 cso30:c:InputProcess connector
c291 cso30:c:InputInhibitor connector
c289 cso30:c:OutputProcess connector
p102_propro_p102
PMID: 17576036
glucocorticoids strongly inhibited dsRNA-induced expression of multiple cytokines and chemokines including interferon beta, IP10 and RANTES, known transcriptional targets of IRF3.
c293 cso30:c:InputAssociation connector
c296 cso30:c:InputInhibitor connector
c292 cso30:c:OutputProcess connector
p103_propro_p103
PMID: 17576036
glucocorticoids strongly inhibited dsRNA-induced expression of multiple cytokines and chemokines including interferon beta, IP10 and RANTES, known transcriptional targets of IRF3.
c294 cso30:c:InputAssociation connector
c297 cso30:c:InputInhibitor connector
c299 cso30:c:OutputProcess connector
p104_propro_p104
PMID: 17576036
glucocorticoids strongly inhibited dsRNA-induced expression of multiple cytokines and chemokines including interferon beta, IP10 and RANTES, known transcriptional targets of IRF3.
c295 cso30:c:InputAssociation connector
c298 cso30:c:InputInhibitor connector
c300 cso30:c:OutputProcess connector
p105_propro_p105
PMID: 17576036
both GRIP1 and IRF3 are conventional interacting partners for CBP/p300, their interaction with each other is CBP-independent.
c301 cso30:c:InputProcess connector
c302 cso30:c:InputProcess connector
c303 cso30:c:OutputProcess connector
p106_propro_p106
PMID: 17576036
TLR4 is the main LPS sensor that can activate IRF3 through both MyD88- and TRIF-dependent pathways.
c304 cso30:c:InputProcess connector
c305 cso30:c:OutputProcess connector
p107_propro_p107
PMID: 17576036, 10094406
casein kinase II-dependent phosphorylation of IRF1 is required for its full transactivation.
c306 cso30:c:InputProcess connector
c307 cso30:c:InputAssociation connector
c308 cso30:c:OutputProcess connector
p108_propro_p108
PMID: 17576036, 16143103
because both GR and IRF3 appear to interact with the Rel domain of p65, IRF3 and GR were proposed to compete for the same binding site on NFkappaB.
c310 cso30:c:InputProcess connector
c311 cso30:c:InputProcess connector
c312 cso30:c:OutputProcess connector
p109_propro_p109
PMID: 17576036, 11468175
IRAK4/1 initiate signaling cascades that lead to the activation of NFkappaB, AP1 and possibly IRF7 and IRF5.
c313 cso30:c:InputProcess connector
c315 cso30:c:InputAssociation connector
c314 cso30:c:OutputProcess connector
p99_propro_p99
PMID: 17576036
Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain.
c281 cso30:c:InputProcess connector
c282 cso30:c:OutputProcess connector
p110_propro_p110
PMID: 17576036
Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain.
c317 cso30:c:InputProcess connector
c318 cso30:c:OutputProcess connector
p111_propro_p111
PMID: 17576036
Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain.
c321 cso30:c:InputProcess connector
c323 cso30:c:InputProcess connector
c327 cso30:c:OutputProcess connector
p112_propro_p112
PMID: 17576036
Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain.
c322 cso30:c:InputProcess connector
c325 cso30:c:InputProcess connector
c329 cso30:c:OutputProcess connector
p113_propro_p113
PMID: 17576036
Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain.
c319 cso30:c:InputProcess connector
c324 cso30:c:InputProcess connector
c328 cso30:c:OutputProcess connector
p114_propro_p114
PMID: 17576036
Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain.
c320 cso30:c:InputProcess connector
c326 cso30:c:InputProcess connector
c330 cso30:c:OutputProcess connector
p99_propro_p115
c331 cso30:c:InputProcess connector
c332 cso30:c:OutputProcess connector
p71_propro_p116
PMID: 17576036, 11468175, 9430225, 17208592
Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X.
PMID: 17576036
In HeLa cervical carcinoma cells, the basal TLR2 expression is low but is induced upon exposure to lipoprotein from the Gram-negative bacterium Haemophilus influenzae and further potentiated by glucocorticoids.
