Entity
Process
TRAF6
--
MO000000212
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m183
10

infinite
0
| InterPro | IPR001841 |
| TRANSPATH | MO000000212 |
--
IkappaB-alpha{p}: NFkappaB
--
MO000000220
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m190
10

infinite
0
| TRANSPATH | MO000000220 |
--
IkappaB-alpha: NFkappaB
--
MO000000233
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m199
10

infinite
0
| InterPro | IPR002110 |
| TRANSPATH | MO000000233 |
--
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 |
--
TLR4
--
MO000019394
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3961
10

infinite
0
| InterPro | IPR000157 |
| TRANSPATH | MO000019394 |
--
dsRNA:TLR3:TRIF
--
MO000041437
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19305
10

infinite
0
| TRANSPATH | MO000041437 |
--
dsRNA:TLR3
--
MO000041446
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19314
10

infinite
0
| TRANSPATH | MO000041446 |
--
TLR9
--
MO000042012
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19828
10

infinite
0
| TRANSPATH | MO000042012 |
--
MyD88:MyD88
--
MO000050640
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m192928
10

infinite
0
| TRANSPATH | MO000050640 |
--
--
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
--
e100
--
e100
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m103
0

infinite
0
--
csml-variable:Double
m104
0

infinite
0
--
TLR4:MyD88: TIRAP
--
e103
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m106
0

infinite
0
--
LPS:TLR4: TIRF
--
e104
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m107
0

infinite
0
--
LPS:TLR4: TIRF: TRAM
--
e105
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m108
0

infinite
0
--
IRF-3 {p}: IRF-3: p300 {nucleus}
--
e106
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m109
0

infinite
0
--
NF-kappaB [activated}
--
e11
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m11
10

infinite
0
| InterPro | IPR008967 |
| TRANSPATH | MO000100032 |
--
IkappaB-alpha{ub}: NFkappaB
--
e12
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m12
0

infinite
0
--
IkappaB-alpha {degraded}
--
e13
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m13
0

infinite
0
--
NF-kappaB [nucleus}
--
e14
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m14
10

infinite
0
| InterPro | IPR008967 |
| TRANSPATH | MO000100032 |
--
IL-1: IL-1RI
--
e15
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m15
0

infinite
0
--
IL-1: IL-1RI: MyD88
--
e16
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m16
0

infinite
0
--
IL-1: IL-1RI: MyD88: IRAK: IRAK-4
--
e17
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
csml-variable:Double
m17
0

infinite
0
--
IL-1: IL-1RI: MyD88: IRAK {p}: IRAK-4: TRAF6
--
e18
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m18
0

infinite
0
--
IL-1: IL-1RI: MyD88: IRAK {p}: IRAK-4
--
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
--
IL-1: IL-1RI: MyD88: IRAK [p}: IRAK-4: TRAF6: Pellino1
--
e20
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
csml-variable:Double
m20
0

infinite
0
--
IRAK {p}: IRAK-4: TRAF6: Pellino1
--
e21
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m21
0

infinite
0
--
IRAK {p}: TRAF6: TAK1: TAB1: TAB2
--
e22
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m22
0

infinite
0
--
IRAK {p}: TRAF6: TAK1 {p}: TAB1: TAB2 {p}
--
e23
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m23
0

infinite
0
--
IRAK-4: Pellino1
--
e24
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m24
0

infinite
0
--
IRAK {p}: TRAF6: TAK1 {p}: TAB1: TAB2 {p}
--
e25
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m25
0

infinite
0
--
IRAK {p}: TRAF6: TAK1 {p}{activated}: TAB1: TAB2 {p}
--
e26
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m26
0

infinite
0
--
MAPK6
--
e27
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m27
0

infinite
0
--
MAPK {activated}
--
e28
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m28
0

infinite
0
--
JNK {activated}
--
e29
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m30
10

infinite
0
| TRANSPATH | MO000000023 |
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0

infinite
0
--
IRAK {p}: TRAF6: TAK1 {p}: TAB1: TAB2 {p} : Ubc13: Uev1A
--
e33
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m34
0

infinite
0
--
Uev1A
--
e34
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m35
0

infinite
0
--
IRAK {p}: TRAF6 {ub}: TAK1 {p}: TAB1: TAB2 {p} : Ubc13: Uev1A
--
e35
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m36
0

