Original Literature | Model OverView |
---|---|
Publication
Title
Triggering the innate antiviral response through IRF-3 activation.
Affiliation
Lady Davis Institute for Medical Research-Jewish General Hospital, Departmentsof Microbiology & Immunology, Medicine, and Oncology, McGill University,Montreal H3T 1E2, Canada. john.hiscott@mcgill.ca
Abstract
Rapid induction of type I interferon (IFN) expression is a central event in theestablishment of the innate immune response against viral infection and requiresthe activation of multiple transcriptional proteins following engagement andsignaling through Toll-like receptor-dependent and -independent pathways. Thetranscription factor interferon regulatory factor-3 (IRF-3) contributes to afirst line of defense against viral infection by inducing the production ofIFN-beta that in turn amplifies the IFN response and the development ofantiviral activity. In murine knock-out models, the absence of IRF-3 and theclosely related IRF-7 ablates IFN production and increases viral pathogenesis,thus supporting a pivotal role for IRF-3/IRF-7 in the development of the hostantiviral response.
PMID
17395583
|
Entity
TRAF6
--
MO000000212
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m183
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000000212 |
--
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-i
--
MO000016608
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1599
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000016608 |
--
TRAF3
--
MO000016963
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m1872
10
infinite
0
InterPro | IPR001841 |
TRANSPATH | MO000016963 |
--
TBK1{active}
--
MO000019331
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m3902
10
infinite
0
InterPro | IPR000719 |
TRANSPATH | MO000019331 |
--
protein remnants
--
MO000019479
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m360980
10
infinite
0
TRANSPATH | MO000019479 |
--
dsRNA
--
MO000022224
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m119368
10
infinite
0
TRANSPATH | MO000022224 |
--
IRAK-4
--
MO000039077
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m17258
10
infinite
0
TRANSPATH | MO000039077 |
--
dsRNA:TLR3:TRIF
--
MO000041437
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19305
10
infinite
0
TRANSPATH | MO000041437 |
--
dsRNA:TLR3
--
MO000041446
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19314
10
infinite
0
TRANSPATH | MO000041446 |
--
IRF-3{p}
--
MO000041456
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19324
10
infinite
0
TRANSPATH | MO000041456 |
--
IRF-7{p}
--
MO000041457
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m19325
10
infinite
0
TRANSPATH | MO000041457 |
--
ATF-2:c-Jun
--
MO000055971
cso30:c:Protein
cso30:i:CC_CellComponent
--
--
csml-variable:Double
m31298
10
infinite
0
TRANSPATH | MO000055971 |
--
--
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
--
(IRF-3{p})2:CBP
--
e11
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m11
0
infinite
0
--
(IRF-3{p})2:p300
--
e12
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m12
0
infinite
0
--
IFN
--
e14
cso30:c:Protein
cso30:i:CC_Extracellular
--
--
csml-variable:Double
m14
0
infinite
0
--
IFN-alpha1
--
e15
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m15
0
infinite
0
--
IFN-alpah4
--
e16
cso30:c:mRNA
cso30:i:CC_NuclearChromosome
--
--
csml-variable:Double
m16
0
infinite
0
--
IFN-alpha7
--
e17
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m17
0
infinite
0
--
IFN-alpha14
--
e18
cso30:c:mRNA
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m18
0
infinite
0
--
cullin1
--
e19
cso30:c:Protein
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
--
cullin1:IRF-3
--
e20
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m20
0
infinite
0
--
cullin1:IRF-3{ub}
--
e21
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m21
0
infinite
0
--
IRF-3{p}:pin1
--
e22
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m22
