PROSITE documentation PDOC00479
TEA domain signature and profile


The TEA domain is a DNA-binding region of ~80 amino acids that has been named after the two proteins that originally defined the domain: TEF-1 and AbaA. It is also referred to as the ATTS domain because of the 4 proteins first found to harbor this motif (AbaA and TEC1 in yeast, TEF1/TEAD1 in vertebrates and Scalloped in fly). The TEA domain is located toward the amino terminus of eukaryotic transcription factors of the TEA/ATTS family. The consensus DNA sequence bound by an isolated TEA domain is N-[ATG]-G-[ATC]-A-T-N-T; where, N=A, T, C. or G [1,2,3,4].

The TEA domain is composed of a three-helix bundle with a homeodomain fold (see <PDB:2HZD>). It has a folded globular structure made of three α-helices, H1, H2, and H3. H1 and H2 are nearly anti-parallel and pack on either side of the H3, which is the DNA-recognition helix of the TEA domain. Two conserved serines are found on the DNA-binding surface. Phosphorylation of one or both of these could interfere with DNA-binding activity, by introducing electrostatic repulsion and/or steric hindrance, and help regulate TEA/ATTS transcription factor activity [3,4].

Some of the proteins that contain a TEA domain are listed below:

  • Mammalian enhancer factor TEF-1. TEF-1 can bind to two distinct sequences in the SV40 enhancer and is a transcriptional activator.
  • Mammalian TEF-3, TEF-4 and TEF-5 [5], putative transcriptional activators highly similar to TEF-1.
  • Drosophila scalloped protein (gene sd), a probable transcription factor that functions in the regulation of cell-specific gene expression during Drosophila development, particularly in the differentiation of the nervous system [6].
  • Emericella nidulans regulatory protein abaA. AbaA is involved in the regulation of conidiation (asexual spore); its expression leads to the cessation of vegetative growth.
  • Yeast trans-acting factor TEC1. TEC1 is involved in the activation of the Ty1 retrotransposon.
  • Caenorhabditis elegans hypothetical protein F28B12.2.

We developed both a pattern and a profile. The pattern covers helices H2 and H3, whereas the profile covers the whole domain.

Last update:

January 2017 / Profile and text revised.


Technical section

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

TEA_2, PS51088; TEA domain profile  (MATRIX)

TEA_1, PS00554; TEA domain signature  (PATTERN)


1AuthorsBuerglin T.R.
TitleThe TEA domain: a novel, highly conserved DNA-binding motif.
SourceCell 66:11-12(1991).
PubMed ID2070413

2AuthorsHwang J.J. Chambon P. Davidson I.
TitleCharacterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1.
SourceEMBO J. 12:2337-2348(1993).
PubMed ID8389695

3AuthorsAnbanandam A. Albarado D.C. Nguyen C.T. Halder G. Gao X. Veeraraghavan S.
TitleInsights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain.
SourceProc. Natl. Acad. Sci. U.S.A. 103:17225-17230(2006).
PubMed ID17085591

4AuthorsLandin-Malt A. Benhaddou A. Zider A. Flagiello D.
TitleAn evolutionary, structural and functional overview of the mammalian TEAD1 and TEAD2 transcription factors.
SourceGene 591:292-303(2016).
PubMed ID27421669

5AuthorsJacquemin P. Hwang J.-J. Martial J.A. Dolle P. Davidson I.
TitleA novel family of developmentally regulated mammalian transcription factors containing the TEA/ATTS DNA binding domain.
SourceJ. Biol. Chem. 271:21775-21785(1996).
PubMed ID8702974

6AuthorsCampbell S. Inamdar M. Rodrigues V. Raghavan V. Palazzolo M. Chovnick A.
TitleThe scalloped gene encodes a novel, evolutionarily conserved transcription factor required for sensory organ differentiation in Drosophila.
SourceGenes Dev. 6:367-379(1992).
PubMed ID1547938

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