Entity
Process
IFN-beta
--
G010228
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m93217
10
infinite
0
TRANSFAC | G010228 |
--
p38
--
MO000000022
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m66
10
infinite
0
TRANSPATH | MO000000022 |
--
c-Jun
--
MO000000049
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m86
10
infinite
0
InterPro | IPR002112 |
TRANSPATH | MO000000049 |
--
NF-kappaB
--
MO000000058
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m77
10
infinite
0
TRANSPATH | MO000000058 |
--
ATF-2
--
MO000000062
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m87
10
infinite
0
InterPro | IPR007087 |
TRANSPATH | MO000000062 |
--
csml-variable:Double
m183
10
infinite
0
--
AP-1
--
MO000000276
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m219
10
infinite
0
TRANSPATH | MO000000276 |
--
TNF-alpha
--
MO000000289
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m230
10
infinite
0
InterPro | IPR003636 |
TRANSPATH | MO000000289 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
IL-12
--
MO000017265
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m2121
10
infinite
0
TRANSPATH | MO000017265 |
--
fibronectin
--
MO000017549
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m2341
10
infinite
0
InterPro | IPR006209 |
TRANSPATH | MO000017549 |
--
TLR4
--
MO000019394
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3961
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000019394 |
--
protein remnants
--
MO000019479
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m360980
10
infinite
0
TRANSPATH | MO000019479 |
--
STAT1{p}
--
MO000019704
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m4238
10
infinite
0
TRANSPATH | MO000019704 |
--
ATF-2{p}
--
MO000038365
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m16575
10
infinite
0
TRANSPATH | MO000038365 |
--
c-Jun{p}
--
MO000038589
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m16780
10
infinite
0
TRANSPATH | MO000038589 |
--
TRIF
--
MO000041125
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m18998
10
infinite
0
TRANSPATH | MO000041125 |
--
dsRNA:TLR3
--
MO000041446
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19314
10
infinite
0
TRANSPATH | MO000041446 |
--
--
e1
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane
--
--
--
csml-variable:Double
m1
0
infinite
0
--
--
e10
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytosol
--
--
--
csml-variable:Double
m10
0
infinite
0
--
PKA
--
e102
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m109
0
infinite
0
--
p38{p}
--
e103
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m110
0
infinite
0
--
Fusion(F)protein : TLR4
--
e11
cso30:c:Complex
cso30:i:CC_Cytoplasm
--
--
csml-variable:Double
m11
0
infinite
0
--
taxol
--
e12
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m12
0
infinite
0
--
taxol:TLR4
--
e13
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m13
0
infinite
0
--
fibronectin:TLR4
--
e14
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m14
0
infinite
0
--
HSP60:TLR4
--
e15
cso30:c:Complex
cso30:i:CC_Cytoplasm
--
--
csml-variable:Double
m15
0
infinite
0
--
HSP70:TLR4
--
e16
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m16
0
infinite
0
--
Hyaluronan:TLR4
--
e17
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m17
0
infinite
0
--
hyaluronan
--
e18
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m18
0
infinite
0
--
TLR2:zymosan
--
e19
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m19
0
infinite
0
--
--
e2
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m2
0
infinite
0
--
zymosan
--
e20
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m20
0
infinite
0
--
TLR2:TLR6
--
e21
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m21
0
infinite
0
--
lipoproteins
--
e22
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m22
0
infinite
0
--
lipoprotein:TLR2:TLR6
--
e23
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m23
0
infinite
0
--
flagellin:TLR5
--
e24
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m24
0
infinite
0
--
ssRNA:TLR7
--
e25
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m25
0
infinite
0
--
ssRNA
--
e26
cso30:c:Rna
cso30:i:CC_Cytoplasm
--
csml-variable:Double
m26
0
infinite
0
--
ssRNA:TLR8
--
e27
cso30:c:Complex
cso30:i:CC_Cytoplasm
--
--
csml-variable:Double
m27
0
infinite
0
--
R848
--
e28
cso30:c:SmallMolecule
cso30:i:CC_Cytoplasm
--
csml-variable:Double
m28
0
infinite
0
--
R848:TLR8
--
e29
cso30:c:Complex
cso30:i:CC_Cytoplasm
--
--
csml-variable:Double
m29
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
R848:TLR7
--
e30
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m30
0
infinite
0
--
CpG DNA
--
e31
cso30:c:Dna
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m31
0
infinite
0
--
CpG DNA:TLR9
--
e32
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m32
0
infinite
0
--
--
e33
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
csml-variable:Double
m33
0
infinite
0
--
--
e34
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
csml-variable:Double
m34
0
infinite
0
--
--
e35
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m35
0
infinite
0
--
LPS:TLR4:MAL
--
e36
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m36
0
infinite
0
--
LPS:TLR4:MAL:MYD88
--
e37
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m37
0
infinite
0
--
LPS:TLR4:MYD88:IRAK4
--
e38
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m38
0
infinite
0
--
LPS:TLR4:MAL:MYD88:IRAK4{p}
--
e39
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m39
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
IRAK1
--
e40
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m40
0
infinite
0
--
LPS:TLR4:MAL:MYD88:IRAK4{p}:IRAK1
--
e41
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m41
0
infinite
0
--
LPS:TLR4:MAL:MYD88:IRAK4{p}:IRAK1{p}
--
e42
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m42
0
infinite
0
--
IRAK4{p}:IRAK1{p}
--
e43
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m43
0
infinite
0
--
LPS:TLR4:MAL:MYD88
--
e44
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m44