infinite
0
--
MEKK3: TRAF6
--
e36
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m37
0

infinite
0
--
dsRNA:TLR3:TRIF:TRAF6:TAK1:TAB2
--
e37
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m38
10

infinite
0
| TRANSPATH | MO000041496 |
--
dsRNA:TLR3:TRIF:TRAF6:TAK1:TAB2: RIP1
--
e38
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m40
0

infinite
0
--
NF-kappaB
--
e39
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m41
10

infinite
0
| InterPro | IPR008967 |
| TRANSPATH | MO000100032 |
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0

infinite
0
--
IRF-3 {p}
--
e40
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m42
10

infinite
0
| InterPro | IPR008984 |
| TRANSPATH | MO000007694 |
--
csml-variable:Double
m43
0

infinite
0
--
TBK1: IKK-i {activated}
--
e42
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m44
0

infinite
0
--
MyD88: TIRAP: ST2
--
e44
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m46
0

infinite
0
--
IL-1: IL-1RI: MyD88: IRAK {p}: IRAK-4: TRAF6: SIGIRR
--
e45
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m47
0

infinite
0
--
IRAK-2d
--
e46
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m48
10

infinite
0
| InterPro | IPR000719 |
| TRANSPATH | MO000016566 |
--
IRAK-2c
--
e47
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m49
10

infinite
0
| InterPro | IPR000719 |
| TRANSPATH | MO000016566 |
--
IKK-alpha: IKK-beta: IKK-gamma
--
e5
cso30:c:Complex
cso30:i:CC_Cytosol
--
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
--
IKK-alpha {p}: IKK-beta {p}: IKK-gamma
--
e6
cso30:c:Complex
cso30:i:CC_Cytosol
--
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
--
IRAK-2c
--
e63
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m65
0

infinite
0
--
LPS: TLR4
--
e64
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m66
0

infinite
0
--
IL-1: IL-1RI: MyD88s
--
e66
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
csml-variable:Double
m68
0

infinite
0
--
MyD88s
--
e67
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m69
0

infinite
0
--
SOCS1
--
e68
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m70
0

infinite
0
--
NO2-
--
e69
cso30:c:SmallMolecule
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
--
csml-variable:Double
m73
0

infinite
0
--
P38 {p}
--
e71
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m74
0

infinite
0
--
TLR6: TLR2
--
e72
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m75
0

infinite
0
--
Uba: ubiquitin
--
e73
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m76
0

infinite
0
--
lipoprotein
--
e74
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m77
0

infinite
0
--
lipoprotein: TLR6: TLR2
--
e76
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m79
0

infinite
0
--
Ubc: ubiquitin
--
e77
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m80
0

infinite
0
--
fagellin
--
e78
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m81
0

infinite
0
--
TLR4{ub}
--
e79
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m82
0

infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0

infinite
0
--
IRF-3 {p}: IRF-3: p300
--
e81
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m84
0

infinite
0
--
Triad3A
--
e82
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m85
0

infinite
0
--
TLR9{ub}
--
e83
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m86
0

infinite
0
--
TLR9 {degraded}
--
e84
cso30:c:EntityBiological
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m87
0

infinite
0
--
TLR4 {degraded}
--
e85
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m88
0

infinite
0
--
TRAF6: TAK1: TAB2
--
e86
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m89
0

infinite
0
--
TRAF6: TAK1 {p}: TAB2
--
e87
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m90
0

infinite
0
--
flagellin
--
e88
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m91
0

infinite
0
--
bacterial DNA
--
e89
cso30:c:Dna
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m92
0

infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0

infinite
0
--
bacterial DNA: TLR9
--
e90
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m93
0

infinite
0
--
R848
--
e91
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
csml-variable:Double
m94
0

infinite
0
--
R848: TLR7
--
e92
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m95
0

infinite
0
--
R848: TLR8
--
e93
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m96
0

infinite
0
--
ssRNA
--
e94
cso30:c:Rna
cso30:i:CC_Extracellular
--
csml-variable:Double
m97
0

infinite
0
--
ssRNA: TLR7
--
e95
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m98
0

infinite
0
--
ssRNA: TLR8
--
e96
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m99
0

infinite
0
--
IRF-3 {p}: IRF-3
--
e97
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m100
0

infinite
0
--
IRF-3 {p}: IRF-3: CBP
--
e98
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m101
0

infinite
0
--
IRF-3 {p}: IRF-3: CBP{nucleus}
--
e99
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m102
0

infinite
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c186 : 1
stoichiometry:c2 : 1
m5*m90*0.1
nodelay
--

