This Reactome event shows phosphorylation of IKK beta (IKBKB) by TGF-\u03b2\u2013activated kinase 1 (TAK1), encoded by the MAP3K7 gene. TAK1 functions downstream of receptor signaling complexes in TLR, TNF-alpha and IL-1 signaling pathways (Xu & Lei 2021). TAK1 appears to be essential for IL-1-induced NF-kappa-B activation since a specific TAK1 inhibitor (5Z)-7-oxozeaenol prevents NF-kappa-B activation in human umbilical vein endothelial cells (HUVEC) (Lammel 2020); also, it prevents NF-kappa-B-mediated TNF production in human myeloid leukaemia U937 cells (Rawlins et al. 1999). TAK1 functions through assembling the TAK1 complex consisting of the coactivators TAB1 and either TAB2 or TAB3 (Shibuya et al. 1996, Sakurai et al. 2000; Xu & Lei 2021). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe (Sakurai et al. 2000; Brown et al. 2005). The TAK1 complex is regulated by polyubiquitination. The binding of TAB2 or TAB3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2, -3 by TRAF6 (Ishitani et al. 2003), which in turn results in conformational changes within the TAK1 complex. TAB2 or -3 is recruited to K63-linked polyubiquitin chains of receptor interacting protein (RIP) kinase RIP1 (RIPK1) via the Zinc finger domain of TAB2 or TAB3. RIPK1 functions as an essential component of inflammatory and immune signaling pathways. Ubiquitination of RIPK1 follows the recruitment of TRADD and TRAF2 or -5 (the latter functions as the E3 ubiquitin ligase, but also cIAP1,-2 can ubiquitinate RIPK1 as a response to TNF receptor engagement (Varfolomeev et al. 2008). The IKK complex is also recruited ubiquitin (Ub) chains via its Ub binding domain. Polyubiquitin chains may function as a scaffold for higher order signaling complexes bringing the TAK1 and IKK complexes in close proximity and allowing TAK1 to phosphorylate IKBKB (IKK2) (Kanayama et al. 2004).
The alternative (non-canonical) pathway can be activated via CD40, LT\u00dfR, BAFF, RANK, and is therefore limited to cells which express these receptors. It leads to NIK-mediated phosphorylation of IKKa (IKK1, CHUK), which phosphorylates the NFKB2 (p52) precursor p100, leading to the ubiquitin-dependent degradation of its C-terminal part (processing of p100 to the mature p52 subunit) and releasing the NFKB2:RelB complex (Sun 2017). In non-stimulated cells NIK is constitutively degraded by the cIAP1/2:TRAF2:TRAF3 Ub ligase complex; following stimulation, the complex is recruited to the respective receptor comlex where cIAPs ubiquitinates TRAF3, resulting it its degradation and stabilization of NIK. NIK then phosphorylates and activates IKK1 (CHUK), leading to the NFKB2:RelB complex activation (Sun 2017). TRAF3 deubiquitylation by OTUD7B downregulates the NIK-mediated NF-kappa-B activation. (Hu et al 2013). In addition, TAK1 has been shown to interact with NIK and with IKK2, and TAK1 can be stimulated by anti-apoptotic protein, XIAP (Hofer-Warbinek et al. 2000). XIAP is an NF-kB dependent gene, therefore its expression represents a positive regulatory circuit. NIK is also involved in the classical pathway, and is activated by TAK1 in the IL-1 signalling pathway (Ninomiya-Tsui et al. 1999) and Hemophilus influenzae-induced TLR2 signalling pathway (Shuto et al. 2001).
RNA-induced liquid phase separation of SARS-CoV-2 nucleocapsid (N) protein serves as a platform to enhance the interaction between TAK1 and IKK complexes promoting NF-kappa-B-dependent inflammatory responses (Wu Y et al. 2021).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-202513"
],
"enzyme_list": [
"O43318-1",
"O15111-1",
"Q9Y4K3-1",
"O14920-1",
"O43353-1",
"P61088-1",
"P51617-1"
],
"evidence": [
{
"id": "R-HSA-168184",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-168184"
}
]
},
{
"id": "R-HSA-177690",
"name": "Activated TLR3:TRIF:K63pUb-TRAF6 recruits TAK1complex",
"equation": "",
"summary": "TAK1-binding protein 2 (TAB2) and/or TAB3, as part of a complex that also contains TAK1 and TAB1, binds polyubiquitinated TRAF6. The TAB2 and TAB3 regulatory subunits of the TAK1 complex contain C-terminal Npl4 zinc finger (NZF) motifs that recognize with Lys63-pUb chains (Kanayama et al. 2004). The recognition mechanism is specific for Lys63-linked ubiquitin chains [Kulathu Y et al 2009]. TAK1 can be activated by unattached Lys63-polyubiquitinated chains when TRAF6 has no detectable polyubiquitination (Xia et al. 2009) and thus the synthesis of these chains by TRAF6 may be the signal transduction mechanism.This binding leads to autophosphorylation and activation of TAK1.",
"cellular_location": "cytosol, endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1"
],
"evidence": [
{
"id": "R-HSA-177690",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-177690"
}
]
},
{
"id": "R-HSA-177692",
"name": "Activation of recruited TAK1 within the activated TLR3 complex",
"equation": "",
"summary": "TAK1 complex consists of transforming growth factor-beta (TGFB)-activated kinase (TAK1) and TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAK1 requires TAB1 for its kinase activity (Shibuya et al. 1996, Sakurai et al. 2000). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001). The TAK1 complex is regulated by polyubiquitination. Binding of TAB2 and TAB3 to Lys63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Binding of multiple TAK1 complexes to the same polyubiquitin chain may promote oligomerization of TAK1, facilitating TAK1 autophosphorylation and subsequent activation of its kinase activity (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that lead to TAK1 activation. Another possibility is that TAB2/3 may recruit the IKK complex by binding to ubiquitinated NEMO; polyubiquitin chains may function as a scaffold for higher order signaling complexes that allow interaction between TAK1 and IKK (Kanayama et al. 2004).",
"cellular_location": "cytosol, endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1"
],
"evidence": [
{
"id": "R-HSA-177692",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-177692"
}
]
},
{
"id": "R-HSA-202500",
"name": "Activation of IKK complex",
"equation": "",
"summary": "The IkB kinase (IKK) complex serves as the master regulator for the activation of NF-kB by various stimuli. It contains two catalytic subunits, IKK alpha and IKK beta, and a regulatory subunit, IKKgamma/NEMO. The activation of IKK complex is dependent on the phosphorylation of IKK alpha/beta at its activation loop and the K63-linked ubiquitination of NEMO. This basic trimolecular complex is referred to as the IKK complex.
