/ H3 / Variant: H3.3

Description

The major replication-independent or replacement H3, important for development, transcription, and chromosome segregation. It typically differs from the canonical H3 by only a few amino acids that are necessary for replication-independent assembly.
Alternate names: hv2, soH3-1, soH3-2

Features

Below, you can explore the features of H3.3 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
Rme2
Human and rat Arginine methylation site
Rme1
Human Arginine methylation site
Rci
Human Arginine citrullination site
Tph
Human Threonine phosphorylation site
Kme3
Human and rat Lysine methylation site
Kac
Human and rat Lysine acetylation site
Kme2
Human and rat Lysine methylation site
Kme1
Human and rat Lysine methylation site
Kbio
Human Lysine biotinylation site
Sph
Human and rat Serine phosphorylation site
Kar
Human Lysine PTM site, newly identified modification by Mass Spectrometry
m
H3.3-specific modification site
Yph
Human Tyrosine phosphorylation site
General histone type features
alphaN
AlphaN-helix
R1
Minor groove arginine at the alphaN DNA binding site, SHL ±6.5
R2
Minor groove arginine at alpha1-alpha1 DNA binding site, SHL ±1.5
alpha1
Alpha1-helix, first helix of histone fold
loopL1
L1 loop connecting first and second helices of histone fold. Part of the L1L2 DNA binding site formed by H3 and H4 at SHL ±0.5.
beta1
Beta-strand in L1L2 DNA binding site
R3
Minor groove arginine at L1L2 DNA binding site, SHL ±2.5
alpha2
Alpha2-helix, second helix of histone fold
loopL2
L2 loop connecting second and third helices of histone fold. Part of L1L2 DNA binding site formed by H3 and H4 at SHL ±2.5.
beta2
Beta-strand in L1L2 DNA binding site
alpha3
Alpha3-helix, third helix of histone fold

References

  1. Talbert PB, Ahmad K, et al. "A unified phylogeny-based nomenclature for histone variants." Epigenetics Chromatin, 2012. PMID: 22650316
  2. Postberg J, Forcob S, et al. "The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms." BMC Evol Biol, 2010. PMID: 20738881
  3. Orsi GA, Couble P, et al. "Epigenetic and replacement roles of histone variant H3.3 in reproduction and development." Int J Dev Biol, 2009. PMID: 19412883
  4. Yuen BT and Knoepfler PS. "Histone H3.3 mutations: a variant path to cancer." Cancer Cell, 2013. PMID: 24229707
  5. Malik HS and Henikoff S. "Phylogenomics of the nucleosome." Nat Struct Biol, 2003. PMID: 14583738
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.
Sequence preview and annotation... LOADING





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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.