0
infinite
0
--
Pin1:IRF-3{ub}n
--
e23
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m23
0
infinite
0
--
IRF-3{p}:ISG15
--
e24
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m24
0
infinite
0
--
ddx58:dsRNA
--
e25
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m25
0
infinite
0
--
dsRNA:IFIH1
--
e26
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m26
0
infinite
0
--
dsRNA:DDX58:MAVS
--
e27
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m27
0
infinite
0
--
dsRNA:IFIH1:MAVS
--
e28
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m28
0
infinite
0
--
LGP2
--
e29
cso30:c:Protein
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
--
DDX58:LGP2
--
e30
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m30
0
infinite
0
--
dsRNA:DDX58:MAVS:TRAF3
--
e31
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m31
0
infinite
0
--
dsRNA:IFIH1:MAVS:TRAF3
--
e32
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m32
0
infinite
0
--
dsRNA:DDX58:MAVS:TRAF3:ikk-i
--
e33
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m33
0
infinite
0
--
IKK{active}
--
e35
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m36
10
infinite
0
TRANSPATH | MO000000248 |
--
ATF-2:c-Jun{active}
--
e37
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m38
10
infinite
0
TRANSPATH | MO000055971 |
--
NF-kappaB
--
e38
cso30:c:Complex
cso30:i:CC_Cytosol
--
--
csml-variable:Double
m39
0
infinite
0
--
NF-kappaB{active}
--
e39
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m40
0
infinite
0
--
--
e4
cso30:c:EntityBiologicalCompartment
cso30:i:CC_PlasmaMembrane_InternalSideOfPlasmaMembrane_
--
--
--
csml-variable:Double
m4
0
infinite
0
--
IFN-beta
--
e40
cso30:c:Dna
cso30:i:CC_Nucleoplasm
--
--
csml-variable:Double
m41
0
infinite
0
--
IFN-beta enhancesome complex
--
e41
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
csml-variable:Double
m42
0
infinite
0
--
dsRNA:TLR3:TRIF:TRAF6
--
e42
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m43
0
infinite
0
--
dsRNA:TLR3:TRIF:TRAF3
--
e43
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m44
0
infinite
0
--
--
e44
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeLumen
--
--
--
csml-variable:Double
m45
0
infinite
0
--
--
e45
cso30:c:EntityBiologicalCompartment
cso30:i:CC_EndosomeMembrane
--
--
--
csml-variable:Double
m46
0
infinite
0
--
--
e46
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Endosome
--
--
--
csml-variable:Double
m47
0
infinite
0
--
dsRNA:TLR7
--
e47
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m48
0
infinite
0
--
dsRNA:TLR9
--
e48
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m49
0
infinite
0
--
dsRNA:TLR9:MYD88
--
e49
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m63
0
infinite
0
--
(IRF-3{p})2
--
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
--
(IRF-3{p})2
--
e6
cso30:c:Complex
cso30:i:CC_Nucleoplasm
--
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
--
dsRNA:TLR9:MYD88:IRAK4
--
e63
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m64
0
infinite
0
--
IRAK1
--
e64
cso30:c:Protein
cso30:i:CC_Cytosol
--
csml-variable:Double
m65
0
infinite
0
--
dsRNA:TLR9:MYD88:IRAK4:IRAK1
--
e65
cso30:c:Complex
cso30:i:CC_Extracellular
--
csml-variable:Double
m66
0
infinite
0
--
dsRNA:TLR9:MYD88:IRAK4:IRAK1:TRAF6
--
e66
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m67
0
infinite
0
--
IRF-7{active}
--
e67
cso30:c:Protein
cso30:i:CC_CellComponent
--
csml-variable:Double
m68
10
infinite
0
TRANSPATH | MO000007702 |
--
dsRNA:TLR7:MYD88
--
e68
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m69
0
infinite
0
--
dsRNA:TLR7:MYD88:IRAK4
--
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
--
dsRNA:TLR7:MYD88:IRAK4:IRAK1
--
e70
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m71
0
infinite
0
--
dsRNA:TLR7:MYD88:IRAK4:IRAK1:TRAF6
--
e71
cso30:c:Complex
cso30:i:CC_Cytosol
--
csml-variable:Double
m72
0
infinite
0
--
--
e8
