Original Literature | Model OverView |
---|---|
Publication
Title
New insights into the regulation of TLR signaling.
Affiliation
School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.miggins@tcd.ie
Abstract
Toll-like receptor (TLR) activation is dictated by a number of factors includingthe ligand itself and the localization of the receptor, in terms of expressionprofile and subcellular localization and the signal transduction pathway thathas been activated. Recent work into TLR signal transduction has revealedcomplex regulation at a number of different levels including regulation byphosphorylation, targeted degradation, and sequestration of signaling molecules.Here, we describe recent advances that have been made in our understanding ofhow TLR signaling is regulated at the biochemical level.
PMID
16698941
|
Entity
Process
IFN-beta
--
G010228
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m93217
10
infinite
0
TRANSFAC | G010228 |
--
NF-kappaB
--
MO000000058
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m44
10
infinite
0
TRANSPATH | MO000000058 |
--
TRAF6
--
MO000000212
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m183
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000000212 |
--
IRAK
--
MO000000213
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m184
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000213 |
--
26S proteasome
--
MO000000218
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m189
10
infinite
0
TRANSPATH | MO000000218 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
IKK-i
--
MO000016608
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1599
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016608 |
--
Caspase-8
--
MO000016900
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m1815
10
infinite
0
TRANSPATH | MO000016900 |
--
TRAF1
--
MO000016962
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1871
10
infinite
0
InterPro | IPR002083 |
TRANSPATH | MO000016962 |
--
TRAF3
--
MO000016963
cso30:c:Protein
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--
csml-variable:Double
m1872
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000016963 |
--
beta-arrestin
--
MO000017072
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1964
10
infinite
0
TRANSPATH | MO000017072 |
--
Tollip
--
MO000019406
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cso30:i:CC_CellComponent
--
csml-variable:Double
m3973
10
infinite
0
InterPro | IPR000008 |
TRANSPATH | MO000019406 |
--
protein remnants
--
MO000019479
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m360980
10
infinite
0
TRANSPATH | MO000019479 |
--
TIRAP
--
MO000022528
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cso30:i:CC_CellComponent
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csml-variable:Double
m6810
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000022528 |
--
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
--
R848
--
e100
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
csml-variable:Double
m102
0
infinite
0
--
beta-arrestin:TRAF6
--
e101
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m103
0
infinite
0
--
IL-1beta
--
e102
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m104
0
infinite
0
--
src kinase
--
e103
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m105
0
infinite
0
--
src kinase:beta arrestin
--
e104
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m106
0
infinite
0
--
Mdm2:beta-arrestin
--
e105
cso30:c:Complex
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--
--
csml-variable:Double
m107
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infinite
0
--
IRAK1{p}:(TRAF6)n
--
e106
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m108
0
infinite
0
--
TRAF1:TRIF
--
e107
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m109
0
infinite
0
--
TRAF1(1?163)
--
e108
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m110
0
infinite
0
--
TRAF1(164?416)
--
e109
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m111
0
infinite
0
--
diacyl lipopreteins:TLR6:TLR2
--
e11
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m11
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infinite
0
--
Mal:TRAF1
--
e110
cso30:c:Complex
cso30:i:CC_Cytosol
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--
csml-variable:Double
m112
0
infinite
0
--
MYD88:TRAF1
--
e111
cso30:c:Complex
cso30:i:CC_Cytosol
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--
csml-variable:Double
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infinite
0
--
TRAF3:IRAK
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e112
cso30:c:Complex
cso30:i:CC_Cytosol
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--
csml-variable:Double
m114
0
infinite
0
--
TRAF3:TRIF
--
e113
cso30:c:Complex
cso30:i:CC_Cytosol
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--
csml-variable:Double
m115
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infinite
0
--
TRAF3:TBK1
--
e114
cso30:c:Complex
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--
csml-variable:Double
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infinite
0
--
IKK-i:TRAF3
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e115
cso30:c:Complex
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--
csml-variable:Double
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infinite
0
--
PKR
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e116
cso30:c:Protein
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--
