Entity
Process
NF-kappaB
--
MO000000058
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m46
10
infinite
0
TRANSPATH | MO000000058 |
--
RIP1{ub}
--
MO000000065
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m83
10
infinite
0
InterPro | IPR000198 |
TRANSPATH | MO000000065 |
--
MAPKs
--
MO000000077
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m76
10
infinite
0
TRANSPATH | MO000000077 |
--
p100{p}
--
MO000000202
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m173
10
infinite
0
TRANSPATH | MO000000202 |
--
IKK-alpha
--
MO000000210
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m181
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000210 |
--
IKK-beta
--
MO000000211
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m182
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000211 |
--
IKK{active}
--
MO000000248
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m207
10
infinite
0
TRANSPATH | MO000000248 |
--
TNF-alpha
--
MO000000289
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m230
10
infinite
0
InterPro | IPR003636 |
TRANSPATH | MO000000289 |
--
IRF-3
--
MO000007694
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m977
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007694 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
TAK1
--
MO000016574
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1573
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016574 |
--
IKK-gamma
--
MO000016599
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1593
10
infinite
0
InterPro | IPR007087 |
TRANSPATH | MO000016599 |
--
IKK-i
--
MO000016608
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1599
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016608 |
--
Caspase-8/10
--
MO000016900
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1815
10
infinite
0
TRANSPATH | MO000016900 |
--
TRAF3
--
MO000016963
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1872
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000016963 |
--
TBK1
--
MO000019331
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3902
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000019331 |
--
TLR4
--
MO000019394
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3961
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000019394 |
--
TLR2
--
MO000019397
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3964
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000019397 |
--
TLR5
--
MO000019399
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3966
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000019399 |
--
flagellin
--
MO000022185
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m6485
10
infinite
0
TRANSPATH | MO000022185 |
--
TIRAP
--
MO000022528
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m6810
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000022528 |
--
IRAK-4
--
MO000039077
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m17258
10
infinite
0
TRANSPATH | MO000039077 |
--
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
--
IRF7{p}:IRF7{p}
--
e100
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m104
0
infinite
0
--
IFN-alpha
--
e101
cso30:c:mRNA
cso30:i:CC_Cytosol
--
csml-variable:Double
m105
0
infinite
0
--
TLR1:TLR2:Triacyl lipopeptides
--
e102
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m106
0
infinite
0
--
TLR1:TLr2:Triacyllioppeptides:TIRAP:MyD88
--
e103
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m107
0
infinite
0
--
TLR1:TLr2:Triacyllioppeptides:TIRAP:MyD88:IRAK-4
--
e104
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m108
0
infinite
0
--
TLR1:TLr2:Triacyllioppeptides:TIRAP:MyD88:IRAK-4{p}
--
e105
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m109
0
infinite
0
--
TLR1:TLr2:Triacyllioppeptides:TIRAP:MyD88:IRAK-4{p}:IRAK1
--
e106
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m110
0
infinite
0
--
TLR1:TLr2:Triacyllioppeptides:TIRAP:MyD88:IRAK-4{p}:IRAK1{p}
--
e107
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m111
0
infinite
0
--
IRAK-4{p}:IRAK1{p}
--
e108
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m112
0
infinite
0
--
IRAK4{p}:IRAK1{p}:TRAF6
--
e109
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m113
0
infinite
0
--
TLR2:Lipoarabinomannan:TLR2
--
e11
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m11
0
infinite
0
--
LPS;TLR4:TIRAP:MyD88:IRAK-4
--
e110
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m114
0
infinite
0
--
LPS;TLR4:TIRAP:MyD88:IRAK-4{p}
--
e111
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m115
0
infinite
0
--
LPS;TLR4:TIRAP:MyD88:IRAK-4{p}:IRAK1
--
e112
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m116
0
infinite
0
--
LPS;TLR4:TIRAP:MyD88:IRAK-4{p}:IRAK1{p}
--
e113
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m117
0
infinite
0
--
cyclohexamide
--
e114
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m118
0
infinite
0
--
TNF-alpha receptor
--
e115
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m119
0
infinite
0
--
TNF-alpha:receptor
--
e116
cso30:c:Complex
cso30:i:CC_NuclearOuterMembrane
--
--
csml-variable:Double
m120
0
infinite
0
--
RIG-1
--
e117
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m121
0
infinite
0
--
Mda5
--
e118
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m122
0
infinite
0
--
IPS-1
--
e119
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m123
0
infinite
0
--
Hemagglutinin
--
e12
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m12
0
infinite
0
--
RIG-1:IPS-1:RNA:FADD:Caspase 8/10,TRA:F3:NEMO
--
e120
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m124
0
infinite
0
--
RIG-1:RNA:IPS-1
--
e121
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m125
0
infinite
0
--
Mda5:IPS-1:RNA:FADD:Caspase 8/10,TRA:F3:NEMO
--
e122
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m126
0
infinite
0
--
RNA
--
e123
cso30:c:mRNA
cso30:i:CC_Extracellular
--
csml-variable:Double
m127
0
infinite
0
--
RIG-1:RNA
--
e124
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m128
0
infinite
0
--
Mda5:RNA
--
e125
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m129
0
infinite
0
--
Mda5:RNA:IPS-1
--
e126
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m130
0
infinite
0
--
dsDNA
--
e128
cso30:c:Dna
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m132
0
infinite
0
--
csml-variable:Double
m133
0
infinite
0
--
Hemagglutinin:TLR2
--
e13
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m13
