PROSITE documentation PDOC51998
DEK C-terminal (DEK-C) domain profile


The DEK-C domain was first detected in the C-terminal region of the chromatin-associated protein DEK. The DEK-C domain is able to bind DNA and induce protein-protein interactions, but its function remains unknown [1].

The DEK C-terminal domain consists of three tightly packed, twisted α-helices that are arranged around a well-packed core of hydrophobic residues (see <PDB:1Q1V>). The middle helix is the shortest and the C-terminal helix is the longest. Despite the structural similarity with winged helix proteins, the DNA-interaction mechanism of the DEK C-terminal domain appears different from that of winged helix proteins, as it uses the second helix to interact with DNA, whereas other winged helix proteins use the third helix to interact with DNA [2].

Some proteins known to contain a DEK-C domain are listed below:

  • Animal DEK, a chromatin associated protein able to modify the structure of DNA and originally described as a proto-oncogene protein. DEK acts as a transcriptional inhibitor [1,2].
  • Arabidopsis thaliana DEK3, a chromatin-associated protein [3].
  • Animal Slingshot (SSH) proteins, phosphatases that specifically dephosphorylate and activate cofilin, an F-actin-severing protein [4].
  • Fungal chitin synthases (ChSs) [5,6].

The profile we developed covers the entire DEK-C domain.

Last update:

April 2022 / First entry.


Technical section

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

DEK_C, PS51998; DEK C-terminal (DEK-C) domain profile  (MATRIX)


1AuthorsKappes F. Scholten I. Richter N. Gruss C. Waldmann T.
TitleFunctional domains of the ubiquitous chromatin protein DEK.
SourceMol. Cell. Biol. 24:6000-6010(2004).
PubMed ID15199153

2AuthorsDevany M. Kotharu N.P. Matsuo H.
TitleSolution NMR structure of the C-terminal domain of the human protein DEK.
SourceProtein. Sci. 13:2252-2259(2004).
PubMed ID15238633

3AuthorsWaidmann S. Kusenda B. Mayerhofer J. Mechtler K. Jonak C.
TitleA DEK domain-containing protein modulates chromatin structure and function in Arabidopsis.
SourcePlant. Cell. 26:4328-4344(2014).
PubMed ID25387881

4AuthorsTakahashi K. Okabe H. Kanno S.I. Nagai T. Mizuno K.
TitleA pleckstrin homology-like domain is critical for F-actin binding and cofilin-phosphatase activity of Slingshot-1.
SourceBiochem. Biophys. Res. Commun. 482:686-692(2017).
PubMed ID27865840

5AuthorsSheng W. Yamashita S. Ohta A. Horiuchi H.
TitleFunctional differentiation of chitin synthases in Yarrowia lipolytica.
SourceBiosci. Biotechnol. Biochem. 77:1275-1281(2013).
PubMed ID23748777

6AuthorsFernandes C. Gow N.A.R. Gonçalves T.
TitleThe importance of subclasses of chitin synthase enzymes with myosin-like domains for the fitness of fungi. Fungal Biol. Rev. 30:1–14(2016).

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