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PROSITE documentation PDOC51156 [for PROSITE entry PS51156]
ELM2 domain profile


Description

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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Technical section

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

ELM2, PS51156; ELM2 domain profile  (MATRIX)


References

1AuthorsSolari F. Bateman A. Ahringer J.
TitleThe 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.
SourceDevelopment 126:2483-2494(1999).
PubMed ID10226007

2AuthorsDing Z. Gillespie L.L. Paterno G.D.
TitleHuman MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain.
SourceMol. Cell. Biol. 23:250-258(2003).
PubMed ID12482978



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