IKK subunits have a N-term kinase domain a leucine zipper (LZ) motifs, a helix-loop-helix (HLH) and a C-ter NEMO binding domain (NBD). IKK catalytic subunits are dimerized through their LZ motifs. IKK beta is the major IKK catalytic subunit for NF-kB activation. Activated TAK1 phosphorylate IKK beta on serine residues (S177 and S181) in the activation loop and thus activate the IKK kinase activity, leading to the IkB alpha phosphorylation and NF-kB activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"O15530-1",
"O15111-1",
"Q9Y4K3-1",
"O14920-1",
"Q9UDY8-1"
],
"evidence": [
{
"id": "R-HSA-202500",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202500"
}
]
},
{
"id": "R-HSA-202510",
"name": "Activation of TAK1-TAB2 complex",
"equation": "",
"summary": "Ubiquitinated TRAF6 recruits TAB2 and activates the TAB2-associated TAK1 kianse by promoting the autophosphorylation of TAK1. TAB2 contains an N-term pseudophosphatase domain, which is indispensable for TAK1 activation, and a C-term domain that binds to and activates TAK1. The activation of TAK1/TAB2 complex requires a ubiquitination reaction catalysed by E1, Ubc13/Uev1A (E2) and TRAF6 (E3). TAK1 undergoes autophosphorylation on residues T184 and T187 and gets activated. Activated TAK1 then phosphorylates and activates IKK beta.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"O15530-1",
"Q9Y4K3-1",
"Q9UDY8-1"
],
"evidence": [
{
"id": "R-HSA-202510",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202510"
}
]
},
{
"id": "R-HSA-2730861",
"name": "Recruitment of TAK1 kinase complex to oligo-K63-pUb-TRAF6",
"equation": "",
"summary": "K-63 linked polyubiquitin (pUb) chain on TRAF6 provides a scaffold to recruit downstream effector molecules to activate NF-kB. Transforming growth factor beta-activated kinase 1 (TAK1) is a member of the mitogen-activated protein kinase (MAPK) kinase kinase family is shown to be an essential intermediate that transmits the upstream signals from the receptor complex to the downstream MAPKs and to the NF-kB pathway (Broglie et al. 2009). TAK1-binding protein 1 (TAB1), TAB2 and TAB3 constitutively bound to TAK1. TAB1 acts as the activation subunit of the TAK1 complex, aiding in the autophosphorylation of TAK1, whereas TAB2 and its homologue TAB3, act as a adaptors of TAK1 that facilitate the assembly of TAK1 complex to TRAF6. The highly conserved C-terminal zinc finger domain of TAB2 and TAB3 binds preferentially to the K-63-linked polyubiquitin chains on TRAF6 (Broglie et al. 2009, Besse et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1",
"Q9UDY8-1",
"Q04759-1"
],
"evidence": [
{
"id": "R-HSA-2730861",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730861"
}
]
},
{
"id": "R-HSA-2730876",
"name": "Phosphorylation of IKK-beta by TAK1",
"equation": "",
"summary": "In humans, the IkB kinase (IKK) complex serves as the master regulator for the activation of NF-kB by various stimuli. It contains two catalytic subunits, IKK alpha and IKK beta, and a regulatory subunit, IKKgamma/NEMO. The activation of IKK complex is dependent on the phosphorylation of IKK alpha/beta at its activation loop and the K63-linked ubiquitination of NEMO. This basic trimolecular complex is referred to as the IKK complex.
