PHF14: Regulation of Protein Degradation (G9678)

Target Name: PHF14

NCBI ID: G9678

PHF14: Regulation of Protein Degradation

PHF14 (Proteasome-Regulated Facilitator 14) is a protein that is expressed in various tissues and cells throughout the body. It plays a crucial role in the regulation of protein degradation, which is a critical process that helps to maintain the stability and integrity of cellular structures and functions.

PHF14 is a member of the Proteasome family of proteins, which are involved in the degradation of proteins using the 26S proteasome. The 26S proteasome is a complex of enzymes that break down proteins into smaller peptides, which can then be recycled and reused by the cell.

PHF14 is expressed in a variety of tissues, including muscle, bone, and the brain, and is involved in the regulation of protein degradation in all of these tissues. It has been shown to play a role in the regulation of muscle protein synthesis and degradation , as well as the regulation of bone formation and resorption.

In addition to its role in protein degradation, PHF14 is also a potential drug target. Researchers have identified several potential drug-like compounds that can inhibit the activity of PHF14, and these compounds have been shown to have a variety of therapeutic effects, including the inhibition of cancer growth and the treatment of neurodegenerative diseases.

One of the challenges in the study of PHF14 and its potential drug targets is the complex structure and function of the protein. PHF14 is a large protein with a molecular weight of approximately 180 kDa, and it consists of several domains, including an N-terminus , a T-terminus, and a middle region that contains multiple conserved secondary structure elements.

The N-terminus of PHF14 contains a putative N-endopeptidic domain, which is involved in the formation of the N-endopeptide that is added to the protein by the 26S proteasome. The T-terminus of PHF14 contains a potential conserved protein-coding region , as well as a putative C-terminal region that is involved in the formation of a distinct protein-coding domain.

The middle region of PHF14 contains several conserved structural elements that are involved in the regulation of protein function. This region includes a hydrophobic domain that is involved in the regulation of protein stability, as well as an aromatic repeat and a putative hydrophobic region that are involved in the regulation of protein-protein interactions.

In addition to its structural features, PHF14 has also been shown to have a variety of functional roles. For example, studies have shown that PHF14 plays a role in the regulation of muscle protein synthesis and degradation, as well as the regulation of bone formation and resorption.

In muscle, PHF14 is involved in the regulation of the translation of the muscle-specific gene P400, which encodes a protein that is involved in the regulation of muscle protein synthesis and degradation. Studies have shown that the activity of P400 is regulated by the levels of PHF14, and that the levels of PHF14 are directly proportional to the levels of muscle protein.

In bone, PHF14 is involved in the regulation of bone formation and resorption. Studies have shown that PHF14 plays a role in the regulation of bone resorption by osteoclasts, which are cells that break down bone tissue. This is accomplished through the regulation of the activity of the protein known as TRPV2, which is involved in the regulation of bone temperature and the production of reactive oxygen species (ROS).

In addition to its roles in muscle and bone, PHF14 has also been shown to play a role in the regulation of other tissues and processes. For example, studies have shown that PHF14 is involved in the regulation of protein synthesis and degradation in the brain, and that it plays a role in the regulation of neurotransmitter

Protein Name: PHD Finger Protein 14

Functions: Histone-binding protein (PubMed:23688586). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (By similarity). Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (By similarity)

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