PRDM9: A Potential Drug Target and Biomarker (G56979)

Target Name: PRDM9

NCBI ID: G56979

PRDM9

PRDM9: A Potential Drug Target and Biomarker

Proteins play a crucial role in the functioning of the human body. They are the building blocks of life and are involved in every cell function. PRDM9, a protein discovered in 2008, has been identified as a potential drug target and biomarker. Its unique structure and function have made it an attractive target for researchers to investigate.

The protein encoded by PRDM9 is a member of the PR domain family, which is a conserved region found in many proteins. PR domain-containing proteins (PCPs) are a subclass of proteins that contain a characteristic domain called the PR domain. This domain is known for its ability to interact with other proteins, either positively or negatively, which can modulate the activity of the target protein. PRDM9 is a 19-kDa protein that contains a single PCP domain.

PRDM9 is involved in various cellular processes that are essential for the growth, development, and survival of living organisms. One of its functions is to interact with the protein p16INK4a. p16INK4a is a negative regulator of the PI3K/Akt signaling pathway, which is involved in various cellular processes, including cell growth, angiogenesis, and inflammation. The interaction between PRDM9 and p16INK4a allows for the regulation of cellular processes and the modulation of protein activity.

PRDM9 has also been shown to interact with the protein heat shock protein (Hsp70) protein. Hsp70 is a protein that plays a role in the regulation of cellular stress responses, and is involved in the detoxification of harmful substances and the protection of cells from oxidative stress. The interaction between PRDM9 and Hsp70 allows for the regulation of cellular stress responses and the modulation of protein activity.

In addition to its interactions with p16INK4a and Hsp70, PRDM9 has also been shown to interact with the protein casein kinase 2 (CK2). CK2 is a protein that is involved in the regulation of cell adhesion, and is known for its role in the development and maintenance of cancer. The interaction between PRDM9 and CK2 allows for the regulation of cell adhesion and the modulation of protein activity.

PRDM9 has also been shown to interact with the protein FAK. FAK is a protein that is involved in the regulation of cell signaling, and is known for its role in the development and maintenance of cancer. The interaction between PRDM9 and FAK allows for the regulation of cell signaling and the modulation of protein activity.

PRDM9 has been shown to play a role in the regulation of cellular processes that are essential for the growth, development, and survival of living organisms. Its unique structure and function have made it an attractive target for researchers to investigate. By studying the interaction between PRDM9 and its target proteins, researchers can gain insights into the regulation of cellular processes and the modulation of protein activity. This knowledge can have potential applications in the development of new drugs and therapies. PRDM9 is a potential drug target and biomarker that has the potential to revolutionize the field of biology and medicine.

Protein Name: PR/SET Domain 9

Functions: Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localization thereby promoting meiotic recombination (PubMed:24634223, PubMed:24095733, PubMed:26833727, PubMed:27129774). Can also methylate all four core histones with H3 being the best substrate and the most highly modified (PubMed:24095733, PubMed:24634223, PubMed:26833727). Is also able, on one hand, to mono and di-methylate H4K20 and on other hand to trimethylate H3K9 with the di-methylated H3K9 as the best substrate (By similarity). During meiotic prophase, binds specific DNA sequences through its zinc finger domains thereby determining hotspot localization where it promotes local H3K4me3 and H3K36me3 enrichment on the same nucleosomes through its histone methyltransferase activity (PubMed:26833727). Thereby promotes double-stranded breaks (DSB) formation, at this subset of PRDM9-binding sites, that initiates meiotic recombination for the proper meiotic progression (By similarity). During meiotic progression hotspot-bound PRDM9 interacts with several complexes; in early leptonema binds CDYL and EHMT2 followed by EWSR1 and CXXC1 by the end of leptonema. EWSR1 joins PRDM9 with the chromosomal axis through REC8 (By similarity). In this way, controls the DSB repair pathway, pairing of homologous chromosomes and sex body formation (By similarity). Moreover plays a central role in the transcriptional activation of genes during early meiotic prophase thanks to H3K4me3 and H3K36me3 enrichment that represents a specific tag for epigenetic transcriptional activation (By similarity). In addition performs automethylation (By similarity). Acetylation and phosphorylation of histone H3 attenuate or prevent histone H3 methylation (By similarity)

The "PRDM9 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PRDM9 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
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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