Original Literature | Model OverView |
---|---|
Publication
Title
TLR signaling.
Affiliation
Department of Host Defense, Research Institute for Microbial Diseases, OsakaUniversity, Yamada-oka, Suita, Osaka, Japan.
Abstract
The TLR family senses the molecular signatures of microbial pathogens, and playsa fundamental role in innate immune responses. TLRs signal via a common pathwaythat leads to the expression of diverse inflammatory genes. In addition, eachTLR elicits specific cellular responses to pathogens owing to differential usageof intracellular adapter proteins. Recent studies have revealed the importanceof the subcellular localization of TLRs in pathogen recognition and signaling.TLR signaling pathways is negatively regulated by a number of cellular proteinsto attenuate inflammation. Here, we describe recent advances in ourunderstanding of the regulation of TLR-mediated signaling.
PMID
17275323
|
Entity
Process
NF-kappaB
--
MO000000058
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m69
10
infinite
0
TRANSPATH | MO000000058 |
--
IKK-alpha
--
MO000000210
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m181
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000000210 |
--
TRAF6
--
MO000000212
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m183
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000000212 |
--
TNF-alpha
--
MO000000289
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m230
10
infinite
0
InterPro | IPR003636 |
TRANSPATH | MO000000289 |
--
PIP2
--
MO000000331
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m290229
10
infinite
0
TRANSPATH | MO000000331 |
--
Btk
--
MO000001935
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m367
10
infinite
0
InterPro | IPR001452 |
TRANSPATH | MO000001935 |
--
IRF-3
--
MO000007694
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m977
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007694 |
--
IRF-7
--
MO000007702
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m980
10
infinite
0
TRANSPATH | MO000007702 |
--
MyD88
--
MO000016573
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1572
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000016573 |
--
IKK-gamma
--
MO000016599
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m1593
10
infinite
0
InterPro | IPR007087 |
TRANSPATH | MO000016599 |
--
IKK-i
--
MO000016608
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1599
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016608 |
--
PKCepsilon
--
MO000016645
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m1629
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016645 |
--
IKK-alpha:IKK-beta:IKK-gamma
--
MO000016661
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m1637
10
infinite
0
TRANSPATH | MO000016661 |
--
IFNgamma
--
MO000016665
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1639
10
infinite
0
InterPro | IPR002069 |
TRANSPATH | MO000016665 |
--
Caspase-8
--
MO000016900
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m1815
10
infinite
0
TRANSPATH | MO000016900 |
--
TRAF3
--
MO000016963
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1872
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000016963 |
--
TRAF4
--
MO000016964
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1873
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000016964 |
--
integrins
--
MO000017291
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m2142
10
infinite
0
TRANSPATH | MO000017291 |
--
TBK1
--
MO000019331
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3902
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000019331 |
--
TLR2
--
MO000019397
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3964
10
infinite
0
InterPro | IPR000157 |
TRANSPATH | MO000019397 |
--
TIRAP
--
MO000022528
cso30:c:Protein
cso30:i:CC_CellComponent
--
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:Complex
cso30:i:CC_CellComponent
--
csml-variable:Double
m19314
10
infinite
0
TRANSPATH | MO000041446 |
--
IRF-3{p}
--
MO000041456
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19324
10
infinite
0
TRANSPATH | MO000041456 |
--
TLR9
--
MO000042012
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19828
10
infinite
0
TRANSPATH | MO000042012 |
--
--
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
--
MyD88: TRAF6: IRF-5 {p}
--
e100
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m107
0
infinite
0
--
ligand: TLR: MyD88: IRAK-4: IRAK-1: TRAF6: IRF-7 {p}: OPN-i: IKK-alpha: TRAF3
--
e101
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m108
0
infinite
0
--
IRF-7 {nucleus}
--
e103
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m110
10
infinite
0
TRANSPATH | MO000007702 |
--
csml-variable:Double
m111
10
infinite
0
Ensembl | ENSG00000147877 |
HGNC | IFNA7 |
OMIM | 147567 |
Proteome | HumanPSD/IFNA7 |
RefSeq | NM_021057 |
TRANSFAC | G000306 |
Unigene | Hs.282274 |
--
IRF-7 {p}
--
e105
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m112
0
infinite
0
--
ARF6 GTPase
--
e106
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m113
0
infinite
0
--
--
e107
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m114
0
infinite
0
--
--
e108
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
csml-variable:Double
m115
0
infinite
0
--
--
e109
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
csml-variable:Double
m116
0
infinite
0
--
csml-variable:Double
m117
0
infinite
0
--
ARF6 GTPase {activated}
--
e112
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m119
0
infinite
0
--
CD11b
--
e113
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m120
0
infinite
0
--
LPS: CD14: TLR4: MD-2: TIRAP: MyD88
--
e114
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m121
0
infinite
0
--
PI5K {activated}
--
e115
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m122
0
infinite
0
--
PI5K
--
e116
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m123
0
infinite
0
--
RP105:MD-1
--
e117
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
csml-variable:Double
m124
0
infinite
0
--
RP105: MD-1: MD-2: TLR4
--
e118
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m125
0
infinite
0
--
MD-2: TLR4
--
e119
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
csml-variable:Double
m126
0
infinite
0
--
csml-variable:Double
m12
0
infinite
0
--
csml-variable:Double
m127
0
infinite
0
--
csml-variable:Double
m128
0
infinite
0
--
TLR9: Triad3A
--
e122
cso30:c:Complex
cso30:i:CC_EndosomeLumen
--
csml-variable:Double
m129
0
infinite
0
--
csml-variable:Double
m130
0
infinite
0
--
TLR9 {degraded}
--
e124
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m131
0
infinite
0
--
TLR4 {degraded}
--
e125
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m132
0
infinite
0
--
MyD88s
--
e126
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m133
0
infinite
0
--
csml-variable:Double
m134
0
infinite
0
--
TIRAP {p}
--
e128
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m135
0
infinite
0
--
csml-variable:Double
m136
0
infinite
0
--
TLR1:TLR2: CD36
--
e13
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m13
0
infinite
0
--
TIRAP {ub}
--
e130
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m137
0
infinite
0
--
TIRAp {degraded}
--
e131
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m138
0
infinite
0
--
csml-variable:Double
m139
0
infinite
0
--
TRAF1 {degraded}
--
e133
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
csml-variable:Double
m140
0
infinite
0
--
TRAF4: TRAF6: TRIF
--
e134
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m141
0
infinite
0
--
ligand: TLR: MyD88: IRAK-4: IRAK-1: TRAF6: OPN-i: IKK-alpha: TRAF3
--
e135
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m142
0
infinite
0
--
T-bet {activated}
--
e136
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m143
10
infinite
0
InterPro | IPR008967 |
TRANSPATH | MO000090987 |
--
IRF-5 {nucleus}
--
e137
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m144
10
infinite
0
InterPro | IPR008984 |
TRANSPATH | MO000007700 |
--
MyD88: TRAF6
--
e138
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m145
0
infinite
0
--
Pin1: IRF-3 {p339}
--
e139
