/ H2A / Variant: macroH2A

Description

macroH2A is involved in X-inactivation and transcriptional regulation; can be found in inactivated X chromosome, gene promoters, and heterochromatin. It contains a ∼30 kDa additional globular macrodomain attached to C-terminus. Its taxonomic span was thought to be restricted to vertebrates, but this is currently disputed.
Alternate names: macroH2A1, macroH2A1.1, macroH2A1.2, macroH2A2, macroH2A2.1, macroH2A2.2, mH2A

Features

Below, you can explore the features of macroH2A from Homo sapiens, if available and how it compares to the canonical histones of the same type (first row). Canonical histone is shown in the first row, the names and descriptions of each feature can be found underneath. To explore variants from other species, please browse our curated sequences, automatically extracted sequences, or by taxonomy.

Keys: red - identical residues, blue - different residues (if more than one sequence).
Variant features
Linker domain
Linker domain
Macro domain
Macro domain, which can bind ADP-ribose.
General histone type features
alpha1ext
Alpha1-extension helix
alpha1
Alpha1-helix, first helix of histone fold
loopL1
L1 loop, connecting first and second helices of histone fold. Part of L1L2 DNA binding site formed by H2A and H2B at SHL ±3.5.
R1
Minor groove arginine at L1L2 DNA binding site, SHL ±3.5
beta1
Beta-strand in L1L2 DNA binding site
alpha2
Alpha2-helix, second helix of histone fold
ap
Acidic patch residues
loopL2
L2 loop, connecting second and third helices of histone fold. Part of L1L2 DNA binding site formed by H2A and H2B at SHL ±5.5.
R2
Minor groove arginine at L1L2 DNA binding site, SHL ±5.5
beta2
Beta-strand in L1L2 DNA binding site
alpha3
Alpha3-helix, third helix of histone fold
Docking domain
Docking domain locking H2A-H2B dimer on H3-H4 tetramer surface
alpha3ext
Alpha3-extension helix
beta3
Beta-strand between H2A and H4

References

  1. Talbert PB, Ahmad K, et al. "A unified phylogeny-based nomenclature for histone variants." Epigenetics Chromatin, 2012. PMID: 22650316
  2. Shaytan AK, Landsman D, et al. "Nucleosome adaptability conferred by sequence and structural variations in histone H2A-H2B dimers." Curr Opin Struct Biol, 2015. PMID: 25731851
  3. Chakravarthy S, Gundimella SK, et al. "Structural characterization of the histone variant macroH2A." Mol Cell Biol, 2005. PMID: 16107708
  4. Gamble MJ and Kraus WL. "Multiple facets of the unique histone variant macroH2A: from genomics to cell biology." Cell Cycle, 2010. PMID: 20543561
  5. Chakravarthy S and Luger K. "The histone variant macro-H2A preferentially forms "hybrid nucleosomes"." J Biol Chem, 2006. PMID: 16803903
A set of manually selected and validated histone sequences is listed in the table. Click on an entry in the table to update the annotated sequence preview: a variant will be compared with the canonical histone from the same species (if available). Alternatively, tick mark the sequences and use toolbar to view MSA, export or add to basket. Use search or filters to find particular entries.
Keys: red - identical residues, blue - different residues (if more than one sequence). For feature legend see summary tab.
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Note: variant classification might be ambigous between very similar variants. Classification scores against all variant models are available via advanced menu.
Features characteristic for a given histone type/variant are marked below the consensus sequence. For feature description see summary tabs of the corresponding variants pages.
Keys: red - 80% identical, blue - 50% identical columns. X-ambigous positions in consensus sequence.