PROSITE documentation PDOC51042CUT domain profile
The CUT domain, first discovered in the Drosophila Cut protein, consists of about 88 amino acids and is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. However, the homeodomain of this gene family has properties quite distinct from the classical homeodomain (see <PDOC00027>). On its own these homeodomain has little DNA-binding affinity or specificity. DNA-binding is mediated mostly by the CUT domain, but the sequence specificity and binding kinetics are greatly influenced by the presence of the homeodomain.
The CUT proteins can be grouped into sub-families according to the presence of one, two, or three cut repeats. Congruent with their structural diversity, these cut-homeoproteins are transcriptional regulators that participate in a variety of functional contexts.
Proteins currently known to contain a CUT domain are:
- The Drosophila Cut protein and its mammalian homologs (CDP/Cux/Clox, and
Cux2 proteins). They generally function as transcriptional repressors in
both proliferating and differentiating cells.
- The SATB1 protein which contains two cut repeats, is thought to function
at the level of chromatin structure to modulate gene activity.
- The mammalian HNF-6 (hepatocyte nuclear factor-6) [2], which defines the
prototypical Onecut proteins. It functions as a key regulator of liver
gene expression.
The profile we developed covers the entire CUT domain.
Last update:November 2004 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Nguyen D.N.T. Rohrbaugh M. Lai Z.-C. |
| Title | The Drosophila homolog of Onecut homeodomain proteins is a neural-specific transcriptional activator with a potential role in regulating neural differentiation. | |
| Source | Mech. Dev. 97:57-72(2000). | |
| PubMed ID | 11025207 |
| 2 | Authors | Lannoy V.J. Buerglin T.R. Rousseau G.G. Lemaigre F.P. |
| Title | Isoforms of hepatocyte nuclear factor-6 differ in DNA-binding properties, contain a bifunctional homeodomain, and define the new ONECUT class of homeodomain proteins. | |
| Source | J. Biol. Chem. 273:13552-13562(1998). | |
| PubMed ID | 9593691 |
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