csml-variable:Double
m118
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infinite
0
--
PKR:TRAF3
--
e117
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
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infinite
0
--
csml-variable:Double
m120
0
infinite
0
--
ST2L
--
e119
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m121
0
infinite
0
--
diacyl lipoproteins
--
e12
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m12
0
infinite
0
--
ST2L:TIRAP
--
e120
cso30:c:Complex
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--
--
csml-variable:Double
m122
0
infinite
0
--
ST2L:MYD88
--
e121
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m123
0
infinite
0
--
Fliih
--
e122
cso30:c:Protein
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--
csml-variable:Double
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infinite
0
--
MYD88:Fliih
--
e123
cso30:c:Complex
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--
--
csml-variable:Double
m125
0
infinite
0
--
MYD88s
--
e124
cso30:c:Protein
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csml-variable:Double
m126
0
infinite
0
--
MYD88:MYD88s
--
e125
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
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infinite
0
--
MYD88:MYD88s:IRAK
--
e126
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m128
0
infinite
0
--
TLR2:TLR1
--
e13
cso30:c:Complex
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--
csml-variable:Double
m13
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infinite
0
--
triacyl lipoprotein:TLR1:TLR2
--
e14
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m14
0
infinite
0
--
triacyl lipoprotein
--
e15
cso30:c:Protein
cso30:i:CC_Cytosol
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--
csml-variable:Double
m15
0
infinite
0
--
--
e16
cso30:c:EntityBiologicalCompartment
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--
--
csml-variable:Double
m16
0
infinite
0
--
--
e17
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m17
0
infinite
0
--
--
e18
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
csml-variable:Double
m18
0
infinite
0
--
imidazoquinoline-like molecule
--
e19
cso30:c:SmallMolecule
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
--
imidazoquinoline-like molecule:TLR7
--
e20
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m20
0
infinite
0
--
ssRNA:TLR7
--
e21
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m21
0
infinite
0
--
ssRNA
--
e22
cso30:c:Rna
cso30:i:CC_Cytosol
--
csml-variable:Double
m22
0
infinite
0
--
loxoribine:TLR7
--
e23
cso30:c:Complex
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--
csml-variable:Double
m23
0
infinite
0
--
loxoribine
--
e24
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m24
0
infinite
0
--
imidazoquinoline
--
e25
cso30:c:SmallMolecule
cso30:i:CC_Cytosol
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--
csml-variable:Double
m25
0
infinite
0
--
imidazoquinoline:TLR8
--
e26
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m26
0
infinite
0
--
ssRNA:TLR8
--
e27
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m27
0
infinite
0
--
CpG DNA
--
e28
cso30:c:Dna
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m28
0
infinite
0
--
CpG DNA:TLR9
--
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
--
flagellin:TLR5
--
e30
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m30
0
infinite
0
--
profilin-like protein
--
e31
cso30:c:Protein
cso30:i:CC_Cytosol
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--
csml-variable:Double
m31
0
infinite
0
--
profilin like protein:TLR11
--
e32
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m32
0
infinite
0
--
IFN-alpha
--
e33
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m33
0
infinite
0
--
csml-variable:Double
m34
0
infinite
0
--
dsRNA:RIG-1
--
e35
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m35
0
infinite
0
--
type I IFNs
--
e36
cso30:c:mRNA
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m36
0
infinite
0
--
LPS:TLR4:TRIAD3A
--
e37
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m37
0
infinite
0
--
Triad3A
--
e38
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m38
0
infinite
0
--
CpG DNA:TLR9:TRIAD3A
--
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
--
LPS:TLR4{ub}
--
e40
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m40
0
infinite
0
--
LPS:TLR4{ub}
--
e41
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m41
0
infinite
0
--
TGF-beta
--
e42
cso30:c:Protein
cso30:i:CC_Extracellular
--
csml-variable:Double
m42
0
infinite
0
--
TLR4
--
e43
cso30:c:mRNA
cso30:i:CC_Cytosol
--
csml-variable:Double
m43
0
infinite
0
--
NF-kappaB{active}
--
e44
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m45
10
infinite
0
TRANSPATH | MO000000058 |
--
LPS:TLR4:TIRAP
--
e45
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m46
0
infinite
0
--
LPS:TLR4:TIRAP:MYD88
--
e46
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m47
0
infinite
0
--
TLR1:TLR2:TIRAP
--
e47
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m48
0
infinite
0
--
TLR1:TLR2:TIRAP:MYD88
--
e48
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m49
0
infinite
0
--
TLR2:TLR6:TIRAP
--
e49
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m63
0
infinite
0
--
LPS:TLR4
--
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
--
TLR2:TLR6
--
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
--
TLR2:TLR6:TIRAP:MYD88
