TRAF-like
IPR008974
Definition
The tumour necrosis factor receptor (TNFR) associated factors (TRAFs) act as signal transducers for both TNFRs and interleukin-1/Toll-like receptors. TRAFs function in immunity, embryonic development, stress response and bone metabolism through their induction of cell proliferation, differentiation, and apoptosis PMID:11865024. TRAFs are characterised by two domains: an N-terminal domain containing RING and zinc finger motifs that is essential for the activation of downstream effectors, and a C-terminal TRAF domain that is essential for self-association and receptor interaction PMID:10518213. The TRAF-domain like fold is a β-sandwich consisting of 8 strands in 2 β-sheets and has a circularly permuted greek-key immunoglobulin-fold topology that contains an extra strand. The substrate-binding domain (SBD) of the SIAH (seven in absentia homologue) family of proteins is structurally highly similar to the TRAF domain. The SIAH SBD interacts with a number of proteins, and is involved in TNF-alpha-mediated NFkappaB activation PMID:11742346.
15 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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