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PROSITE documentation PDOC00287 |
Histone H3 is one of the four histones, along with H2A, H2B and H4, which forms the eukaryotic nucleosome core. It is a highly conserved protein of 135 amino acid residues [1,2,E1].
The following proteins have been found to contain a C-terminal H3-like domain:
We developed two signature patterns, The first one corresponds to a perfectly conserved heptapeptide in the N-terminal part of H3. The second one is derived from a conserved region in the central section of H3.
Last update:December 2004 / Pattern and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Wells D.E. Brown D. |
Title | Histone and histone gene compilation and alignment update. | |
Source | Nucleic Acids Res. 19:2173-2188(1991). | |
PubMed ID | 2041803 |
2 | Authors | Thatcher T.H. Gorovsky M.A. |
Title | Phylogenetic analysis of the core histones H2A, H2B, H3, and H4. | |
Source | Nucleic Acids Res. 22:174-179(1994). | |
PubMed ID | 8121801 |
3 | Authors | Sullivan K.F. Hechenberger M. Masri K. |
Title | Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere. | |
Source | J. Cell Biol. 127:581-592(1994). | |
PubMed ID | 7962047 |
4 | Authors | Stoler S. Keith K.C. Curnick K.E. Fitzgerald-Hayes M. |
Title | A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis. | |
Source | Genes Dev. 9:573-586(1995). | |
PubMed ID | 7698647 |
E1 | Title | https://www.ncbi.nlm.nih.gov/projects/HistoneDB2.0/index.fcgi/browse/ |