0
infinite
0
--
ZBP1:dsDNA:TBK1:IKKi
--
e130
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m134
0
infinite
0
--
IRF7{p}
--
e131
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m135
0
infinite
0
--
ubiquitin
--
e132
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
csml-variable:Double
m136
0
infinite
0
--
IKK-beta{p}
--
e133
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m137
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000211 |
--
p50
--
e134
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m138
0
infinite
0
--
Ikk-alpha:IKK-alpha
--
e135
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m139
0
infinite
0
--
p52:RelB
--
e137
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
csml-variable:Double
m141
0
infinite
0
--
mRNA
--
e138
cso30:c:mRNA
cso30:i:CC_Nucleolus
--
--
csml-variable:Double
m142
0
infinite
0
--
TRAF6{ub}:TABs:TAK1
--
e139
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m143
0
infinite
0
--
tGPI-mutin
--
e14
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m14
0
infinite
0
--
IKK-gamma{ub}:TABs:TAK1
--
e140
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m144
0
infinite
0
--
RIP1:TRAF6:TAK1:TRIF
--
e141
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m145
0
infinite
0
--
tGPI-mutin:TLR2
--
e15
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m15
0
infinite
0
--
TLR2:TLR1
--
e16
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m16
0
infinite
0
--
Triacyl lipopeptide:TLR1:TLR2
--
e17
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m17
0
infinite
0
--
Tri-acyl Lipopeptide
--
e18
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m18
0
infinite
0
--
TLR2:TLR6
--
e19
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m19
0
infinite
0
--
--
e2
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m2
0
infinite
0
--
Diacyl lipopeptide:TLR2:TLR6
--
e20
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m20
0
infinite
0
--
Di-acyl Lipopeptide
--
e21
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m21
0
infinite
0
--
LPS:TLR4
--
e22
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m22
0
infinite
0
--
MPLA
--
e23
cso30:c:SmallMolecule
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m23
0
infinite
0
--
MPLA:TLR4
--
e24
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m24
0
infinite
0
--
Envelope protein
--
e25
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m25
0
infinite
0
--
Envelope protein:TLR4
--
e26
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m26
0
infinite
0
--
Flagellin:TLR5
--
e27
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m27
0
infinite
0
--
Lamina Propria
--
e28
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m28
0
infinite
0
--
TLR5:Lamina Propria
--
e29
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m29
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
Uropathogenic bacteria components
--
e30
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m30
0
infinite
0
--
TLR11:Uropathogenic components
--
e31
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m31
0
infinite
0
--
profilin like molecules
--
e32
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m32
0
infinite
0
--
Profilin like molecules
--
e33
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m33
0
infinite
0
--
Poly IC
--
e34
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m34
0
infinite
0
--
Poly IC:TLR3
--
e35
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m35
0
infinite
0
--
ssRNA
--
e36
cso30:c:Rna
cso30:i:CC_Cytosol
--
csml-variable:Double
m36
0
infinite
0
--
TLR7:ssRNA
--
e37
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m37
0
infinite
0
--
Imidazoquinolines
--
e38
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
csml-variable:Double
m38
0
infinite
0
--
TLR7:Imidazoquinolines
--
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
--
TLR8:ssRNA
--
e40
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m40
0
infinite
0
--
TLR8:Imidazoquinolines
--
e41
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
--
csml-variable:Double
m41
0
infinite
0
--
CpG motifs
--
e42
cso30:c:Dna
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m42
0
infinite
0
--
TLR9:CpGmotifs
--
e43
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m43
0
infinite
0
--
Hemozoin
--
e44
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m44
0
infinite
0
--
TLR9:Hemozoin
--
e45
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m45
0
infinite
0
--
csml-variable:Double
m47
0
infinite
0
--
NF-KappaB:IKappaB
--
e47
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m48
0
infinite
0
--
NF-KappaB:IKappaB{p}
--
e48
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m49
0
infinite
0
--
NF-KappaB:IKappaB{p}{ub}
--
e49
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m63
0
infinite
0
--
--
e5
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
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
--
--
e6
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
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
--
26s proteosome
--
e63
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m64
0
infinite
0
--
proteosome remnant
--
e64
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
csml-variable:Double
m65
0
infinite
0
--
NF-kappaB{active}
--
e65
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m66
10
infinite
0
TRANSPATH | MO000000058 |
--
NF-kappaB{active}
--
e66
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m67
10
infinite
0
TRANSPATH | MO000000058 |
--
LPS;TLR4:TIRAP:MyD88
--
e67
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m68
0
infinite
0
--
LPS:TLR4:TIRAP
--
e68
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m69
0
infinite
0
--
TRAF6{ub}
--
e69
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m70
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000000212 |
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m7
0
infinite
0
--
Uev1A
--
e71
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m72
0
infinite
0
--
NAK
--
e73
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m74
0
infinite
0
--
MAPKs{active}
--
e75
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m77
10
infinite
0
TRANSPATH | MO000000077 |
--
Inflammatory cytokines
--
e77
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m79
0
infinite
0
--
LPS:TLR4:TRAM
--
e78
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m80
0
infinite
0
--
LPS:TLR4:TRAM:TRIF
--
e79
