
TRAF family proteins. TRAF1 to TRAF6 share a conserved coiled-coil (CC)/TRAF-C domain, and TRAF7 has a series of 40 amino acid peptide repeats terminating in tryptophan (W) and aspartic acid (D) residues (WD40) domains. TRAFs, with the exception of TRAF1, have an N-terminal really interesting new gene (RING) domain and zinc finger motifs (Zn). Data are based on UniProt (https://www.uniprot.org). TRAF1, Q13077; TRAF2, Q12933; TRAF3, Q13114; TRAF4, Q9BUZ4; TRAF5, O00463; TRAF6, Q9Y4K3; TRAF7, Q6Q0C0
We thank the Life Science Research Center, University of Toyama and the Institute for Animal Experimentation, Tohoku University Graduate School of Medicine for technical support. We thank members of Laboratory of Molecular Cell Biology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, and Department of Microbiology and Immunology, Tohoku University Graduate School of Medicine for their assistance and help. We also thank Michael Croft and Hiroyasu Nakano for Traf5−/− mice and for their encouragement at the start of the project.
TS and NI: Supervision. TS and MHK: Writing—original draft. TS, NI and MHK: Writing—review & editing. All authors read and approved the submitted version.
The authors declare that there are no conflicts of interest.
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The study was approved by Japan Society for the Promotion of Science KAKENHI [Grants JP15H04640 (T.S.), JP18H02572 (T.S.)]. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
© The Author(s) 2023.