TAK1 is a ubiquitin-dependent kinase of MKK and IKK

By chen wang, L. Deng, Mei Hong, G. Akkaraju, J. Inoue, Zhijian J. Chen. Nature, 2001

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TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. (2005, background): “In vitro biochemical studies have demonstrated that TRIKA1 (a complex of Ubc13 and Uev1A) and TRIKA2 (the complex of TAK1, TAB1, and TAB2) are key signal-transducing complexes that activate IKK and MKK6 in a manner dependent upon ubiquitination of TRAF6 (Wang et al. 2001).”
Bcl10 activates the NF-κB pathway through ubiquitination of NEMO (2004, background): “As UBC13 and MMS2 form an E2 complex that functions with certain E3 ubiquitin ligases such as TRAF2, TRAF6, or RAD5 to catalyse K63-linked polyubiquitinatio”
The IKK complex, a central regulator of NF-kappaB activation. (2010, background): “Another necessary component of TRAF6-dependent NF-kB activation turned out to be a complex containing the kinase TAK1 and its two cofactors TAB1 and TAB2 (Wang et al. 2001).”
Mammalian MAPK signal transduction pathways activated by stress and inflammation: a 10-year update. (2012, background): “IIID4) leading to autophosphorylation at the classical Thr180/Tyr182 activating phosphoacceptor sites (FIGURE 3).”
CARMA1 is a critical lipid raft–associated regulator of TCR-induced NF-κB activation (2002, background): “, whereas TRAF6 mediates interleukin 1 (IL-1) and lipopolysaccharide–induced NF-κB activation by recruitment and ubiquitin-dependent activation of the IKK-activating kinase transforming growth factor-β–activated kinase (TAK1”