NSMCE1: A Drug Target / Disease Biomarker (G197370)

Target Name: NSMCE1

NCBI ID: G197370

NSMCE1

NSMCE1: A Drug Target / Disease Biomarker

NSMCE1 (Nucleotide-Sensitive Metal-Chaperone Enzyme 1) is a protein that plays a critical role in the regulation of DNA double-strand break repair in eukaryotic cells. It is a nucleotide-sensitive enzyme that uses metal ions as chaperones to facilitate the repair of double-strand breaks in DNA.

NSMCE1 is a member of the DNA damage repair machinery, which is responsible for repairing damage to DNA that can occur during various cellular processes, including DNA replication, transcription, and transcription factor binding. DNA double-strand breaks are one of the most damaging types of DNA damage, and NSMCE1 is involved in repairing these breaks by using metal ions as chaperones to facilitate the formation of a double-strand repair complex.

In addition to its role in DNA double-strand break repair, NSMCE1 has also been shown to play a key role in the regulation of gene expression. It is a negative regulator of the nuclear factor of activated T cells (NFAT), a transcription factor that regulates the expression of genes involved in cell signaling and differentiation.

NSMCE1 is also involved in the regulation of DNA replication, specifically in the repair of DNA double-strand breaks. It is a critical enzyme in the repair of single-strand breaks, which are the most common type of DNA damage that can occur during DNA replication.

NSMCE1 is a protein that is expressed in a variety of tissues and cells, including muscle, pancreas, and testes. It is also expressed in various cell types, including neurons and macrophages.

In conclusion, NSMCE1 is a protein that plays a critical role in the regulation of DNA double-strand break repair and gene expression. Its involvement in these processes makes it an attractive target for drug development. Further research is needed to fully understand the role of NSMCE1 in the regulation of DNA double-strand break repair and gene expression, and to develop effective treatments for these conditions.

Protein Name: NSE1 Homolog, SMC5-SMC6 Complex Component

Functions: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair (PubMed:29225034, PubMed:20864041). NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair (PubMed:18086888). MAGEF1-NSMCE1 ubiquitin ligase promotes proteasomal degradation of MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19 impairs the activity of several DNA repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters as cofactors (PubMed:29225034)

The "NSMCE1 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 NSMCE1 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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