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cell_WithoutCellWall_
--
--
--
csml-variable:Double
m8
0
infinite
0
--
--
e9
cso30:c:EntityBiologicalCompartment
cso30:i:CC_Cytoplasm
--
--
--
csml-variable:Double
m9
0
infinite
0
--
p1
p1
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c5 : 1
stoichiometry:c7 : 1
stoichiometry:c2 : 1
m977*m3902*m119368*0.1
nodelay
--
0
PMID: 17395583, 9463386, 12692549, 9566918, 12702806 Transcriptional activity of IRF-3 is controlled by virus and dsRNA-induced, C-terminal phosphorylation events on serines 385 and 386, as well as the serine/threonine cluster between amino acids 396 and 405, mediated by the IKK-related kinases TBK-1 and IKK{epsilon}
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
m13*0.1
nodelay
--
0
PMID: 17395583, 10805757 Inactive IRF-3 constitutively shuttles into and out of the nucleus
p11
p11
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c27 : 1
stoichiometry:c29 : 1
stoichiometry:c28 : 1
m980*m1599*0.1
nodelay
--
0
PMID: 17395583, 12692549, 12702806 An important breakthrough in the understanding of innate immune response signaling was the demonstration that IRF-3 and IRF-7 are the primary in vivo targets of the IKK-related kinases, TBK-1/NAK/T2K and IKK{epsilon}/IKKi. PMID: 17395583, 15367631, 14679297 Both kinases directly phosphorylate IRF-3 and IRF-7 in their C-terminal signal-responsive domain
p12
p12
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c30 : 1
stoichiometry:c32 : 1
stoichiometry:c31 : 1
m980*m3902*0.1
nodelay
--
0
PMID: 17395583, 12692549, 12702806 An important breakthrough in the understanding of innate immune response signaling was the demonstration that IRF-3 and IRF-7 are the primary in vivo targets of the IKK-related kinases, TBK-1/NAK/T2K and IKK{epsilon}/IKKi. PMID: 17395583, 15367631, 14679297 Both kinases directly phosphorylate IRF-3 and IRF-7 in their C-terminal signal-responsive domain
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c36 : 1
stoichiometry:c33 : 1
m14*0.1
nodelay
--
0
PMID: 17395583, 10924517 IFN and lipopolysaccharide treatment modulates transcription of the IRF-7 gene.
p14
p14
cso30:i:ME_Transcription
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c35 : 1
stoichiometry:c34 : 1
m155666*0.1
nodelay
--
0
PMID: 17395583, 10924517 IFN and lipopolysaccharide treatment modulates transcription of the IRF-7 gene.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c38 : 1
stoichiometry:c37 : 1
m11*0.1
nodelay
--
0
PMID: 17395583, 10938111 Human IFN-beta, IFN-{alpha}1, and RANTES (regulated on activation normal T cell expressed and secreted) promoters are stimulated by IRF-3 coexpression, whereas IFN-{alpha}4, -{alpha}7, and -{alpha}14 promoters are preferentially induced by IRF-7 only.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c40 : 1
stoichiometry:c39 : 1
m11*0.1
nodelay
--
0
PMID: 17395583, 10938111 Human IFN-beta, IFN-{alpha}1, and RANTES (regulated on activation normal T cell expressed and secreted) promoters are stimulated by IRF-3 coexpression, whereas IFN-{alpha}4, -{alpha}7, and -{alpha}14 promoters are preferentially induced by IRF-7 only.
p17
p17
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c42 : 1
stoichiometry:c41 : 1
m19325*0.1
nodelay
--
0
PMID: 17395583, 10938111 Human IFN-beta, IFN-{alpha}1, and RANTES (regulated on activation normal T cell expressed and secreted) promoters are stimulated by IRF-3 coexpression, whereas IFN-{alpha}4, -{alpha}7, and -{alpha}14 promoters are preferentially induced by IRF-7 only.
p18
p18
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c44 : 1
stoichiometry:c43 : 1
m19325*0.1
nodelay
--
0
PMID: 17395583, 10938111 Human IFN-beta, IFN-{alpha}1, and RANTES (regulated on activation normal T cell expressed and secreted) promoters are stimulated by IRF-3 coexpression, whereas IFN-{alpha}4, -{alpha}7, and -{alpha}14 promoters are preferentially induced by IRF-7 only.