IKK subunits have a N-term kinase domain a leucine zipper (LZ) motifs, a helix-loop-helix (HLH) and a C-ter NEMO binding domain (NBD). IKK catalytic subunits are dimerized through their LZ motifs. IKK beta is the major IKK catalytic subunit for NF-kB activation. Activated TAK1 phosphorylate IKK beta on S177 and S181 (S176 and S180 in IKK alpha) in the activation loop and thus activate the IKK kinase activity, leading to the IkB alpha phosphorylation and NF-kB activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"O15111-1",
"Q9Y4K3-1",
"O14920-1",
"Q9UDY8-1",
"Q04759-1"
],
"evidence": [
{
"id": "R-HSA-2730876",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730876"
}
]
},
{
"id": "R-HSA-2730900",
"name": "Activation of TAK1 complex bound to pUb-TRAF6",
"equation": "",
"summary": "Binding of TAB2 and TAB3 to K63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Phosphorylation of TAK1 within the activation loop of the kinase is absolutely required for TAK1 activity. TAB1 is known to augment TAK1 catalytic activity by mediating spontaneous oligomerization and induces autophosphorylation of TAK1 (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that leads to the activation of TAK1. Some biochemical studies revealed that free K63 polyubiquitin chains, which are not conjugated to any cellular protein, can directly activate the TAK1 kinase complex (Xia et al. 2009).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1",
"Q9UDY8-1",
"Q04759-1"
],
"evidence": [
{
"id": "R-HSA-2730900",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2730900"
}
]
},
{
"id": "R-HSA-4332356",
"name": "CAMK2 binds MAP3K7",
"equation": "",
"summary": "Several studies in C. elegans and vertebrates suggest that a TAK1-NLK kinase cascade regulates the activity of the canonical WNT signaling pathway (Ishitani et al, 1999; Meneghini et al, 1999; Shin et al, 1999; Rocheleau et al, 1999). Activation of this MAPK cascade depends on CAMK2 activity downstream of WNT5a non-canonical signaling (Ishitani et al, 2003a, b). CAMK2 co-precipitates with TAK1/MAP3K7 upon co-transfection in HEK293 cells and calcium signaling activates MAP3K7 in a CAMK2-dependent manner (Ishitani et al, 2003a).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9UQM7-1"
],
"evidence": [
{
"id": "R-HSA-4332356",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4332356"
}
]
},
{
"id": "R-HSA-4332388",
"name": "Activation of MAP3K7 in response to WNT",
"equation": "",
"summary": "Endogenous MAP3K7 is phosphorylated in a CAMK2-dependent fashion upon co-expression of WNT5A or after stimulation of calcium signaling (Ishitani et al, 2003a). Despite evidence that co-precipitated MAP3K7 is phosphorylated in vitro in the presence of CAMK2, direct phosphorylation of MAP3K7 by CAMK2 using purified proteins has not been demonstrated (Ishitani et al, 2003a). The roles of polyubiquitination and accessory proteins TAB1, 2 or 3 in MAP3K7 activation have not been investigated in the context of non-canonical WNT signaling and are therefore omitted from this reaction (reviewed in Dai et al, 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-206014"
],
"enzyme_list": [
"O43318-1",
"Q9UQM7-1"
],
"evidence": [
{
"id": "R-HSA-4332388",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4332388"
}
]
},
{
"id": "R-HSA-4411402",
"name": "Activation of NLK",
"equation": "",
"summary": "NLK is activated in response to WNT5A in a CAMK2- and MAP3K7- dependent manner (Ishitani et al, 1999; Ishitani et al, 2003a,b). Homodimerization is required for NLK autophosphorylation at T298 and subsequent nuclear localization; mutation of C437 abolishes dimerization, kinase activity and nuclear translocation (Ishitani et al, 2011).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBE8-1",
"O43318-1"
],
"evidence": [
{
"id": "R-HSA-4411402",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4411402"
}
]
},
{
"id": "R-HSA-446870",
"name": "Polyubiquitinated TRAF6 binds the TAK1 complex",
"equation": "",
"summary": "TAK1-binding protein 2 (TAB2) and/or TAB3, as part of a complex that also contains TAK1 and TAB1, binds polyubiquitinated TRAF6. The TAB2 and TAB3 regulatory subunits of the TAK1 complex contain C-terminal Npl4 zinc finger (NZF) motifs that recognize with Lys63-pUb chains (Kanayama et al. 2004). The recognition mechanism is specific for Lys63-linked ubiquitin chains (Kulathu Y et al 2009). TAK1 can be activated by unattached Lys63-polyubiquitinated chains when TRAF6 has no detectable polyubiquitination (Xia et al. 2009) and thus the synthesis of these chains by TRAF6 may be the signal transduction mechanism.
As a de-ubiquitinating/de-ISGylating enzyme, severe acute respiratory syndrome coronavirus type 1 (SARS-CoV-1) 1a-encoded papain-like protease (PLPro or nsp3) antagonizes the host type I interferon (IFN) response by removing Lys63-linked ubiquitin chains of TRAF3 and TRAF6 (Li SW et al. 2016).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q9Y4K3-1", "P51617-1" ], "evidence": [ { "id": "R-HSA-446870", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-446870" } ] }, { "id": "R-HSA-450187", "name": "TAK1 is activated within the TAK1 complex", "equation": "", "summary": "The TAK1 complex consists of Transforming growth factor-beta (TGFB)-activated kinase (TAK1) and TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAK1 requires TAB1 for its kinase activity (Shibuya et al. 1996, Sakurai et al. 2000). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001). The TAK1 complex is regulated by polyubiquitination. Binding of TAB2 and TAB3 to Lys63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Binding of multiple TAK1 complexes to the same polyubiquitin chain may promote oligomerization of TAK1, facilitating TAK1 autophosphorylation and subsequent activation of its kinase activity (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that lead to TAK1 activation. Another possibility is that TAB2/3 may recruit the IKK complex by binding to ubiquitinated NEMO; polyubiquitin chains may function as a scaffold for higher order signaling complexes that allow interaction between TAK1 and IKK (Kanayama et al. 2004).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q9Y4K3-1", "P61088-1", "P51617-1" ], "evidence": [ { "id": "R-HSA-450187", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-450187" } ] }, { "id": "R-HSA-450337", "name": "Activated TAK1 phosphorylates MKK4/MKK7", "equation": "", "summary": "In human, phosphorylation of MKK4 (MAP2K4) and MKK7 (MAP2K7) by TAK1 occurs at the typical Ser-Xaa-Ala-Xaa-Thr motif in their activation loops.