PMID: 17576036,16765091
in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block.
c333 cso30:c:InputAssociation connector
c335 cso30:c:InputInhibitor connector
c334 cso30:c:OutputProcess connector
p117_propro_p117
PMID: 17576036, 11468175, 9430225, 17208592
Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X.
c336 cso30:c:InputAssociation connector
c256 cso30:c:OutputProcess connector
TLRs_enti_MO000019395
TLRs
TLR2_enti_MO000019397
TLR2
TLR3_enti_MO000019398
TLR3
GR: Hsp90: Hsp70_enti_e11
GR: Hsp90: Hsp70
glucocorticoids_enti_MO000021732
glucocorticoids
glucocorticoids: GR: Hsp90: Hsp70_enti_e12
glucocorticoids: GR: Hsp90: Hsp70
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}_enti_e13
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}
simple GRE_enti_e14
simple GRE
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: simple GRE_enti_e15
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: simple GRE
SGK_enti_G012572
SGK
tyrosine hydroxylase_enti_G010592
tyrosine hydroxylase
chromogranin A_enti_G026383
chromogranin A
osteocalcin_enti_G010241
osteocalcin
pro-opiomelanocortin_enti_G010266
pro-opiomelanocortin
POMC_enti_MO000062960
POMC
osteocalcin_enti_MO000066783
osteocalcin
NF-kappaB_enti_MO000000058
NF-kappaB
STAT3_enti_MO000013122
STAT3
STAT5_enti_MO000016876
STAT5
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: NF-kappaB_enti_e16
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: NF-kappaB
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: STAT5_enti_e17
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: STAT5
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: STAT3_enti_e18
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: STAT3
AF-2_enti_e19
AF-2
GRIP1_enti_MO000074564
GRIP1
SRC-1_enti_MO000033624
SRC-1
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: AF-2_enti_e20
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: AF-2
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: SRC-1_enti_e21
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: SRC-1
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: GRIP1_enti_e22
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: GRIP1
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: SRC-3_enti_e23
glucocorticoids: GR: Hsp90: Hsp70 {nucleus}: SRC-3
SRC-3_enti_e24
SRC-3
p160_enti_MO000038964
p160
Fli-1_enti_MO000005192
Fli-1
Cocoa_enti_MO000062794
Cocoa
GAC63_enti_MO000086608
GAC63
BAF57_enti_MO000079932
BAF57
p160: Fli-1_enti_e25
p160: Fli-1
p160: Cocoa_enti_e26
p160: Cocoa
p160: GAC63_enti_e27
p160: GAC63
p160: BAF57_enti_e28