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m81
0
infinite
0
--
TLR2:PGN
--
e8
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m8
0
infinite
0
--
TRIF:RIP1{ub}
--
e80
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m82
0
infinite
0
--
TRIF:TRAF6:RIP1{p}
--
e82
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m85
0
infinite
0
--
dsRNA:TLR3:TRIF
--
e83
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m86
0
infinite
0
--
dsRNA:TLR3:TRIF:TRAF3
--
e84
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m87
0
infinite
0
--
TRAF3:TBK1:IKK-i
--
e85
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m88
0
infinite
0
--
IRF-3{p}
--
e86
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m89
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007694 |
--
IRF3{p}:IRF3{p}
--
e87
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m90
0
infinite
0
--
IRF3{p}:IRF3{p}
--
e88
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m91
0
infinite
0
--
TBK1:TANK
--
e89
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m92
0
infinite
0
--
Lipoarabinomannan
--
e9
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m9
0
infinite
0
--
TBK1:IKK-i
--
e90
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m93
0
infinite
0
--
csml-variable:Double
m94
0
infinite
0
--
csml-variable:Double
m95
0
infinite
0
--
TLR9:CpGmotifs:MyD88
--
e93
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m97
0
infinite
0
--
TLR9:CpGmotifs:MyD88:IRAk-4:IRAk1:TRAF6:TRAF3:IRf7
--
e94
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
csml-variable:Double
m98
0
infinite
0
--
IRAK1
--
e95
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m99
0
infinite
0
--
IRF7
--
e96
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m100
0
infinite
0
--
TLR9:CpGmotifs:MyD88:IRAk-4:IRAk1:TRAF6:TRAF3:IRf7{p}
--
e97
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
csml-variable:Double
m101
0
infinite
0
--
IRF7{p}:IRF7{p}
--
e98
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m102
0
infinite
0
--
TLR9:CpGmotifs:MyD88:IRAk-4:IRAk1:TRAF6:TRAF3
--
e99
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
csml-variable:Double
m103
0
infinite
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m155701*m3964*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c28 : 1
stoichiometry:c29 : 1
stoichiometry:c30 : 1
m3961*m23*0.1
nodelay
--
0
PMID: 18029230 TLR4 recognizes bacterial LPS and synthetic MPLA as well as envelope proteins from respiratory syncytial virus (RSV) and mouse mammary tumor virus (MMTV).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c303 : 1
stoichiometry:c304 : 1
m135*0.1
nodelay
--
0
PMID: 18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi?IRF3/7 axis
p101
p101
cso30:i:ME_UnknownDegradation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c305 : 1
stoichiometry:c306 : 1
stoichiometry:c308 : 1
stoichiometry:c307 : 1
m136*m171*0.1
nodelay
--
0
PMID: 18029230 Ubiquitin-dependent proteolytic degradation of the C-terminal region of p105 and p100 results in the generation of mature p50 and p52
p101
p102
cso30:i:ME_UnknownDegradation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c309 : 1
stoichiometry:c310 : 1
stoichiometry:c312 : 1
stoichiometry:c311 : 1
m136*m173*0.1
nodelay
--
0
PMID: 18029230 Ubiquitin-dependent proteolytic degradation of the C-terminal region of p105 and p100 results in the generation of mature p50 and p52
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c313 : 1
stoichiometry:c314 : 1
m181*0.1
nodelay
--
0
PMID: 18029230 Importantly, p100 phosphorylation is mediated by the IKKgreek small letter alpha?IKKgreek small letter alpha homodimer, which does not require IKKbeta and NEMO.
p104
p104
cso30:i:ME_Phosphorylation
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c315 : 1
stoichiometry:c316 : 1
stoichiometry:c317 : 1
m139*m140*0.1
nodelay
--
0
p105
p105
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c318 : 1
stoichiometry:c319 : 1
stoichiometry:c320 : 1
m168*m167*0.1
nodelay
--
0
PMID: 18029230 p52 then forms a heterodimer with RelB to regulate expression of target genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c321 : 1
stoichiometry:c322 : 1
m141*0.1
nodelay
--
0
PMID: 18029230 p52 then forms a heterodimer with RelB to regulate expression of target genes.
p107
p107
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c324 : 1
stoichiometry:c156 : 1
stoichiometry:c325 : 1
m182*m71*0.1
nodelay
--
0
PMID: 18029230,11460167 It has been suggested that TAK1 can phosphorylate IKK¦Â and increase its enzymatic activity
p37
p108
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c328 : 1
stoichiometry:c329 : 1
stoichiometry:c330 : 1
stoichiometry:c331 : 1
stoichiometry:c332 : 1
stoichiometry:c333 : 1
m73*m1583*m6433*m1573*m19389*0.1
nodelay
--
0
PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-¦Â-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway
p38
p109
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c117 : 1
stoichiometry:c335 : 1
stoichiometry:c336 : 1
m144*m75*0.1
nodelay
--
0
PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-¦Â-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c31 : 1
stoichiometry:c32 : 1
stoichiometry:c33 : 1
m25*m3961*0.1
nodelay
--
0
PMID: 18029230 TLR4 recognizes bacterial LPS and synthetic MPLA as well as envelope proteins from respiratory syncytial virus (RSV) and mouse mammary tumor virus (MMTV).
p39
p110
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c337 : 1
stoichiometry:c338 : 1
stoichiometry:c339 : 1
m144*m76*0.1
nodelay
--
0
PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-¦Â-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c136 : 1
stoichiometry:c341 : 1
stoichiometry:c342 : 1
stoichiometry:c343 : 1
m70*m82*m1573*0.1
nodelay
--
0
PMID: 18029230,16115877 Notably, RIP1 is polyubiquitinated to form a complex with TRAF6 and TAK1, resulting in NF-¦ÊB activation
p112
p112
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c344 : 1
stoichiometry:c108 : 1
stoichiometry:c346 : 1
m145*m46*0.1
nodelay
--
0
PMID: 18029230,16115877 Notably, RIP1 is polyubiquitinated to form a complex with TRAF6 and TAK1, resulting in NF-¦ÊB activation
p113
p113
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c145 : 1
stoichiometry:c146 : 1
stoichiometry:c347 : 1
m74*m182*0.1
nodelay
--
0
PMID: 18029230 t has been shown that NAK enhances the enzymatic activity of IKK¦Â through direct phosphorylation, contributing to NF-¦ÊB activation.