--
e63
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m64
0
infinite
0
--
dsRNA:TLR3:TRIF
--
e64
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m65
0
infinite
0
--
LPS:TLR4:TRAM
--
e65
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m66
0
infinite
0
--
LPS:TLR4:TRAM:TRIF
--
e66
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m67
0
infinite
0
--
LPS:TLR4:TIRAP:MYD88:IRAK4
--
e67
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m68
0
infinite
0
--
LPS:TLR4:TIRAP:IRAK4:IRAK
--
e68
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m69
0
infinite
0
--
LPS:TLR4:TIRAP:IRAK4:IRAK:Tollip
--
e69
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m70
0
infinite
0
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
LPS:TLR4:TIRAP:IRAK4:IRAK{p}:Tollip:TRAF6
--
e70
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m71
0
infinite
0
--
LPS:TLR4:TIRAP:IRAK4:IRAK{p}:Tollip:TRAF6
--
e71
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m72
0
infinite
0
--
LPS:TLR4:TIRAP:IRAK4:IRAK{p}:Tollip:TRAF6
--
e72
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m73
0
infinite
0
--
LPS:TLR4:TIRAP:IRAK4:IRAK{p}:Tollip{p}:TRAF6
--
e73
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m74
0
infinite
0
--
IRAK{p}:TRAF6
--
e74
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m75
0
infinite
0
--
IRAK1{p}:TRAF6{ub}n
--
e75
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m76
0
infinite
0
--
TAK1:TAB1:TAB2:TAB3
--
e76
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m77
0
infinite
0
--
TAK1:TAB1:TAB2:TAB3{active}
--
e77
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m78
0
infinite
0
--
IkappaB:NF-kappaB
--
e79
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m80
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
IkappaB:NF-kappaB
--
e80
cso30:c:Complex
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m81
0
infinite
0
--
NF-kappaB{active}
--
e81
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m82
10
infinite
0
TRANSPATH | MO000000058 |
--
LPS:TLR4:TRAM:TRIF:TBK1:IKK-i
--
e82
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m83
0
infinite
0
--
{IRF-3(p)}2
--
e83
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m84
0
infinite
0
--
{IRF-3(p)}2
--
e84
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m85
0
infinite
0
--
csml-variable:Double
m86
0
infinite
0
--
csml-variable:Double
m87
0
infinite
0
--
LPS:TLR4:TRAM:TRIF:RIP1:TRAF6
--
e87
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m89
0
infinite
0
--
Mal:TRAF6
--
e88
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m90
0
infinite
0
--
dsRNA:TLR3:TRIF:TRAF6
--
e89
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m91
0
infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0
infinite
0
--
TIRAP{p}
--
e90
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m92
0
infinite
0
--
TRAM{p}
--
e91
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m93
0
infinite
0
--
MYD88{p}
--
e92
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m94
0
infinite
0
--
TRIF{p}
--
e93
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m95
0
infinite
0
--
socs-1:Mal{p}
--
e94
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m96
0
infinite
0
--
Socs-1:TIRAP{p}{ub}
--
e95
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m97
0
infinite
0
--
IRAK2c
--
e96
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m98
0
infinite
0
--
IRAK1c
--
e97
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m99
0
infinite
0
--
IRAK2
--
e98
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m100
0
infinite
0
--
IRAK1c:IRAK2:MYD88:TRAF6:Tollip
--
e99
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m101
0
infinite
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m3961*m155666*0.1
nodelay
--
0
PMID: 16698941 lipopolysaccharides (LPS) from Gram-negative bacteria are recognized by TLR4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c28 : 1
stoichiometry:c29 : 1
stoichiometry:c30 : 1
m19828*m28*0.1
nodelay
--
0
PMID: 16698941 TLR9 recognizes bacterial and viral CpG DNA motifs.
p100
p100
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c289 : 1
stoichiometry:c290 : 1
stoichiometry:c291 : 1
m124*m1572*0.1
nodelay
--
0
PMID: 16698941, 16424162 Another molecule, Fliih, has been shown to modulate TLR signaling by interacting with MyD88 and acting as a negative regulator.
p101
p101
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c293 : 1
stoichiometry:c294 : 1
stoichiometry:c295 : 1
m126*m1572*0.1
nodelay
--
0
PMID: 16698941 overexpression of MyD88s favors formation of MyD88s-MyD88 heterodimers over MyD88 homodimers.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c296 : 1
stoichiometry:c297 : 1
stoichiometry:c298 : 1
m127*m184*0.1
nodelay
--
0
PMID: 16698941 In the presence of these heterodimers, IRAK1 is recruited via the death domain (DD), but it is no longer phosphorylated.
p11
p11
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c31 : 1
stoichiometry:c32 : 1
stoichiometry:c33 : 1
m6485*m3966*0.1
nodelay
--
0
PMID: 16698941, 15001781 TLR5 recognizes flagellin, and human TLR11 recognizes uropathogenic Escherichia coli.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c34 : 1
stoichiometry:c36 : 1
stoichiometry:c35 : 1
m19944*m31*0.1
nodelay
--
0
PMID: 16698941, 16111920, 15860593 The first defined ligand for TLR11 has been described in mice as a profilin-like protein, a class of actin-binding proteins present in apicomplexan protozoa.
