Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains.
Downstream regulator TANK binds to the CD40 recognition site on TRAF3.
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Crystal structure of a TANK peptide (174-194) bound to TRAF3 shows TANK engages the same CD40-recognition surface of the TRAF3 TRAF-C domain; point mutations (Q182A, T184A, D185A) abolish TANK binding to TRAF2/TRAF3.
A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.
Huntingtin interacting proteins are genetic modifiers of neurodegeneration.
SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK.
Enhanced binding of TBK1 by an optineurin mutant that causes a familial form of primary open angle glaucoma.
Network organization of the human autophagy system.
Inducible SUMO modification of TANK alleviates its repression of TLR7 signalling.
Protein interactome reveals converging molecular pathways among autism disorders.
Zinc finger protein tristetraprolin interacts with CCL3 mRNA and regulates tissue inflammation.
Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
Vaccinia virus protein C6 is a virulence factor that binds TBK-1 adaptor proteins and inhibits activation of IRF3 and IRF7.
Functional dissection of the TBK1 molecular network.
Toward an understanding of the protein interaction network of the human liver.
Structure homology and interaction redundancy for discovering virus-host protein interactions.
A proteome-scale map of the human interactome network.
Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.
TRAF Family Member-associated NF-κB Activator (TANK) Inhibits Genotoxic Nuclear Factor κB Activation by Facilitating Deubiquitinase USP10-dependent Deubiquitination of TRAF6 Ligase.
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TANK scaffolds a complex with ZC3H12A/MCPIP1 and the deubiquitinase USP10 that mediates USP10-dependent deubiquitination of TRAF6, restraining genotoxic- and IL-1/LPS-induced canonical NF-kappaB activation. CRISPR deletion of TANK enhances NF-kappaB activation, cell survival and cytokine production after genotoxic stress. TANK has no DUB domain of its own.
A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface.
Architecture of the human interactome defines protein communities and disease networks.
Quantitative Proteomics Identified TTC4 as a TBK1 Interactor and a Positive Regulator of SeV-Induced Innate Immunity.
A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
SARS-CoV-2 Membrane Protein Inhibits Type I Interferon Production Through Ubiquitin-Mediated Degradation of TBK1.
Multimodal cell maps as a foundation for structural and functional genomics.
I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction.
Phosphorylation of IRF-3/IRF7 and their release from the activated TLR complex
IRF3/IRF7 recruitment to p-TBK1/p-IKK epsilon bound to the activated TLR4
TANK binds K63-poly-Ub-TRAF3:TICAM1:activated TLR4
TANK is ubiquitinated within TANK:K63polyUb-TRAF3:TRIF:activated TLR4
Phosphorylation of IRF-3/IRF7 and their release from the activated TLR3 complex
IRF3/IRF7 recruitment to p-TBK1/p-IKK epsilon bound to the activated TLR3
TANK binds K63-poly-Ub-TRAF3:TICAM1:activated TLR3
TANK is ubiquitinated within TANK:K63polyUb-TRAF3:TICAM1:TLR3:viral dsRNA
Phosphorylation and release of IRF7
Recruitment of TBK1/IKK epsilon complex to TANK:TRAF6
Recruitment of TANK to TRAF6
Recruitment of IRF7 to TRAF6
TBK1, IKBKE form homodimers
Phosphorylation of TBK1/IKBKE
TBK1 is ubiquitinated within TBK1:K63polyUb-TANK:K63polyUb-TRAF3:TRIF:activated TLR4
TBK1 is phosphorylated within the activated TLR4 complex
Recruitment of TBK1 to K63polyUb-TANK:K63polyUb-TRAF3:TRIF:activated TLR4
Recruitment of IKKε (IKBKE) to K63polyUb-TANK:K63polyUb-TRAF3:TRIF:activated TLR4
OPTN binds TBK1 within the activated TLR4 complex
IKKε (IKBKE) is ubiquitinated within the activated TLR4
IKKε (IKBKE) is phosphorylated within the activated TLR4 complex
TBK1 binds K63-pUb-TANK:K63-pUb-TRAF3:TRIF:activated TLR3
TBK1 is ubiquitinated within TBK1:K63polyUb-TANK:K63polyUb-TRAF3:TRIF:activated TLR3
IKKε (IKBKE) binds K63-pUb-TANK:K63-pUb-TRAF3:TRIF:activated TLR3
TBK1 is phosphorylated within the activated TLR3 complex
OPTN binds TBK1 within the activated TLR3 complex
IKKε (IKBKE) is phosphorylated within the activated TLR3 complex
IKKε (IKBKE) is ubiquitinated within the activated TLR3 complex