H1-4

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a replication-dependent histone that is a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.

Full Name

H1.4 linker histone, cluster member

Alternative Names

H1E; H1.4; H1F4; RMNS; H1s-4; HIST1H1E; dJ221C16.5

Function

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).

Biological Process

Chromosome condensation
Negative regulation of DNA recombinationSource:GO_Central
Negative regulation of transcription by RNA polymerase IISource:Ensembl
Nucleosome assembly

Cellular Location

Nucleus
Chromosome
Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.

Involvement in disease

Rahman syndrome (RMNS):
An autosomal dominant syndrome characterized by intellectual disability and overgrowth manifesting as increased birth length, height, weight, and/or head circumference.

PTM

H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.
Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.
ADP-ribosylated on Ser-150 in response to DNA damage.