p160: BAF57
p160: CBP: p300_enti_e30
p160: CBP: p300
p160: CRAM1_enti_e31
p160: CRAM1
p160: MEF2c_enti_e32
p160: MEF2c
p160: PRMT1_enti_e33
p160: PRMT1
p160: Myogenin_enti_e34
p160: Myogenin
p160: pCAF_enti_e35
p160: pCAF
p160: pRb_enti_e36
p160: pRb
p160: E2F1_enti_e37
p160: E2F1
p160: MyoD_enti_e38
p160: MyoD
p160: NF-kappaB_enti_e39
p160: NF-kappaB
pCAF_enti_e40
pCAF
CRAM1_enti_e41
CRAM1
PRMT1_enti_MO000060849
PRMT1
MEF2C_enti_e42
MEF2C
Myogenin_enti_MO000037106
Myogenin
pRb_enti_MO000011894
pRb
E2F-1_enti_MO000004272
E2F-1
MyoD_enti_MO000018808
MyoD
STATs_enti_MO000016656
STATs
p160: STATs_enti_e43
p160: STATs
p160: IRFs_enti_e44
p160: IRFs
IRFs_enti_e45
IRFs
TLR ligand_enti_e46
TLR ligand
TLR ligand : TLR_enti_e47
TLR ligand : TLR
MyD88_enti_MO000016573
MyD88
TLR ligand : TLR: TLR_enti_e48
TLR ligand : TLR: TLR
TIRAP_enti_MO000022528
TIRAP
TRAM_enti_MO000041132
TRAM
TLR ligand : TLR: TLR: TIRAP: MyD88_enti_e49
TLR ligand : TLR: TLR: TIRAP: MyD88
TRIF_enti_MO000041125
TRIF
IRAK1_enti_e63
IRAK1
TLR ligand : TLR: TLR: TIRAP: MyD88: IRAK-4: IRAK1_enti_e64
TLR ligand : TLR: TLR: TIRAP: MyD88: IRAK-4: IRAK1
IRAK-4_enti_MO000039077
IRAK-4
TRAF6_enti_MO000000212
TRAF6
TLR ligand : TLR: TLR: TIRAP: MyD88: IRAK-4: IRAK1 {p}_enti_e65
TLR ligand : TLR: TLR: TIRAP: MyD88: IRAK-4: IRAK1 {p}
TLR ligand : TLR: TLR: TRIF: TRAM_enti_e66
TLR ligand : TLR: TLR: TRIF: TRAM
IRAK1 {p}_enti_e67
IRAK1 {p}
IRAK1 {p}: TRAF6_enti_e68
IRAK1 {p}: TRAF6
IRAK1{p}: TRAF6 {p}_enti_e69
IRAK1{p}: TRAF6 {p}
TAK1_enti_MO000016574
TAK1
IRAK1{p}: TRAF6 {p}: TAK1_enti_e70
IRAK1{p}: TRAF6 {p}: TAK1
IRAK1{p}: TRAF6 {p}: TAK1 {p}_enti_e71
IRAK1{p}: TRAF6 {p}: TAK1 {p}
IKK_enti_MO000000248
IKK
IKK {p}_enti_e72
IKK {p}
MKK3_enti_MO000016966
MKK3
MKK4_enti_MO000016917
MKK4
MKK4{p}_enti_MO000038341
MKK4{p}
MKK3 {p}_enti_e73
MKK3 {p}
MKK6_enti_MO000019005
MKK6
MKK6{p}_enti_MO000038355
MKK6{p}
JNK_enti_MO000000023
JNK
JNK {p}_enti_e74
JNK {p}
p38_enti_MO000000022
p38
p38 {p}_enti_e75
p38 {p}
IkappaB:NF-kappaB_enti_MO000000215
IkappaB:NF-kappaB
IkappaB {p}:NF-kappaB_enti_e76
IkappaB {p}:NF-kappaB
IkappaB remnants_enti_e77
NF-kappaB {cytoplasm}_enti_e78
NF-kappaB {cytoplasm}
AP-1_enti_MO000000276
AP-1
AP-1 {activated}_enti_e79
AP-1 {activated}
dsRNA_enti_MO000022224
dsRNA
dsRNA:TLR3_enti_MO000041446
dsRNA:TLR3
dsRNA:TLR3: TRIF_enti_e80
dsRNA:TLR3: TRIF
IKK-i_enti_MO000016608
IKK-i
TBK1_enti_MO000019331
TBK1
IRF-3_enti_MO000007694
IRF-3
dsRNA:TLR3: TRIF: IRF3: IKK-i: TBK1_enti_e81
dsRNA:TLR3: TRIF: IRF3: IKK-i: TBK1
IRF3 {p}_enti_e82
IRF3 {p}
dsRNA:TLR3: TRIF: IKK-i: TBK1_enti_e83
