{PDOC50134}
{PS50134; ZF_TAZ}
{BEGIN}
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* Zinc finger TAZ-type profile *
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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 alpha 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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2002 / First entry.

[ 1] Giles R.H., Peters D.J., Breuning M.H.
     "Conjunction dysfunction: CBP/p300 in human disease."
     Trends Genet. 14:178-183(1998).
     PubMed=9613201
[ 2] Ponting C.P., Blake D.J., Davies K.E., Kendrick-Jones J., Winder S.J.
     "ZZ and TAZ: new putative zinc fingers in dystrophin and other
     proteins."
     Trends Biochem. Sci. 21:11-13(1996).
     PubMed=8848831
[ 3] De Guzman R.N., Liu H.Y., Martinez-Yamout M., Dyson H.J., Wright P.E.
     J. Mol. Biol. 303:243-253(2000).

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