The bacterial metabolite ADP-heptose activates the mammalian protein kinase ALPK1 (alpha protein kinase 1), which then phosphorylates TIFA (TRAF interacting protein with FHA domain). This leads to the oligomerisation of TIFA and the recruitment and oligomerisation of TRAF6 (TNF receptor-associated factor 6), activating a signalling network that culminates in the production of inflammatory mediators that mount responses to combat microbial infection. To identify other protein(s) that associate with TRAF6 in ADP-heptose-stimulated cells, we re-expressed FLAG-TRAF6 in TRAF6 KO cells, stimulated the cells with ADP-heptose and immunoprecipitated TRAF6 from the cell extracts using a FLAG antibody. Proteins associated with TRAF6 were identified by mass spectrometry and included the components of LUBAC (the linear ubiquitin assembly complex), the components of the TAK1 and IB kinase (IKK) complexes, TRAF2 and c-IAP1, providing insight into the molecular details and mode of operation of the ADP-heptose signalling pathway. In parallel experiments the cells were stimulated with IL-1b, a cytokine that also signals via TRAF6, which served as a control.