Phospho-Histone (H1.3(T17)+H1.4(T17)) Recombinant Rabbit Monoclonal Antibody [SR38-03] (ET1602-11)

UNIPROT #

P10412

PROTEIN NAME

Phospho-Histone (H1.3(T17)+H1.4(T17))

SYNONYMS

Histone H1.3;Histone H1c;Histone H1s-2;HIST1H1DH1F3;Histone H1.4;Histone H1b;Histone H1s-4;HIST1H1EH1F4

SEQUENCE SIMILARITIES

Belongs to the histone H1/H5 family.

POST-TRANSLATIONAL MODIFICATION

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.

SUBCELLULAR LOCATION

Nucleus, Chromosome.

FUNCTION

Eukaryotic histones are basic and water soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene, that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.