p19
p19
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c46 : 1
stoichiometry:c45 : 1
m19325*0.1
nodelay
--
0
PMID: 17395583, 10938111 Human IFN-beta, IFN-{alpha}1, and RANTES (regulated on activation normal T cell expressed and secreted) promoters are stimulated by IRF-3 coexpression, whereas IFN-{alpha}4, -{alpha}7, and -{alpha}14 promoters are preferentially induced by IRF-7 only.
p2
p2
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c3 : 1
stoichiometry:c6 : 1
stoichiometry:c8 : 1
stoichiometry:c4 : 1
m977*m1599*m119368*0.1
nodelay
--
0
PMID: 17395583, 9463386, 12692549, 9566918, 12702806 Transcriptional activity of IRF-3 is controlled by virus and dsRNA-induced, C-terminal phosphorylation events on serines 385 and 386, as well as the serine/threonine cluster between amino acids 396 and 405, mediated by the IKK-related kinases TBK-1 and IKK{epsilon}
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c47 : 1
stoichiometry:c48 : 1
stoichiometry:c49 : 1
m977*m19*0.1
nodelay
--
0
PMID: 17395583, 17015689 IRF-3 is recruited to Cullin1 following virus infection, and expression of a dominant-negative Cullin1 inhibits IRF-3 degradation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c50 : 1
stoichiometry:c51 : 1
m20*0.1
nodelay
--
0
PMID: 17395583, 17015689, 9566918 IRF-3 is targeted for proteasomal degradation (9) following virus infection, and polyubiquitination is required for IRF-3 degradation.
p22
p22
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c52 : 1
stoichiometry:c53 : 1
stoichiometry:c54 : 1
m21*0.1
nodelay
--
0
p23
p23
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c55 : 1
stoichiometry:c56 : 1
stoichiometry:c57 : 1
m19324*m2065*0.1
nodelay
--
0
PMID: 17395583 After stimulation by dsRNA, phosphorylation of the Ser339?Pro340 motif of IRF-3 results in the interaction with Pin1, polyubiquitination, and then proteasome-dependent degradation of IRF-3
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c58 : 1
stoichiometry:c66 : 1
stoichiometry:c59 : 1
m22*0.1
nodelay
--
0
PMID: 17395583 After stimulation by dsRNA, phosphorylation of the Ser339?Pro340 motif of IRF-3 results in the interaction with Pin1, polyubiquitination, and then proteasome-dependent degradation of IRF-3 PMID: 17395583 ISGylation subverts ubiquitin-mediated degradation of IRF-3 and enhances IRF-3-dependent gene activity
p25
p25
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c60 : 1
stoichiometry:c61 : 1
stoichiometry:c62 : 1
m23*0.1
nodelay
--
0
PMID: 17395583 After stimulation by dsRNA, phosphorylation of the Ser339?Pro340 motif of IRF-3 results in the interaction with Pin1, polyubiquitination, and then proteasome-dependent degradation of IRF-3
p26
p26
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c63 : 1
stoichiometry:c64 : 1
stoichiometry:c65 : 1
m43938*m19324*0.1
nodelay
--
0
PMID: 17395583 IRF-3 can also be stabilized in infected cells; both IFN treatment and RNA virus infection increase conjugation of the IFN-induced, ubiquitin-like protein ISG15 to IRF-3.