0

PMID: 15662540 Activation of the IKK complex involves the phosphorylation of two serine residues located in the activation loop within the kinase domain of IKK¦Á (S176 and S180) or IKK¦Â (S177 and S181). PMID: 15662540 Once activated, TAK1 can directly phosphorylate IKK¦Â and mitogen-activated protein kinase kinase 6. PMID: 15662540 TRAF6-TAK1-TAB2 are then translocated to the cytosol, where TAK1 is phosphorylated and activated, leading to the activation of IKK and NF¦ÊB.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c23 : 1
stoichiometry:c118 : 1
stoichiometry:c26 : 1
m17*0.1
nodelay
--

0

PMID: 15662540 During the formation of Complex I IRAK4 is activated, leading to the hyperphosphorylation of IRAK. PMID: 15662540 Unlike MyD88, MyD88s does not bind IRAK4, and overexpression of MyD88s does not induce IRAK phosphorylation.
p11
p11
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c28 : 1
stoichiometry:c29 : 1
stoichiometry:c30 : 1
m19287*m18*0.1
nodelay
--

0

PMID: 15662540, 12496252 During the formation of Complex I IRAK4 is activated, leading to the hyperphosphorylation of IRAK, which creates an interface for its interaction with adapter Pellino 1.
p12
p12
cso30:i:ME_Dissociation
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c31 : 1
stoichiometry:c98 : 1
stoichiometry:c32 : 1
stoichiometry:c33 : 1
m20*0.1
nodelay
--

0

PMID: 15662540 The formation of Pellino 1-IRAK4-IRAKTRAF6 causes conformational changes in the receptor complex (Complex I), releasing these signaling molecules from the receptor. PMID: 15662540 IRAKM prevents the dissociation of the IRAK-IRAK4 from MyD88 thereby inhibiting the formation of the IRAK-TRAF6 interaction.
p13
p13
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c34 : 1
stoichiometry:c35 : 1
stoichiometry:c36 : 1
stoichiometry:c37 : 1
stoichiometry:c38 : 1
stoichiometry:c41 : 1
m21*m1573*m1583*m6433*0.1
nodelay
--

0

PMID: 15662540 The released components then interact with the membrane-bound preassociated transforming growth factor ¦Â activated kinase (TAK) 1?transforming growth factor ¦Â activated protein kinase 1 binding protein (TAB) 1?TAB2 [28], resulting in the formation of Complex II (IRAK-TRAF6-TAK1-TAB1-TAB2).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c39 : 1
stoichiometry:c40 : 1
m22*0.1
nodelay
--

0

PMID: 15662540 TAK1 and TAB2 are phosphorylated in the membrane-bound Complex II.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c42 : 1
stoichiometry:c43 : 1
m23*0.1
nodelay
--

0

PMID: 15662540 TAK1 and TAB2 are phosphorylated in the membrane-bound Complex II, triggering the dissociation and translocation of TRAF6-TAK1-TAB1-TAB2 (Complex III) from the membrane to the cytosol.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c64 : 1
stoichiometry:c61 : 1
m36*0.1
nodelay
--

0

PMID: 15662540 The translocated Complex III interacts with additional factors in the cytosol, leading to TAK1 activation. PMID: 15662540 The activation of TAK1 eventually leads to the activation of IKK. PMID: 15662540 Furthermore, it was shown that the TAK1 complex (TAK1-TAB1-TAB2) is activated by association with ubiquitinated TRAF6.
p17
p17
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c65 : 1
stoichiometry:c66 : 1
stoichiometry:c67 : 1
m183*m1116*0.1
nodelay
--

0

PMID: 15662540 It has been shown that MEKK3 forms a complex with TRAF6 in response to IL-1 and is crucial for IL-1 induced NF¦ÊB activation.
p18
p18
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c51 : 1
stoichiometry:c50 : 1
stoichiometry:c52 : 1
m29*m28*0.1
nodelay
--

