Anti-TRAF-6

Human TRAF6 is a 522 amino acid protein. The TRAF (TNF receptor-associated factor) family is a group of adapter proteins (TRAFs 1-6) that link a wide variety of cell surface receptors to diverse signaling cascades leading to the activation of NF-kB and mitogen-activated protein kinases. TRAFs are major signal transducers for both the TNF and IL- 1/TLR receptor superfamilies and collectively play important functions in both adaptive and innate immunity. The carboxy-terminal region of TRAFs is required for self-association and interaction with receptor cytoplasmic domains following ligand-induced oligomerization. TRAFs interact with a variety of proteins that regulate receptor-induced cell death or survival, and TRAF-mediated signaling can promote cell survival or interfere with death receptor-induced apoptosis. Protein function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN. May be essential for the formation of functional osteoclasts. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c- Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. [The UniProt Consortium]