0
infinite
0
--
TRAF6{p}
--
e45
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m45
0
infinite
0
--
TRAF6[ub}
--
e46
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m46
0
infinite
0
--
TAK1:TAB1:TAB2
--
e47
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m47
0
infinite
0
--
TRAF6{ub}:TAK1:TAB1:TAB2
--
e48
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m48
0
infinite
0
--
TRAF6{ub}:TAK1{active}:TAB1:TAB2
--
e49
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m49
0
infinite
0
--
LPS:TLR4
--
e5
cso30:c:Complex
cso30:i:CC_Cytoplasm
--
csml-variable:Double
m5
0
infinite
0
--
--
e50
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelopeLumen
--
--
--
csml-variable:Double
m50
0
infinite
0
--
--
e51
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearPore
--
--
--
csml-variable:Double
m51
0
infinite
0
--
--
e52
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearInnerMembrane
--
--
--
csml-variable:Double
m52
0
infinite
0
--
--
e53
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearLumen
--
--
--
csml-variable:Double
m53
0
infinite
0
--
--
e54
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearOuterMembrane
--
--
--
csml-variable:Double
m54
0
infinite
0
--
--
e55
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleus
--
--
--
csml-variable:Double
m55
0
infinite
0
--
--
e56
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleoplasm
--
--
--
csml-variable:Double
m56
0
infinite
0
--
--
e57
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearBody
--
--
--
csml-variable:Double
m57
0
infinite
0
--
--
e58
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Nucleolus
--
--
--
csml-variable:Double
m58
0
infinite
0
--
--
e59
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearEnvelope
--
--
--
csml-variable:Double
m59
0
infinite
0
--
fusion (F) protein
--
e6
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m6
0
infinite
0
--
--
e60
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Chromatin
--
--
--
csml-variable:Double
m60
0
infinite
0
--
--
e61
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearChromosome
--
--
--
csml-variable:Double
m61
0
infinite
0
--
--
e62
cso30:c:EntityBiologicalCompartment
cso30:i:CC_NuclearCentromere
--
--
--
csml-variable:Double
m62
0
infinite
0
--
IKK{active}
--
e63
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m63
10
infinite
0
TRANSPATH | MO000000248 |
--
p38{active}
--
e65
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m67
10
infinite
0
TRANSPATH | MO000000022 |
--
AP-1{active}
--
e66
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m68
10
infinite
0
TRANSPATH | MO000000276 |
--
e67
--
e67
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m69
0
infinite
0
--
LPS:TLR4:TRAM:TRIF
--
e68
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
csml-variable:Double
m70
0
infinite
0
--
LPS:TLR4:TRAM:TRIF:IKK-i:TBK1
--
e69
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m71
0
infinite
0
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
IRF-3{active}
--
e70
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m72
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007694 |
--
IRF-7{active}
--
e71
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m73
10
infinite
0
TRANSPATH | MO000007702 |
--
IFN-beta
--
e72
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m74
0
infinite
0
--
dsRNA:TLR3:TRIF
--
e73
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m75
0
infinite
0
--
IRAK4{p}:IRAK1{p}:TRAF6
--
e74
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m76
0
infinite
0
--
IkappaB-zeta
--
e75
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m78
0
infinite
0
--
NF-kappaB:IkappaBzeta
--
e76
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m79
0
infinite
0
--
JunB:JunD
--
e77
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m80
0
infinite
0
--
JunB:JunD{active}
--
e78
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m81
0
infinite
0
--
Ig light chain
--
e79
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m82
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
csml-variable:Double
m83
0
infinite
0
--
csml-variable:Double
m88
0
infinite
0
--
PAM3CSK4
--
e84
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m89
0
infinite
0
--
TLR2:TLR6:PAM3CSK4
--
e85
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m90
0
infinite
0
--
(IRF-3)2
--
e88
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m94
0
infinite
0
--
p50:p65
--
e89
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m95
0
infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0
infinite
0
--
p50:p65{active}
--
e90
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m96
0
infinite
0
--
IRF-3{p}:p65
--
e91
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m97
0
infinite
0
--
IFN-betaR
--
e92
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m98
0
infinite
0
--
IFN-beta:IFN-betaR
--
e93
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m99
0
infinite
0
--
IFN-alpha
--
e94
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m100
0
infinite
0
--
IFN-alpha
--
e95
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m101
0
infinite
0
--
MYD88{ub}
--
e96
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m102
0
infinite
0
--
TGF-beta
--
e97
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m103
0
infinite
0
--
MYD88s
--
e98
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m104
0
infinite
0
--
NS3/4A
--
e99
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m105
0
infinite
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m3961*m155666*0.1
nodelay
--
0
PMID: 17934330, 10644670, 11062499, 11150311, 10623794, 11777948, 17400552 TLR4 recognizes not only LPS but also taxol, fusion (F) protein of respiratory syncytial virus, extra domain A of fibronectin, heat shock protein (HSP) 60, HSP 70 and hyaluronan.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c28 : 1
stoichiometry:c29 : 1
stoichiometry:c30 : 1
m22*m21*0.1
nodelay
--
0
PMID: 17934330, 11095740 TLR6 associates with TLR2 and recognizes lipoproteins from mycoplasma.