p27
p27
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c67 : 1
stoichiometry:c68 : 1
stoichiometry:c69 : 1
m119368*m41844*0.1
nodelay
--
0
PMID: 17395583, 15208624, 15563593 Antiviral immune responses can be triggered by dsRNA and the 5'-triphosphate RNA structure of viral nucleic acids.These structures are "sensed" by the cytoplasmic RNA helicase proteins RIG-I and MDA5
p28
p28
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c70 : 1
stoichiometry:c71 : 1
stoichiometry:c72 : 1
m119368*m76904*0.1
nodelay
--
0
PMID: 17395583, 15208624, 15563593 Antiviral immune responses can be triggered by dsRNA and the 5'-triphosphate RNA structure of viral nucleic acids.These structures are "sensed" by the cytoplasmic RNA helicase proteins RIG-I and MDA5
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c73 : 1
stoichiometry:c74 : 1
stoichiometry:c75 : 1
m25*m68199*0.1
nodelay
--
0
PMID: 17395583, 16177806, 16153868, 16125763, 16127453, 15563593 The protein responsible for downstream signaling is a mitochondrial adapter, known as MAVS/IPS-1/ VISA/Cardif that interacts with RIG-I via CARD domain interactions.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c9 : 1
stoichiometry:c10 : 1
m19324*0.1
nodelay
--
0
PMID: 17395583, 10082512 Based on available biochemical data, a model for IRF-3 activation proposes that C-terminal phosphorylation induces a conformational change in IRF-3 that allows homo- and heterodimerization, nuclear localization, and association with the co-activator CBP/p300.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c76 : 1
stoichiometry:c77 : 1
stoichiometry:c78 : 1
m26*m68199*0.1
nodelay
--
0
PMID: 17395583, 16177806, 16153868, 16125763, 16127453, 15563593 The protein responsible for downstream signaling is a mitochondrial adapter, known as MAVS/IPS-1/ VISA/Cardif that interacts with RIG-I via CARD domain interactions.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c79 : 1
stoichiometry:c80 : 1
stoichiometry:c81 : 1
m41844*m29*0.1
nodelay
--
0
PMID: 17395583, 17190814 LGP2 was shown to interact directly with RIG-I to block RIG-I dimerization and downstream signaling to the IFN response.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c82 : 1
stoichiometry:c83 : 1
stoichiometry:c84 : 1
m1872*m27*0.1
nodelay
--
0
PMID: 17395583 MAVS links RIG-I and MDA5 to TRAF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c85 : 1
stoichiometry:c86 : 1
stoichiometry:c87 : 1
m28*m1872*0.1
nodelay
--
0
PMID: 17395583 MAVS links RIG-I and MDA5 to TRAF3.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c88 : 1
stoichiometry:c89 : 1
stoichiometry:c90 : 1
m1599*m31*0.1
nodelay
--
0
PMID: 17395583 TRAF-dependent induction of the kinases JNK, IKK{alpha}, IKKbeta, IKK{epsilon}, TBK-1, and IRAK1 induce the binding of ATF2-c-Jun, NF-{kappa}B (p50-p65 complex), IRF-3, and IRF-7 to sequence-specific PRDs located in the IFN-beta enhancer.
p35
p35
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c91 : 1
stoichiometry:c93 : 1
stoichiometry:c92 : 1
m34*m33*0.1
nodelay
--
0
PMID: 17395583 TRAF-dependent induction of the kinases JNK, IKK{alpha}, IKKbeta, IKK{epsilon}, TBK-1, and IRAK1 induce the binding of ATF2-c-Jun, NF-{kappa}B (p50-p65 complex), IRF-3, and IRF-7 to sequence-specific PRDs located in the IFN-beta enhancer.
p36
p36
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c94 : 1
stoichiometry:c96 : 1
stoichiometry:c95 : 1
m207*m33*0.1
nodelay
--
0
PMID: 17395583 TRAF-dependent induction of the kinases JNK, IKK{alpha}, IKKbeta, IKK{epsilon}, TBK-1, and IRAK1 induce the binding of ATF2-c-Jun, NF-{kappa}B (p50-p65 complex), IRF-3, and IRF-7 to sequence-specific PRDs located in the IFN-beta enhancer.
p37
p37
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c97 : 1
stoichiometry:c99 : 1
stoichiometry:c98 : 1
m37*m33*0.1
nodelay
--
0
PMID: 17395583 TRAF-dependent induction of the kinases JNK, IKK{alpha}, IKKbeta, IKK{epsilon}, TBK-1, and IRAK1 induce the binding of ATF2-c-Jun, NF-{kappa}B (p50-p65 complex), IRF-3, and IRF-7 to sequence-specific PRDs located in the IFN-beta enhancer.