p13
p13
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c42 : 1
stoichiometry:c37 : 1
m19314*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c43 : 1
stoichiometry:c39 : 1
m27*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c41 : 1
stoichiometry:c38 : 1
m5*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c44 : 1
stoichiometry:c40 : 1
m21*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c46 : 1
stoichiometry:c45 : 1
m29*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
p18
p18
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c53 : 1
stoichiometry:c47 : 1
m19314*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c54 : 1
stoichiometry:c48 : 1
m29*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c5 : 1
stoichiometry:c6 : 1
m12*m6*0.1
nodelay
--
0
PMID: 16698941 TLR2, in combination with TLR1 or TLR6, recognizes triacyl lipopeptides and diacyl lipopeptides, respectively
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c50 : 1
m27*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c52 : 1
stoichiometry:c51 : 1
m5*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c55 : 1
stoichiometry:c49 : 1
m21*0.1
nodelay
--
0
PMID: 16698941 In addition, antiviral type I interferons (IFNs; IFN-? and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c57 : 1
stoichiometry:c58 : 1
stoichiometry:c59 : 1
m119368*m34*0.1
nodelay
--
0
PMID: 16698941, 16474426, 15208624 viral-derived dsRNA may also be recognized by the cytosolic RNA helicase retinoic acid-inducible gene-I, inducing type I IFN in a TLR-independent manner.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c61 : 1
stoichiometry:c60 : 1
m35*0.1
nodelay
--
0
PMID: 16698941, 16474426, 15208624 viral-derived dsRNA may also be recognized by the cytosolic RNA helicase retinoic acid-inducible gene-I, inducing type I IFN in a TLR-independent manner.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c62 : 1
stoichiometry:c64 : 1
stoichiometry:c63 : 1
m5*m38*0.1
nodelay
--
0
PMID: 16698941, 15107846 TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c65 : 1
stoichiometry:c66 : 1
stoichiometry:c67 : 1
m29*m38*0.1
nodelay
--
0
PMID: 16698941, 15107846 TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c68 : 1
stoichiometry:c69 : 1
stoichiometry:c70 : 1
m37*0.1
nodelay
--
0
PMID: 16698941, 15107846 TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
p28
p28
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c71 : 1
stoichiometry:c72 : 1
m40*0.1
nodelay
--
0
PMID: 16698941, 15107846 TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c73 : 1
stoichiometry:c74 : 1
stoichiometry:c75 : 1
m39*0.1
nodelay
--
0
PMID: 16698941, 15107846 TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
stoichiometry:c9 : 1
m15*m13*0.1
nodelay
--
0
PMID: 16698941 TLR2, in combination with TLR1 or TLR6, recognizes triacyl lipopeptides and diacyl lipopeptides, respectively
p30
p30
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c76 : 1
stoichiometry:c77 : 1
m41*0.1
nodelay
--
0
PMID: 16698941, 15107846 TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c79 : 1
stoichiometry:c78 : 1
1.0*0.1
nodelay
--
0
PMID: 16698941, 15004187 Transforming growth factor-? (TGF-?) suppresses the expression of TLR4
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c80 : 1
stoichiometry:c82 : 1
stoichiometry:c81 : 1
m43*0.1
nodelay
--
0
PMID: 16698941, 15004187 Transforming growth factor-? (TGF-?) suppresses the expression of TLR4
p33
p33
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c83 : 1
stoichiometry:c85 : 1
stoichiometry:c89 : 1
stoichiometry:c84 : 1
m44*m5*0.1
nodelay
--
0
PMID: 16698941, 15107846 overexpression of TRIAD3A reduced TLR4- and TLR9-mediated nuclear factor (NF)-{kappa}B activation in response to L and CpG but not pI:C
p34
p34
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c86 : 1
stoichiometry:c88 : 1
stoichiometry:c90 : 1
stoichiometry:c87 : 1
m44*m29*0.1
nodelay
--
0
PMID: 16698941, 15107846 overexpression of TRIAD3A reduced TLR4- and TLR9-mediated nuclear factor (NF)-{kappa}B activation in response to L and CpG but not pI:C
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c91 : 1
stoichiometry:c92 : 1
stoichiometry:c93 : 1
m5*m6810*0.1
nodelay
--
0
PMID: 16698941, 16410796 Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c94 : 1
stoichiometry:c95 : 1
stoichiometry:c96 : 1
m46*m1572*0.1
nodelay
--
0
PMID: 16698941, 16410796 Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c97 : 1
stoichiometry:c98 : 1
stoichiometry:c99 : 1
m14*m6810*0.1
nodelay
--
0
PMID: 16698941, 16410796 Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c100 : 1
stoichiometry:c101 : 1
stoichiometry:c102 : 1
m48*m1572*0.1
nodelay
--
0
PMID: 16698941, 16410796 Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c103 : 1
stoichiometry:c104 : 1
stoichiometry:c105 : 1
m11*m6810*0.1
nodelay
--
0