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m146
0
infinite
0
--
TLR6: TLR2
--
e14
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m14
0
infinite
0
--
IRF-3 {p339}
--
e140
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m147
0
infinite
0
--
csml-variable:Double
m148
0
infinite
0
--
IRF-3 {degraded}
--
e142
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m149
0
infinite
0
--
MyD88: IRF-4
--
e143
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m150
0
infinite
0
--
TLR6: TLR2: CD36
--
e15
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m15
0
infinite
0
--
triacyl-lipopeptide: TLR1:TLR2: CD36
--
e16
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m16
0
infinite
0
--
triacyl-lipopeptide
--
e17
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m17
0
infinite
0
--
diacyl-lipopeptide
--
e18
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m18
0
infinite
0
--
diacyl-lipopeptide: TLR6: TLR2: CD36
--
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
--
TLR1: TLR10
--
e20
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m20
0
infinite
0
--
TLR2: TLR10
--
e21
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m21
0
infinite
0
--
flagellin: TLR5
--
e22
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m22
0
infinite
0
--
profilin-like molecule
--
e23
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m23
0
infinite
0
--
profilin-like molecule: TLR11
--
e24
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m24
0
infinite
0
--
loxoribidine
--
e25
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m25
0
infinite
0
--
loxoribidine: TLR7
--
e26
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m26
0
infinite
0
--
csml-variable:Double
m27
0
infinite
0
--
ssRNA: TLR7
--
e28
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m28
0
infinite
0
--
imidazoquinolines
--
e29
cso30:c:SmallMolecule
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m29
0
infinite
0
--
--
e3
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
--
csml-variable:Double
m3
0
infinite
0
--
ssRNA: TLR8
--
e30
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m30
0
infinite
0
--
imidazoquinolines: TLR8
--
e31
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m31
0
infinite
0
--
csml-variable:Double
m32
0
infinite
0
--
CpG DNA: TLR9
--
e33
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m33
0
infinite
0
--
csml-variable:Double
m34
0
infinite
0
--
hemozoin: TLR9
--
e35
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m35
0
infinite
0
--
TLR
--
e37
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m37
0
infinite
0
--
ligand
--
e38
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m38
0
infinite
0
--
ligand: TLR
--
e39
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m39
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
ligand: TLR: MyD88
--
e40
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m40
0
infinite
0
--
ligand: TLR: MyD88: IRAK-4
--
e41
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m41
0
infinite
0
--
ligand: TLR: MyD88: IRAK1
--
e42
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m42
0
infinite
0
--
ligand: TLR: MyD88: IRAK-M
--
e43
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m43
0
infinite
0
--
ligand: TLR: MyD88: IRAK-2
--
e44
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m44
0
infinite
0
--
csml-variable:Double
m45
0
infinite
0
--
ligand: TLR: MyD88: IRAK
--
e46
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m46
0
infinite
0
--
ligand: TLR: MyD88: IRAK {p}
--
e47
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m47
0
infinite
0
--
csml-variable:Double
m48
10
infinite
0
HGNC | UBE2V1 |
OMIM | 602995 |
Proteome | HumanPSD/UBE2V1 |
RefSeq | NM_001032288 |
TRANSPATH | MO000087842 |
Unigene | Hs.420529 |
UniProt | Q13404-1 |
--
csml-variable:Double
m49
0
infinite
0
--
CD14: TLR4: MD-2
--
e5
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
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
--
LPS: CD14: TLR4: MD-2
--
e6
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
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: TRAF6: Ubc13: Uev1A
--
e63
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m63
0
infinite
0
--
IRAK: TRAF6 {ub}: Ubc13: Uev1A: TAK1: TAB1: TAB2: TAB3
--
e64
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m64
0
infinite
0
--
IRAK: TRAF6: Ubc13: Uev1A: TAK1: TAB1: TAB2: TAB3
--
e65
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m65
0
infinite
0
--
IKK-alpha:IKK-beta:IKK-gamma {activated}
--
e66
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m66
10
infinite
0
TRANSPATH | MO000016661 |
--
degraded IkappaB
--
e67
cso30:c:EntityBiological
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m67
0
infinite
0
--
csml-variable:Double
m68
0
infinite
0
--
NF-kappaB {nucleus}
--
e69
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m70
10
infinite
0
TRANSPATH | MO000000058 |
--
--
e7
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell
--
--
--
csml-variable:Double
m7
0
infinite
0
--
MAPKs {activated}
--
e70
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m72
10
infinite
0
TRANSPATH | MO000000077 |
--
IRAK: TRAF6: Ubc13: Uev1A: TAK1{ub}: TAB1: TAB2: TAB3
--
e72
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m74
0
infinite
0
--
IKK-gamma(m.s.){ub}
--
e73
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m75
10
infinite
0
TRANSPATH | MO000048690 |
--
ABIN2
--
e77
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m83
0
infinite
0
--
diacyl-lipopeptide: TLR6: TLR2: CD36: TIRAP
--
e79
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m85
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
triacyl-lipopeptide: TLR1:TLR2: CD36: TIRAP
--
e80
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m86
0
infinite
0
--
LPS: CD14: TLR4: MD-2: TIRAP
--
e81
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m87
0
infinite
0
--
dsRNA:TLR3: TRIF
--
e82
cso30:c:Protein
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
csml-variable:Double
m88
0
infinite
0
--
LPS: CD14: TLR4: MD-2: TRIF
--
e83
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
csml-variable:Double
m89
0
infinite
0
--
dsRNA:TLR3: TRIF: TBK1: IKK-i
--
e84
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m90
0
infinite
0
--
LPS: CD14: TLR4: MD-2: TRIF: TBK1: IKK-i
--
e85
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m91
0
infinite
0
--
IRF-3{p}: IRF-3
--
e86
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m92
0
infinite
0
--
IRF-3{p}: IRF-3 {nucleus}
--
e87
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m93
0
infinite
0
--
csml-variable:Double
m94
0
infinite
0
--
csml-variable:Double
m95
0
infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0
infinite
0
--
NF-kappaB {activated}
--
e90
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m96
10
infinite
0
TRANSPATH | MO000000058 |
--
TRIF: TRAF6: RIP1
--
e91
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m98
0
infinite
0
--
ligand: TLR: MyD88: IRAK-4: IRAK-1: TRAF6: IRF-7
--
e92
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m99
0
infinite
0
--
ligand: TLR: MyD88: IRAK-4: IRAK-1: TRAF6: IRF-7 {p}
--
e93
cso30:c:Complex
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
csml-variable:Double
m100
0
infinite
0
--
OPN-i
--
e94
cso30:c:Protein
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m101
0
infinite
0
--
IL-12 p35
--
e95
cso30:c:mRNA
cso30:i:CC_Nucleolus
--
--
csml-variable:Double
m102
0
infinite
0
--
NOS
--
e96
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m103
0
infinite
0
--
MyD88: IRF1
--
e97
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m104
0
infinite
0
--
IRF-1 {nucleus}
--
e98
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m105
10
infinite
0
InterPro | IPR001346 |
TRANSPATH | MO000007685 |
--
csml-variable:Double
m106
0
infinite
0
--
p1
p1
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
stoichiometry:c4 : 1
m2828*m6438*m3961*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR4, together with its extracellular components such as MD-2 and CD14, recognizes lipopolysaccharide (LPS) from Gram-negative bacteria, which causes septic shock.