p11
p11
cso30:i:ME_Binding
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c31 : 1
stoichiometry:c32 : 1
stoichiometry:c33 : 1
m6485*m3966*0.1
nodelay
--
0
PMID: 17934330, 11323673 TLR5 mediates the induction of the immune response by bacterial flagellins.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c34 : 1
stoichiometry:c36 : 1
stoichiometry:c35 : 1
m26*m19940*0.1
nodelay
--
0
PMID: 17934330, 11130078, 14976262, 14976261 Recent studies showed that ssRNA is the natural ligand for TLR7/8.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c37 : 1
stoichiometry:c38 : 1
stoichiometry:c39 : 1
m19823*m26*0.1
nodelay
--
0
PMID: 17934330, 11130078, 14976262, 14976261 Recent studies showed that ssRNA is the natural ligand for TLR7/8.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c40 : 1
stoichiometry:c41 : 1
stoichiometry:c42 : 1
m19823*m28*0.1
nodelay
--
0
PMID: 17934330, 11812998, 12032557, 10346978 A synthetic compound (imidazoquinoline compound R848) with antiviral activity has been described as a ligand for TLR7 and TLR8.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c43 : 1
stoichiometry:c44 : 1
stoichiometry:c45 : 1
m28*m19940*0.1
nodelay
--
0
PMID: 17934330, 11812998, 12032557, 10346978 A synthetic compound (imidazoquinoline compound R848) with antiviral activity has been described as a ligand for TLR7 and TLR8.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c46 : 1
stoichiometry:c47 : 1
stoichiometry:c48 : 1
m19828*m31*0.1
nodelay
--
0
PMID:17934330, 11130078 TLR9 has been shown to recognize unmethylated bacterial CpG DNA.
p17
p17
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c49 : 1
stoichiometry:c50 : 1
stoichiometry:c51 : 1
m119368*m3965*0.1
nodelay
--
0
PMID: 17934330, 11607032 TLR3 recognizes double stranded RNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c52 : 1
stoichiometry:c54 : 1
stoichiometry:c53 : 1
m43675*m5*0.1
nodelay
--
0
PMID: 17934330 The primary function of MAL in TLR signaling seems to control the recruitment of MyD88 to TLR4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c55 : 1
stoichiometry:c56 : 1
stoichiometry:c57 : 1
m1572*m36*0.1
nodelay
--
0
PMID: 17934330 MyD88 binds with the TIR domain of the receptor and phosphorylates IRAK4 which in turn phosphorylates IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m3961*m6*0.1
nodelay
--
0
PMID: 17934330, 10644670, 11062499, 11150311, 10623794, 11777948, 17400552 TLR4 recognizes not only LPS but also taxol, fusion (F) protein of respiratory syncytial virus, extra domain A of fibronectin, heat shock protein (HSP) 60, HSP 70 and hyaluronan.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c58 : 1
stoichiometry:c59 : 1
stoichiometry:c253 : 1
stoichiometry:c60 : 1
m37*m17258*0.1
nodelay
--
0
PMID: 17934330 MyD88 binds with the TIR domain of the receptor and phosphorylates IRAK4 which in turn phosphorylates IRAK1. PMID: 17934330 MyD88s does not interact with IRAK4 because it lacks a region that is important for IRAK4 recruitment. So, IRAK4 is not recruited to the IL-1R, thereby preventing the association of IRAK1 and IRAK4 and thus the phosphorylation of IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c61 : 1
stoichiometry:c62 : 1
m38*0.1
nodelay
--
0
PMID: 17934330 MyD88 binds with the TIR domain of the receptor and phosphorylates IRAK4 which in turn phosphorylates IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c63 : 1
stoichiometry:c64 : 1
stoichiometry:c254 : 1
stoichiometry:c65 : 1
m39*m40*0.1
nodelay
--
0
PMID: 17934330 MyD88s does not interact with IRAK4 because it lacks a region that is important for IRAK4 recruitment. So, IRAK4 is not recruited to the IL-1R, thereby preventing the association of IRAK1 and IRAK4 and thus the phosphorylation of IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c66 : 1
stoichiometry:c255 : 1
stoichiometry:c67 : 1
m41*0.1
nodelay
--
0
PMID: 17934330 IRAK1 undergoes autophosphorylation. PMID: 17934330 MyD88s does not interact with IRAK4 because it lacks a region that is important for IRAK4 recruitment. So, IRAK4 is not recruited to the IL-1R, thereby preventing the association of IRAK1 and IRAK4 and thus the phosphorylation of IRAK1.