PMID: 16698941, 16410796 Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
p4
p4
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c10 : 1
stoichiometry:c11 : 1
stoichiometry:c12 : 1
m119368*m3965*0.1
nodelay
--
0
PMID: 16698941 TLR3 recognizes double-stranded (ds)RNA, which is produced from many viruses during replication.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c106 : 1
stoichiometry:c107 : 1
stoichiometry:c108 : 1
m63*m1572*0.1
nodelay
--
0
PMID: 16698941, 16410796 Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
p41
p41
cso30:i:ME_Binding
cso30:i:CC_EndosomeLumen
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c109 : 1
stoichiometry:c110 : 1
stoichiometry:c111 : 1
m19314*m18998*0.1
nodelay
--
0
PMID: 16698941, 12471095 Trif interacts directly with TLR3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c112 : 1
stoichiometry:c113 : 1
stoichiometry:c114 : 1
m5*m19005*0.1
nodelay
--
0
PMID: 16698941, 14556004 Tram is thought to act as a bridging adaptor between Trif and TLR4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c115 : 1
stoichiometry:c116 : 1
stoichiometry:c117 : 1
m66*m18998*0.1
nodelay
--
0
PMID: 16698941, 14556004 Tram is thought to act as a bridging adaptor between Trif and TLR4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c118 : 1
stoichiometry:c119 : 1
stoichiometry:c120 : 1
m47*m17258*0.1
nodelay
--
0
PMID: 16698941 MyD88 recruits IL-1R-associated kinase 4 (IRAK4) and TNF receptor-associated factor 6 (TRAF6) upon ligand stimulation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c121 : 1
stoichiometry:c122 : 1
stoichiometry:c123 : 1
m68*m184*0.1
nodelay
--
0
PMID: 16698941 Upon activation of TLR signaling, IRAK-1 and IRAK-4 are recruited to the receptor complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c124 : 1
stoichiometry:c125 : 1
stoichiometry:c126 : 1
m69*m3973*0.1
nodelay
--
0
PMID: 16698941 At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6.
p47
p47
cso30:i:ME_Phosphorylation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c130 : 1
stoichiometry:c292 : 1
stoichiometry:c131 : 1
m71*0.1
nodelay
--
0
PMID: 16698941 At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6. PMID: 16698941, 12885415 MyD88s inhibits the ability of IRAK4 to phosphorylate IRAK1, as unlike full-length MyD88, it is unable to interact with IRAK4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c127 : 1
stoichiometry:c128 : 1
stoichiometry:c129 : 1
m70*m183*0.1
nodelay
--
0
PMID: 16698941 At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6.
p49
p49
cso30:i:ME_Autophosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c134 : 1
stoichiometry:c133 : 1
m72*0.1
nodelay
--
0
PMID: 16698941 Tollip interacts with IRAK-1, and IRAK-1 autophosphorylation is suppressed in the presence of Tollip.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c15 : 1
stoichiometry:c14 : 1
m19940*m19*0.1
nodelay
--
0
PMID: 16698941 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, and single-stranded (ss)RNA derived from viruses such as human immunodeficiency virus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c135 : 1
stoichiometry:c136 : 1
m73*0.1
nodelay
--
0
PMID: 16698941, 11751856 Following TLR stimulation, IRAK-1 phosphorylates Tollip, and this may lead to the release of Tollip from the Tollip:IRAK-1 complex, thus overcoming negative regulation.
p51
p51
cso30:i:ME_Dissociation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c137 : 1
stoichiometry:c138 : 1
stoichiometry:c139 : 1
stoichiometry:c140 : 1
m74*0.1
nodelay
--
0
PMID: 16698941 At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6. PMID: 16698941, 11751856 Following TLR stimulation, IRAK-1 phosphorylates Tollip, and this may lead to the release of Tollip from the Tollip:IRAK-1 complex, thus overcoming negative regulation
p52
p52
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c249 : 1
stoichiometry:c251 : 1
stoichiometry:c142 : 1
m108*0.1
nodelay
--
0
PMID: 16698941 IRAK then becomes phosphorylated and dissociates from MyD88, which results in TRAF6 being activated, followed by TAK1/TAB1/TAB2/TAB3 complex formation and activation via K63-linked ubiquitination.
p53
p53
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c143 : 1
stoichiometry:c144 : 1
stoichiometry:c146 : 1
stoichiometry:c147 : 1
stoichiometry:c145 : 1
m1573*m1583*m6433*m19389*0.1
nodelay
--
0
PMID: 16698941 IRAK then becomes phosphorylated and dissociates from MyD88, which results in TRAF6 being activated, followed by TAK1/TAB1/TAB2/TAB3 complex formation and activation via K63-linked ubiquitination.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c148 : 1
stoichiometry:c150 : 1
stoichiometry:c149 : 1
m77*m76*0.1
nodelay
--
0
PMID: 16698941 IRAK then becomes phosphorylated and dissociates from MyD88, which results in TRAF6 being activated, followed by TAK1/TAB1/TAB2/TAB3 complex formation and activation via K63-linked ubiquitination.
