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TRAF proteins were isolated first by their ability to interact with TNF
receptor . They are involved in different cytoplasmic signal transduction
pathways. TRAF proteins are composed of 3 structural domains: a RING finger
(see <PDOC00449>) 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.
January 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
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.
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