PROSITE documentation PDOC51083
Zinc finger HIT-type profile


The HIT-type zinc finger contains 7 conserved cysteines and one histidine that can potentially coordinate two zinc atoms. It has been named after the first protein that originally defined the domain: the yeast HIT1 protein [1]. The HIT-type zinc finger displays some sequence similarities to the MYND-type zinc finger (see <PDOC50865>). The function of this domain is unknown but it is mainly found in nuclear proteins involved in gene regulation and chromatin remodeling.

Some proteins known to contain a HIT-type zinc finger are listed below:

  • Mammalian thyroid hormone receptors interacting protein 3 (Trip3). It also interacts with the retinoid X receptor and activates the transcriptional factor HNF-4α [2].
  • Mammalian FON protein.
  • Yeast HIT1 protein. It is required for high temperature growth.
  • Yeast VPS71 protein. It is a component of the chromatin remodeling complex Swr1, which catalyzes the exchange of histone H2A to histone variant H2AZ. This step has an important influence on gene expression [3].

The profile we developed covers the whole HIT-type zinc finger.

Last update:

February 2005 / First entry.


Technical section

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

ZF_HIT, PS51083; Zinc finger HIT-type profile  (MATRIX)


1AuthorsKawakami K. Shafer B.K. Garfinkel D.J. Strathern J.N. Nakamura Y.
TitleTy element-induced temperature-sensitive mutations of Saccharomyces cerevisiae.
SourceGenetics 131:821-832(1992).
PubMed ID1325386

2AuthorsIwahashi H. Yamagata K. Yoshiuchi I. Terasaki J. Yang Q. Fukui K. Ihara A. Zhu Q. Asakura T. Cao Y. Imagawa A. Namba M. Hanafusa T. Miyagawa J. Matsuzawa Y.
TitleThyroid hormone receptor interacting protein 3 (trip3) is a novel coactivator of hepatocyte nuclear factor-4alpha.
SourceDiabetes 51:910-914(2002).
PubMed ID11916906

3AuthorsMizuguchi G. Shen X. Landry J. Wu W.H. Sen S. Wu C.
TitleATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex.
SourceScience 303:343-348(2004).
PubMed ID14645854

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