p55
p55
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c151 : 1
stoichiometry:c153 : 1
stoichiometry:c152 : 1
m207*m78*0.1
nodelay
--
0
PMID: 16698941 Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c154 : 1
stoichiometry:c156 : 1
stoichiometry:c155 : 1
m81*m79*0.1
nodelay
--
0
PMID: 16698941 Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c160 : 1
stoichiometry:c161 : 1
m45*0.1
nodelay
--
0
PMID: 16698941 Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
p58
p58
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c157 : 1
stoichiometry:c158 : 1
stoichiometry:c159 : 1
m80*0.1
nodelay
--
0
PMID: 16698941 Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
p59
p59
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c162 : 1
stoichiometry:c163 : 1
stoichiometry:c165 : 1
stoichiometry:c164 : 1
m67*m3902*m1599*0.1
nodelay
--
0
PMID: 16698941 TLR4 also recruits TRAM and Trif, which interacts with Traf family member-associated NF-{kappa}B activator-binding protein (TBK1), and TBK1, together with inducible IKK (IKKi), mediates phosphorylation of IFN regulatory factor 3 (IRF3).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c18 : 1
stoichiometry:c17 : 1
m19940*m22*0.1
nodelay
--
0
PMID: 16698941 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, and single-stranded (ss)RNA derived from viruses such as human immunodeficiency virus.
p60
p60
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c166 : 1
stoichiometry:c168 : 1
stoichiometry:c167 : 1
m977*m83*0.1
nodelay
--
0
PMID: 16698941 TLR4 also recruits TRAM and Trif, which interacts with Traf family member-associated NF-{kappa}B activator-binding protein (TBK1), and TBK1, together with inducible IKK (IKKi), mediates phosphorylation of IFN regulatory factor 3 (IRF3).
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c169 : 1
stoichiometry:c170 : 1
m19324*0.1
nodelay
--
0
PMID: 16698941 Phosphorylated IRF3 is dimerized and translocated into the nucleus to bind DNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c171 : 1
stoichiometry:c172 : 1
m84*0.1
nodelay
--
0
PMID: 16698941 Phosphorylated IRF3 is dimerized and translocated into the nucleus to bind DNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c173 : 1
stoichiometry:c174 : 1
stoichiometry:c175 : 1
m85*m87*0.1
nodelay
--
0
PMID: 16698941 Phosphorylated IRF3 is dimerized and translocated into the nucleus to bind DNA.
p64
p64
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c176 : 1
stoichiometry:c177 : 1
stoichiometry:c178 : 1
stoichiometry:c179 : 1
m88*m183*m67*0.1
nodelay
--
0
PMID: 16698941 Trif also interacts with TRAF6 and receptor-interacting protein kinase 1 (RIP1), which mediate NF-{kappa}B activation.
p65
p65
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c180 : 1
stoichiometry:c182 : 1
stoichiometry:c181 : 1
m44*m89*0.1
nodelay
--
0
PMID: 16698941 Trif also interacts with TRAF6 and receptor-interacting protein kinase 1 (RIP1), which mediate NF-{kappa}B activation.
p66
p66
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c183 : 1
stoichiometry:c184 : 1
stoichiometry:c185 : 1
m6810*m183*0.1
nodelay
--
0
PMID: 16698941, 15247281 Mal interacts directly with TRAF6 to mediate NF-{kappa}B activation through TLR2 and TLR4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c186 : 1
stoichiometry:c187 : 1
stoichiometry:c188 : 1
m65*m183*0.1
nodelay
--
0
PMID: 16698941, 14530355 Trif was found to mediate TLR3-induced activation of NF-{kappa}B via association with TRAF6.
p68
p68
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c189 : 1
stoichiometry:c191 : 1
stoichiometry:c259 : 1
stoichiometry:c190 : 1
m44*m91*0.1
nodelay
--
0
PMID: 16698941, 14530355 Trif was found to mediate TLR3-induced activation of NF-{kappa}B via association with TRAF6. PMID: 16698941 it was shown that TRAF1 is cleaved by caspase-8 generating two fragments, TRAF1(1?163) and TRAF1(164?416), and it is TRAF1(1?163) that is responsible for its inhibitory effects on Trif-mediated signaling. PMID: 16698941, 16323247 TRAF1 inhibited Trif and TLR3-mediated activation of NF-{kappa}B, IFN-stimulated response element, and IFN-? promoter activity
p69
p69
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c192 : 1
stoichiometry:c194 : 1
stoichiometry:c201 : 1
stoichiometry:c193 : 1
m6810*m367*m5*0.1
nodelay
--
0
PMID: 16698941, 16415872, 16439361 We identified the Tec kinase, Bruton¡Çs tyrosine kinase (Btk), as the kinase responsible for phosphorylating Mal. PMID: 16698941 we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c21 : 1
stoichiometry:c20 : 1
m19940*m24*0.1
nodelay
--
0
PMID: 16698941 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, and single-stranded (ss)RNA derived from viruses such as human immunodeficiency virus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c195 : 1
stoichiometry:c196 : 1
m19005*0.1
nodelay
--
0
PMID: 16698941, 12616480, 12721283, 14530355 It has also been reported that MyD88, Trif, and TRAM undergo phosphorylation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c197 : 1
stoichiometry:c198 : 1
m1572*0.1
nodelay
--
0
PMID: 16698941, 12616480, 12721283, 14530355 It has also been reported that MyD88, Trif, and TRAM undergo phosphorylation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c199 : 1
stoichiometry:c200 : 1
m18998*0.1
nodelay
--
0
PMID: 16698941, 12616480, 12721283, 14530355 It has also been reported that MyD88, Trif, and TRAM undergo phosphorylation.