Residues involved in activation of these protein kinases correspond to human Ser271, Thr275 in MKK7 and Ser257, Thr261 in MKK4.
Cell lines lacking MKK4 exhibit defective activation of JNK and AP-1 dependent transcription activity in response to some cellular stresses; JNK and p38 MAPK activities were decreased by around 80% and 20%, respectively, following deletion of the mkk4 gene.", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14733-1", "O43318-1", "Q9Y4K3-1", "O43353-1", "P61088-1", "P45985-1", "P51617-1" ], "evidence": [ { "id": "R-HSA-450337", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-450337" } ] }, { "id": "R-HSA-450346", "name": "activated human TAK1 phosphorylates MKK3/MKK6", "equation": "", "summary": "Human MKK3 (MAP2K4) and MKK6 (MAP2K6) are two closely related dual-specificity protein kinases. Both are activated by cellular stress and inflammatory cytokines, and both phosphorylate and activate p38 MAP kinase at its activation site Thr-Gly-Tyr but do not phosphorylate or activate Erk1/2 or SAPK/JNK.
Activation of MKK3 and MKK6 occurs through phosphorylation of serine and threonine residues at the typical Ser-Xaa-Ala-Xaa-Thr motif in their activation loop. Residues involved into these protein kinases activation correspond to human sites Ser189 and Thr193 for MKK3 and Ser207 and Thr211 for MKK6 .",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1",
"O43353-1",
"P61088-1",
"P52564-1",
"P46734-1",
"P51617-1"
],
"evidence": [
{
"id": "R-HSA-450346",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-450346"
}
]
},
{
"id": "R-HSA-5357860",
"name": "TNF:TNFR1:TRADD:TRAF2:K63polyUb-RIPK1:BIRC2/3:LUBAC recruits TAK1 complex",
"equation": "",
"summary": "Polyubiquitinated RIPK1 binds to TAB2 resulting in the recruitment of the TAB2:TAK1 complex. The K63-linked ubiqitination on Lys377 of RIPK1 was shown to mediate the association of RIPK1 with the TAB2:TAK1 complex (Li H et al. 2006)",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q96EP0-1",
"Q9BYM8-1",
"Q5VV17-1",
"O43318-1",
"Q12933-1",
"Q13107-1",
"O75604-1",
"P98170-1",
"Q13546-1",
"P21580-1",
"Q13490-1",
"Q13489-1",
"Q6GQQ9-1",
"Q9NQC7-1",
"Q9UK80-1"
],
"evidence": [
{
"id": "R-HSA-5357860",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5357860"
}
]
},
{
"id": "R-HSA-5607732",
"name": "K63polyUb-TAK1 autophosphorylates",
"equation": "",
"summary": "TAK1-binding protein 1 (TAB1) is a TAK1-interacting protein and induces TAK1 (Transforming growth factor beta-associated kinase 1) kinase activity through promoting autophosphorylation of key serine/threonine sites of the kinase activation loop. There are four phosphorylation sites in the activation loop and analysis of these site mutants indicate that autophosphorylation of S192, is followed by sequential phosphorylation of T178, T187, and finally T184 (Scholz et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1",
"Q9UDY8-1"
],
"evidence": [
{
"id": "R-HSA-5607732",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5607732"
}
]
},
{
"id": "R-HSA-5607742",
"name": "K63polyUb-p-3T,1S-TAK1 phosphorylates IKK-beta",
"equation": "",
"summary": "In humans, the IkB kinase (IKK) complex serves as the master regulator for the activation of NF-kB by various stimuli. It contains two catalytic subunits, IKK alpha and IKK beta, and a regulatory subunit, IKKgamma/NEMO. The activation of IKK complex is dependent on the phosphorylation of IKK alpha/beta at its activation loop and the K63-linked ubiquitination of NEMO. This basic trimolecular complex is referred to as the IKK complex.
