DTX2: A Key Enzyme in The Ubiquitin System (G113878)

Target Name: DTX2

NCBI ID: G113878

DTX2: A Key Enzyme in The Ubiquitin System

Deltex 2 (DTX2), also known as E3 ubiquitin ligase, is a protein that plays a crucial role in the regulation of gene expression and cell signaling. It is a key enzyme in the ubiquitin system, which is responsible for the degradation of damaged or unnecessary proteins. Mutations in the DTX2 gene have been linked to a range of diseases, including cancer, neurodegenerative diseases, and developmental disorders. As a result, targetingDTX2 has become an attractive research topic in recent years.

DTX2 is a 21-kDa protein that is expressed in a variety of tissues, including muscle, liver, and brain. It is highly conserved, with a calculated pI of 5.5. DTX2 is composed of a 166 amino acid residue protein and has a calculated molecular mass of 19.1 kDa. It has a single transmembrane domain and a nucleotide binding site in the cytoplasm.

DTX2 is a key enzyme in the ubiquitin system, as it catalyzes the formation of ubiquitin chains on target proteins. This process is critical for protein stability, localization, and degradation. DTX2 uses a specific template to recognize and attach to the target protein. It then guides the formation of a ubiquitin chain and activates the protein for degradation. This process is regulated by various factors, including the activity of other ubiquitin enzymes and the presence of specific ubiquitin chains.

DTX2 has been shown to play a role in a variety of cellular processes, including cell signaling, DNA repair, and protein degradation. It has been shown to interact with numerous protein substrates, including activating transcription factor A (ATF-A1),

Protein Name: Deltex E3 Ubiquitin Ligase 2

Functions: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity

More Common Targets