p38
p38
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c100 : 1
stoichiometry:c102 : 1
stoichiometry:c101 : 1
m31298*m35*0.1
nodelay
--
0
PMID: 17395583 TRAF-dependent induction of the kinases JNK, IKK{alpha}, IKKbeta, IKK{epsilon}, TBK-1, and IRAK1 induce the binding of ATF2-c-Jun, NF-{kappa}B (p50-p65 complex), IRF-3, and IRF-7 to sequence-specific PRDs located in the IFN-beta enhancer.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c103 : 1
stoichiometry:c105 : 1
stoichiometry:c104 : 1
m39*m36*0.1
nodelay
--
0
PMID: 17395583 TRAF-dependent induction of the kinases JNK, IKK{alpha}, IKKbeta, IKK{epsilon}, TBK-1, and IRAK1 induce the binding of ATF2-c-Jun, NF-{kappa}B (p50-p65 complex), IRF-3, and IRF-7 to sequence-specific PRDs located in the IFN-beta enhancer.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c11 : 1
stoichiometry:c12 : 1
m5*0.1
nodelay
--
0
PMID: 17395583, 10082512 Based on available biochemical data, a model for IRF-3 activation proposes that C-terminal phosphorylation induces a conformational change in IRF-3 that allows homo- and heterodimerization, nuclear localization, and association with the co-activator CBP/p300.
p40
p40
cso30:i:ME_DNABinding
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c106 : 1
stoichiometry:c108 : 1
stoichiometry:c109 : 1
stoichiometry:c110 : 1
stoichiometry:c111 : 1
stoichiometry:c107 : 1
m41*m40*m38*m13*m19325*0.1
nodelay
--
0
PMID: 17395583 TRAF-dependent induction of the kinases JNK, IKK{alpha}, IKKbeta, IKK{epsilon}, TBK-1, and IRAK1 induce the binding of ATF2-c-Jun, NF-{kappa}B (p50-p65 complex), IRF-3, and IRF-7 to sequence-specific PRDs located in the IFN-beta enhancer.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c112 : 1
stoichiometry:c113 : 1
m42*0.1
nodelay
--
0
PMID: 17395583 Coordinated assembly of these factors forms the IFN-beta enhanceosome, which is responsible for the transcriptional induction of this antiviral cytokine.
p42
p42
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c114 : 1
stoichiometry:c115 : 1
stoichiometry:c116 : 1
m3965*m119368*0.1
nodelay
--
0
PMID: 17395583 Viral pathogen-associated molecular patterns trigger multiple signaling cascades through Toll-like receptor-dependent (TLR-3, TLR-7, and TLR-9) and -independent (RIG-I and MDA5) pathways leading to kinase activation through TRAF family members.
p43
p43
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c117 : 1
stoichiometry:c119 : 1
stoichiometry:c118 : 1
m19314*m18998*0.1
nodelay
--
0
PMID: 17395583 Viral pathogen-associated molecular patterns trigger multiple signaling cascades through Toll-like receptor-dependent (TLR-3, TLR-7, and TLR-9) and -independent (RIG-I and MDA5) pathways leading to kinase activation through TRAF family members.
p44
p44
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c120 : 1
stoichiometry:c121 : 1
stoichiometry:c122 : 1
m19305*m183*0.1
nodelay
--
0
PMID: 17395583 Viral pathogen-associated molecular patterns trigger multiple signaling cascades through Toll-like receptor-dependent (TLR-3, TLR-7, and TLR-9) and -independent (RIG-I and MDA5) pathways leading to kinase activation through TRAF family members.
p45
p45
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c123 : 1
stoichiometry:c124 : 1
stoichiometry:c125 : 1
m19305*m1872*0.1
nodelay
--
0
PMID: 17395583 Viral pathogen-associated molecular patterns trigger multiple signaling cascades through Toll-like receptor-dependent (TLR-3, TLR-7, and TLR-9) and -independent (RIG-I and MDA5) pathways leading to kinase activation through TRAF family members.
p46
p46
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c126 : 1
stoichiometry:c128 : 1
stoichiometry:c127 : 1
m37*m44*0.1
nodelay
--
0
PMID: 17395583 Viral pathogen-associated molecular patterns trigger multiple signaling cascades through Toll-like receptor-dependent (TLR-3, TLR-7, and TLR-9) and -independent (RIG-I and MDA5) pathways leading to kinase activation through TRAF family members.