p10
p10
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c29 : 1
stoichiometry:c30 : 1
stoichiometry:c31 : 1
m3964*m19942*0.1
nodelay
--
0
PMID: 17275323, 16497588 In addition, human TLR10 is thought to heterodimerize with TLR2 and TLR1, although a ligand for these heterodimers remains unknown.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c293 : 1
stoichiometry:c294 : 1
stoichiometry:c295 : 1
m1572*m133*0.1
nodelay
--
0
PMID: 17275323 MyD88s forms a heterodimer with MyD88.
p101
p101
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c296 : 1
stoichiometry:c297 : 1
stoichiometry:c300 : 1
stoichiometry:c298 : 1
m6810*m367*m19*0.1
nodelay
--
0
PMID: 17275323, 16415872 TIRAP is phosphorylated by a tyrosine kinase, Btk, in response to TLR2 and TLR4 ligands, and interacts with SOCS1, which subsequently targets TIRAP for ubiquitination and degradation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c302 : 1
stoichiometry:c303 : 1
stoichiometry:c304 : 1
m135*m1906*0.1
nodelay
--
0
PMID: 17275323, 16415872 TIRAP is phosphorylated by a tyrosine kinase, Btk, in response to TLR2 and TLR4 ligands, and interacts with SOCS1, which subsequently targets TIRAP for ubiquitination and degradation.
p103
p103
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c305 : 1
stoichiometry:c306 : 1
stoichiometry:c307 : 1
m136*0.1
nodelay
--
0
PMID: 17275323, 16415872 TIRAP is phosphorylated by a tyrosine kinase, Btk, in response to TLR2 and TLR4 ligands, and interacts with SOCS1, which subsequently targets TIRAP for ubiquitination and degradation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c308 : 1
stoichiometry:c309 : 1
m137*0.1
nodelay
--
0
PMID: 17275323, 16415872 TIRAP is phosphorylated by a tyrosine kinase, Btk, in response to TLR2 and TLR4 ligands, and interacts with SOCS1, which subsequently targets TIRAP for ubiquitination and degradation.
p105
p105
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c310 : 1
stoichiometry:c311 : 1
stoichiometry:c312 : 1
m18998*m1871*0.1
nodelay
--
0
PMID: 17275323, 16323247 TRAF1 interacts with TRIF and overexpression of TRIF causes Caspase 8-dependent cleavage of TRAF1.
p106
p106
cso30:i:ME_UnknownDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c313 : 1
stoichiometry:c316 : 1
stoichiometry:c314 : 1
stoichiometry:c315 : 1
m139*m1815*0.1
nodelay
--
0
PMID: 17275323, 16323247 TRAF1 interacts with TRIF and overexpression of TRIF causes Caspase 8-dependent cleavage of TRAF1.
p107
p107
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c319 : 1
stoichiometry:c320 : 1
stoichiometry:c321 : 1
stoichiometry:c322 : 1
m1873*m183*m18998*0.1
nodelay
--
0
PMID: 17275323, 16052631 TRAF4 interacts with TRIF and TRAF6, and its overexpression results in inhibition of NF-kappaB activation induced by TRIF and TRAF6.
p108
p108
cso30:i:ME_Translocation
cso30:i:CC_NuclearEnvelopeLumen
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c324 : 1
stoichiometry:c325 : 1
stoichiometry:c326 : 1
m108*0.1
nodelay
--
0
PMID: 17275323 In this complex, IRF7 is directly phosphorylated by IRAK1, and then translocated to the nucleus to induce expression of type I IFN and IFN-inducible genes.
p109
p109
cso30:i:ME_UnknownActivation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c327 : 1
stoichiometry:c331 : 1
stoichiometry:c328 : 1
m64461*m33*0.1
nodelay
--
0
PMID: 17275323 In pDC, OPN expression is upregulated by TLR9 ligand through T-bet, a master transcription factor driving Th1 differentiation.
p11
p11
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c32 : 1
stoichiometry:c33 : 1
stoichiometry:c34 : 1
m3966*m6485*0.1
nodelay
--
0
PMID: 17275323, 16497588, 16829963 TLR5 is expressed abundantly in intestinal CD11c-positive lamina propria cells where it senses bacterial flagellin.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c329 : 1
stoichiometry:c330 : 1
m143*0.1
nodelay
--
0
PMID: 17275323 In pDC, OPN expression is upregulated by TLR9 ligand through T-bet, a master transcription factor driving Th1 differentiation.
p111
p111
cso30:i:ME_Translocation
cso30:i:CC_NuclearOuterMembrane
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c332 : 1
stoichiometry:c333 : 1
stoichiometry:c334 : 1
m104*0.1
nodelay
--
0
PMID: 17275323 IRF1 is recruited to MyD88 when it is induced by IFNgamma stimulation, and translocates into the nucleus in response to TLR stimulation to induce a set of genes including IFNbeta in conventional DC.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c335 : 1
stoichiometry:c336 : 1
stoichiometry:c337 : 1
m107*0.1
nodelay
--
0
PMID: 17275323 IRF5 binds MyD88 and TRAF6 and moves to the nucleus after phosphorylation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c341 : 1
stoichiometry:c343 : 1
stoichiometry:c344 : 1
m2065*m147*0.1
nodelay
--
0
PMID: 17275323 The cytoplasmic peptidyl-prolyl-isomerase Pin1, which catalyzes the cis-trans isomerization of peptide-bonds located N-terminal to proline to modulate substrate function, binds IRF3 when it is phosphorylated at Ser339, triggering ubiquitination and subsequent degradation of IRF3 by a proteasome-dependent pathway to terminate IFN responses.
