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TBK1 binding protein 1

TBKBP1 is an adaptor protein that binds to TBK1 (MIM 604834) and is part of the interaction network in the TNF (MIM 191160)/NFKB (see MIM 164011) pathway (Bouwmeester et al., 2004 [PubMed 14743216]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: TBK1, Interferon Regulatory Factor-3, CAN, V1a, fibrillin-1
Papers on Sintbad
SUMO modification of TBK1 at the adaptor-binding C-terminal coiled-coil domain contributes to its antiviral activity.
Schmitz et al., Gießen, Germany. In Biochim Biophys Acta, 2015
Mass spectrometry allowed identifying K694 as the SUMO acceptor site, a residue located in the C-terminal coiled-coil domain which is exclusively responsible for the association with the adaptor proteins NAP1, Sintbad and TANK.
TRIM11 negatively regulates IFNβ production and antiviral activity by targeting TBK1.
Kwon et al., Taejŏn, South Korea. In Plos One, 2012
This interaction was enhanced in the presence of the TBK1 adaptor proteins, NAP1 (NF-κB activating kinase-associated protein-1), SINTBAD (similar to NAP1 TBK1 adaptor) or TANK (TRAF family member-associated NF-κB activator).
Vaccinia virus protein C6 is a virulence factor that binds TBK-1 adaptor proteins and inhibits activation of IRF3 and IRF7.
Bowie et al., Dublin, Ireland. In Plos Pathog, 2011
Consistent with this notion, C6 immunoprecipitated with the TBK1 complex scaffold proteins TANK, SINTBAD and NAP1.
Novel splice variants of human IKKε negatively regulate IKKε-induced IRF3 and NF-kB activation.
Adam-Klages et al., Kiel, Germany. In Eur J Immunol, 2011
The lack of IRF3 activation is likely caused by the failure of the splice variants to interact with the adapter proteins TANK, NAP1, and/or SINTBAD.
Functional dissection of the TBK1 molecular network.
Superti-Furga et al., Vienna, Austria. In Plos One, 2010
They are associated with three adaptor proteins called TANK, Sintbad (or TBKBP1) and NAP1 (or TBKBP2, AZI2) whose functional relationship to TBK1 and IKK-i is poorly understood.
The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria.
Randow et al., Cambridge, United Kingdom. In Nat Immunol, 2009
Here we show that NDP52, not previously known to contribute to innate immunity, recognizes ubiquitin-coated Salmonella enterica in human cells and, by binding the adaptor proteins Nap1 and Sintbad, recruits TBK1.
Are the IKKs and IKK-related kinases TBK1 and IKK-epsilon similarly activated?
Chariot et al., Liège, Belgium. In Trends Biochem Sci, 2008
Recent data provide insight into the requirement for scaffold proteins in complex assembly; NF-kappaB essential modulator coordinates some IKK complexes, whereas TANK, NF-kappaB-activating kinase-associated protein 1 (NAP1) or similar to NAP1 TBK1 adaptor (SINTBAD) assemble TBK1 and IKK-epsilon complexes.
SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK.
Randow et al., Cambridge, United Kingdom. In Embo J, 2007
results suggest that efficient signal transduction upon viral infection requires SINTBAD, TANK and NAP1 because they link TBK1 and IKKi to virus-activated signalling cascades
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