dsRNA:TLR3: TRIF: IKK-i: TBK1
IRF3 {p} : IRF3_enti_e84
IRF3 {p} : IRF3
IRF3 {p} : IRF3_enti_e85
IRF3 {p} : IRF3
RIP1_enti_MO000000065
RIP1
dsRNA:TLR3: TRIF: RIP1_enti_e86
dsRNA:TLR3: TRIF: RIP1
MKP_enti_e87
MKP
SOCS/CIS family_enti_MO000017115
SOCS/CIS family
TIRAp ramnents_enti_e88
TIRAP {ub}_enti_e89
TIRAP {ub}
Jak_enti_e90
Jak
SOCS/CIS family: Jak_enti_e91
SOCS/CIS family: Jak
STATs {cytoplasm}_enti_e92
STATs {cytoplasm}
STATs {cytoplasm}: Jak_enti_e93
STATs {cytoplasm}: Jak
Jak {ub}_enti_e94
Jak {ub}
Jak remnants_enti_e95
E3s_enti_MO000000286
E3s
SOCS-1_enti_MO000017004
SOCS-1
SOCS1_enti_G010539
SOCS1
GILZ_enti_e5
GILZ
TLR2_enti_G010962
TLR2
BCL2L1_enti_G011271
BCL2L1
GILZ: NF-kappaB_enti_e6
GILZ: NF-kappaB
GILZ: Raf-1_enti_e96
GILZ: Raf-1
Raf-1_enti_MO000000015
Raf-1
Raf-1{p}_enti_MO000038411
Raf-1{p}
ERK1_enti_MO000004670
ERK1
ERK2_enti_MO000004676
ERK2
ERK2 {activated}_enti_e97
ERK2 {activated}
ERK1 {activated}_enti_e98
ERK1 {activated}
GILZ: Fos_enti_e99
GILZ: Fos
GILZ: Jun_enti_e100
GILZ: Jun
c-Fos_enti_MO000000279
c-Fos
c-Jun_enti_MO000000049
c-Jun
GILZ: GILZ_enti_e101
GILZ: GILZ
GILZ_enti_e102
GILZ
TLR2 ligand_enti_e103
TLR2 ligand
TLR2 ligand: TLR2_enti_e104
TLR2 ligand: TLR2
TNF-alpha_enti_G010329
TNF-alpha
IL18_enti_G010909
IL18
IL-1beta_enti_G010389
IL-1beta
IL-6_enti_G010262
IL-6
IL-12 p40_enti_G010657
IL-12 p40
IL8_enti_e105
IL8
Tlr4_enti_G010693
Tlr4
TNF-alpha receptor_enti_e106
TNF-alpha receptor
TNF-alpha_enti_MO000000289
TNF-alpha
TNF-alpha: TNF-alpha receptor_enti_e107
TNF-alpha: TNF-alpha receptor
IFNgamma_enti_MO000016665
IFNgamma
IFN-gamma receptor_enti_e108
IFN-gamma receptor
IFN-gamma: IFN-gamma receptor_enti_e109
IFN-gamma: IFN-gamma receptor
p300:CBP_enti_e111
p300:CBP
p300: CBP: IRF3 {p} : IRF3_enti_e112
p300: CBP: IRF3 {p} : IRF3
GRIP1: IRF3 {p} : IRF3_enti_e113
GRIP1: IRF3 {p} : IRF3
IFN-beta_enti_G010228
IFN-beta
IP-10_enti_e114
IP-10
RANTES_enti_G010522
RANTES
p300:CBP: GRIP1_enti_e115
p300:CBP: GRIP1
IRF-1_enti_MO000007685
IRF-1
IRF-1 {p}_enti_e116
IRF-1 {p}
casein kinase II_enti_e117
casein kinase II
IRF3 {p} : IRF3: NF-kappaB_enti_e118
IRF3 {p} : IRF3: NF-kappaB
IRF-7_enti_MO000007702
IRF-7
IRF-7 {activated}_enti_e119
IRF-7 {activated}
IRF-2_enti_MO000007690
IRF-2
IRF-1 {p} {nucleus}_enti_e110
IRF-1 {p} {nucleus}
IRF-5_enti_MO000007700
IRF-5
IRF-7 {nucleus}}_enti_e120
IRF-7 {nucleus}}
p300: CBP: IRF-7{nucleus}_enti_e121
p300: CBP: IRF-7{nucleus}
p300:CBP: IRF-2_enti_e122
p300:CBP: IRF-2
p300:CBP: IRF-1{p} {nucleus}_enti_e123
p300:CBP: IRF-1{p} {nucleus}
p300: CBP: IRF-5_enti_e124
p300: CBP: IRF-5