p114
p114
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c340 : 1
stoichiometry:c342 : 1
m977*0.1
nodelay
--
0
PMID: 17275323 The cytoplasmic peptidyl-prolyl-isomerase Pin1, which catalyzes the cis-trans isomerization of peptide-bonds located N-terminal to proline to modulate substrate function, binds IRF3 when it is phosphorylated at Ser339, triggering ubiquitination and subsequent degradation of IRF3 by a proteasome-dependent pathway to terminate IFN responses.
p115
p115
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c360 : 1
stoichiometry:c345 : 1
stoichiometry:c346 : 1
m146*0.1
nodelay
--
0
PMID: 17275323 The cytoplasmic peptidyl-prolyl-isomerase Pin1, which catalyzes the cis-trans isomerization of peptide-bonds located N-terminal to proline to modulate substrate function, binds IRF3 when it is phosphorylated at Ser339, triggering ubiquitination and subsequent degradation of IRF3 by a proteasome-dependent pathway to terminate IFN responses.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c347 : 1
stoichiometry:c348 : 1
m148*0.1
nodelay
--
0
PMID: 17275323 The cytoplasmic peptidyl-prolyl-isomerase Pin1, which catalyzes the cis-trans isomerization of peptide-bonds located N-terminal to proline to modulate substrate function, binds IRF3 when it is phosphorylated at Ser339, triggering ubiquitination and subsequent degradation of IRF3 by a proteasome-dependent pathway to terminate IFN responses.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c350 : 1
stoichiometry:c349 : 1
m6*0.1
nodelay
--
0
PMID: 17275323 LPS stimulation leads to the expression of ATF3, a member of the ATF/CREB family of transcription factors.
p118
p118
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c351 : 1
stoichiometry:c352 : 1
stoichiometry:c353 : 1
m1572*m978*0.1
nodelay
--
0
PMID: 17275323, 16236719 IRF4 is reported to bind MyD88.
p101
p119
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c356 : 1
stoichiometry:c357 : 1
stoichiometry:c299 : 1
stoichiometry:c301 : 1
m367*m86*m6810*0.1
nodelay
--
0
PMID: 17275323, 16415872 TIRAP is phosphorylated by a tyrosine kinase, Btk, in response to TLR2 and TLR4 ligands, and interacts with SOCS1, which subsequently targets TIRAP for ubiquitination and degradation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c35 : 1
stoichiometry:c36 : 1
stoichiometry:c37 : 1
m23*m19944*0.1
nodelay
--
0
PMID: 17275323 Mouse TLR11 recognizes as yet unknown components of uropathogenic bacteria, and a profilin-like molecule of the protozoan parasite Toxoplasma gondii.
p101
p120
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c64 : 1
stoichiometry:c355 : 1
stoichiometry:c358 : 1
stoichiometry:c359 : 1
m367*m121*m6810*0.1
nodelay
--
0
PMID: 17275323, 16415872 TIRAP is phosphorylated by a tyrosine kinase, Btk, in response to TLR2 and TLR4 ligands, and interacts with SOCS1, which subsequently targets TIRAP for ubiquitination and degradation.
p87
p121
cso30:i:ME_UnknownProduction
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c362 : 1
stoichiometry:c363 : 1
m120*0.1
nodelay
--
0
PMID: 17275323 Integrin signaling regulates the production of PIP2 through the activation of ARF6 GTPase and PI5K.
p87
p122
cso30:i:ME_UnknownProduction
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c255 : 1
stoichiometry:c364 : 1
m119*0.1
nodelay
--
0
PMID: 17275323 Integrin signaling regulates the production of PIP2 through the activation of ARF6 GTPase and PI5K.
p13
p13
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c38 : 1
stoichiometry:c39 : 1
stoichiometry:c40 : 1
m3965*m119368*0.1
nodelay
--
0
PMID: 17275323 TLR3 was shown to recognize double stranded RNA (dsRNA), which is produced by many viruses during replication.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c41 : 1
stoichiometry:c42 : 1
stoichiometry:c43 : 1
m25*m19940*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single stranded RNA (ssRNA) derived from various viruses and small interfering RNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c44 : 1
stoichiometry:c45 : 1
stoichiometry:c46 : 1
m19940*m27*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single stranded RNA (ssRNA) derived from various viruses and small interfering RNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c47 : 1
stoichiometry:c48 : 1
stoichiometry:c49 : 1
m19823*m27*0.1
nodelay
--
0
PMID: 17275323 Human TLR8, which has the highest homology to TLR7, participates in the recognition of imidazoquinolines and ssRNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c50 : 1
stoichiometry:c51 : 1
stoichiometry:c52 : 1
m19823*m29*0.1
nodelay
--
0
PMID: 17275323 Human TLR8, which has the highest homology to TLR7, participates in the recognition of imidazoquinolines and ssRNA.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c53 : 1
stoichiometry:c54 : 1
stoichiometry:c55 : 1
m19828*m32*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR9 recognizes CpG DNA motifs present in bacterial and viral genomes as well as non-nucleic acids such as hemozoin from the malaria parasite.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c57 : 1
stoichiometry:c58 : 1
m19828*m34*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR9 recognizes CpG DNA motifs present in bacterial and viral genomes as well as non-nucleic acids such as hemozoin from the malaria parasite.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c5 : 1
stoichiometry:c6 : 1
stoichiometry:c274 : 1
stoichiometry:c7 : 1
m155666*m5*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR4, together with its extracellular components such as MD-2 and CD14, recognizes lipopolysaccharide (LPS) from Gram-negative bacteria, which causes septic shock. PMID: 17275323, 9686597 the RP105-MD-1 complex interacts with a TLR4-MD-2 complex to prevent LPS binding to TLR4-MD-2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c59 : 1
stoichiometry:c60 : 1
stoichiometry:c61 : 1
m38*m37*0.1
nodelay
--
0
PMID: 17275323 Following stimulation, all TLRs except for TLR3 recruit MyD88, IRAKs and TRAF6 to activate the Ubc13/TAK1 pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c62 : 1
stoichiometry:c63 : 1
stoichiometry:c65 : 1
m39*m1572*0.1
nodelay
--
0
PMID: 17275323 Following stimulation, all TLRs except for TLR3 recruit MyD88, IRAKs and TRAF6 to activate the Ubc13/TAK1 pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c66 : 1
stoichiometry:c78 : 1
stoichiometry:c68 : 1
m40*m17258*0.1
nodelay
--
0
PMID: 17275323 The association of TLRs and MyD88 stimulates the recruitment of members of the IRAK family, including IRAK1, IRAK2, IRAK4 and IRAK-M.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c69 : 1
stoichiometry:c70 : 1
stoichiometry:c71 : 1
m40*m36*0.1
nodelay
--
0
PMID: 17275323 The association of TLRs and MyD88 stimulates the recruitment of members of the IRAK family, including IRAK1, IRAK2, IRAK4 and IRAK-M.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c72 : 1
stoichiometry:c73 : 1
stoichiometry:c74 : 1
m40*m1571*0.1
nodelay
--
0
PMID: 17275323 The association of TLRs and MyD88 stimulates the recruitment of members of the IRAK family, including IRAK1, IRAK2, IRAK4 and IRAK-M.
