PROSITE documentation PDOC51156ELM2 domain profile
The ELM2 (EGL-27 and MTA1 homology) domain was first described in Egl-27, a Caenorhabditis elegans protein that plays a fundamental role in patterning during embryonic development [1]. Most ELM2 domain-containing proteins also possess a SANT domain, implying a structural and/or functional relationship between these two motifs. Many proteins containing an ELM2 domain are known components of characterized transcription- and chromatin-regulatory complexes containing one or more histone deacetylases (HDACs). The evolutionarily conserved ELM2 domain has been shown to function as a transcriptional repression domain through recruitment of HDAC activity [2].
Some proteins known to contain a ELM2 domain are listed below:
- Vertebrate mesoderm induction early response 1 (MI-ER1), a nuclear protein that contains an N-terminal acidic domain with potent transcriptional activity.
- Vertebrate CoREST, a developmental regulator.
- Mammalian metastasis-associated protein MTA1, a component of the NURD complex, which has histone deacetylase and ATP-dependent nucleosome remodelling activities.
- Mammalian metastasis-associated protein MTA2, a component of a chromatin regulatory complex.
- Mammalian metastasis-associated protein MTA3.
- Drosophila melanogaster MTA1-like.
- Drosophila melanogaster GRUNGE (Gug).
- Drosophila melanogaster transcriptional corepressor Atro.
- Caenorhabditis elegans Egl-27 and Egr-1. They are redundantly required for embryonic patterning.
The profile we developed covers the entire extended ELM2 domain [2].
Last update:October 2005 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Solari F. Bateman A. Ahringer J. |
Title | The Caenorhabditis elegans genes egl-27 and egr-1 are similar to MTA1, a member of a chromatin regulatory complex, and are redundantly required for embryonic patterning. | |
Source | Development 126:2483-2494(1999). | |
PubMed ID | 10226007 |
2 | Authors | Ding Z. Gillespie L.L. Paterno G.D. |
Title | Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain. | |
Source | Mol. Cell. Biol. 23:250-258(2003). | |
PubMed ID | 12482978 |
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