{PDOC50145} {PS50145; ZF_TRAF} {BEGIN} ********************************* * Zinc finger TRAF-type profile * ********************************* TRAF proteins were isolated first by their ability to interact with TNF receptor [1]. They are involved in different cytoplasmic signal transduction pathways. TRAF proteins are composed of 3 structural domains: a RING finger (see ) in the N terminal part of the protein, TRAF zinc fingers in the middle part and the TRAF domain in the C terminal part. TRAF zinc fingers contain 8 possible ligands for one or two zinc atoms. This domain is found only in TRAF and TRAF-related proteins and its function is not yet known. The profile we developed covers the whole domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: January 2002 / First entry. [ 1] Rothe M., Wong S.C., Henzel W.J., Goeddel D.V. "A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor." Cell 78:681-692(1994). PubMed=8069916 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}