Target Name: H2AC13
NCBI ID: G8329
Other Name(s): Histone H2A/p | H2A/c | H2A clustered histone 13 | histone cluster 1 H2A family member i | Histone 1, H2ag | H2AC17 | HIST1H2AL | histone cluster 1, H2ai | H2A histone family, member N | Histone H2A/e | H2AC11 | H2AFC | histone H2A/ptl | Histone 1, H2ai | H2A histone family, member D | HIST1H2AI | HIST1H2AM | H2A histone family, member I | H2A histone family, member P | histone 1, H2ai | Histone H2A type 1 | HIST1H2AG | Histone 1, H2am | H2AC16 | H2A1_HUMAN | Histone 1, H2al | Histone 1, H2ak | H2A.1 | HIST1H2AK | Histone H2A/ptl | H2AC15 | H2A histone family, member C | Histone H2A type 1-J | FLJ92027

Histone H2A/p: A Protein Regulator of Gene Expression and Cell Signaling

Histone H2A/p (H2AC13) is a protein that plays a critical role in the regulation of gene expression and cell signaling. It is a key component of histones, which are small non-coding RNAs that make up the nucleosome, the basic unit of DNA in a cell. Histones help to organize DNA in a specific way, ensuring that genes are properly transcribed and translated into proteins.

One of the key functions of histones is to interact with DNA. Histone H2A/p is specifically designed to interact with the protein histone H2B, which is the most abundant histone in the cell. This interaction allows histone H2A/p to play a role in the regulation of gene expression.

Histone H2A/p is also involved in the regulation of cell signaling pathways. It has been shown to play a role in the regulation of cell cycle progression, and it has been shown to interact with proteins that are involved in cell signaling pathways such as tyrosine kinase signaling, G-protein-coupled receptor signaling, and T-cell receptor signaling.

In addition to its role in cell signaling, histone H2A/p is also a potential drug target. Researchers have identified several potential drugs that can inhibit histone H2A/p, and these drugs have been shown to have a variety of therapeutic effects. For example , one class of drugs that have been shown to inhibit histone H2A/p is called histone deacetylases (HDACs). HDACs are enzymes that remove acetyl groups from histones, which can alter their stability and interaction with other proteins.

Studies have shown that HDACs can have a variety of therapeutic effects, including the inhibition of cancer growth, the treatment of neurodegenerative diseases, and the treatment of autoimmune diseases. In addition to its potential therapeutic uses, histone H2A/p is also a valuable biomarker for the diagnosis and prognosis of certain diseases.

One of the challenges in the study of histone H2A/p is its complex structure. Histones are highly conserved proteins, but they can differ in their levels of different post-translational modifications, such as acetylation and polyglutamylation. This complexity can make it difficult to study the protein in a controlled manner.

In order to study histone H2A/p more effectively, researchers have developed a variety of techniques to purify and manipulate the protein. These techniques include affinity purification, protein fragmentation, and mass spectrometry. Affinity purification can be used to selectively remove specific modifications from the protein, such as HDACs, while protein fragmentation can be used to increase the amount of protein available for study. Mass spectrometry can be used to identify and quantify the different modifications of the protein.

Despite these advances in the study of histone H2A/p, much work remains to be done. The protein is still a relatively unstudied protein, and there are many questions that remain about its functions and potential therapeutic uses. Additionally, the complexity of the protein's structure makes it difficult to study it in a controlled manner, and the development of new techniques for its study is an ongoing priority.

In conclusion, histone H2A/p is a protein that plays a critical role in the regulation of gene expression and cell signaling. It is a key component of histones, which are small non-coding RNAs that make up the nucleosome, and it is involved in the regulation of cell cycle progression, cell signaling pathways, and the development of certain diseases. While the study of histone H2A/p is an ongoing process, the potential therapeutic uses of this protein are vast, and new techniques for its study are being developed to further our understanding of its functions.

Protein Name: H2A Clustered Histone 13

Functions: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling

More Common Targets

H2AC14 | H2AC15 | H2AC16 | H2AC17 | H2AC18 | H2AC20 | H2AC21 | H2AC25 | H2AC3P | H2AC4 | H2AC6 | H2AC7 | H2AJ | H2AP | H2AX | H2AZ1 | H2AZ1-DT | H2AZ2 | H2AZ2-DT | H2AZP2 | H2BC1 | H2BC10 | H2BC11 | H2BC12 | H2BC12L | H2BC13 | H2BC14 | H2BC15 | H2BC17 | H2BC18 | H2BC20P | H2BC21 | H2BC26 | H2BC27P | H2BC3 | H2BC4 | H2BC5 | H2BC6 | H2BC7 | H2BC8 | H2BC9 | H2BP1 | H2BP2 | H2BP3 | H2BW1 | H2BW2 | H2BW4P | H3-3A | H3-3B | H3-4 | H3-5 | H3-7 | H3C1 | H3C10 | H3C11 | H3C12 | H3C13 | H3C14 | H3C15 | H3C2 | H3C3 | H3C4 | H3C6 | H3C7 | H3C8 | H3P16 | H3P36 | H3P37 | H3P44 | H3P5 | H3P6 | H4C1 | H4C11 | H4C12 | H4C13 | H4C14 | H4C15 | H4C16 | H4C2 | H4C3 | H4C4 | H4C5 | H4C6 | H4C7 | H4C8 | H4C9 | H6PD | HAAO | HABP2 | HABP4 | HACD1 | HACD2 | HACD3 | HACD4 | HACE1 | HACL1 | HADH | HADHA | HADHAP1 | HADHB