p25
p25
cso30:i:ME_Binding
cso30:i:CC_PlasmaMembrane_IntegralToPlasmaMembrane_
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c75 : 1
stoichiometry:c76 : 1
stoichiometry:c77 : 1
m40*m1569*0.1
nodelay
--
0
PMID: 17275323 The association of TLRs and MyD88 stimulates the recruitment of members of the IRAK family, including IRAK1, IRAK2, IRAK4 and IRAK-M.
p26
p26
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c67 : 1
stoichiometry:c88 : 1
stoichiometry:c338 : 1
stoichiometry:c84 : 1
m183*m49*0.1
nodelay
--
0
PMID: 17275323 Once phosphorylated, IRAKs dissociate from MyD88 and interact with TRAF6, a member of the TRAF family. PMID: 17275323 TRAF4 may serve to antagonize TRAF6 function by preventing recruitment of TRAF6 to the adapter complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c79 : 1
stoichiometry:c80 : 1
stoichiometry:c81 : 1
m40*m6176*0.1
nodelay
--
0
PMID: 17275323 Once phosphorylated, IRAKs dissociate from MyD88 and interact with TRAF6, a member of the TRAF family.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c83 : 1
stoichiometry:c82 : 1
m46*0.1
nodelay
--
0
PMID: 17275323 Once phosphorylated, IRAKs dissociate from MyD88 and interact with TRAF6, a member of the TRAF family.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c85 : 1
stoichiometry:c86 : 1
stoichiometry:c87 : 1
m47*0.1
nodelay
--
0
PMID: 17275323 Once phosphorylated, IRAKs dissociate from MyD88 and interact with TRAF6, a member of the TRAF family.
p3
p3
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c8 : 1
stoichiometry:c9 : 1
stoichiometry:c10 : 1
m3963*m3964*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR2 forms heterodimers with TLR1, TLR6 and non-TLRs such as CD36 to discriminate a wide variety of PAMPs, including peptidoglycan, lipopeptides and lipoproteins of Gram-positive bacteria, mycoplasma lipopeptides and fungal zymosan.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c89 : 1
stoichiometry:c90 : 1
stoichiometry:c91 : 1
stoichiometry:c92 : 1
m6443*m48*m45*0.1
nodelay
--
0
PMID; 17275323, 16056267 TRAF6, an E3 ligase, forms a complex with Ubc13 and Uev1A to promote the synthesis of lysine 63-linked polyubiquitin chains, which in turn activate TAK1, a MAPKKK.
p31
p31
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c101 : 1
stoichiometry:c103 : 1
stoichiometry:c102 : 1
m1637*m74*0.1
nodelay
--
0
PMID: 17275323 TAK1, in combination with TAB1, TAB2 and TAB3, activates two downstream pathways involving the IKK complex and the MAPK family.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c99 : 1
stoichiometry:c339 : 1
stoichiometry:c100 : 1
m65*0.1
nodelay
--
0
PMID; 17275323, 16056267 TRAF6, an E3 ligase, forms a complex with Ubc13 and Uev1A to promote the synthesis of lysine 63-linked polyubiquitin chains, which in turn activate TAK1, a MAPKKK. PMID: 17275323, 16862162 Although in vitro analyses have implicated Ubc13 in the activation of NF-kappaB and MAPK, via ubiquitination of TAK1, studies on mice with a conditionally deleted Ubc13 gene in various tissues have shown that it has a dispensable role in NF-kappaB activation. PMID: 17275323, 15334086 A20, an inducible de-ubiqutination enzyme, removes ubiquitin moieties from TRAF6 to terminate TLR signaling.
p33
p33
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c93 : 1
stoichiometry:c97 : 1
stoichiometry:c94 : 1
stoichiometry:c95 : 1
stoichiometry:c96 : 1
stoichiometry:c98 : 1
m63*m1573*m1583*m6433*m19389*0.1
nodelay
--
0
PMID: 17275323 TAK1, in combination with TAB1, TAB2 and TAB3, activates two downstream pathways involving the IKK complex and the MAPK family.
p34
p34
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c104 : 1
stoichiometry:c105 : 1
stoichiometry:c106 : 1
m66*m186*0.1
nodelay
--
0
PMID: 17275323 The IKK complex, composed of the catalytic subunits IKKalpha and IKKbeta and a regulatory subunit IKKgamma/NEMO, catalyzes the phosphorylation of IkappaB proteins.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c107 : 1
stoichiometry:c108 : 1
stoichiometry:c109 : 1
m68*0.1
nodelay
--
0
PMID: 17275323 Phosphorylated IkappaB proteins are degraded by a proteasome-dependent pathway, allowing NF-kappaB to translocate to the nucleus.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c189 : 1
stoichiometry:c111 : 1
m96*0.1
nodelay
--
0
PMID: 17275323 Phosphorylated IkappaB proteins are degraded by a proteasome-dependent pathway, allowing NF-kappaB to translocate to the nucleus.
p37
p37
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c112 : 1
stoichiometry:c119 : 1
stoichiometry:c113 : 1
m71*m74*0.1
nodelay
--
0
PMID: 17275323 TAK1 also activates the MAPK pathway, which mediates AP-1 activation.
p38
p38
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c115 : 1
stoichiometry:c117 : 1
stoichiometry:c116 : 1
m219*m72*0.1
nodelay
--
0
PMID: 17275323 TAK1 also activates the MAPK pathway, which mediates AP-1 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c114 : 1
stoichiometry:c118 : 1
m64*0.1
nodelay
--
0
PMID: 17275323, 16862162 Although in vitro analyses have implicated Ubc13 in the activation of NF-kappaB and MAPK, via ubiquitination of TAK1, studies on mice with a conditionally deleted Ubc13 gene in various tissues have shown that it has a dispensable role in NF-kappaB activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c11 : 1
stoichiometry:c12 : 1
stoichiometry:c13 : 1
m11*m12*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR2 forms heterodimers with TLR1, TLR6 and non-TLRs such as CD36 to discriminate a wide variety of PAMPs, including peptidoglycan, lipopeptides and lipoproteins of Gram-positive bacteria, mycoplasma lipopeptides and fungal zymosan.