IKK subunits have a N-term kinase domain a leucine zipper (LZ) motifs, a helix-loop-helix (HLH) and a C-ter NEMO binding domain (NBD). IKK catalytic subunits are dimerized through their LZ motifs. IKK beta is the major IKK catalytic subunit for NF-kB activation. Activated TAK1 phosphorylate IKK beta on S177 and S181 (S176 and S180 in IKK alpha) in the activation loop and thus activate the IKK kinase activity, leading to the IkB alpha phosphorylation and NF-kB activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"O15111-1",
"Q9Y4K3-1",
"O14920-1",
"Q9UDY8-1"
],
"evidence": [
{
"id": "R-HSA-5607742",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5607742"
}
]
},
{
"id": "R-HSA-5607757",
"name": "K63polyUb-TRAF6 ubiquitinates TAK1",
"equation": "",
"summary": "TAK1-binding protein 2 (TAB2), or its homologue TAB3, binds preferentially to K63-linked polyubiquitin chains in TRAF6 and links TRAF6 (TNF receptor-associated factor 6) to TAK1 (Transforming growth factor beta-associated kinase 1). TRAF6 ubiquitinates TAK1 on K34 and K158 and this triggers conformational changes in TAK1 that lead to autophosphorylation and activation (Fan et al. 2010, Hamidi et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1",
"Q9UDY8-1",
"P61088-1"
],
"evidence": [
{
"id": "R-HSA-5607757",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5607757"
}
]
},
{
"id": "R-HSA-5607759",
"name": "TRIKA2 binds K63polyUb-TRAF6 oligomer",
"equation": "",
"summary": "K-63 linked polyubiquitin (pUb) chain on TRAF6 provides a scaffold to recruit downstream effector molecules to activate NF-kB. Transforming growth factor beta-associated kinase 1 (TAK1) is a member of the mitogen-activated protein kinase (MAPK) kinase kinase family that is shown to be an essential intermediate that transmits the upstream signals from the receptor complex to the downstream MAPKs and to the NF-kB pathway (Broglie et al. 2009). As a member of the MAP3K family, TAK1 is unique in that its activity requires its binding proteins TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAB1 acts as the kinase subunit of the TAK1 complex, aiding in the autophosphorylation of TAK1, whereas TAB2 and its homologue TAB3, acts as an adaptor of TAK1 that facilitate the assembly of TAK1 complex to TRAF6 (Takaesu et al. 2000, Ishitani et al. 2003). This protein kinase complex containing the kinase subunit TAK1 and the regulatory subunits TAB1 and TAB2/TAB3 is also known as TRIKA2 (TRAF6-regulated IKK activator 2) (Adhikari et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1",
"Q9UDY8-1"
],
"evidence": [
{
"id": "R-HSA-5607759",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5607759"
}
]
},
{
"id": "R-HSA-5696534",
"name": "USP18 deubiquitinates TAK1:TAB1",
"equation": "",
"summary": "Ubiquitination plays a key role in the regulation of signaling via TAK1 (Chen 2012). USP18 catalyzes the deubiquitination of the TAK1:TAB1 complex, reversing TAK1 activating ubiquitination, which restricts activation of NF-kappaB, NFAT and JNK and in decreases the expression of IL2 in T cells after TCR activation (Liu et al. 2013).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9UMW8-1"
],
"evidence": [
{
"id": "R-HSA-5696534",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696534"
}
]
},
{
"id": "R-HSA-688985",
"name": "K63 polyubiquitinated RIP2 associates with the TAK1 complex",
"equation": "",
"summary": "K63-polyubiquitinated RIP2 is able to recruit the components of the TAK1 complex, which consists of TAK1, TAB1 and TAB2.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"O43353-1"
],
"evidence": [
{
"id": "R-HSA-688985",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-688985"
}
]
},
{
"id": "R-HSA-706479",
"name": "TAK1 is activated",
"equation": "",
"summary": "The TAK1 complex consists of Transforming growth factor-beta (TGFB)-activated kinase (TAK1) and TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAK1 requires TAB1 for its kinase activity (Shibuya et al. 1996, Sakurai et al. 2000). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001). The TAK1 complex is regulated by polyubiquitination. Binding of TAB2 and TAB3 to Lys63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Binding of multiple TAK1 complexes to the same polyubiquitin chain may promote oligomerization of TAK1, facilitating TAK1 autophosphorylation and subsequent activation of its kinase activity (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that lead to TAK1 activation. Another possibility is that TAB2/3 may recruit the IKK complex by binding to ubiquitinated NEMO; polyubiquitin chains may function as a scaffold for higher order signaling complexes that allow interaction between TAK1 and IKK (Kanayama et al. 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"O43353-1"
],
"evidence": [
{
"id": "R-HSA-706479",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-706479"
}
]
},
{
"id": "R-HSA-727819",
"name": "TAK1 phosphorylates MKK6",
"equation": "",
"summary": "Within the TAK1 complex (TAK1 plus TAB1 and TAB2/3) activated TAK1 phosphorylates IKKB, MAPK kinase 6 (MKK6) and other MAPKs to activate the NFkappaB and MAPK signaling pathways. TAB2 within the TAK1 complex can be linked to polyubiquitinated TRAF6; current models of IL-1 signaling suggest that the TAK1 complex is linked to TRAF6, itself complexed with polyubiquitinated IRAK1 which is linked via NEMO to the IKK complex. The TAK1 complex is also essential for NOD signaling; NOD receptors bind RIP2 which recruits the TAK1 complex (Hasegawa et al. 2008).",
"cellular_location": "cytosol",
"input_participant_list": [
"R-HSA-167998"
],
"output_participant_list": [
"R-HSA-206255"
],
"enzyme_list": [
"O43318-1",
"P52564-1"
],
"evidence": [
{
"id": "R-HSA-727819",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-727819"
}
]
},
{
"id": "R-HSA-847070",
"name": "Phosphorylated TAK1 dissociates from the TLR3 receptor complex",
"equation": "",
"summary": "Phosphorylated TAK1 complexed with TRAF6-TAB1-TAB2/TAB3 leaves the activated TLR4 complex and translocates to the cytosol",
"cellular_location": "cytosol, endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1"
],
"evidence": [
{
"id": "R-HSA-847070",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-847070"
}
]
},
{
"id": "R-HSA-936947",
"name": "Activated TLR4:TICAM1:K63pUb-TRAF6 recruits TAK1complex",
"equation": "",
"summary": "TAK1-binding protein 2 (TAB2) and/or TAB3, as part of a complex that also contains TAK1 and TAB1, binds polyubiquitinated TRAF6. The TAB2 and TAB3 regulatory subunits of the TAK1 complex contain C-terminal Npl4 zinc finger (NZF) motifs that recognize with Lys63-pUb chains (Kanayama et al. 2004). The recognition mechanism is specific for Lys63-linked ubiquitin chains (Kulathu Y et al 2009). TAK1 can be activated by unattached Lys63-polyubiquitinated chains when TRAF6 has no detectable polyubiquitination (Xia et al. 2009) and thus the synthesis of these chains by TRAF6 may be the signal transduction mechanism.
