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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 <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:

ZF_TRAF, PS50145; Zinc finger TRAF-type profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Domain architecture view of Swiss-Prot proteins matching PS50145 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50145 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50145 • Scan Swiss-Prot/TrEMBL entries against PS50145 • view ligand binding statistics

Matching PDB structures: 2EOD 2YRE 2YUC 3HCS [ALL]

1	Authors	Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.
	Title	A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.
	Source	Cell 78:681-692(1994).
	PubMed ID	8069916

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