p40
p40
cso30:i:ME_Ubiquitination
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c120 : 1
stoichiometry:c122 : 1
stoichiometry:c121 : 1
m1593*m6443*0.1
nodelay
--
0
PMID: 17275323, 16862162 Notably, in Ubc13-deficient cells, there is a reduction in the stimulus-dependent ubiquitination of IKKgamma/NEMO, suggesting a link between Ubc13-dependent IKKgamma/NEMO ubiquitination and MAPK activation.
p41
p41
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c123 : 1
stoichiometry:c125 : 1
stoichiometry:c137 : 1
stoichiometry:c138 : 1
stoichiometry:c124 : 1
m76*m6*m82*m83*0.1
nodelay
--
0
PMID: 17275323, 11163183 LPS-stimulated ERKactivation and TNFalpha production is severely impaired in Tpl2-deficient macrophages, whereas activation of JNK and p38 is normal. PMID: 17275323, 16633345 It has been reported that ABIN2 (A20-binding inhibitor of NF-kappaB 2) increases the stability of Tpl2 to facilitate ERK activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c126 : 1
stoichiometry:c128 : 1
m6*0.1
nodelay
--
0
PMID: 17275323, 11163183 LPS-stimulated ERKactivation and TNFalpha production is severely impaired in Tpl2-deficient macrophages, whereas activation of JNK and p38 is normal.
p43
p43
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c127 : 1
stoichiometry:c130 : 1
stoichiometry:c129 : 1
m6*m93309*0.1
nodelay
--
0
PMID: 17275323, 11163183 LPS-stimulated ERKactivation and TNFalpha production is severely impaired in Tpl2-deficient macrophages, whereas activation of JNK and p38 is normal.
p44
p44
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c131 : 1
stoichiometry:c133 : 1
stoichiometry:c132 : 1
m78*m6*0.1
nodelay
--
0
PMID: 17275323, 11163183 LPS-stimulated ERKactivation and TNFalpha production is severely impaired in Tpl2-deficient macrophages, whereas activation of JNK and p38 is normal.
p45
p45
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c134 : 1
stoichiometry:c135 : 1
stoichiometry:c136 : 1
m6*m80*0.1
nodelay
--
0
PMID: 17275323, 11163183 LPS-stimulated ERKactivation and TNFalpha production is severely impaired in Tpl2-deficient macrophages, whereas activation of JNK and p38 is normal.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c139 : 1
stoichiometry:c140 : 1
m6*0.1
nodelay
--
0
PMID: 17275323, 14661019 Macrophages deficient for MEKK3 show defective JNK and p38 activation and IL-6 production after LPS treatment.
p47
p47
cso30:i:ME_Translation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c142 : 1
stoichiometry:c143 : 1
stoichiometry:c141 : 1
m93248*m6*0.1
nodelay
--
0
PMID: 17275323, 14661019 Macrophages deficient for MEKK3 show defective JNK and p38 activation and IL-6 production after LPS treatment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c144 : 1
stoichiometry:c146 : 1
m6*0.1
nodelay
--
0
PMID: 17275323 LPS-induced ROS production is implicated in facilitating the TRAF6-ASK1-p38 signaling axis.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c145 : 1
stoichiometry:c148 : 1
stoichiometry:c147 : 1
m6*m84*0.1
nodelay
--
0
p5
p5
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c14 : 1
stoichiometry:c15 : 1
stoichiometry:c16 : 1
m3987*m3964*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR2 forms heterodimers with TLR1, TLR6 and non-TLRs such as CD36 to discriminate a wide variety of PAMPs, including peptidoglycan, lipopeptides and lipoproteins of Gram-positive bacteria, mycoplasma lipopeptides and fungal zymosan.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c151 : 1
stoichiometry:c152 : 1
stoichiometry:c154 : 1
m6810*m16*0.1
nodelay
--
0
PMID: 17275323 TIRAP is recruited to TLR4, TLR1/2 and TLR2/6, activating the MyD88-dependent pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c149 : 1
stoichiometry:c150 : 1
stoichiometry:c153 : 1
m19*m6810*0.1
nodelay
--
0
PMID: 17275323 TIRAP is recruited to TLR4, TLR1/2 and TLR2/6, activating the MyD88-dependent pathway.
p52
p52
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c155 : 1
stoichiometry:c156 : 1
stoichiometry:c259 : 1
stoichiometry:c276 : 1
stoichiometry:c157 : 1
m6810*m6*m290229*0.1
nodelay
--
0
PMID: 17275323 TIRAP is recruited to TLR4, TLR1/2 and TLR2/6, activating the MyD88-dependent pathway. PMID: 17275323 These findings suggest that TLR4 recruits TIRAP to the plasma membrane as a result of CD11b-mediated production of PIP2, which subsequently recruits MyD88 after which the signaling complex is assembled to initiate the MyD88-dependent signaling. PMID: 17275323 ST2L sequesters MyD88 and TIRAP to inhibit the recruitment of these adapters to TLR4.
p53
p53
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c158 : 1
stoichiometry:c159 : 1
stoichiometry:c160 : 1
m19314*m18998*0.1
nodelay
--
0
PMID: 17275323 TRIF is recruited to TLR3 and TLR4, and interacts with TBK1 and IKKi, which mediate phosphorylation of IRF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c161 : 1
stoichiometry:c162 : 1
stoichiometry:c163 : 1
m6*m18998*0.1
nodelay
--
0
PMID: 17275323 TRIF is recruited to TLR3 and TLR4, and interacts with TBK1 and IKKi, which mediate phosphorylation of IRF3.
p55
p55
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c164 : 1
stoichiometry:c165 : 1
stoichiometry:c166 : 1
stoichiometry:c167 : 1
m3902*m1599*m88*0.1
nodelay
--
0
PMID: 17275323 TRIF is recruited to TLR3 and TLR4, and interacts with TBK1 and IKKi, which mediate phosphorylation of IRF3.
p56
p56
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c169 : 1
stoichiometry:c170 : 1
stoichiometry:c168 : 1
m3902*m1599*0.1
nodelay
--
0
PMID: 17275323 TRIF is recruited to TLR3 and TLR4, and interacts with TBK1 and IKKi, which mediate phosphorylation of IRF3.
p57
p57
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c171 : 1
stoichiometry:c174 : 1
stoichiometry:c172 : 1
m977*m91*0.1
nodelay
--
0
PMID: 17275323 TRIF is recruited to TLR3 and TLR4, and interacts with TBK1 and IKKi, which mediate phosphorylation of IRF3.
