InterPro : IPR005818

Name  Linker histone H1/H5, domain H15 Short Name  Histone_H1/H5_H15
Type  Domain Description  Histone proteins have central roles in both chromatin organisation (asstructural units of the nucleosome) and gene regulation (as dynamic componentsthat have a direct impact on DNA transcription and replication). EukaryoticDNA wraps around a histone octamer to form a nucleosome, the first order ofcompaction of eukaryotic chromatin. The core histone octamer is composed of acentral H3-H4 tetramer and two flanking H2A-H2B dimers. Each of the corehistone contains a common structural motif, called the histone fold, whichfacilitates the interactions between the individual core histones.In addition to the core histones, there is a "linker histone" called H1 (or H5 in avian species). The linker histones present in all multicellular eukaryotes are the most divergent group of histones, with numerous cell type- and stage-specific variant. Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures.Histone H5 performs the same function as histone H1, and replaces H1 in certain cells. The structure of GH5, the globular domain of the linker histone H5 is known [, ]. The fold is similar to the DNA-binding domain of the catabolite gene activator protein, CAP, thus providing a possible model for the binding of GH5 to DNA.The linker histones, which do not contain the histone fold motif, are critical to the higher-order compaction of chromatin, because they bind to internucleosomal DNA and facilitate interactions between individual nucleosomes. In addition, H1 variants have been shown to be involved in the regulation of developmental genes. A common feature of this protein family is a tripartite structure in which a globular (H15) domain of about 80 amino acids is flanked by two less structured N- and C-terminal tails. The H15domain is also characterised by high sequence homology among the family oflinker histones. The highly conserved H15 domain is essential for the bindingof H1 or H5 to the nucleosome. It consists of a three helix bundle (I-III),with a beta-hairpin at the C terminus. There is also a short three-residuestretch between helices I and II that is in the beta-strand conformation.Together with the C-terminal beta-hairpin, this strand forms the third strandof an antiparallel beta-sheet [, , , ].Proteins known to contain a H15 domain are:- Eukaryotic histone H1. The histones H1 constitute a family with many variants, differing in their affinity for chromatin. Several variants aresimultaneously present in a single cell. For example, the nucleatederythrocytes of birds contain both H1 and H5, the latter being an extremevariant of H1.- Eukaryotic MHYST family of histone acetyltransferase. Histoneacetyltransferases transfer an acetyl group from acetyl-CoA to the epsylon-amino group of lysine within the basic NH2-termini of histones, which bindthe acidic phosphates of DNA [].This entry represents the H15 domain.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR005819 Histone H5 Histone_H5 Family

1 Parent Features

Id Name Short Name Type
IPR011991 Winged helix-turn-helix DNA-binding domain WHTH_DNA-bd_dom Domain

6 Publications

First Author Title Year Journal Volume Pages
Ramakrishnan V Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. 1993 Nature 362 219-23
Zarbock J Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure. 1986 Proc Natl Acad Sci U S A 83 7628-32
Ono K The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. 2003 Nucleic Acids Res 31 7199-207
Mariño-Ramírez L The Histone Database: a comprehensive resource for histones and histone fold-containing proteins. 2006 Proteins 62 838-42
Cerf C Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: sequential assignment and secondary structure. 1993 Biochemistry 32 11345-51
Moore SD Uterine leiomyomata with t(10;17) disrupt the histone acetyltransferase MORF. 2004 Cancer Res 64 5570-7

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)