0

PMID: 15662540 Once activated, TAK1 can directly phosphorylate IKK¦Â and mitogen-activated protein kinase kinase 6, leading to the activation of both the c-Jun N-terminal kinase and NF¦ÊB signaling pathways.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c53 : 1
stoichiometry:c55 : 1
stoichiometry:c54 : 1
m31*m30*0.1
nodelay
--

0

PMID: 15662540 Activated TAK1 has also been implicated in the IL-1 induced activation of mitogen-activated protein kinase kinase 6 and c-Jun N-terminal kinase [46], leading to the activation of other transcription factors, including activating transcription factor and activator protein 1.
p2
p2
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c3 : 1
stoichiometry:c5 : 1
stoichiometry:c135 : 1
stoichiometry:c136 : 1
stoichiometry:c4 : 1
m199*m6*m66*0.1
nodelay
--

0

PMID: 15662540 The IKK¦Á and IKK¦Â subunits preferentially form heterodimers, and both can directly phosphorylate the critical S32 and S36 residues of I¦ÊB¦Á. PMID: 15662540 LPS-induced I¦ÊB and p38 phosphorylation are upregulated in SOCS1- deficient macrophages. Moreover, forced expression of SOCS1 suppresses LPS-induced NF¦ÊB activation.
p20
p20
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c58 : 1
stoichiometry:c57 : 1
m219*m30*0.1
nodelay
--

0

PMID: 15662540 Activated TAK1 has also been implicated in the IL-1 induced activation of mitogen-activated protein kinase kinase 6 and c-Jun N-terminal kinase [46], leading to the activation of other transcription factors, including activating transcription factor and activator protein 1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c45 : 1
stoichiometry:c44 : 1
stoichiometry:c62 : 1
stoichiometry:c59 : 1
m25*m6443*m35*0.1
nodelay
--

0

PMID: 15662540 TRAF6 functions as part of a unique E3 complex, with Ubc13 and Uev1A, and TRAF6 itself is the target of ubiquitination.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c60 : 1
stoichiometry:c63 : 1
m34*0.1
nodelay
--

0

PMID: 15662540 TRAF6 functions as part of a unique E3 complex, with Ubc13 and Uev1A, and TRAF6 itself is the target of ubiquitination.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c47 : 1
stoichiometry:c49 : 1
stoichiometry:c48 : 1
m27*m26*0.1
nodelay
--

0

PMID: 15662540 Once activated, TAK1 can directly phosphorylate IKK¦Â and mitogen-activated protein kinase kinase 6.
p24
p24
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c99 : 1
stoichiometry:c104 : 1
stoichiometry:c106 : 1
stoichiometry:c246 : 1
stoichiometry:c102 : 1
m41*m63*0.1
nodelay
--

0

PMID: 15662540 When over expressed, IRAK2a and IRAK2b potentiate NF¦ÊB activation by LPS. Interestingly, IRAK2c and IRAK2d were inhibitory.
p25
p25
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c69 : 1
stoichiometry:c70 : 1
m119368*m3965*0.1
nodelay
--

0

PMID: 15662540, 11607032 TLR3 recognizes doublestranded RNA (dsRNA).
p26
p26
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c71 : 1
stoichiometry:c75 : 1
stoichiometry:c72 : 1
m19314*m18998*0.1
nodelay
--

0

PMID: 15662540, 12872135, 12855817 TRIF was recently identified as an adapter for TLR3.
p27
p27
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c73 : 1
stoichiometry:c76 : 1
stoichiometry:c77 : 1
stoichiometry:c78 : 1
stoichiometry:c74 : 1
m19305*m183*m6433*m1573*0.1
nodelay
--

0

PMID: 15662540 adapter molecule TRIF recruits TRAF6?TAK1?TAB2 to TLR3 through its TRAF6-binding site.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c79 : 1
stoichiometry:c80 : 1
stoichiometry:c81 : 1
m38*m39*0.1
nodelay
--

0

PMID: 15662540 receptor interacting protein (RIP) 1 has also been implicated in TLR3/TRIFmediated NF¦ÊB activation.
p29
p29
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c82 : 1
stoichiometry:c84 : 1
stoichiometry:c107 : 1
stoichiometry:c243 : 1
stoichiometry:c83 : 1
m41*m40*0.1
nodelay
--

