Modified Histone Proteins

Histone methyltransferase (HMT) proteins are involved in the post-translational modification called histone methylation which causes transcription repression or activation, depending on the target sites. Protein arginine methyltransferases (PRMTs) catalyze the methylation of arginine residues and histone methyltransferases (HMTs) catalyze the methylation of lysine residues.

Histone demethylase (HDM) proteins are involved in the post-translational modification called histone demethylation which entails the removal of methyl groups in modified histone proteins. Protein arginine demethylase (PRDM) catalyzes the removal of methyl groups from arginine residues while lysine demethylase (KDM) catalyzes the removal from lysine demethylase (KDM).

Histone acetyltransferase (HATs) proteins are involved in histone acetylation, or the addition of an acetyl group to lysine residues in the N-terminal tail and on the surface of the nucelosome core of histone proteins. They play a role in adjusting chromatin structure, leading to increased or decreased gene transcription levels. In general, histone acetylation is associated with increased gene expression.

Histone deacetylase (HDAC) proteins are involved in histone deacetylation, or the removal of an acetyl group to lysine residues in the N-terminal tail and on the surface of the nucelosome core of histone proteins. They play a role in adjusting chromatin structure, leading to increased or decreased gene transcription levels. In general, histone deacetylation is linked to transcriptional repression.

Histone phosphorylation has been shown to impact an assortment of processes such as chromosome condensation, transcription, DNA repair, and apoptosis. An increase in phosphorylation is linked to gene activation and cell growth. Investigating the changes in histone phosphorylation levels using histone phosphorylation proteins such as Aurora Kinase A (AURKA) and MSK1 will aid researchers in understanding diseases and their pathological processes and can advance the creation of protein ki...

These histone proteins are involved in sumoylation, a post-translational modification directed by an enzymatic cascade in which Small Ubiquitin-like Modifier (SUMO) proteins are attached to or detached from other proteins to change their function in cells. Detection of SUMO conjugation or protein Sumoylation can help researchers understand how this modification plays a role in regulating nuclear protein activity and in certain cellular processes, such as transcriptional regulation, apo...