p24
p24
cso30:i:ME_Phosphorylation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c73 : 1
stoichiometry:c72 : 1
stoichiometry:c127 : 1
m76*0.1
nodelay
--
0
PMID: 17934330 IRAK1 phosphorylates TRAF6 leading to the ubiquitination of TAK complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c69 : 1
stoichiometry:c70 : 1
m42*0.1
nodelay
--
0
PMID: 17934330 Upon stimulation, IRAK4 and IRAK1 are sequentially phosphorylated and dissociated from MyD88, which results in activation of TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c74 : 1
stoichiometry:c75 : 1
m45*0.1
nodelay
--
0
PMID: 17934330, 15125833 TRAF6 is ubiquitinated at K63 chains and this K63 polyubiquitinated TRAF6 mediates activation of the next component in the pathway, which is most likely to be TGF-¦Â activated kinase-1 (TAK1)
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c76 : 1
stoichiometry:c77 : 1
stoichiometry:c78 : 1
m46*m47*0.1
nodelay
--
0
PMID: 17934330 TAK1-TAB complex associates with K63-ubiquitinated TRAF6 to activate TAK1 kinase, which then activates the IKK complex as well as the JNK kinases.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c79 : 1
stoichiometry:c80 : 1
m48*0.1
nodelay
--
0
PMID: 17934330 TAK1-TAB complex associates with K63-ubiquitinated TRAF6 to activate TAK1 kinase, which then activates the IKK complex as well as the JNK kinases.
p29
p29
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c81 : 1
stoichiometry:c83 : 1
stoichiometry:c82 : 1
m207*m49*0.1
nodelay
--
0
PMID: 17934330 TAK1-TAB complex associates with K63-ubiquitinated TRAF6 to activate TAK1 kinase, which then activates the IKK complex as well as the JNK kinases.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
stoichiometry:c9 : 1
m3961*m12*0.1
nodelay
--
0
PMID: 17934330, 10644670, 11062499, 11150311, 10623794, 11777948, 17400552 TLR4 recognizes not only LPS but also taxol, fusion (F) protein of respiratory syncytial virus, extra domain A of fibronectin, heat shock protein (HSP) 60, HSP 70 and hyaluronan.
p30
p30
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c84 : 1
stoichiometry:c86 : 1
stoichiometry:c85 : 1
m64*m49*0.1
nodelay
--
0
PMID: 17934330 TAK1-TAB complex associates with K63-ubiquitinated TRAF6 to activate TAK1 kinase, which then activates the IKK complex as well as the JNK kinases.
p31
p31
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c87 : 1
stoichiometry:c89 : 1
stoichiometry:c88 : 1
m66*m49*0.1
nodelay
--
0
PMID: 17934330 TAK1-TAB complex associates with K63-ubiquitinated TRAF6 to activate TAK1 kinase, which then activates the IKK complex as well as the JNK kinases.
p32
p32
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c90 : 1
stoichiometry:c92 : 1
stoichiometry:c91 : 1
m219*m65*0.1
nodelay
--
0
PMID: 17934330 TAK1-TAB complex associates with K63-ubiquitinated TRAF6 to activate TAK1 kinase, which then activates the IKK complex as well as the JNK kinases.
p33
p33
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c93 : 1
stoichiometry:c95 : 1
stoichiometry:c94 : 1
m219*m67*0.1
nodelay
--
0
PMID: 17934330 TAK1-TAB complex associates with K63-ubiquitinated TRAF6 to activate TAK1 kinase, which then activates the IKK complex as well as the JNK kinases.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c96 : 1
stoichiometry:c97 : 1
stoichiometry:c98 : 1
m5*m19005*0.1
nodelay
--
0
PMID: 17934330 The role of TRAM in LPS signaling appears to act as a bridging adapter connecting TLR4 and TRIF.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c99 : 1
stoichiometry:c100 : 1
stoichiometry:c101 : 1
m69*m18998*0.1
nodelay
--
0
PMID: 17934330 The role of TRAM in LPS signaling appears to act as a bridging adapter connecting TLR4 and TRIF.
p36
p36
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c106 : 1
stoichiometry:c108 : 1
stoichiometry:c107 : 1
m977*m71*0.1
nodelay
--
0
PMID: 17934330, 12692549 Two noncanonical I¦ÊB kinases (IKKs), TBK1 (TANK-binding kinase 1) and IKK¦Å (I¦ÊB kinase ¦Å), interact with TRIF, activate IRF3/IRF7 and finally lead to IFN-¦Â production.
p37
p37
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c102 : 1
stoichiometry:c103 : 1
stoichiometry:c104 : 1
stoichiometry:c105 : 1
m70*m1599*m3902*0.1
nodelay
--
0
PMID: 17934330, 12692549 Two noncanonical I¦ÊB kinases (IKKs), TBK1 (TANK-binding kinase 1) and IKK¦Å (I¦ÊB kinase ¦Å), interact with TRIF, activate IRF3/IRF7 and finally lead to IFN-¦Â production.