0

PMID: 15662540 it is possible that RIP1 directly cooperates with the TRAF6-containing complex, facilitating the NF¦ÊB activation process. PMID: 15662540 When over expressed, IRAK2a and IRAK2b potentiate NF¦ÊB activation by LPS. Interestingly, IRAK2c and IRAK2d were inhibitory.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c6 : 1
stoichiometry:c7 : 1
m190*0.1
nodelay
--

0

PMID: 15662540 Phospho-I¦ÊB is then recognized by the ¦Â-transducin repeat containing protein containing Skp1/Cullin/F-box ubiquitin ligase complex, leading to its ubiquitination and degradation by the proteasome.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c85 : 1
stoichiometry:c89 : 1
stoichiometry:c86 : 1
m43*m108*0.1
nodelay
--

0

PMID; 15662540 TRIF leads to the activation of TBK1/IKK¦Å, resulting in IRF3 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c205 : 1
stoichiometry:c206 : 1
m42*0.1
nodelay
--

0

PMID: 15662540 Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c92 : 1
stoichiometry:c91 : 1
stoichiometry:c93 : 1
m41575*m18*0.1
nodelay
--

0

PMID:15662540, 12925853 The fact that SIGIRR forms a complex with the IL-1 receptor, IRAK, and TRAF6 upon IL-1 stimulation suggests that SIGIRR functions through its interaction with the TIR complex.
p33
p33
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c94 : 1
stoichiometry:c95 : 1
stoichiometry:c96 : 1
stoichiometry:c97 : 1
m1572*m6810*m22456*0.1
nodelay
--

0

PMID: 15662540 Overexpression of ST2 was found to inhibit NF¦ÊB activation because ST2 associated with, and probably sequestered, MyD88 and TIRAP.Overexpression of ST2 was found to inhibit NF¦ÊB activation because ST2 associated with, and probably sequestered, MyD88 and TIRAP.
p34
p34
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c100 : 1
stoichiometry:c103 : 1
stoichiometry:c105 : 1
stoichiometry:c247 : 1
stoichiometry:c101 : 1
m41*m64*0.1
nodelay
--

0

PMID: 15662540 When over expressed, IRAK2a and IRAK2b potentiate NF¦ÊB activation by LPS. Interestingly, IRAK2c and IRAK2d were inhibitory.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c108 : 1
stoichiometry:c109 : 1
m66*0.1
nodelay
--

0

PMID: 15662540 LPS induces the expression of IRAK2c.
p36
p36
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c110 : 1
stoichiometry:c111 : 1
stoichiometry:c112 : 1
m155666*m3961*0.1
nodelay
--

0

PMID: 15662540 LPS induces the expression of IRAK2c.
p37
p37
cso30:i:ME_Dimerization
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c17 : 1
stoichiometry:c113 : 1
m1572*0.1
nodelay
--

0

PMID: 15662540 MyD88 forms homodimers through DD-DD and TIR-TIR domain interactions and exists as a dimer when recruited to the receptor complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c115 : 1
stoichiometry:c46 : 1
stoichiometry:c117 : 1
m15*m1572*0.1
nodelay
--

0

PMID: 15662540 Unlike MyD88, MyD88s does not bind IRAK4, and overexpression of MyD88s does not induce IRAK phosphorylation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c119 : 1
stoichiometry:c120 : 1
m66*0.1
nodelay
--

0

PMID: 15662540 MyD88s is induced in monocytes upon LPS stimulation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c8 : 1
stoichiometry:c9 : 1
stoichiometry:c10 : 1
m12*0.1
nodelay
--

0

PMID: 15662540 Phospho-I¦ÊB is then recognized by the ¦Â-transducin repeat containing protein containing Skp1/Cullin/F-box ubiquitin ligase complex, leading to its ubiquitination and degradation by the proteasome.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c121 : 1
stoichiometry:c116 : 1
m69*0.1
nodelay
--

0

PMID: 15662540 MyD88s is induced in monocytes upon LPS stimulation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c123 : 1
stoichiometry:c124 : 1
m66*0.1
nodelay
--

0

PMID: 15662540 LPS induces the expression of SOCS1 in macrophages.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c125 : 1
stoichiometry:c126 : 1
m93501*0.1
nodelay
--