As a de-ubiquitinating/de-ISGylating enzyme, severe acute respiratory syndrome coronavirus type 1 (SARS-CoV-1) 1a-encoded papain-like protease (PLPro or nsp3) antagonizes the host type I interferon (IFN) response by removing Lys63-linked ubiquitin chains of TRAF3 and TRAF6 (Li SW et al. 2016).", "cellular_location": "cytosol, endosome membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q9Y4K3-1" ], "evidence": [ { "id": "R-HSA-936947", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936947" } ] }, { "id": "R-HSA-936951", "name": "Activation of TAK1 complex bound to activated TLR4 complex", "equation": "", "summary": "The TAK1 complex consists of Transforming growth factor-beta (TGFB)-activated kinase (TAK1) and TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAK1 requires TAB1 for its kinase activity (Shibuya et al. 1996, Sakurai et al. 2000). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001). The TAK1 complex is regulated by polyubiquitination. Binding of TAB2 and TAB3 to Lys63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Binding of multiple TAK1 complexes to the same polyubiquitin chain may promote oligomerization of TAK1, facilitating TAK1 autophosphorylation and subsequent activation of its kinase activity (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that lead to TAK1 activation. Another possibility is that TAB2/3 may recruit the IKK complex by binding to ubiquitinated NEMO; polyubiquitin chains may function as a scaffold for higher order signaling complexes that allow interaction between TAK1 and IKK (Kanayama et al. 2004).", "cellular_location": "cytosol, endosome membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q9Y4K3-1" ], "evidence": [ { "id": "R-HSA-936951", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936951" } ] }, { "id": "R-HSA-936960", "name": "Activated TRAF6:p-IRAK2 interacts with TAK1 complex", "equation": "", "summary": "TAK1-binding protein 2 (TAB2) and/or TAB3, as part of a complex that also contains TAK1 and TAB1, binds polyubiquitinated TRAF6. The TAB2 and TAB3 regulatory subunits of the TAK1 complex contain C-terminal Npl4 zinc finger (NZF) motifs that recognize with Lys63-pUb chains (Kanayama et al. 2004). The recognition mechanism is specific for Lys63-linked ubiquitin chains (Kulathu Y et al 2009). TAK1 can be activated by unattached Lys63-polyubiquitinated chains when TRAF6 has no detectable polyubiquitination (Xia et al. 2009) and thus the synthesis of these chains by TRAF6 may be the signal transduction mechanism.
As a de-ubiquitinating/de-ISGylating enzyme, severe acute respiratory syndrome coronavirus type 1 (SARS-CoV-1) 1a-encoded papain-like protease (PLPro or nsp3) antagonizes the host type I interferon (IFN) response by removing Lys63-linked ubiquitin chains of TRAF3 and TRAF6 (Li SW et al. 2016).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q9Y4K3-1" ], "evidence": [ { "id": "R-HSA-936960", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936960" } ] }, { "id": "R-HSA-936991", "name": "Auto phosphorylation of TAK1 bound to p-IRAK2:pUb oligo-TRAF6: free K63 pUb:TAB1:TAB2/TAB3", "equation": "", "summary": "The TAK1 complex consists of Transforming growth factor-beta (TGFB)-activated kinase (TAK1) and TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAK1 requires TAB1 for its kinase activity (Shibuya et al. 1996, Sakurai et al. 2000). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001). The TAK1 complex is regulated by polyubiquitination. Binding of TAB2 and TAB3 to Lys63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Binding of multiple TAK1 complexes to the same polyubiquitin chain may promote oligomerization of TAK1, facilitating TAK1 autophosphorylation and subsequent activation of its kinase activity (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that lead to TAK1 activation. Another possibility is that TAB2/3 may recruit the IKK complex by binding to ubiquitinated NEMO; polyubiquitin chains may function as a scaffold for higher order signaling complexes that allow interaction between TAK1 and IKK (Kanayama et al. 2004).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q9Y4K3-1" ], "evidence": [ { "id": "R-HSA-936991", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936991" } ] }, { "id": "R-HSA-937075", "name": "Phosphorylated TAK1 leaves activated TLR receptor complex", "equation": "", "summary": "Phosphorylated TAK1 complexed with TRAF6-TAB1-TAB2/TAB3 leaves the activated TLR4 complex and translocates to the cytosol", "cellular_location": "cytosol, endosome membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q9Y4K3-1" ], "evidence": [ { "id": "R-HSA-937075", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-937075" } ] }, { "id": "R-HSA-9645406", "name": "ALPK1:ADP-heptose:p-T9-TIFA oligomer:K63pUb-TRAF6 oligomer recruits MAP3K7 (TAK1)", "equation": "", "summary": "TAK1-binding protein 2 (TAB2) and/or TAB3, as part of a complex that also contains