p12
p12
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c34 : 1
stoichiometry:c35 : 1
stoichiometry:c36 : 1
m6485*m3966*0.1
nodelay
--
0
PMID: 18029230 TLR5 detects bacterial flagellin expressed in intestinal epithelial cells as well as CD11c-positive lamina propria in DCs
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c37 : 1
stoichiometry:c38 : 1
stoichiometry:c39 : 1
m3966*m28*0.1
nodelay
--
0
PMID: 18029230 TLR5 detects bacterial flagellin expressed in intestinal epithelial cells as well as CD11c-positive lamina propria in DCs
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c40 : 1
stoichiometry:c41 : 1
stoichiometry:c42 : 1
m30*m19944*0.1
nodelay
--
0
PMID: 18029230 In mice, TLR11 recognizes as yet unknown components of uropathogenic bacteria, and a profilin-like molecule of Toxoplasma gondii.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c43 : 1
stoichiometry:c44 : 1
stoichiometry:c45 : 1
m32*m33*m19944*0.1
nodelay
--
0
PMID: 18029230 In mice, TLR11 recognizes as yet unknown components of uropathogenic bacteria, and a profilin-like molecule of Toxoplasma gondii.
p16
p16
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c46 : 1
stoichiometry:c47 : 1
stoichiometry:c48 : 1
m119368*m3965*0.1
nodelay
--
0
PMID: 18029230 TLR3, 7, 8 and 9, which are localized to endosomes, detect nucleic acids derived from viruses and bacteria. PMID: 18029230 TLR3 recognizes dsRNA, which is produced by many viruses during replication, and poly IC.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c49 : 1
stoichiometry:c50 : 1
stoichiometry:c51 : 1
m34*m3965*0.1
nodelay
--
0
PMID: 18029230 TLR3, 7, 8 and 9, which are localized to endosomes, detect nucleic acids derived from viruses and bacteria. PMID: 18029230 TLR3 recognizes dsRNA, which is produced by many viruses during replication, and poly IC.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c52 : 1
stoichiometry:c53 : 1
stoichiometry:c54 : 1
m19940*m36*0.1
nodelay
--
0
PMID: 18029230 TLR7 recognizes ssRNA derived from various viruses and synthetic imidazoquinolines with antitumor properties.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c55 : 1
stoichiometry:c56 : 1
stoichiometry:c57 : 1
m19940*m38*0.1
nodelay
--
0
PMID: 18029230 TLR7 recognizes ssRNA derived from various viruses and synthetic imidazoquinolines with antitumor properties.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m3964*m9*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c58 : 1
stoichiometry:c59 : 1
stoichiometry:c60 : 1
m36*m19823*0.1
nodelay
--
0
PMID:18029230 Human TLR8 also participates in the recognition of ssRNA and imidazoquinolines, whereas the function of mouse TLR8 remains unclear.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c61 : 1
stoichiometry:c62 : 1
stoichiometry:c63 : 1
m38*m19823*0.1
nodelay
--
0
PMID:18029230 Human TLR8 also participates in the recognition of ssRNA and imidazoquinolines, whereas the function of mouse TLR8 remains unclear.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c64 : 1
stoichiometry:c65 : 1
stoichiometry:c66 : 1
m42*m19828*0.1
nodelay
--
0
PMID: 18029230 LR9 recognizes CpG DNA motifs present in bacterial and viral genomes as well as non-nucleic acids such as hemozoin from Plasmodium.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c67 : 1
stoichiometry:c68 : 1
stoichiometry:c69 : 1
m44*m19828*0.1
nodelay
--
0
PMID: 18029230 LR9 recognizes CpG DNA motifs present in bacterial and viral genomes as well as non-nucleic acids such as hemozoin from Plasmodium.
p24
p24
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c70 : 1
stoichiometry:c71 : 1
stoichiometry:c72 : 1
m166*m47*0.1
nodelay
--
0
PMID: 18029230,17072327 The most frequently activated form of NF-¦ÊB in TLR signaling is a heterodimer composed of RelA and p50
p25
p25
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c77 : 1
stoichiometry:c73 : 1
stoichiometry:c74 : 1
m46*m186*0.1
nodelay
--
0
PMID: 18029230 Under unstimulated conditions, NF-¦ÊB is sequestered in the cytoplasm as an inactive form by interaction with a family of inhibitor proteins known as I¦ÊB proteins PMID: 18029230 The RelA?p50 heterodimer is kept in the cytoplasm as a latent and inactive form by interaction with I¦ÊB proteins in unstimulated cells
p26
p26
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c75 : 1
stoichiometry:c76 : 1
stoichiometry:c78 : 1
stoichiometry:c79 : 1
m1593*m182*m181*0.1
nodelay
--
0
PMID: 18029230 Stimulation with TLR ligands triggers the rapid phosphorylation of specific serine residues of I¦ÊB proteins by a multiprotein complex termed the IKK complex, which consists of two catalytic components, IKKgreek small letter alpha and IKK¦Â, and a regulatory component, NEMO (NF-¦ÊB essential modifier, also known as IKK¦Ã).