p38
p38
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c109 : 1
stoichiometry:c111 : 1
stoichiometry:c110 : 1
m980*m71*0.1
nodelay
--
0
PMID: 17934330, 12692549 Two noncanonical I¦ÊB kinases (IKKs), TBK1 (TANK-binding kinase 1) and IKK¦Å (I¦ÊB kinase ¦Å), interact with TRIF, activate IRF3/IRF7 and finally lead to IFN-¦Â production.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c112 : 1
stoichiometry:c113 : 1
m72*0.1
nodelay
--
0
PMID: 17934330, 12692549 Two noncanonical I¦ÊB kinases (IKKs), TBK1 (TANK-binding kinase 1) and IKK¦Å (I¦ÊB kinase ¦Å), interact with TRIF, activate IRF3/IRF7 and finally lead to IFN-¦Â production.
p4
p4
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c10 : 1
stoichiometry:c11 : 1
stoichiometry:c12 : 1
m3961*m2341*0.1
nodelay
--
0
PMID: 17934330, 10644670, 11062499, 11150311, 10623794, 11777948, 17400552 TLR4 recognizes not only LPS but also taxol, fusion (F) protein of respiratory syncytial virus, extra domain A of fibronectin, heat shock protein (HSP) 60, HSP 70 and hyaluronan.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c114 : 1
stoichiometry:c115 : 1
m73*0.1
nodelay
--
0
PMID: 17934330, 12692549 Two noncanonical I¦ÊB kinases (IKKs), TBK1 (TANK-binding kinase 1) and IKK¦Å (I¦ÊB kinase ¦Å), interact with TRIF, activate IRF3/IRF7 and finally lead to IFN-¦Â production.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c116 : 1
stoichiometry:c120 : 1
stoichiometry:c117 : 1
m93217*m72*0.1
nodelay
--
0
PMID: 17934330, 12692549 Two noncanonical I¦ÊB kinases (IKKs), TBK1 (TANK-binding kinase 1) and IKK¦Å (I¦ÊB kinase ¦Å), interact with TRIF, activate IRF3/IRF7 and finally lead to IFN-¦Â production.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c118 : 1
stoichiometry:c121 : 1
stoichiometry:c119 : 1
m93217*m73*0.1
nodelay
--
0
PMID: 17934330, 12692549 Two noncanonical I¦ÊB kinases (IKKs), TBK1 (TANK-binding kinase 1) and IKK¦Å (I¦ÊB kinase ¦Å), interact with TRIF, activate IRF3/IRF7 and finally lead to IFN-¦Â production.
p43
p43
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c122 : 1
stoichiometry:c123 : 1
stoichiometry:c124 : 1
m19314*m18998*0.1
nodelay
--
0
PMID: 17934330 TRIF is an adapter for TLR3 and TLR4, and is associated with the MyD88-independent cascade.
p44
p44
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c125 : 1
stoichiometry:c126 : 1
stoichiometry:c259 : 1
stoichiometry:c71 : 1
m43*m183*0.1
nodelay
--
0
PMID: 17934330, 12140561 IRAK1 has three TRAF6 (tumor necrosis factor receptorassociated factor 6) binding motifs to mediate the interaction with TRAF6. PMID: 17934330, 12150927 TRAF6 and IRAK association is prevented by IRAKM.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c128 : 1
stoichiometry:c129 : 1
stoichiometry:c130 : 1
m78*m77*0.1
nodelay
--
0
PMID: 17934330, 15618216, 15522867 IkB¦Æ to interact with NF-¦ÊB via a C terminal ankyrin repeat domain in the nucleus to induce IL-6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c131 : 1
m79*0.1
nodelay
--
0
PMID: 17934330, 15618216, 15522867 IkB¦Æ to interact with NF-¦ÊB via a C terminal ankyrin repeat domain in the nucleus to induce IL-6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c133 : 1
stoichiometry:c134 : 1
m93248*0.1
nodelay
--
0
PMID: 17934330, 15618216, 15522867 IkB¦Æ to interact with NF-¦ÊB via a C terminal ankyrin repeat domain in the nucleus to induce IL-6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c135 : 1
stoichiometry:c136 : 1
m5*m80*0.1
nodelay
--
0
PMID: 17934330, 15226448 LPS stimulation in precursor B cells and primary dendritic cells leads to JUND and JUNB activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c139 : 1
stoichiometry:c138 : 1
m81*0.1
nodelay
--
0
PMID: 17934330, 15226448 JunB and JunD complex in turn are required for high-level sustained induction of chemokine receptor 7 (CCR-7) and Ig light chain expression and production of surface IgM.
p5
p5
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c14 : 1
stoichiometry:c15 : 1
m3961*m4645*0.1
nodelay
--
0
PMID: 17934330, 10644670, 11062499, 11150311, 10623794, 11777948, 17400552 TLR4 recognizes not only LPS but also taxol, fusion (F) protein of respiratory syncytial virus, extra domain A of fibronectin, heat shock protein (HSP) 60, HSP 70 and hyaluronan.