TAK1 (MAP3K7) and TAB1, binds polyubiquitinated TRAF6. The TAB2 and TAB3 regulatory subunits of the TAK1 complex contain C-terminal Npl4 zinc finger (NZF) motifs that recognize Lys63-pUb chains (Kanayama et al. 2004). The recognition mechanism is specific for Lys63-linked ubiquitin chains (Kulathu Y et al 2009). TAK1 can be activated by unattached Lys63-polyubiquitinated chains when TRAF6 has no detectable polyubiquitination (Xia et al. 2009) and thus the synthesis of these chains by TRAF6 may be the signal transduction mechanism. This binding leads to autophosphorylation and activation of TAK1.", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q96QP1-1", "Q9Y4K3-1" ], "evidence": [ { "id": "R-HSA-9645406", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9645406" } ] }, { "id": "R-HSA-9645442", "name": "Auto phosphorylation of TAK1 within the ALPK1:ADP-heptose:p-T9-TIFA:pUb-TRAF6: free K63 pUb:TAB1:TAB2/TAB3 :MAP3K7 complex", "equation": "", "summary": "The TAK1 complex consists of transforming growth factor-beta (TGFB)-activated kinase (TAK1 or MAP3K7), TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAK1 requires TAB1 for its kinase activity (Shibuya et al. 1996, Sakurai et al. 2000). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001). The TAK1 complex is regulated by polyubiquitination. Binding of TAB2 and TAB3 to Lys63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Binding of multiple TAK1 complexes to the same polyubiquitin chain may promote oligomerization of TAK1, facilitating TAK1 autophosphorylation and subsequent activation of its kinase activity (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that lead to TAK1 activation. Another possibility is that TAB2/3 may recruit the IKK complex by binding to ubiquitinated NEMO; polyubiquitin chains may function as a scaffold for higher-order signaling complexes that allow interaction between TAK1 and IKK (Kanayama et al. 2004). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O43318-1", "Q96QP1-1", "Q9Y4K3-1" ], "evidence": [ { "id": "R-HSA-9645442", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9645442" } ] }, { "id": "R-HSA-975097", "name": "Activated TRAF6:p-IRAK2 interacts with TAK1 complex upon TLR7/8 or 9 stimulation", "equation": "", "summary": "TAK1-binding protein 2 (TAB2) and/or TAB3, as part of a complex that also contains TAK1 and TAB1, binds polyubiquitinated TRAF6. The TAB2 and TAB3 regulatory subunits of the TAK1 complex contain C-terminal Npl4 zinc finger (NZF) motifs that recognize with Lys63-pUb chains (Kanayama et al. 2004). The recognition mechanism is specific for Lys63-linked ubiquitin chains (Kulathu Y et al 2009). TAK1 can be activated by unattached Lys63-polyubiquitinated chains when TRAF6 has no detectable polyubiquitination (Xia et al. 2009) and thus the synthesis of these chains by TRAF6 may be the signal transduction mechanism.
As a de-ubiquitinating/de-ISGylating enzyme, severe acute respiratory syndrome coronavirus type 1 (SARS-CoV-1) 1a-encoded papain-like protease (PLPro or nsp3) antagonizes the host type I interferon (IFN) response by removing Lys63-linked ubiquitin chains of TRAF3 and TRAF6 (Li SW et al. 2016).",
"cellular_location": "cytosol, endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1"
],
"evidence": [
{
"id": "R-HSA-975097",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-975097"
}
]
},
{
"id": "R-HSA-975103",
"name": "Auto phosphorylation of TAK1 bound to p-IRAK2:pUb oligo-TRAF6: free K63 pUb:TAB1:TAB2/TAB3 upon TLR7/8 or 9 activation",
"equation": "",
"summary": "The TAK1 complex consists of Transforming growth factor-beta (TGFB)-activated kinase (TAK1) and TAK1-binding protein 1 (TAB1), TAB2 and TAB3. TAK1 requires TAB1 for its kinase activity (Shibuya et al. 1996, Sakurai et al. 2000). TAB1 promotes TAK1 autophosphorylation at the kinase activation lobe, probably through an allosteric mechanism (Brown et al. 2005, Ono et al. 2001). The TAK1 complex is regulated by polyubiquitination. Binding of TAB2 and TAB3 to Lys63-linked polyubiquitin chains leads to the activation of TAK1 by an uncertain mechanism. Binding of multiple TAK1 complexes to the same polyubiquitin chain may promote oligomerization of TAK1, facilitating TAK1 autophosphorylation and subsequent activation of its kinase activity (Kishimoto et al. 2000). The binding of TAB2/3 to polyubiquitinated TRAF6 may facilitate polyubiquitination of TAB2/3 by TRAF6 (Ishitani et al. 2003), which might result in conformational changes within the TAK1 complex that lead to TAK1 activation. Another possibility is that TAB2/3 may recruit the IKK complex by binding to ubiquitinated NEMO; polyubiquitin chains may function as a scaffold for higher order signaling complexes that allow interaction between TAK1 and IKK (Kanayama et al. 2004).",
"cellular_location": "cytosol, endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q9Y4K3-1"
],
"evidence": [
{
"id": "R-HSA-975103",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-975103"