p73
p73
cso30:i:ME_Phosphorylation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c202 : 1
stoichiometry:c204 : 1
stoichiometry:c205 : 1
stoichiometry:c203 : 1
m6810*m14*m367*0.1
nodelay
--
0
PMID: 16698941, 16415872, 16439361 We identified the Tec kinase, Bruton¡Çs tyrosine kinase (Btk), as the kinase responsible for phosphorylating Mal. PMID: 16698941 we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c206 : 1
stoichiometry:c208 : 1
stoichiometry:c207 : 1
m92*m1906*0.1
nodelay
--
0
PMID: 16698941 we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c209 : 1
stoichiometry:c210 : 1
m96*0.1
nodelay
--
0
PMID: 16698941 we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
p76
p76
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c211 : 1
stoichiometry:c214 : 1
stoichiometry:c212 : 1
stoichiometry:c213 : 1
m97*m189*0.1
nodelay
--
0
PMID: 16698941 we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
p77
p77
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c215 : 1
stoichiometry:c217 : 1
stoichiometry:c216 : 1
m1572*m42*0.1
nodelay
--
0
PMID: 16698941, 15623538 TGF-? induces MyD88 degradation by the proteasome and so down-regulates TLR signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c219 : 1
stoichiometry:c218 : 1
m5*0.1
nodelay
--
0
PMID: 16698941, 15082713 treatment of the mouse macrophage cell line RAW264.7 with LPS for 1 and 3 h resulted in an increase in IRAK2c mRNA levels, indicating a possible negative-feedback loop.
p79
p79
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c220 : 1
stoichiometry:c221 : 1
stoichiometry:c222 : 1
stoichiometry:c223 : 1
stoichiometry:c224 : 1
stoichiometry:c225 : 1
m99*m183*m1572*m3973*m100*0.1
nodelay
--
0
PMID: 16698941 Unlike IRAK-1, the spliced variant IRAK-1c lacks kinase activity and cannot be phosphorylated by IRAK-4 but still retains its ability to interact with IRAK-2, MyD88, Tollip, and TRAF6.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c22 : 1
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m19823*m25*0.1
nodelay
--
0
PMID: 16698941 TLR8 mediates the recognition of imidazoquinolines and ssRNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c230 : 1
stoichiometry:c226 : 1
1.0*0.1
nodelay
--
0
PMID: 16698941, 12096038 A similar mechanism of decreased IRAK-1 protein was evident following exposure of peritoneal macrophages to the TLR7/8 ligand, R848.
p81
p81
cso30:i:ME_Translation
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c227 : 1
stoichiometry:c229 : 1
stoichiometry:c228 : 1
m94019*0.1
nodelay
--
0
PMID: 16698941, 12096038 A similar mechanism of decreased IRAK-1 protein was evident following exposure of peritoneal macrophages to the TLR7/8 ligand, R848.
p82
p82
cso30:i:ME_Deubiquitination
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c231 : 1
stoichiometry:c233 : 1
stoichiometry:c232 : 1
m76*m1585*0.1
nodelay
--
0
PMID: 16698941, 15334086 It has been shown that the de-ubiquitination enzyme A20 terminates TLR signaling by removing ubiquitin moieties from TRAF6.
p83
p83
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c234 : 1
stoichiometry:c235 : 1
stoichiometry:c237 : 1
stoichiometry:c236 : 1
m1964*m183*m5*0.1
nodelay
--
0
PMID: 16698941 it has been shown that ?-arrestins interact with TRAF6 in response to LPS and IL-1? stimulation
p84
p84
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c238 : 1
stoichiometry:c240 : 1
stoichiometry:c241 : 1
stoichiometry:c239 : 1
m1964*m183*m104*0.1
nodelay
--
0
PMID: 16698941 it has been shown that ?-arrestins interact with TRAF6 in response to LPS and IL-1? stimulation
p85
p85
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c242 : 1
stoichiometry:c243 : 1
stoichiometry:c244 : 1
m1964*m105*0.1
nodelay
--
0
PMID: 16698941, 10209148, 12488444, 11588219 ?-Arrestins, in addition to their established roles in receptor desensitization and endocytosis, bind to signaling molecules such as the Src family kinases and the E3 ligase Mdm2.