p50
p50
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c140 : 1
stoichiometry:c142 : 1
stoichiometry:c141 : 1
m94106*m81*0.1
nodelay
--
0
PMID: 17934330, 15226448 JunB and JunD complex in turn are required for high-level sustained induction of chemokine receptor 7 (CCR-7) and Ig light chain expression and production of surface IgM.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c144 : 1
stoichiometry:c143 : 1
m81*0.1
nodelay
--
0
PMID: 17934330, 15226448 JunB and JunD complex in turn are required for high-level sustained induction of chemokine receptor 7 (CCR-7) and Ig light chain expression and production of surface IgM.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c145 : 1
stoichiometry:c147 : 1
stoichiometry:c146 : 1
m82*m81*0.1
nodelay
--
0
PMID: 17934330, 15226448 JunB and JunD complex in turn are required for high-level sustained induction of chemokine receptor 7 (CCR-7) and Ig light chain expression and production of surface IgM.
p53
p53
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c148 : 1
stoichiometry:c150 : 1
stoichiometry:c149 : 1
m997*m32*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p54
p54
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c151 : 1
stoichiometry:c153 : 1
stoichiometry:c152 : 1
m1818*m32*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p55
p55
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c154 : 1
stoichiometry:c156 : 1
stoichiometry:c155 : 1
m66*m32*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p56
p56
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c157 : 1
stoichiometry:c159 : 1
stoichiometry:c158 : 1
m86*m85*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p57
p57
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c160 : 1
stoichiometry:c162 : 1
stoichiometry:c161 : 1
m86*m84*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p58
p58
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c163 : 1
stoichiometry:c165 : 1
stoichiometry:c164 : 1
m86*m67*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p59
p59
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c166 : 1
stoichiometry:c172 : 1
stoichiometry:c167 : 1
m87*m85*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p6
p6
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c17 : 1
stoichiometry:c18 : 1
stoichiometry:c16 : 1
m3961*m5956*0.1
nodelay
--
0
PMID: 17934330, 10644670, 11062499, 11150311, 10623794, 11777948, 17400552 TLR4 recognizes not only LPS but also taxol, fusion (F) protein of respiratory syncytial virus, extra domain A of fibronectin, heat shock protein (HSP) 60, HSP 70 and hyaluronan.
p60
p60
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c168 : 1
stoichiometry:c173 : 1
stoichiometry:c169 : 1
m87*m84*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
p61
p61
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c170 : 1
stoichiometry:c174 : 1
stoichiometry:c171 : 1
m87*m67*0.1
nodelay
--
0
PMID: 17934330, 9799232 CpG-DNA induces activation of JNK1/2 and p38 in murine macrophages and dendritic cells leading to the phosphorylation of c-JUN and ATF2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c176 : 1
stoichiometry:c175 : 1
m67*0.1
nodelay
--
0
PMID: 17934330 This activation via p38 is necessary for the full induction of TNF-¦Á and IL-12 as inhibition of p38 abrogates this biological response.
p63
p63
cso30:i:ME_Translation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c177 : 1
stoichiometry:c179 : 1
stoichiometry:c269 : 1
stoichiometry:c178 : 1
m93309*m67*0.1
nodelay
--
0
PMID: 17934330 This activation via p38 is necessary for the full induction of TNF-¦Á and IL-12 as inhibition of p38 abrogates this biological response. PMID: 17934330 TGF-¦Â potently inhibited LPS-induced NF-¦ÊB activation and TNF-¦Á release from RAW 264.7 cells but had no effect on IFN-¦Â promoter activation.
p64
p64
cso30:i:ME_Translation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c182 : 1
stoichiometry:c184 : 1
stoichiometry:c180 : 1
m88*m67*0.1
nodelay
--
0
PMID: 17934330 This activation via p38 is necessary for the full induction of TNF-¦Á and IL-12 as inhibition of p38 abrogates this biological response.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c183 : 1
stoichiometry:c181 : 1
m67*0.1
nodelay
--
0
PMID: 17934330 This activation via p38 is necessary for the full induction of TNF-¦Á and IL-12 as inhibition of p38 abrogates this biological response.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c185 : 1
stoichiometry:c186 : 1
stoichiometry:c187 : 1
m21*m89*0.1
nodelay
--
0
PMID: 17934330, 15067049 TLR2 stimulation by PAM3CSK4 in DCs leads to the enhanced induction of c-FOS and induces high production of IL-10 but low level of IL-12.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c191 : 1
stoichiometry:c188 : 1
m90*0.1
nodelay
--
0
PMID: 17934330, 15067049 TLR2 stimulation by PAM3CSK4 in DCs leads to the enhanced induction of c-FOS and induces high production of IL-10 but low level of IL-12.
