KAT7: A Protein Involved in Multiple Cellular Processes and Potential Drug Target

Target Name: KAT7

NCBI ID: G11143

KAT7

KAT7: A Protein Involved in Multiple Cellular Processes and Potential Drug Target

Histone acetyltransferase (HAT) is a enzyme involved in the histamine response to stimuli, including allergens and stress hormones. HATs have been implicated in a wide range of physiological processes, including inflammation, stress, and cancer. The protein KAT7 has been shown to be a key regulator of HAT activity and is the focus of ongoing research as a potential drug target.

KAT7 is a 22-kDa protein that is expressed in a variety of tissues, including the brain, heart, liver, and intestine. It is a member of the KAT family, which includes several related proteins that share a conserved catalytic core. KAT7 is expressed in a highly tissue-specific manner, with high levels in the brain and low levels in the liver and other tissues.

KAT7 functions as a histone acetyltransferase, which means it adds an acetyl group to the histone proteins that make up the nucleosome. The nucleosome is the basic unit of chromatin and is composed of a core of DNA, a protein complex known as histone histone proteins (H1), and several other proteins that help to organize and maintain the nucleosome. By acetylating the histones, KAT7 helps to regulate the distribution of genetic information in the nucleus.

In addition to its role in regulating the nucleosome, KAT7 is also involved in the regulation of cellular processes that are critical for the survival and growth of cells. For example, KAT7 has been shown to play a role in the regulation of cell death, as well as in the regulation of cell proliferation and differentiation.

KAT7 has also been shown to be involved in the regulation of inflammation. In response to an allergen or other stressor, KAT7 is activated and has been shown to play a role in the regulation of the immune response. This is thought to be due to the fact that KAT7 is involved in the regulation of the production of pro-inflammatory cytokines, as well as the regulation of the production of anti-inflammatory cytokines.

KAT7 has also been shown to be involved in the regulation of pain. In response to pain, KAT7 is activated and has been shown to play a role in the regulation of the production of pro-inflammatory cytokines. This is thought to be due to the fact that KAT7 is involved in the regulation of the production of opioids, which are involved in the relief of pain.

Despite the many important functions of KAT7, the precise mechanisms that regulate its activity are not well understood. Several studies have shown that KAT7 is involved in the regulation of a wide range of cellular processes, including the regulation of DNA replication, gene expression, and cell death. In addition, several studies have shown that KAT7 is involved in the regulation of the immune response, the regulation of inflammation, and the regulation of pain.

Given the many important functions of KAT7, it is a promising target for drug development. Several studies have shown that inhibitors of KAT7 have the potential to treat a wide range of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. In addition, KAT7 has been shown to be involved in the regulation of many different cellular processes, making it a useful target for the development of new therapeutic strategies.

In conclusion, KAT7 is a protein that is involved in the regulation of a wide range of cellular processes, including the regulation of the nucleosome, cell death, inflammation, and pain. Its functions make it an attractive target for drug development, with potential for the treatment of a wide range of diseases. Further research is needed to fully understand the mechanisms that regulate KAT7 activity and to develop new therapeutic strategies for the treatment of diseases that are dependent on its function.

Protein Name: Lysine Acetyltransferase 7

Functions: Catalytic subunit of histone acetyltransferase HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance and embryonic development (PubMed:16387653, PubMed:21753189, PubMed:24065767, PubMed:26620551, PubMed:31767635, PubMed:31827282). Some complexes also catalyze acetylation of histone H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac, respectively), regulating DNA replication initiation, regulating DNA replication initiation (PubMed:10438470, PubMed:19187766, PubMed:20129055, PubMed:24065767). Specificity of the HBO1 complexes is determined by the scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE (JADE1, JADE2 and JADE3) scaffold direct KAT7/HBO1 specificity towards histone H4 (PubMed:19187766, PubMed:20129055, PubMed:24065767, PubMed:26620551). H3K14ac promotes transcriptional elongation by facilitating the processivity of RNA polymerase II (PubMed:31827282). Acts as a key regulator of hematopoiesis by forming a complex with BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and promoting erythroid differentiation (PubMed:21753189). H3K14ac is also required for T-cell development (By similarity). KAT7/HBO1-mediated acetylation facilitates two consecutive steps, licensing and activation, in DNA replication initiation: H3K14ac facilitates the activation of replication origins, and histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes, promoting DNA replication licensing (PubMed:10438470, PubMed:11278932, PubMed:18832067, PubMed:19187766, PubMed:20129055, PubMed:21856198, PubMed:24065767, PubMed:26620551). Acts as a positive regulator of centromeric CENPA assembly: recruited to centromeres and mediates histone acetylation, thereby preventing centromere inactivation mediated by SUV39H1, possibly by increasing histone turnover/exchange (PubMed:27270040). Involved in nucleotide excision repair: phosphorylation by ATR in response to ultraviolet irradiation promotes its localization to DNA damage sites, where it mediates histone acetylation to facilitate recruitment of XPC at the damaged DNA sites (PubMed:28719581). Acts as an inhibitor of NF-kappa-B independently of its histone acetyltransferase activity (PubMed:16997280)

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•   general information;
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•   protein biological mechanisms;
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•   expression level;
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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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