TBK1 is a non-canonical IKK kinase, which phosphorylates the nuclear factor kB. Consisting of 729 amino acids, TBK1 includes four main domains: an N-terminal kinase domain (KD; 1-307), a ubiquitin-like domain (ULD; 308-384), and two coiled-coil domains (CCD1; 407-657 and CCD2; 659-713). The KD is responsible for the catalytic activity of TBK1. It adopts a typical protein kinase fold and contains the active site for phosphorylation reactions. The ULD, located adjacent to the KD, plays a role in regulating TBK1 activity and interactions. The CCD1, also referred to as scaffold dimerization domain (SDD), harbors a leucine zipper domain (LZ; 499-527) and a helixloop-helix domain (HLH; 591-632), both of which mediate dimerization of TBK1 molecules. It forms extensive interactions with both the KD and ULD, contributing to the overall stability of the TBK1 structure. The CCD2 at the C-terminus holds an adaptor-binding motif which assists the interaction of TBK1 with adaptor proteins, such as TANK, NAK-associated protein, TBKBP1, or optineurin. TBK1 forms an intimate dimer through extensive interactions between the SDDs, KDs, and ULDs of two TBK1 molecules. This dimerization is crucial for TBK1 function and regulation. The various domains of TBK1 allow it to participate in multiple cellular processes, including: (i) immune response: TBK1 phosphorylates and activates IRF3 and IRF7, leading to the production of type I interferons in response to viral infection; (ii) NF-κB pathway: TBK1 can activate the NF-κB pathway, promoting the expression of pro-inflammatory cytokines; (iii) autophagy: by phosphorylating autophagy-related proteins, TBK1 regulates the degradation of cellular components, which is important for cellular homeostasis and defense against pathogens; (iv) cell proliferation and survival: TBK1 is involved in pathways that control cell growth and survival, linking it to cancer biology. Journal publications related to TBK1 have grown rapidly and consistently over the last two decades, nearly doubling between 2020 and 2023 as seen from data leveraged from the CAS Content Collection . This active and rapid increase is indicative of interest in TBK1 from the scientific community. Growth in patent publications on the other hand has been slow, speaking to potential difficulties in targeting TBK1 (elaborated briefly in later sections). The journal-to-patent ratio was >12X for the year 2023 (Figure ). Patenting activity is dominated by corporate players as compared to academics (Figure ). Merck, MetaProteomics, and Arvinas have the highest number of patent applications among commercial entities, while Max-Planck Institute, the Korea Institute of Science and Technology (KIST), and Purdue University are the leaders among the academic organizations. Using data from CAS Content Collection, we determined co-occurrences of TBK1 with other protein targets as well as diseases (shown in the Sankey graph in Figure ). Below we discuss briefly the role of TBK1 in diseases it co-occurs with in our data.