p68
p68
cso30:i:ME_Translation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c190 : 1
stoichiometry:c192 : 1
stoichiometry:c189 : 1
m93203*m90*0.1
nodelay
--
0
PMID: 17934330, 15067049 TLR2 stimulation by PAM3CSK4 in DCs leads to the enhanced induction of c-FOS and induces high production of IL-10 but low level of IL-12.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c196 : 1
stoichiometry:c193 : 1
m90*0.1
nodelay
--
0
PMID: 17934330, 15067049 TLR2 stimulation by PAM3CSK4 in DCs leads to the enhanced induction of c-FOS and induces high production of IL-10 but low level of IL-12.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c20 : 1
stoichiometry:c21 : 1
stoichiometry:c19 : 1
m18*m3961*0.1
nodelay
--
0
PMID: 17934330, 10644670, 11062499, 11150311, 10623794, 11777948, 17400552 TLR4 recognizes not only LPS but also taxol, fusion (F) protein of respiratory syncytial virus, extra domain A of fibronectin, heat shock protein (HSP) 60, HSP 70 and hyaluronan.
p70
p70
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c195 : 1
stoichiometry:c197 : 1
stoichiometry:c194 : 1
m94230*m90*0.1
nodelay
--
0
PMID: 17934330, 15067049 TLR2 stimulation by PAM3CSK4 in DCs leads to the enhanced induction of c-FOS and induces high production of IL-10 but low level of IL-12.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c199 : 1
stoichiometry:c198 : 1
m90*0.1
nodelay
--
0
PMID: 17934330, 15067049 TLR2 stimulation by PAM3CSK4 in DCs leads to the enhanced induction of c-FOS and induces high production of IL-10 but low level of IL-12.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c201 : 1
stoichiometry:c202 : 1
stoichiometry:c200 : 1
m88*m90*0.1
nodelay
--
0
PMID: 17934330, 15067049 TLR2 stimulation by PAM3CSK4 in DCs leads to the enhanced induction of c-FOS and induces high production of IL-10 but low level of IL-12.
p75
p75
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c209 : 1
stoichiometry:c214 : 1
stoichiometry:c210 : 1
m977*m92*0.1
nodelay
--
0
PMID: 17934330, 15502848 Phosphatidylinositol 3-kinase has also been implicate in IRF3 activation and seems to be required for full activation of IRF3 following TLR3 signaling.
p76
p76
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c211 : 1
stoichiometry:c213 : 1
stoichiometry:c212 : 1
m91*m19314*0.1
nodelay
--
0
PMID: 17934330, 15502848 Phosphatidylinositol 3-kinase has also been implicate in IRF3 activation and seems to be required for full activation of IRF3 following TLR3 signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c215 : 1
stoichiometry:c217 : 1
stoichiometry:c216 : 1
m72*m19314*0.1
nodelay
--
0
PMID: 17934330, 12692549 Stimulation via TLR3 leads to the nuclear localization of IRF3 which binds as a dimer to induce IP-10 and IFN-¦Â genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c218 : 1
stoichiometry:c219 : 1
m93*0.1
nodelay
--
0
PMID: 17934330, 12692549 Stimulation via TLR3 leads to the nuclear localization of IRF3 which binds as a dimer to induce IP-10 and IFN-¦Â genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c221 : 1
stoichiometry:c220 : 1
m94*0.1
nodelay
--
0
PMID: 17934330, 12692549 Stimulation via TLR3 leads to the nuclear localization of IRF3 which binds as a dimer to induce IP-10 and IFN-¦Â genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c23 : 1
stoichiometry:c24 : 1
stoichiometry:c22 : 1
m20*m3964*0.1
nodelay
--
0
PMID: 17934330, 10549626, 10623793, 10548109, 10588727 TLR2 responds to mycobacteria, yeast cell wall component zymosan, and Gram-positive bacteria.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c222 : 1
stoichiometry:c223 : 1
m94*0.1
nodelay
--
0
PMID: 17934330, 12692549 Stimulation via TLR3 leads to the nuclear localization of IRF3 which binds as a dimer to induce IP-10 and IFN-¦Â genes.
p81
p81
cso30:i:ME_UnknownActivation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c224 : 1
stoichiometry:c226 : 1
stoichiometry:c225 : 1
m95*m63*0.1
nodelay
--
0
PMID: 17934330, 9346241 IKK activated by TLR4 signaling activates the p65/p50 dimer.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c228 : 1
stoichiometry:c203 : 1
stoichiometry:c229 : 1
m166*m72*0.1
nodelay
--
0
PMID: 17934330, 14557267 IRF3 activated by TBK1 forms dimer with p65 to induce IP-10 and IFN-¦Â.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c231 : 1
stoichiometry:c230 : 1
m97*0.1
nodelay
--
0
PMID: 17934330, 14557267 IRF3 activated by TBK1 forms dimer with p65 to induce IP-10 and IFN-¦Â.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c233 : 1
stoichiometry:c232 : 1
m97*0.1
nodelay
--
0
PMID: 17934330, 14557267 IRF3 activated by TBK1 forms dimer with p65 to induce IP-10 and IFN-¦Â.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c235 : 1
stoichiometry:c234 : 1
m96*0.1
nodelay
--
0
PMID: 17934330, 15315758 IP-10 and proinflammatory cytokines can be induced by p65/p50 dimers.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c236 : 1
stoichiometry:c237 : 1
stoichiometry:c238 : 1
m74*m98*0.1
nodelay
--
0
PMID: 17934330, 9786932, 9822609 Studies of IFN regulation also suggest that the autocrine/paracrine action of INF-¦Â produced by IRF3 can induce IRF7 de novo which activates IFN-¦Á.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c240 : 1
stoichiometry:c239 : 1
m99*0.1
nodelay
--
0
PMID: 17934330, 9786932, 9822609 Studies of IFN regulation also suggest that the autocrine/paracrine action of INF-¦Â produced by IRF3 can induce IRF7 de novo which activates IFN-¦Á.