0

PMID: 15662540 LPS induces the expression of SOCS1 in macrophages.
p43
p43
cso30:i:ME_ChangeInMaterialConcentration
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c127 : 1
stoichiometry:c129 : 1
stoichiometry:c128 : 1
m66*0.1
nodelay
--

0

PMID: 15662540 LPS-induced NO2¡Ý synthesis and tumor necrosis factor ¦Á production are augmented in SOCS1- deficient macrophages.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c133 : 1
m93309*0.1
nodelay
--

0

PMID: 15662540 LPS-induced NO2¡Ý synthesis and tumor necrosis factor ¦Á production are augmented in SOCS1- deficient macrophages.
p45
p45
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c130 : 1
stoichiometry:c134 : 1
stoichiometry:c131 : 1
m66*0.1
nodelay
--

0

PMID: 15662540 LPS-induced NO2¡Ý synthesis and tumor necrosis factor ¦Á production are augmented in SOCS1- deficient macrophages.
p46
p46
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c139 : 1
stoichiometry:c140 : 1
stoichiometry:c138 : 1
m72*m66*0.1
nodelay
--

0

PMID: 15662540 LPS-induced I¦ÊB and p38 phosphorylation are upregulated in SOCS1- deficient macrophages.
p47
p47
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c143 : 1
stoichiometry:c144 : 1
stoichiometry:c146 : 1
m3964*m3987*0.1
nodelay
--

0

PMID: 15662540, 11095740 TLR6 associates with TLR2 and recognizes lipoproteins from microplasma.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c141 : 1
stoichiometry:c142 : 1
stoichiometry:c145 : 1
m73*m3556*0.1
nodelay
--

0

PMID: 15662540 In an initial step the ubiquitin-activating enzyme (E1 or Uba) forms a thioester bond with the C-terminus of ubiquitin.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c162 : 1
stoichiometry:c167 : 1
stoichiometry:c209 : 1
m4512*m100*0.1
nodelay
--

0

PMID: 15662540 Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization and interaction with the coactivaotors cAMP-response element binding protein binding protein and p300.
p5
p5
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c11 : 1
stoichiometry:c14 : 1
stoichiometry:c15 : 1
m185*m1589*0.1
nodelay
--

0

PMID: 15662540 The Ig domain subgroup includes IL-1 receptor (IL-1R) 1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c149 : 1
stoichiometry:c150 : 1
stoichiometry:c153 : 1
m75*m77*0.1
nodelay
--

0

PMID: 15662540, 11095740 TLR6 associates with TLR2 and recognizes lipoproteins from microplasma.
p51
p51
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c157 : 1
stoichiometry:c158 : 1
stoichiometry:c161 : 1
stoichiometry:c160 : 1
stoichiometry:c178 : 1
m3961*m80*m83*0.1
nodelay
--

0

PMID:15662540 In the final step the E2 enzyme donates ubiquitin to a lysine residue of the target protein, either directly or with the assistance of ubiquitin protein ligase (E3 or Ubr).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c155 : 1
stoichiometry:c163 : 1
stoichiometry:c159 : 1
m3961*m85*0.1
nodelay
--

0

PMID: 15662540 Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
p53
p53
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c164 : 1
stoichiometry:c165 : 1
stoichiometry:c169 : 1
stoichiometry:c170 : 1
stoichiometry:c177 : 1
m80*m83*m19828*0.1
nodelay
--

0

PMID:15662540 In the final step the E2 enzyme donates ubiquitin to a lysine residue of the target protein, either directly or with the assistance of ubiquitin protein ligase (E3 or Ubr).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c168 : 1
stoichiometry:c171 : 1
stoichiometry:c172 : 1
m85*m19828*0.1
nodelay
--

0

PMID: 15662540 Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
p55
p55
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c173 : 1
stoichiometry:c174 : 1
m86*0.1
nodelay
--

0

PMID: 15662540 Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
p56
p56
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c175 : 1
stoichiometry:c176 : 1
m82*0.1
nodelay
--

0

PMID: 15662540 Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c181 : 1
stoichiometry:c182 : 1
stoichiometry:c183 : 1
m38*0.1
nodelay
--

0

PMID: 15662540 TRAF6-TAK1-TAB2 are then translocated to the cytosol.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c184 : 1
stoichiometry:c185 : 1
m89*0.1
nodelay
--