p47
p47
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c129 : 1
stoichiometry:c131 : 1
stoichiometry:c130 : 1
m207*m43*0.1
nodelay
--
0
PMID: 17395583 Viral pathogen-associated molecular patterns trigger multiple signaling cascades through Toll-like receptor-dependent (TLR-3, TLR-7, and TLR-9) and -independent (RIG-I and MDA5) pathways leading to kinase activation through TRAF family members.
p48
p48
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c133 : 1
stoichiometry:c134 : 1
m19940*m119368*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
p49
p49
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c135 : 1
stoichiometry:c136 : 1
stoichiometry:c137 : 1
m19828*m119368*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c15 : 1
stoichiometry:c14 : 1
m6*m2282*0.1
nodelay
--
0
PMID: 17395583, 10082512 Based on available biochemical data, a model for IRF-3 activation proposes that C-terminal phosphorylation induces a conformational change in IRF-3 that allows homo- and heterodimerization, nuclear localization, and association with the co-activator CBP/p300.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c138 : 1
stoichiometry:c139 : 1
stoichiometry:c140 : 1
m1572*m49*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c141 : 1
stoichiometry:c143 : 1
stoichiometry:c142 : 1
m63*m17258*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c144 : 1
stoichiometry:c145 : 1
stoichiometry:c146 : 1
m64*m65*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c147 : 1
stoichiometry:c148 : 1
stoichiometry:c149 : 1
m66*m183*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
p54
p54
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c150 : 1
stoichiometry:c152 : 1
stoichiometry:c151 : 1
m980*m67*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
p55
p55
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c153 : 1
stoichiometry:c166 : 1
stoichiometry:c154 : 1
m980*m72*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c155 : 1
stoichiometry:c156 : 1
stoichiometry:c157 : 1
m48*m1572*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c158 : 1
stoichiometry:c159 : 1
stoichiometry:c160 : 1
m69*m17258*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c161 : 1
stoichiometry:c162 : 1
stoichiometry:c163 : 1
m70*m65*0.1
nodelay
--
0
PMID: 17395583 In plasmacytoid dendritic cells, TLR-7 or TLR-9 engagement leads to direct activation of IRF-7 through MyD88/TRAF6/IRAK4/IRAK1 recruitment.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c164 : 1
stoichiometry:c165 : 1
stoichiometry:c167 : 1
m183*m71*0.1
nodelay
--
0
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c17 : 1
stoichiometry:c18 : 1
m6*m4512*0.1
nodelay
--
0
PMID: 17395583, 10082512 Based on available biochemical data, a model for IRF-3 activation proposes that C-terminal phosphorylation induces a conformational change in IRF-3 that allows homo- and heterodimerization, nuclear localization, and association with the co-activator CBP/p300.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c20 : 1
m11*0.1
nodelay
--
0
PMID: 17395583, 10805757 phosphorylation-dependent association with CBP/p300 retains IRF-3 in the nucleus and induces transcription of IFN-beta and other genes. PMID: 17395583, 10938111 Human IFN-beta, IFN-{alpha}1, and RANTES (regulated on activation normal T cell expressed and secreted) promoters are stimulated by IRF-3 coexpression, whereas IFN-{alpha}4, -{alpha}7, and -{alpha}14 promoters are preferentially induced by IRF-7 only. PMID: 17395583 IRF-3 possesses a restricted DNA binding site specificity and interacts with CBP.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c21 : 1
stoichiometry:c22 : 1
m12*0.1
nodelay
--
0
PMID: 17395583, 10805757 phosphorylation-dependent association with CBP/p300 retains IRF-3 in the nucleus and induces transcription of IFN-beta and other genes. PMID: 17395583, 10938111 Human IFN-beta, IFN-{alpha}1, and RANTES (regulated on activation normal T cell expressed and secreted) promoters are stimulated by IRF-3 coexpression, whereas IFN-{alpha}4, -{alpha}7, and -{alpha}14 promoters are preferentially induced by IRF-7 only.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m977*0.1
nodelay
--
0
PMID: 17395583, 10805757 Inactive IRF-3 constitutively shuttles into and out of the nucleus
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c: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: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:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c: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:InputProcess
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: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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c: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:OutputProcess
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:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--