p86
p86
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c245 : 1
stoichiometry:c246 : 1
stoichiometry:c247 : 1
m3461*m1964*0.1
nodelay
--
0
PMID: 16698941, 10209148, 12488444, 11588219 ?-Arrestins, in addition to their established roles in receptor desensitization and endocytosis, bind to signaling molecules such as the Src family kinases and the E3 ligase Mdm2.
p87
p87
cso30:i:ME_Oligomerization
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c141 : 1
stoichiometry:c250 : 1
stoichiometry:c248 : 1
m75*0.1
nodelay
--
0
PMID: 16698941, 16378096 In terms of TLR signaling, it has been shown that ?-arrestins negatively regulate TLR signaling by preventing oligomerization of TRAF6, thereby inhibiting its autoubiquitination and subsequent signaling pathways such as NF-{kappa}B and AP-1 activation.
p88
p88
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c252 : 1
stoichiometry:c253 : 1
stoichiometry:c254 : 1
m1871*m18998*0.1
nodelay
--
0
PMID: 16698941 a recent study has shown that the C-domain of TRAF1 interacts with the TIR domain of Trif
p89
p89
cso30:i:ME_ProteinCleavage
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c255 : 1
stoichiometry:c256 : 1
stoichiometry:c257 : 1
stoichiometry:c258 : 1
m1871*m1815*0.1
nodelay
--
0
PMID: 16698941 it was shown that TRAF1 is cleaved by caspase-8 generating two fragments, TRAF1(1?163) and TRAF1(164?416), and it is TRAF1(1?163) that is responsible for its inhibitory effects on Trif-mediated signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
stoichiometry:c27 : 1
m19823*m22*0.1
nodelay
--
0
PMID: 16698941 TLR8 mediates the recognition of imidazoquinolines and ssRNA.
p90
p90
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c260 : 1
stoichiometry:c261 : 1
stoichiometry:c262 : 1
m1871*m6810*0.1
nodelay
--
0
PMID: 16698941, 16323247 Mal and MyD88 interact with TRAF1, suggesting that TRAF1 may negatively regulate Mal and MyD88 signaling, although this remains to be fully explored.
p91
p91
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c263 : 1
stoichiometry:c264 : 1
stoichiometry:c265 : 1
m1871*m1572*0.1
nodelay
--
0
PMID: 16698941, 16323247 Mal and MyD88 interact with TRAF1, suggesting that TRAF1 may negatively regulate Mal and MyD88 signaling, although this remains to be fully explored.
p92
p92
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c266 : 1
stoichiometry:c267 : 1
stoichiometry:c268 : 1
m1872*m184*0.1
nodelay
--
0
PMID: 16698941, 16306937, 16306936 TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
p93
p93
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c270 : 1
stoichiometry:c269 : 1
stoichiometry:c271 : 1
m18998*m1872*0.1
nodelay
--
0
PMID: 16698941, 16306937, 16306936 TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
p94
p94
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c272 : 1
stoichiometry:c273 : 1
stoichiometry:c274 : 1
m1872*m3902*0.1
nodelay
--
0
PMID: 16698941, 16306937, 16306936 TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
p95
p95
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c275 : 1
stoichiometry:c276 : 1
stoichiometry:c277 : 1
m1872*m1599*0.1
nodelay
--
0
PMID: 16698941, 16306937, 16306936 TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c278 : 1
stoichiometry:c279 : 1
stoichiometry:c280 : 1
m118*m1872*0.1
nodelay
--
0
PMID: 16698941, 16306937, 16306936 TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c281 : 1
stoichiometry:c282 : 1
m86*0.1
nodelay
--
0
PMID: 16698941, 12692549, 14679297 Activated Trif recruits TBK1 and together with IKKi, mediate IRF3 phosphorylation, dimerization, and nuclear translocation mediating type 1 IFN induction.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c283 : 1
stoichiometry:c284 : 1
stoichiometry:c285 : 1
m121*m6810*0.1
nodelay
--
0
PMID: 16698941 we have shown that ST2L, a type I transmembrane protein with three extracellular immunoglobulin-like domains and an intracellular TIR domain, interacts with and sequesters MyD88 and Mal, but not Trif or IRAK
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c286 : 1
stoichiometry:c287 : 1
stoichiometry:c288 : 1
m121*m1572*0.1
nodelay
--
0
PMID: 16698941 we have shown that ST2L, a type I transmembrane protein with three extracellular immunoglobulin-like domains and an intracellular TIR domain, interacts with and sequesters MyD88 and Mal, but not Trif or IRAK
cso30:c:InputProcess
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