Understanding UBE2W: A Protein Crucial for Cell Regulation (G55284)

Target Name: UBE2W

NCBI ID: G55284

UBE2W

Understanding UBE2W: A Protein Crucial for Cell Regulation

UBE2W (E2 ubiquitin-conjugating enzyme W) is a protein that plays a crucial role in the regulation of protein degradation in the cell. It is a member of the ubiquitin family of proteins and is responsible for the covalent attachment of certain proteins to ubiquitin, a protein that plays a central role in the degradation of damaged or dysfunctional proteins. UBE2W is widely expressed in many different cell types and is involved in a wide range of cellular processes, including cell signaling, DNA replication, and stress response.

One of the key functions of UBE2W is its role in the degradation of damaged proteins. When a protein is damaged or dysfunctional, it can be targeted for degradation by the ubiquitin-proteasome system, a complex of enzymes that removes damaged or dysfunctional proteins from the cell. UBE2W is part of this system and is involved in the covalent attachment of proteins to ubiquitin, which is then used to ubiquitinate the protein and facilitate its degradation.

In addition to its role in protein degradation, UBE2W is also involved in the regulation of DNA replication. During DNA replication, UBE2W is required for the accurate duplication of DNA sequences. It is a component of the DNA replication machinery and is involved in the formation of the double helix.

UBE2W is also involved in a number of other cellular processes, including cell signaling, stress response, and inflammation. It is a signaling molecule that can interact with a variety of different signaling pathways and is involved in the regulation of cell proliferation, apoptosis, and autophagy. It is also involved in the regulation of inflammation and has been shown to play a role in the development of certain diseases, such as cancer.

Despite its involvement in a wide range of cellular processes, UBE2W is not well understood. There are currently no known drugs that target UBE2W specifically, and research into its function and potential as a drug target is in its infancy. However, its role in the regulation of protein degradation and DNA replication makes it an attractive target for future research and development.

In conclusion, UBE2W (E2 ubiquitin-conjugating enzyme W) is a protein that plays a crucial role in the regulation of protein degradation, DNA replication, and other cellular processes. Its role in these processes makes it an attractive target for future research and development, and its potential as a drug target is an exciting area of study. Further research is needed to fully understand the function of UBE2W and its potential as a therapeutic agent.

Protein Name: Ubiquitin Conjugating Enzyme E2 W

Functions: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed:20061386, PubMed:21229326). Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini (PubMed:23560854, PubMed:23696636, PubMed:25436519). Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway (PubMed:19111657, PubMed:21229326). In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate (PubMed:25436519)

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