}
]
},
{
"id": "R-HSA-9755757",
"name": "SARS-CoV-2 N binds TAK1",
"equation": "",
"summary": "Several studies showed that viral RNA binding to SARS-CoV-2 nucleocapsid (N) protein induces liquid-liquid phase separation (LLPS) (Wu Y et al. 2021; Wang S et al. 2021; Cubuk J et al. 2021; Lu S et al. 2021). Viral N protein:RNA LLPS recruits TGF-beta-activated kinase 1 (TAK1) and I\u03baB kinase (IKK) complexes and enhances their interaction which in turn promotes NF-kappaB activation and expression of pro-inflammatory cytokines (Wu Y et al. 2021). The C-terminal domain (CTD) of viral N is essential for LLPS (Wu Y et al. 2021; Wang S et al. 2021) and induction of NF-kappaB signaling in mammalian cells (Wu Y et al. 2021). Deletion of CTD abolished SARS-CoV-2 N LLPS and the recruitment of TAK1/IKK complexes. Co-immunoprecipitation analysis revealed that SARS-CoV-2 N protein interacted with the components of the TAK1 complex and the IKK complex, including TAK1, TAB1, TAB2, IKBKA (CHUK), IKBKB, and NEMO (IKBKG) upon co-expression in human embryonic kidney 293T (HEK293T) cells (Wu Y et al. 2021). Endogenous IKK and TAK1 immunoprecipitated together with N in human lung cancer Calu3 cells infected with SARS-CoV-2. Immunofluorescence analysis further revealed the enhanced co-localization between N protein and IKBKB after SARS-CoV-2 infection in human hepatoma Huh7 cells. These data sugget that SARS-CoV-2 N:RNA LLPS serves as a platform to enhance the interaction between TAK1 and IKK complexes promoting NF-kappaB-dependent inflammatory responses (Wu Y et al. 2021).
",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1"
],
"evidence": [
{
"id": "R-HSA-9755757",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9755757"
}
]
},
{
"id": "R-HSA-9758604",
"name": "Ubiquitination of IKBKG by TRAF6",
"equation": "",
"summary": "During the phosphorylation of the IKK beta (IKBKB), the regulatory subunit NEMO (IKBKG) undergoes K-63-linked polyubiquitination. Ubiquitinated TRAF6 acts as a E3 ligase and induces this ubiquitination. Studies of different NF-kappa-B signaling pathways revealed several potential ubiquitination sites on IKBKG (e.g., K285, K277, K309 and K399) (Fuminori et al. 2009).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O43318-1",
"Q96QP1-1",
"O15111-1",
"Q9Y4K3-1",
"O14920-1",
"P61088-1",
"Q9UMW8-1",
"P51617-1"
],
"evidence": [
{
"id": "R-HSA-9758604",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9758604"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-167998",
"participant_name": "MAP2K6 [cytosol]",
"crossref": [
{
"id": "P52564",
"database": "UniProt",
"url": ""
},
{
"id": "3VN9",
"database": "PDB",
"url": ""
},
{
"id": "MP2K6_HUMAN",
"database": "ZINC - Biogenic",
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},
{
"id": "P52564",
"database": "ZINC target",
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{
"id": "P52564",
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},
{
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},
{
"id": "MP2K6_HUMAN",
"database": "ZINC - World Drugs",
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},
{
"id": "ENSG00000108984",
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},
{
"id": "P52564",
"database": "Pharos - Targets",
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},
{
"id": "3ENM",
"database": "PDB",
"url": ""
},
{
"id": "MP2K6_HUMAN",
"database": "ZINC - FDA approved",
"url": ""
},
{
"id": "8P7J",
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"url": ""
},
{
"id": "MP2K6_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "ENSP00000468348",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000108984",
"database": "Ensembl",
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},
{
"id": "ENST00000590474",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000589647",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000467213",
"database": "Ensembl",
"url": ""
},
{
"id": "8A8M",
"database": "PDB",
"url": ""
},
{
"id": "P52564",
"database": "GeneCards",
"url": ""
},
{
"id": "ENSG00000108984-MAP2K6",
"database": "HPA",
"url": ""
},
{
"id": "NP_002749.2",
"database": "RefSeq",
"url": ""
},
{
"id": "2Y8O",
"database": "PDB",
"url": ""
}
]
},
{
"participant_id": "R-HSA-202513",
"participant_name": "CHUK:p-S177,S181-IKBKB:IKBKG [cytosol]",
"crossref": [
{
"id": "CPX-3269",
"database": "ComplexPortal",
"url": ""
}
]
},
{
"participant_id": "R-HSA-206014",
"participant_name": "p-T187-MAP3K7 [cytosol]",
"crossref": [
{
"id": "NP_663304.1",
"database": "RefSeq",
"url": ""
},
{
"id": "5J8I",
"database": "PDB",
"url": ""
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{
"id": "7NTH",
"database": "PDB",
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{
"id": "M3K7_HUMAN",
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{
"id": "5GJG",
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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