PROSITE documentation PDOC50134
Zinc finger TAZ-type profile


Cyclic-AMP response element binding protein (CBP) and the related protein p300 are large nuclear molecules that interact with transcriptional activators and repressors. They belong to a class of protein containing an histone acetyltransferase activity, which suggests a role in chromatin remodeling. They have been implicated in biological function as diverse as cell growth, differentiation, or apoptosis [1].

CBP/P300 proteins contain in their N and C terminal parts the so-called transcriptional adaptor zinc finger (TAZ finger). A TAZ domain is about a 100 amino acid long and shows an internal imperfect triplication of a His-x3-Cys-x12-Cys-x4-Cys module [2]. The binding sites for YY1, E1A and TFIIB in CBP and P300 proteins have been mapped in the region that contain TAZ fingers, suggesting a possible protein-binding function for this domain.

The 3D structure of the TAZ finger has been determined [3]. It folds in a compact globular structure consisting of 4 α helices that coordinates 3 zinc atoms (see <PDB:1F81>). Zinc binding sites are in the loops connecting helices.

This domain has been identified only in proteins belonging to the CBP/P300 family.

The profile we developed covers the entire TAZ domain.

Last update:

September 2002 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ZF_TAZ, PS50134; Zinc finger TAZ-type profile  (MATRIX)


1AuthorsGiles R.H. Peters D.J. Breuning M.H.
TitleConjunction dysfunction: CBP/p300 in human disease.
SourceTrends Genet. 14:178-183(1998).
PubMed ID9613201

2AuthorsPonting C.P. Blake D.J. Davies K.E. Kendrick-Jones J. Winder S.J.
TitleZZ and TAZ: new putative zinc fingers in dystrophin and other proteins.
SourceTrends Biochem. Sci. 21:11-13(1996).
PubMed ID8848831

3AuthorsDe Guzman R.N. Liu H.Y. Martinez-Yamout M. Dyson H.J. Wright P.E.
SourceJ. Mol. Biol. 303:243-253(2000).

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