Understanding RPS13: A Protein Implicated in Many Cellular Processes

Target Name: RPS13

NCBI ID: G6207

RPS13

Understanding RPS13: A Protein Implicated in Many Cellular Processes

RNA-protein interactions play a crucial role in many cellular processes, including gene regulation, translation, and post-translational modification. One of the key protein-protein interactions that have been extensively studied is the RNA-protein interaction between transcription factor RPS13 (RNA -protein interactions are also known as RNA-protein interactions or RNA-protein domains) and its target proteins. RPS13 is a key regulator of gene expression and has been implicated in many diseases, including cancer, neurodegenerative diseases, and neurodevelopmental disorders.

The RPS13 protein is a key component of the RNA-protein interaction network. It is a small non-coding RNA molecule that contains a unique RNA-protein domain. The RPS13 protein functions as a scaffold to recruit and localize RISC (ribonucleoprotein-associated small nucleotide regulatory proteins) and other RNA-protein interactions to their target proteins.

The RPS13 protein has been shown to interact with a wide range of target proteins, including coding genes, non-coding RNAs, and protein-protein interactions. It has been implicated in many cellular processes, including gene regulation, translation, DNA replication, and post-translational modification.

One of the key functions of RPS13 is its role in gene regulation. RPS13 has been shown to interact with many transcription factors, including activator protein 1 (AP-1), nuclear factor of activator of transcription (NFAT), and p53. These interactions play a crucial role in regulating gene expression and are often targeted by drugs that are used to treat diseases associated with these factors.

Another function of RPS13 is its role in translation. RPS13 has been shown to interact with the protein translation factore4 (PTF2), which is involved in the regulation of protein synthesis. These interactions may be important for the regulation of protein synthesis and could be potential drug targets for diseases associated with protein synthesis.

RPS13 has also been implicated in DNA replication. It has been shown to interact with the protein DNA replication factor1 (DNRC1), which is involved in the regulation of DNA replication. These interactions may be important for the regulation of DNA replication and could be potential drug targets for diseases associated with DNA replication.

In addition to its role in gene regulation, RPS13 has also been implicated in post-translational modification. It has been shown to interact with the protein ubiquitin, which is involved in the modification of proteins for degradation. These interactions may be important for the regulation of protein degradation and could be potential drug targets for diseases associated with protein homeostasis.

Despite the many functions of RPS13, little is known about its biology. The precise mechanisms of RPS13's interaction with other proteins are not well understood, and further research is needed to fully understand its role in gene regulation and cellular processes.

In conclusion, RPS13 is a protein that has been shown to interact with a wide range of other proteins, including coding genes, non-coding RNAs, and protein-protein interactions. Its functions in gene regulation, translation, DNA replication, and post- translational modification are of great interest to researchers, and further research is needed to fully understand its biology.

Protein Name: Ribosomal Protein S13

Functions: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. 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)

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