p58
p58
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c175 : 1
stoichiometry:c173 : 1
stoichiometry:c318 : 1
stoichiometry:c176 : 1
m977*m90*0.1
nodelay
--
0
PMID: 17275323 TRIF is recruited to TLR3 and TLR4, and interacts with TBK1 and IKKi, which mediate phosphorylation of IRF3. PMID: 17275323 The cleaved fragment of TRAF1 can inhibit TRIF-dependent activation of NF-kappaB and IRF3, suggesting that TRIF-induced cleavage of TRAF1 is responsible for shutdown of the TRIFdependent pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c177 : 1
stoichiometry:c178 : 1
m19324*0.1
nodelay
--
0
PMID: 17275323 Phosphorylated IRF3 dimerizes and is translocated to the nucleus to induce expression of type I IFN and IFN-inducible genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c17 : 1
stoichiometry:c18 : 1
stoichiometry:c19 : 1
m12*m14*0.1
nodelay
--
0
PMID: 17275323, 16497588 TLR2 forms heterodimers with TLR1, TLR6 and non-TLRs such as CD36 to discriminate a wide variety of PAMPs, including peptidoglycan, lipopeptides and lipoproteins of Gram-positive bacteria, mycoplasma lipopeptides and fungal zymosan.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c179 : 1
stoichiometry:c180 : 1
m92*0.1
nodelay
--
0
PMID: 17275323 Phosphorylated IRF3 dimerizes and is translocated to the nucleus to induce expression of type I IFN and IFN-inducible genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c181 : 1
stoichiometry:c182 : 1
m93*0.1
nodelay
--
0
PMID: 17275323 Phosphorylated IRF3 dimerizes and is translocated to the nucleus to induce expression of type I IFN and IFN-inducible genes.
p62
p62
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
stoichiometry:c186 : 1
m1599*m3902*m1872*0.1
nodelay
--
0
PMID: 17275323 TRAF3 forms a complex with TBK1 and IKKi.
p63
p63
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c188 : 1
stoichiometry:c187 : 1
stoichiometry:c208 : 1
stoichiometry:c192 : 1
m183*m18998*m109*0.1
nodelay
--
0
PMID: 17275323, 16115877 RIP1 is reportedly polyubiquitinated and forms a complex with TRAF6 and TAK1.
p64
p64
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c110 : 1
stoichiometry:c193 : 1
stoichiometry:c317 : 1
stoichiometry:c323 : 1
stoichiometry:c190 : 1
m69*m98*0.1
nodelay
--
0
PMID: 17275323 TRIF interacts with TRAF6 and RIP1, which mediate NF-kappaB activation. PMID: 17275323 The cleaved fragment of TRAF1 can inhibit TRIF-dependent activation of NF-kappaB and IRF3, suggesting that TRIF-induced cleavage of TRAF1 is responsible for shutdown of the TRIFdependent pathway. PMID: 17275323, 16052631 TRAF4 interacts with TRIF and TRAF6, and its overexpression results in inhibition of NF-kappaB activation induced by TRIF and TRAF6.
p65
p65
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c194 : 1
stoichiometry:c195 : 1
stoichiometry:c196 : 1
stoichiometry:c197 : 1
stoichiometry:c198 : 1
m41*m36*m183*m980*0.1
nodelay
--
0
PMID: 17275323 In pDC, a signaling complex consisting of MyD88-TRAF6-IRAK4-IRAK1-IRF7 is formed.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c199 : 1
stoichiometry:c200 : 1
m99*0.1
nodelay
--
0
PMID: 17275323 In this complex, IRF7 is directly phosphorylated by IRAK1, and then translocated to the nucleus to induce expression of type I IFN and IFN-inducible genes.
p67
p67
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c201 : 1
stoichiometry:c202 : 1
stoichiometry:c203 : 1
stoichiometry:c226 : 1
stoichiometry:c204 : 1
m1872*m101*m181*m100*0.1
nodelay
--
0
PMID: 17275323 OPN-i, TRAF3 and IKKalpha are also involved in this complex.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c205 : 1
stoichiometry:c206 : 1
m93*0.1
nodelay
--
0
PMID: 17275223 Phosphorylated IRF3 forms a dimer, which translocates from cytoplasm to the nucleus to induce expression of target genes including IFNbeta.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c191 : 1
stoichiometry:c207 : 1
m97*0.1
nodelay
--
0
PMID: 17275323, 16115877 RIP1 is reportedly polyubiquitinated and forms a complex with TRAF6 and TAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c20 : 1
stoichiometry:c21 : 1
stoichiometry:c22 : 1
m13*m17*0.1
nodelay
--
0
PMID: 17275323, 16497588 In particular, TLR1/2 and TLR2/6 can discriminate triacyl- and diacyl-lipopeptide, respectively.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c209 : 1
stoichiometry:c210 : 1
m110*0.1
nodelay
--
0
PMID: 17275323 IRF7 potently activates the promoter of IFNbeta and various IFNalpha genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c212 : 1
stoichiometry:c211 : 1
m110*0.1
nodelay
--
0
PMID: 17275323 IRF7 potently activates the promoter of IFNbeta and various IFNalpha genes.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c214 : 1
stoichiometry:c213 : 1
m33*0.1
nodelay
--
0
PMID: 17275323, 12356687, 12626561 Notably, TLR7- and TLR9-mediated type I IFN induction is elicited by the MyD88-dependent pathway, but not by the TRIF-dependent pathway.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c215 : 1
stoichiometry:c216 : 1
m28*0.1
nodelay
--
0
PMID: 17275323, 12356687, 12626561 Notably, TLR7- and TLR9-mediated type I IFN induction is elicited by the MyD88-dependent pathway, but not by the TRIF-dependent pathway.
p74
p74
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c217 : 1
stoichiometry:c219 : 1
stoichiometry:c218 : 1
m980*m95*0.1
nodelay
--
0
PMID: 17275323 TRAF3 is also required for TBK1/IKKi-dependent IRF7 and IRF3 activation in TLR3 and RIG-I/Mda5-signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c221 : 1
stoichiometry:c220 : 1
m112*0.1
nodelay
--
0
PMID: 17275323 IRF7 also participates in type I IFN induction activated by the cytosolic RNA helicases RIG-I and Mda5, which recognize viral dsRNA, in conventional DC, macrophages and fibroblast cells.
