JARID2: A Protein Implicated in Cellular Processes (G3720)

Target Name: JARID2

NCBI ID: G3720

JARID2

JARID2: A Protein Implicated in Cellular Processes

JARID2, a protein that belongs to the JARID family, is a protein that plays a critical role in the interaction between the journal article and the protein AT-rich domain. JARID2 is highly conserved across various species, including humans, and is found in various cellular compartments, including the endoplasmic reticulum, the cytosol, and the nucleus. The JARID2 protein has been implicated in various cellular processes, including the regulation of protein-protein interactions, the detoxification of xenobiotics, and the regulation of gene expression.

JARID2 is a protein that is composed of 254 amino acid residues and has a calculated molecular mass of 33.1 kDa. It has a unique structure that is composed of a distinct N-terminal region, a long amino acid region, and a C-terminal region. The N-terminal region is composed of a single amino acid residue, while the long amino acid region is composed of multiple amino acid residues that include a variety of different conserved domains, including a leucine-rich repeat (LRR), a conserved domain, and a putative transmembrane domain (TMD). The C-terminal region is composed of a single amino acid residue that is similar to the N-terminal region.

The JARID2 protein is involved in the interaction between the journal article and the protein AT-rich domain. The AT-rich domain is a conserved protein that is found in various cellular compartments and is involved in various cellular processes, including protein-protein interactions, DNA repair, and cell signaling. The JARID2 protein has been shown to interact with the AT-rich domain in a variety of cellular processes, including the regulation of protein-protein interactions, the detoxification of xenobiotics, and the regulation of gene expression.

JARID2 has been shown to play a critical role in the regulation of protein-protein interactions in various cellular processes. For example, JARID2 has been shown to interact with the protein Myb, which is involved in the detoxification of xenobiotics. The interaction between JARID2 and Myb has been shown to play a critical role in the detoxification of xenobiotics, such as polycyclic aromatic hydrocarbons (PAHs) and polycyclic aromatic nitrogen compounds (PANs).

JARID2 has also been shown to play a critical role in the regulation of gene expression in various cellular processes. For example, JARID2 has been shown to interact with the protein p21, which is involved in the regulation of cell apoptosis (programmed cell death). The interaction between JARID2 and p21 has been shown to play a critical role in the regulation of cell apoptosis, including the regulation of neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.

JARID2 has also been shown to play a critical role in the regulation of protein-protein interactions in various cellular processes. For example, JARID2 has been shown to interact with the protein Bcl-2, which is involved in the regulation of cell growth and apoptosis. The interaction between JARID2 and Bcl-2 has been shown to play a critical role in the regulation of cell growth and apoptosis, including the regulation of cancer.

JARID2 is a protein that has been implicated in various cellular processes, including the regulation of protein-protein interactions, the detoxification of xenobiotics, and the regulation of gene expression. The JARID2 protein has a unique structure that is composed of a distinct N-terminal region, a long amino acid region, and a C-terminal region. The JARID2 protein is highly conserved across various species, including humans, and is found in various cellular compartments, including the endoplasmic reticulum, the cytosol, and the nucleus. Further research is needed to fully understand the role of JARID2 in

Protein Name: Jumonji And AT-rich Interaction Domain Containing 2

Functions: Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis (PubMed:20075857). Acts as an accessory subunit for the core PRC2 (Polycomb repressive complex 2) complex, which mediates histone H3K27 (H3K27me3) trimethylation on chromatin (PubMed:20075857, PubMed:29499137, PubMed:31959557). Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells, thereby playing a key role in stem cell differentiation and normal embryonic development (PubMed:20075857). In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases (By similarity). Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5 (By similarity). Participates in the negative regulation of cell proliferation signaling (By similarity). Does not have histone demethylase activity (By similarity)

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