p27
p27
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c80 : 1
stoichiometry:c81 : 1
stoichiometry:c82 : 1
m207*m48*0.1
nodelay
--
0
PMID: 18029230 Stimulation with TLR ligands triggers the rapid phosphorylation of specific serine residues of I¦ÊB proteins by a multiprotein complex termed the IKK complex, which consists of two catalytic components, IKKgreek small letter alpha and IKK¦Â, and a regulatory component, NEMO (NF-¦ÊB essential modifier, also known as IKK¦Ã).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c83 : 1
stoichiometry:c84 : 1
m49*0.1
nodelay
--
0
PMID: 18029230 Phosphorylated I¦ÊB proteins are subsequently polyubiquitinated and degraded by the 26S proteasome, allowing NF-¦ÊB to move into the nucleus.
p29
p29
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c85 : 1
stoichiometry:c86 : 1
stoichiometry:c87 : 1
stoichiometry:c88 : 1
m63*m64*0.1
nodelay
--
0
PMID: 18029230 Phosphorylated I¦ÊB proteins are subsequently polyubiquitinated and degraded by the 26S proteasome, allowing NF-¦ÊB to move into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c8 : 1
stoichiometry:c9 : 1
stoichiometry:c7 : 1
m12*m3964*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c89 : 1
stoichiometry:c90 : 1
m66*0.1
nodelay
--
0
PMID: 18029230 Phosphorylated I¦ÊB proteins are subsequently polyubiquitinated and degraded by the 26S proteasome, allowing NF-¦ÊB to move into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c91 : 1
stoichiometry:c92 : 1
m67*0.1
nodelay
--
0
PMID: 18029230,17072327 This pathway is called the ¡Æcanonical pathway¡Ç and is responsible for TLR-mediated induction of inflammatory cytokines such as tumor necrosis factor-greek small letter alpha (TNF-greek small letter alpha) and IL-6
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c93 : 1
stoichiometry:c94 : 1
m67*0.1
nodelay
--
0
PMID: 18029230,17072327 This pathway is called the ¡Æcanonical pathway¡Ç and is responsible for TLR-mediated induction of inflammatory cytokines such as tumor necrosis factor-greek small letter alpha (TNF-greek small letter alpha) and IL-6
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c95 : 1
stoichiometry:c96 : 1
stoichiometry:c97 : 1
m22*m6810*0.1
nodelay
--
0
PMID: 18029230 TLR4 uses four adaptors, MyD88, TIRAP, TRIF and TRAM. TLR3 uses TRIF as the sole adaptor PMID: 18029230
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c98 : 1
stoichiometry:c99 : 1
stoichiometry:c100 : 1
m1572*m69*0.1
nodelay
--
0
PMID: 18029230 TLR4 uses four adaptors, MyD88, TIRAP, TRIF and TRAM. TLR3 uses TRIF as the sole adaptor PMID: 18029230
p46
p35
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c134 : 1
stoichiometry:c135 : 1
stoichiometry:c137 : 1
stoichiometry:c140 : 1
m18998*m183*m83*0.1
nodelay
--
0
PMID: 18029230,15064760 he TRIF C-terminal region contains the Rip homotypic interaction motif (RHIM), which is responsible for interaction with RIP1 (receptor-interacting protein-1), a member of the RIP family involved in TNF-receptor-mediated NF-¦ÊB activation 29 E. Meylan et al., RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappaB activation
p35
p36
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c106 : 1
stoichiometry:c110 : 1
stoichiometry:c111 : 1
stoichiometry:c348 : 1
stoichiometry:c107 : 1
m1593*m72*m6443*m113*0.1
nodelay
--
0
PMID: 18029230,17496917,16858426 TRAF6 is a RING-domain E3 ubiquitin ligase, and together with E2, Ubc13 and Uev1A, it promotes Lys63-linked polyubiquitination of target proteins, including TRAF6 itself and NEMO
p37
p37
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c113 : 1
stoichiometry:c114 : 1
stoichiometry:c323 : 1
stoichiometry:c326 : 1
stoichiometry:c101 : 1
stoichiometry:c327 : 1
m6433*m1573*m19389*m1583*m70*0.1
nodelay
--
0
PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-¦Â-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway
p38
p38
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c115 : 1
stoichiometry:c334 : 1
stoichiometry:c116 : 1
m75*m143*0.1
nodelay
--
0
PMID: 18029230 The activated TAK1 complex then activates the IKK complex consisting of IKKgreek small letter alpha, IKK¦Â and NEMO, which catalyzes the phosphorylation of I¦ÊB proteins (P)
p39
p39
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c119 : 1
stoichiometry:c118 : 1
stoichiometry:c120 : 1
m76*m143*0.1
nodelay
--
0
PMID: 18029230 Simultaneously, the TAK1 complex activates the MAPK pathway, which results in the phosphorylation (P) and activation of AP-1 PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-¦Â-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c10 : 1
stoichiometry:c11 : 1
stoichiometry:c12 : 1
m14*m15*m3964*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma.
