Target Name: NAT10
NCBI ID: G55226
Review Report on NAT10 Target / Biomarker Content of Review Report on NAT10 Target / Biomarker
NAT10
Other Name(s): Kre33 | RNA cytidine acetyltransferase isoform a | NAT10 variant 1 | RNA cytidine acetyltransferase | RNA cytidine acetyltransferase isoform b | N-acetyltransferase 10, transcript variant 1 | N-acetyltransferase 10 (GCN5-related) | 18S rRNA cytosine acetyltransferase | N-acetyltransferase 10, transcript variant 2 | N-acetyltransferase-like protein | KIAA1709 | NAT10 variant 2 | N-acetyltransferase 10 | ALP | hALP | NAT10_HUMAN | NET43

NAT10 and Krce33: Unlocking The Regulator of Cellular Processes

NAT10 (Kre33) is a protein that is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is a member of the nucleotide-binding oligomerization domain (NOD) family, which is a group of proteins that play a critical role in regulating gene expression and DNA replication.

Kre33 is a small molecule that is able to interact with NAT10 and cause it to change its structure. This interaction between NAT10 and Krce33 is important for the function of NAT10, as it allows the protein to perform its role in regulating gene expression and DNA replication.

One of the key functions of NAT10 is its role in regulating the production of RNA. RNA is a critical molecule that is involved in the regulation of many cellular processes, including the development and maintenance of tissues, the replication of genetic information, and the regulation of various signaling pathways. NAT10 plays a key role in the production of RNA by helping to ensure that the necessary genetic information is copied and translated into RNA.

Another important function of NAT10 is its role in regulating DNA replication. DNA replication is the process by which a cell makes an exact copy of its genetic material. NAT10 plays a critical role in regulating the accuracy and efficiency of DNA replication by helping to ensure that the necessary genetic information is copied and translated into RNA.

In addition to its role in regulating DNA replication and RNA production, NAT10 also plays a key role in the regulation of cellular signaling pathways. Many cellular processes are regulated by the signaling pathways that are activated by various molecules. NAT10 plays a critical role in the regulation of these signaling pathways by helping to ensure that the necessary genetic information is copied and translated into RNA.

Despite the importance of its role in cellular regulation, NAT10 is not yet a well-studied protein. There is limited research on the mechanism of its interaction with Krce33, and the precise function of NAT10 in cellular regulation is not yet fully understood. However, the potential implications of NAT10 as a drug target or biomarker are significant.

In conclusion, NAT10 (Kre33) is a protein that plays a critical role in the regulation of various cellular processes, including the production of RNA, DNA replication, and cellular signaling pathways. Its interaction with Krce33 is important for the function of NAT10, and its potential as a drug target or biomarker make it an attractive target for further research.

Protein Name: N-acetyltransferase 10

Functions: RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)

The "NAT10 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 NAT10 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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