p76
p76
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c222 : 1
stoichiometry:c223 : 1
m1872*0.1
nodelay
--
0
PMID: 17275323 TRAF3 is also necessary for the induction of anti-inflammatory cytokine IL- 10, but not pro-inflammatory cytokines, in response to ligands specific for TLR3, 4, 7 and 9.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c225 : 1
stoichiometry:c224 : 1
m70*0.1
nodelay
--
0
PMID: 17275323, 16604075 pDC isolated from either T-bet- or OPN deficient mice have defects in the induction of type I IFN in response to TLR9-ligand, but they can produce NF-kappaB-driven IL-6 as usual.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c229 : 1
stoichiometry:c227 : 1
m33*0.1
nodelay
--
0
PMID: 17275323 Conventional DC derived from IRF1-deficient mice display impaired induction of IFNbeta, inducible nitric-oxide synthase and IL-12 p35, in response to a TLR9 ligand.
p79
p79
cso30:i:ME_GeneExpression
cso30:i:CC_NuclearOuterMembrane
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c230 : 1
stoichiometry:c228 : 1
m33*0.1
nodelay
--
0
PMID: 17275323 Conventional DC derived from IRF1-deficient mice display impaired induction of IFNbeta, inducible nitric-oxide synthase and IL-12 p35, in response to a TLR9 ligand.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c23 : 1
stoichiometry:c24 : 1
stoichiometry:c25 : 1
m15*m18*0.1
nodelay
--
0
PMID: 17275323, 16497588 In particular, TLR1/2 and TLR2/6 can discriminate triacyl- and diacyl-lipopeptide, respectively.
p80
p80
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c231 : 1
stoichiometry:c232 : 1
stoichiometry:c234 : 1
stoichiometry:c233 : 1
m1572*m970*m1639*0.1
nodelay
--
0
PMID: 17275323 IRF1 is recruited to MyD88 when it is induced by IFNgamma stimulation, and translocates into the nucleus in response to TLR stimulation to induce a set of genes including IFNbeta in conventional DC.
p81
p81
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c235 : 1
stoichiometry:c236 : 1
m1639*0.1
nodelay
--
0
PMID: 17275323 IFNgamma stimulation induces IRF1 expression.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c238 : 1
stoichiometry:c237 : 1
m105*0.1
nodelay
--
0
PMID: 17275323 IRF1 is recruited to MyD88 when it is induced by IFNgamma stimulation, and translocates into the nucleus in response to TLR stimulation to induce a set of genes including IFNbeta in conventional DC.
p83
p83
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c239 : 1
stoichiometry:c241 : 1
stoichiometry:c242 : 1
stoichiometry:c354 : 1
stoichiometry:c240 : 1
m1572*m979*m183*0.1
nodelay
--
0
PMID: 17275323 IRF5 binds MyD88 and TRAF6 and moves to the nucleus after phosphorylation. PMID: 17275323 As expression of the IRF4 gene is upregulated after exposure with TLR ligands, the induced IRF4 might associate with MyD88 to prevent recruitment of IRF5, thereby attenuating IRF5-dependent inflammatory responses.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c243 : 1
stoichiometry:c244 : 1
m106*0.1
nodelay
--
0
PMID: 17275323 IRF5 binds MyD88 and TRAF6 and moves to the nucleus after phosphorylation.
p85
p85
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c245 : 1
stoichiometry:c246 : 1
stoichiometry:c248 : 1
stoichiometry:c247 : 1
m6*m19005*m1629*0.1
nodelay
--
0
PMID: 17275323, 16757566 TRAM is phosphorylated at serine 16 by PKCepsilon in response to LPS.
p87
p87
cso30:i:ME_UnknownProduction
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c361 : 1
stoichiometry:c250 : 1
m122*0.1
nodelay
--
0
PMID: 17275323 Integrin signaling regulates the production of PIP2 through the activation of ARF6 GTPase and PI5K.
p88
p88
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c252 : 1
stoichiometry:c256 : 1
stoichiometry:c253 : 1
m113*m2142*0.1
nodelay
--
0
PMID: 17275323 Integrin signaling regulates the production of PIP2 through the activation of ARF6 GTPase and PI5K.
p9
p9
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c26 : 1
stoichiometry:c27 : 1
stoichiometry:c28 : 1
m3963*m19942*0.1
nodelay
--
0
PMID: 17275323, 16497588 In addition, human TLR10 is thought to heterodimerize with TLR2 and TLR1, although a ligand for these heterodimers remains unknown.
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:c275 : 1
stoichiometry:c262 : 1
m87*m1572*0.1
nodelay
--
0
PMID: 17275323 These findings suggest that TLR4 recruits TIRAP to the plasma membrane as a result of CD11b-mediated production of PIP2, which subsequently recruits MyD88 after which the signaling complex is assembled to initiate the MyD88-dependent signaling. PMID: 17275323 ST2L sequesters MyD88 and TIRAP to inhibit the recruitment of these adapters to TLR4.
p91
p91
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c263 : 1
stoichiometry:c265 : 1
stoichiometry:c264 : 1
m123*m2142*0.1
nodelay
--
0
p93
p93
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c268 : 1
stoichiometry:c269 : 1
stoichiometry:c270 : 1
m1632*m6500*0.1
nodelay
--
0
PMID: 17275323 The LRR of RP105 associate with MD-1 to form a complex on the cell surface.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c271 : 1
stoichiometry:c273 : 1
stoichiometry:c272 : 1
m124*m126*0.1
nodelay
--
0
PMID: 17275323, 9686597 the RP105-MD-1 complex interacts with a TLR4-MD-2 complex to prevent LPS binding to TLR4-MD-2.
p95
p95
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c277 : 1
stoichiometry:c278 : 1
stoichiometry:c279 : 1
stoichiometry:c280 : 1
m41575*m6176*m183*0.1
nodelay
--
0
PMID: 17275323 SIGIRR interacts with IRAKs and TRAF6 to block TLR signaling.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c281 : 1
stoichiometry:c282 : 1
stoichiometry:c286 : 1
m128*m3961*0.1
nodelay
--
0
PMID: 17275323 Triad3A is an E3 ligase that binds the TIR domain of TLR4 and 9, but not that of TLR2.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c283 : 1
stoichiometry:c284 : 1
stoichiometry:c285 : 1
m19828*m128*0.1
nodelay
--
0
PMID: 17275323 Triad3A is an E3 ligase that binds the TIR domain of TLR4 and 9, but not that of TLR2.
p98
p98
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c288 : 1
stoichiometry:c289 : 1
stoichiometry:c292 : 1
m129*0.1
nodelay
--
0
PMID: 17275323 Triad3 overexpression promotes degradation of TLR4 and 9 via a proteasome-dependent pathway.
p99
p99
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c287 : 1
stoichiometry:c290 : 1
stoichiometry:c291 : 1
m130*0.1
nodelay
--
0
PMID: 17275323 Triad3 overexpression promotes degradation of TLR4 and 9 via a proteasome-dependent pathway.
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c: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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c: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:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c: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:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
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: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:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
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:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--