0

PMID: 15662540 TRAF6-TAK1-TAB2 are then translocated to the cytosol, where TAK1 is phosphorylated and activated.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c12 : 1
stoichiometry:c13 : 1
m11*0.1
nodelay
--

0

PMID: 15662540, 10837071, 10713156 The destruction of I¦ÊB unmasks the nuclear localization signal of NF¦ÊB, leading to its nuclear translocation and binding to the promoters of target genes.
p60
p60
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_ExternalSideOfPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c154 : 1
stoichiometry:c156 : 1
stoichiometry:c166 : 1
m3966*m81*0.1
nodelay
--

0

PMID: 15662540, 11323673 While TLR5 mediates the induction of the immune response by bacterial flagellins.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c179 : 1
stoichiometry:c180 : 1
stoichiometry:c189 : 1
m19828*m92*0.1
nodelay
--

0

PMID: 15662540, 11130078 TLR9 has been shown to recognize bacterial DNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c190 : 1
stoichiometry:c191 : 1
stoichiometry:c192 : 1
m19940*m94*0.1
nodelay
--

0

PMID: 15662540, 11812998, 10346978 While 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:c193 : 1
stoichiometry:c194 : 1
stoichiometry:c195 : 1
m94*m19823*0.1
nodelay
--

0

11812998, 10346978 While 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:c196 : 1
stoichiometry:c197 : 1
stoichiometry:c198 : 1
m97*m19940*0.1
nodelay
--

0

PMID: 15662540, 14976261, 14976262, 15034168 recent studies showed that ssRNA is the natural ligand for TLR7/8.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c199 : 1
stoichiometry:c200 : 1
stoichiometry:c201 : 1
m97*m19823*0.1
nodelay
--

0

PMID: 15662540, 14976261, 14976262, 15034168 recent studies showed that ssRNA is the natural ligand for TLR7/8.
p66
p66
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c202 : 1
stoichiometry:c204 : 1
stoichiometry:c244 : 1
stoichiometry:c245 : 1
stoichiometry:c203 : 1
m41*m37*0.1
nodelay
--

0

PMID: 15662540 It has been shown that MEKK3 forms a complex with TRAF6 in response to IL-1 and is crucial for IL-1 induced NF¦ÊB activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c87 : 1
stoichiometry:c88 : 1
stoichiometry:c90 : 1
m44*m45*0.1
nodelay
--

0

PMID; 15662540 TRIF leads to the activation of TBK1/IKK¦Å, resulting in IRF3 activation. PMID: 15662540 Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c207 : 1
stoichiometry:c208 : 1
stoichiometry:c210 : 1
m100*m2282*0.1
nodelay
--

0

PMID: 15662540 Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization and interaction with the coactivaotors cAMP-response element binding protein binding protein and p300.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c211 : 1
stoichiometry:c212 : 1
m101*0.1
nodelay
--

0

PMID: 15662540 The IRF3 complex then translocates to the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c114 : 1
stoichiometry:c18 : 1
m15*m192928*0.1
nodelay
--

0

PMID: 15662540 Upon IL-1 stimulation adapter molecule MyD88 is first recruited to the IL-1 receptor.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c214 : 1
stoichiometry:c213 : 1
m102*0.1
nodelay
--

0

PMID: 15662540 The IRF3 complex then translocates to the nucleus, where it activates promoters containing IRF-binding sites.
p71
p71
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c216 : 1
stoichiometry:c217 : 1
stoichiometry:c218 : 1
m1572*m66*0.1
nodelay
--

0

PMID: 15662540, 10435584 TLR4-mediated NF¦ÊB activation was greatly reduced in MyD88- deficient mice, indicating the requirement of MyD88 for TLR4 signaling.
p72
p72
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c219 : 1
stoichiometry:c220 : 1
stoichiometry:c221 : 1
m6810*m105*0.1
nodelay
--

0

PMID: 15662540, 12447442, 12447441 Interestingly, TIRAP-deficient mice showed defects in activation of the MyD88-dependent signaling pathway through TLR4, but not IL-1R, indicating specificity of the TLR4-mediated MyD88-dependent pathway.
p73
p73
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c222 : 1
stoichiometry:c224 : 1
stoichiometry:c242 : 1
stoichiometry:c248 : 1
stoichiometry:c223 : 1
m41*m106*0.1
nodelay
--