p40
p40
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c121 : 1
stoichiometry:c122 : 1
stoichiometry:c123 : 1
m77*m15167*0.1
nodelay
--
0
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c124 : 1
stoichiometry:c125 : 1
m78*0.1
nodelay
--
0
PMID: 18029230 NF-¦ÊB and AP-1 control inflammatory responses through the induction of inflammatory cytokines
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c126 : 1
stoichiometry:c127 : 1
m67*0.1
nodelay
--
0
PMID: 18029230 NF-¦ÊB and AP-1 control inflammatory responses through the induction of inflammatory cytokines
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c128 : 1
stoichiometry:c129 : 1
stoichiometry:c130 : 1
m22*m19005*0.1
nodelay
--
0
PMID: 18029230 TIRAP and TRAM are required for the activation of the MyD88- and the TRIF-dependent pathways, respectively.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c131 : 1
stoichiometry:c133 : 1
m18998*m80*0.1
nodelay
--
0
PMID: 18029230 TIRAP and TRAM are required for the activation of the MyD88- and the TRIF-dependent pathways, respectively.
p46
p46
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c138 : 1
stoichiometry:c340 : 1
stoichiometry:c139 : 1
m83*m18998*0.1
nodelay
--
0
PMID: 18029230,15064760 he TRIF C-terminal region contains the Rip homotypic interaction motif (RHIM), which is responsible for interaction with RIP1 (receptor-interacting protein-1), a member of the RIP family involved in TNF-receptor-mediated NF-¦ÊB activation 29 E. Meylan et al., RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappaB activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c141 : 1
stoichiometry:c142 : 1
m84*0.1
nodelay
--
0
PMID: 18029230,16115877 Notably, RIP1 is polyubiquitinated to form a complex with TRAF6 and TAK1, resulting in NF-¦ÊB activation
p48
p48
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c143 : 1
stoichiometry:c144 : 1
stoichiometry:c155 : 1
m85*m1573*0.1
nodelay
--
0
PMID:18029230 These findings indicate that TRIF recruits TRAF6 and RIP1 via distinct regions and that these molecules appear to cooperative to facilitate TAK1 activation, resulting in robust NF-¦ÊB activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c147 : 1
stoichiometry:c148 : 1
m46*0.1
nodelay
--
0
PMID:18029230 These findings indicate that TRIF recruits TRAF6 and RIP1 via distinct regions and that these molecules appear to cooperative to facilitate TAK1 activation, resulting in robust NF-¦ÊB activation
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c14 : 1
stoichiometry:c15 : 1
m3964*m3963*0.1
nodelay
--
0
p50
p50
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c149 : 1
stoichiometry:c150 : 1
stoichiometry:c151 : 1
m18998*m19314*0.1
nodelay
--
0
PMID: 18029230 TLR3 uses TRIF as the sole adaptor.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c152 : 1
stoichiometry:c153 : 1
stoichiometry:c154 : 1
m86*m1872*0.1
nodelay
--
0
PMID: 18029230 TRIF recruits TRAF3, which then interacts with TBK1 and IKKi.
p53
p53
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c159 : 1
stoichiometry:c160 : 1
stoichiometry:c161 : 1
m88*m977*0.1
nodelay
--
0
PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c162 : 1
stoichiometry:c163 : 1
m89*0.1
nodelay
--
0
PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c164 : 1
stoichiometry:c165 : 1
m90*0.1
nodelay
--
0
PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription
p56
p56
cso30:i:ME_GeneExpression
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c166 : 1
stoichiometry:c175 : 1
stoichiometry:c176 : 1
stoichiometry:c167 : 1
m91*m96*m67*0.1
nodelay
--
0
PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription PMID: 18029230,16979567 n the nucleus, IRF3 together with NF-¦ÊB and ATF2/c-Jun form a multiprotein complex called an enhanceosome, which binds the promoter?enhancer region of the IFN-¦Â gene
p57
p57
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c168 : 1
stoichiometry:c169 : 1
stoichiometry:c170 : 1
m3897*m3902*0.1
nodelay
--
0
PMID: 18029230 TBK1 was identified as a protein kinase interacting with TANK (also known as I-TRAF), a TRAF-binding protein
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c158 : 1
stoichiometry:c171 : 1
stoichiometry:c269 : 1
stoichiometry:c270 : 1
m87*m93*0.1
nodelay
--
0
PMID: 18029230 TRIF recruits TRAF3, which then interacts with TBK1 and IKKi.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c172 : 1
stoichiometry:c173 : 1
stoichiometry:c174 : 1
m91*m95*0.1
nodelay
--
0
PMID: 18029230 This allows IRF3 to form a homodimer, translocate into the nucleus and bind its target sequences, such as IFN-stimulated response element (ISRE).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c17 : 1
stoichiometry:c18 : 1
m18*m16*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 TLR2/1 and TLR2/6 discriminate the lipid structures between triacyl- and diacyl-lipopeptide, respectively
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c177 : 1
stoichiometry:c178 : 1
stoichiometry:c179 : 1
m43*m1572*0.1
nodelay
--
0
PMID: 18029230 TLR1, 2 and 6 utilize MyD88 and TIRAP as adaptors while TLR5, 7, 9 and 11 utilize MyD88.