p88
p88
cso30:i:ME_Translation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c241 : 1
stoichiometry:c243 : 1
stoichiometry:c242 : 1
m93631*m99*0.1
nodelay
--
0
PMID: 17934330, 9786932, 9822609 Studies of IFN regulation also suggest that the autocrine/paracrine action of INF-¦Â produced by IRF3 can induce IRF7 de novo which activates IFN-¦Á.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c244 : 1
stoichiometry:c204 : 1
stoichiometry:c245 : 1
m100*m73*0.1
nodelay
--
0
PMID: 17934330, 9786932, 9822609 Studies of IFN regulation also suggest that the autocrine/paracrine action of INF-¦Â produced by IRF3 can induce IRF7 de novo which activates IFN-¦Á.
p9
p9
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
stoichiometry:c27 : 1
m3987*m3964*0.1
nodelay
--
0
PMID: 17934330, 11095740 TLR6 associates with TLR2 and recognizes lipoproteins from mycoplasma.
p90
p90
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c247 : 1
stoichiometry:c249 : 1
stoichiometry:c248 : 1
m1572*m103*0.1
nodelay
--
0
PMID: 17934330, 15623538 TGF-¦Â facilitates ubiquitination and proteasomal degradation of MyD88 and attenuates MyD88-dependent signaling by decreasing cellular levels of MyD88 protein.
p91
p91
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c250 : 1
stoichiometry:c251 : 1
stoichiometry:c252 : 1
m102*m103*0.1
nodelay
--
0
PMID: 17934330, 15623538 TGF-¦Â facilitates ubiquitination and proteasomal degradation of MyD88 and attenuates MyD88-dependent signaling by decreasing cellular levels of MyD88 protein.
p92
p92
cso30:i:ME_ProteinCleavage
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c256 : 1
stoichiometry:c258 : 1
stoichiometry:c257 : 1
m18998*m105*0.1
nodelay
--
0
PMID: 17934330, 15710891 The hepatitis C virus protein NS3/4A causes specific proteolysis of TRIF, an adaptor protein linking TLR3 to kinases responsible for activating transcription factors controlling a multiplicity of antiviral defenses.
p93
p93
cso30:i:ME_UnknownActivation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c260 : 1
stoichiometry:c262 : 1
stoichiometry:c263 : 1
stoichiometry:c264 : 1
stoichiometry:c261 : 1
m106*m5*0.1
nodelay
--
0
PMID: 17934330, 15699069 LPS induced ERK activation is prevented by the inhibitory adapter DOK1 (downstream of kinase 1) and DOK2.
p94
p94
cso30:i:ME_UnknownActivation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c265 : 1
stoichiometry:c267 : 1
stoichiometry:c268 : 1
stoichiometry:c266 : 1
m108*m63*0.1
nodelay
--
0
PMID: 17934330 TGF-¦Â potently inhibited LPS-induced NF-¦ÊB activation and TNF-¦Á release from RAW 264.7 cells but had no effect on IFN-¦Â promoter activation.
p95
p95
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c270 : 1
stoichiometry:c272 : 1
stoichiometry:c271 : 1
m66*m109*0.1
nodelay
--
0
PMID: 17934330, 16125054 PKA phosphorylates p38 with a delayed kinetics forming the crosstalk point between G protein coupled receptors and TLRs.
p96
p96
cso30:i:ME_Phosphorylation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c273 : 1
stoichiometry:c275 : 1
stoichiometry:c274 : 1
m1357*m67*0.1
nodelay
--
0
PMID: 17934330, 12811837 p38 phosphorylate STAT1 forming another crosstalk with IFN signaling pathways.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c277 : 1
stoichiometry:c276 : 1
m5*0.1
nodelay
--
0
PMID: 17934330, 11947920 When stimulated with TLR4 ligand LPS, macrophages increase TLR9, and thus respond to CpG DNA more effectively.
p98
p98
cso30:i:ME_Translation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c278 : 1
stoichiometry:c280 : 1
stoichiometry:c279 : 1
m95738*m5*0.1
nodelay
--
0
PMID: 17934330, 11947920 When stimulated with TLR4 ligand LPS, macrophages increase TLR9, and thus respond to CpG DNA more effectively.
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--