0

PMID: 15662540 LPS-induced, TLR4-mediated signaling employs multiple TIR-domain containing adaptors, MyD88/TIRAP to mediate NF¦ÊB activation.
p74
p74
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c225 : 1
stoichiometry:c226 : 1
stoichiometry:c227 : 1
m18998*m66*0.1
nodelay
--

0

PMID: 15662540, 12855817 Such TLR4-mediated MyD88-independent activities were abolished in TRIF-deficient mice.
p75
p75
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c228 : 1
stoichiometry:c229 : 1
stoichiometry:c230 : 1
m107*m19005*0.1
nodelay
--

0

PMID: 15662540 TLR4- but not TLR3-mediated MyD88-independent IRF3 activation and interferon ¦Â production was abolished in TRAM-deficient mice.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c232 : 1
stoichiometry:c231 : 1
m108*0.1
nodelay
--

0

PMID: 15662540 LPS still stimulates the expression of certain genes, including interferon ¦Â, in MyD88- deficient mice.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c233 : 1
stoichiometry:c215 : 1
stoichiometry:c234 : 1
m45*m104*0.1
nodelay
--

0

PMID: 15662540 Recently the IKK-related kinases IKK¦Å and TRAF family member associated NF¦ÊB activator binding kinase binding kinase 1 have been implicated in the phosphorylation and activation of IRF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c235 : 1
stoichiometry:c237 : 1
stoichiometry:c236 : 1
m45*m108*0.1
nodelay
--

0

PMID: 15662540 LPS-induced, TLR4-mediated signaling employs multiple TIR-domain containing adaptors, MyD88/TIRAP to mediate NF¦ÊB activation, TRIF/TRAM for IRF3 activation.
p79
p79
cso30:i:ME_Transference
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c147 : 1
stoichiometry:c148 : 1
stoichiometry:c151 : 1
stoichiometry:c152 : 1
m76*m78*0.1
nodelay
--

0

PMID: 15662540 In an initial step the ubiquitin-activating enzyme (E1 or Uba) forms a thioester bond with the C-terminus of ubiquitin, which is then transferred to a specific cysteine residue of an ubiquitinconjugating enzyme (E2 or Ubc).
p8
p8
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
stoichiometry:c22 : 1
m184*m17258*m16*0.1
nodelay
--

0

PMID: 15662540, 11960013, 8599092 Upon IL-1 stimulation adapter molecule MyD88 is first recruited to the IL-1 receptor, followed by the recruitment of two serine-threonine kinases, IRAK4 and IRAK.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c238 : 1
stoichiometry:c239 : 1
m109*0.1
nodelay
--

0

PMID: 15662540 The IRF3 complex then translocates to the nucleus, where it activates promoters containing IRF-binding sites.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c240 : 1
stoichiometry:c241 : 1
m84*0.1
nodelay
--

0

PMID: 15662540 The IRF3 complex then translocates to the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c249 : 1
stoichiometry:c251 : 1
stoichiometry:c250 : 1
m5*m26*0.1
nodelay
--

0

PMID: 15662540 Activation of the IKK complex involves the phosphorylation of two serine residues located in the activation loop within the kinase domain of IKK¦Á (S176 and S180) or IKK¦Â (S177 and S181). PMID: 15662540 Once activated, TAK1 can directly phosphorylate IKK¦Â and mitogen-activated protein kinase kinase 6. PMID: 15662540 TRAF6-TAK1-TAB2 are then translocated to the cytosol, where TAK1 is phosphorylated and activated, leading to the activation of IKK and NF¦ÊB.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c24 : 1
stoichiometry:c27 : 1
stoichiometry:c25 : 1
m183*m19*0.1
nodelay
--

0

PMID: 15662540, 8837778 Upon IL-1 stimulation adapter molecule MyD88 is first recruited to the IL-1 receptor, followed by the recruitment of two serine-threonine kinases, IRAK4 and IRAK and the adapter TNF receptor associated factor (TRAF) 6.
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:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
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:InputInhibitor
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
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: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: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: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: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: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: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: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:InputAssociation
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: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:OutputProcess
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:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
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: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:InputAssociation
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
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: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:InputAssociation
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:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--