p61
p61
cso30:i:ME_Binding
cso30:i:CC_EndosomeLumen
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c180 : 1
stoichiometry:c181 : 1
stoichiometry:c183 : 1
stoichiometry:c184 : 1
stoichiometry:c185 : 1
stoichiometry:c186 : 1
stoichiometry:c187 : 1
stoichiometry:c182 : 1
m97*m17258*m99*m181*m70*m1872*m100*0.1
nodelay
--
0
PMID: 18029230 In pDCs, IRF7 forms a signaling complex with MyD88, IRAK4, TRAF6, IRAK1 and IKKalpha PMID: 18029230 IRAK1, but not IRAK4, physically interacts with IRF7 PMID: 18029230 TRAF3 binds to a MyD88?IRAK1?IRF7 complex and pDCs derived from TRAF3-deficient mice have defects in IFN-greek small letter alpha production
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c188 : 1
stoichiometry:c189 : 1
m98*0.1
nodelay
--
0
PMID: 18029230 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1 and IKKalpha
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c190 : 1
stoichiometry:c191 : 1
stoichiometry:c192 : 1
m101*0.1
nodelay
--
0
PMID: 18029230 n response to ligand stimulation, IRF7 is phosphorylated by IRAK1 and IKKgreek small letter alpha, dimerizes and is then translocated into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c193 : 1
stoichiometry:c194 : 1
m102*0.1
nodelay
--
0
PMID: 18029230 n response to ligand stimulation, IRF7 is phosphorylated by IRAK1 and IKKgreek small letter alpha, dimerizes and is then translocated into the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c195 : 1
stoichiometry:c196 : 1
m104*0.1
nodelay
--
0
PMID: 18029230 IRF7 regulates the expression of type I IFNs, including IFN-greek small letter alpha and IFN-¦Â
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c197 : 1
stoichiometry:c198 : 1
m104*0.1
nodelay
--
0
PMID: 18029230 IRF7 regulates the expression of type I IFNs, including IFN-greek small letter alpha and IFN-¦Â
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c200 : 1
stoichiometry:c199 : 1
stoichiometry:c201 : 1
m6810*m17*0.1
nodelay
--
0
PMID: 18029230 TLR1, 2 and 6 utilize MyD88 and TIRAP as adaptors
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c202 : 1
stoichiometry:c203 : 1
stoichiometry:c204 : 1
m1572*m106*0.1
nodelay
--
0
PMID: 18029230 TLR1, 2 and 6 utilize MyD88 and TIRAP as adaptors
p69
p69
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c238 : 1
stoichiometry:c105 : 1
stoichiometry:c112 : 1
stoichiometry:c237 : 1
m46*m22*0.1
nodelay
--
0
PMID: 18029230 Pretreatment of MyD88-deficient cells with cyclohexamide, a protein synthesis inhibitor, results in an abrogation of LPS-induced NF-¦ÊB activation, thus suggesting that late phase NF-¦ÊB activation is likely to require protein synthesis. PMID: 18029230 LPS induces TNF-greek small letter alpha synthesis via a MyD88-independent mechanism, and the newly synthesized TNF-greek small letter alpha subsequently binds TNF receptor to initiate the late phase NF-¦ÊB activation in an autocrine manner, at least in MEF cells.
p6
p7
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c20 : 1
stoichiometry:c21 : 1
m3964*m3987*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 TLR2/1 and TLR2/6 discriminate the lipid structures between triacyl- and diacyl-lipopeptide, respectively
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c205 : 1
stoichiometry:c206 : 1
stoichiometry:c207 : 1
m17258*m107*0.1
nodelay
--
0
PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M,
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c208 : 1
stoichiometry:c209 : 1
m108*0.1
nodelay
--
0
PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c210 : 1
stoichiometry:c211 : 1
stoichiometry:c212 : 1
m109*m99*0.1
nodelay
--
0
PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M,
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c213 : 1
stoichiometry:c214 : 1
m110*0.1
nodelay
--
0
PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c215 : 1
stoichiometry:c216 : 1
stoichiometry:c217 : 1
m111*0.1
nodelay
--
0
PMID: 18029230 After IRAK4 and IRAK1 have been sequentially phosphorylated, they dissociate from MyD88 and interact with TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c218 : 1
stoichiometry:c219 : 1
stoichiometry:c220 : 1
m112*m183*0.1
nodelay
--
0
PMID: 18029230 After IRAK4 and IRAK1 have been sequentially phosphorylated, they dissociate from MyD88 and interact with TRAF6.
p35
p76
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c221 : 1
stoichiometry:c103 : 1
stoichiometry:c109 : 1
stoichiometry:c222 : 1
m113*m6443*m72*0.1
nodelay
--
0
PMID: 18029230,17496917,16858426 TRAF6 is a RING-domain E3 ubiquitin ligase, and together with E2, Ubc13 and Uev1A, it promotes Lys63-linked polyubiquitination of target proteins, including TRAF6 itself and NEMO
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c223 : 1
stoichiometry:c224 : 1
stoichiometry:c225 : 1
m68*m17258*0.1
nodelay
--
0
PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M,
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c226 : 1
stoichiometry:c227 : 1
m114*0.1
nodelay
--
0
PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c228 : 1
stoichiometry:c229 : 1
stoichiometry:c230 : 1
m115*m99*0.1
nodelay
--
0
PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M,
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c22 : 1
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m21*m19*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 TLR2/1 and TLR2/6 discriminate the lipid structures between triacyl- and diacyl-lipopeptide, respectively
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c231 : 1
stoichiometry:c232 : 1
m116*0.1
nodelay
--
0
PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c233 : 1
stoichiometry:c234 : 1
stoichiometry:c235 : 1
m117*0.1
nodelay
--
0
PMID: 18029230 After IRAK4 and IRAK1 have been sequentially phosphorylated, they dissociate from MyD88 and interact with TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c239 : 1
stoichiometry:c240 : 1
m93309*0.1
nodelay
--
0
PMID: 18029230 LPS induces TNF-greek small letter alpha synthesis via a MyD88-independent mechanism, and the newly synthesized TNF-greek small letter alpha subsequently binds TNF receptor to initiate the late phase NF-¦ÊB activation in an autocrine manner, at least in MEF cells.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c241 : 1
stoichiometry:c242 : 1
stoichiometry:c243 : 1
m119*m230*0.1
nodelay
--
0
PMID: 18029230 LPS induces TNF-greek small letter alpha synthesis via a MyD88-independent mechanism, and the newly synthesized TNF-greek small letter alpha subsequently binds TNF receptor to initiate the late phase NF-¦ÊB activation in an autocrine manner, at least in MEF cells.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c246 : 1
stoichiometry:c259 : 1
stoichiometry:c250 : 1
m123*m128*0.1
nodelay
--
0
PMID: 18029230 RIG-I and Mda5 contain CARD-like structures that mediate interaction with the adaptor IPS-1
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c249 : 1
stoichiometry:c258 : 1
stoichiometry:c260 : 1
m123*m129*0.1
nodelay
--
0
PMID: 18029230 RIG-I and Mda5 contain CARD-like structures that mediate interaction with the adaptor IPS-1
p86
p86
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c251 : 1
stoichiometry:c261 : 1
stoichiometry:c247 : 1
stoichiometry:c252 : 1
stoichiometry:c264 : 1
stoichiometry:c265 : 1
m1872*m125*m1593*m1814*m1815*0.1
nodelay
--
0
PMID: 18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi?IRF3/7 axis PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-¦ÊB activation PMID: 18029230,17468758 NEMO is shown to participate in both NF-¦ÊB and IRF3 activation in RIG-I and Mda5 signaling pathways
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c254 : 1
stoichiometry:c245 : 1
stoichiometry:c248 : 1
m127*m121*0.1
nodelay
--
0
PMID: 18029230 Cells express cytoplasmic RNA helicases (RIG-I and Mda5) that recognize RNA derived from actively replicating RNA viruses.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c255 : 1
stoichiometry:c256 : 1
stoichiometry:c257 : 1
m127*m122*0.1
nodelay
--
0
PMID: 18029230 Cells express cytoplasmic RNA helicases (RIG-I and Mda5) that recognize RNA derived from actively replicating RNA viruses.
p86
p89
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c253 : 1
stoichiometry:c262 : 1
stoichiometry:c263 : 1
stoichiometry:c266 : 1
stoichiometry:c267 : 1
stoichiometry:c268 : 1
m1814*m1872*m1593*m130*m1815*0.1
nodelay
--
0
PMID: 18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi?IRF3/7 axis PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-¦ÊB activation PMID: 18029230,17468758 NEMO is shown to participate in both NF-¦ÊB and IRF3 activation in RIG-I and Mda5 signaling pathways
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
stoichiometry:c27 : 1
m155666*m3961*0.1
nodelay
--
0
PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand)
p90
p90
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c271 : 1
stoichiometry:c272 : 1
stoichiometry:c273 : 1
stoichiometry:c274 : 1
m124*m3902*m1599*0.1
nodelay
--
0
PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi?IRF3/7 axis
p90
p91
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c275 : 1
stoichiometry:c276 : 1
stoichiometry:c277 : 1
stoichiometry:c278 : 1
m126*m3902*m1599*0.1
nodelay
--
0
PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi?IRF3/7 axis
p92
p92
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c279 : 1
stoichiometry:c102 : 1
stoichiometry:c281 : 1
m124*m46*0.1
nodelay
--
0
PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-¦ÊB activation
p92
p93
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c282 : 1
stoichiometry:c104 : 1
stoichiometry:c284 : 1
m126*m46*0.1
nodelay
--
0
PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-¦ÊB activation
p94
p94
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c285 : 1
stoichiometry:c286 : 1
stoichiometry:c287 : 1
m1599*m1357*0.1
nodelay
--
0
PMID: 18029230 IKKi can phosphorylate a serine residue in STAT1 that is crucial for the transcriptional activity
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c288 : 1
stoichiometry:c289 : 1
stoichiometry:c290 : 1
m36323*m132*0.1
nodelay
--
0
PMID: 18029230,17618271 Recently, DAI (DNA-dependent activator of interferon-regulatory factors, also known as DLM-1 and ZBP1) has been identified as a cytosolic sensor for dsDN PMID: 18029230 DAI is an IFN-inducible gene that has dsDNA-binding properties
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c291 : 1
stoichiometry:c292 : 1
stoichiometry:c293 : 1
m133*m93*0.1
nodelay
--
0
PMID: 18029230 Whereas DAI activates IRF3 via direct interactions with TBK1 and IRF3, pathways for NF-¦ÊB activation remain unknown.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c294 : 1
stoichiometry:c295 : 1
stoichiometry:c296 : 1
m134*m977*0.1
nodelay
--
0
PMID: 18029230 Whereas DAI activates IRF3 via direct interactions with TBK1 and IRF3, pathways for NF-¦ÊB activation remain unknown.
p98
p98
cso30:i:ME_Phosphorylation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c297 : 1
stoichiometry:c298 : 1
stoichiometry:c299 : 1
m93*m977*0.1
nodelay
--
0
PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi?IRF3/7 axis
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c300 : 1
stoichiometry:c301 : 1
stoichiometry:c302 : 1
m93*m100*0.1
nodelay
--
0
PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi?IRF3/7 PMID: 18029230,12702806 TBK1 and IKKi can also phosphorylate and activate IRF7, which is the member of IRF family most closely related to IRF3
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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:InputProcess
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:InputProcess
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: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:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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:InputProcess
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:InputProcess
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:OutputProcess
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:InputProcess
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:InputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputProcess
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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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: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:InputProcess
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:InputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
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: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:InputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
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:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
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: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: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:InputAssociation
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: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:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--