Target Name: RARS2
NCBI ID: G57038
Review Report on RARS2 Target / Biomarker Content of Review Report on RARS2 Target / Biomarker
RARS2
Other Name(s): Arginyl-tRNA synthetase-like | Arginine--tRNA ligase (isoform 3) | Probable arginine--tRNA ligase, mitochondrial (isoform 1) | ArgRS | DALRD2 | Arginyl-tRNA synthetase 2, mitochondrial, transcript variant 1 | arginyl-tRNA synthetase 2, mitochondrial | Arginine-tRNA ligase | PRO1992 | RARSL | Arginyl-tRNA synthetase | probable arginyl-tRNA synthetase, mitochondrial | Probable arginyl-tRNA synthetase, mitochondrial | Arginine--tRNA ligase | PCH6 | SYRM_HUMAN | MGC14993 | OTTHUMP00000016833 | Arginyl-tRNA synthetase 2, mitochondrial | Probable arginine--tRNA ligase, mitochondrial | Arginyl-tRNA synthetase 2, mitochondrial, transcript variant 4 | MGC23778 | RARS2 variant 1 | dJ382I10.6 | RARS2 variant 4

RARS2: A Promising Drug Target for Cancer and Neurodegenerative Diseases

RARS2 (Arginyl-tRNA synthetase-like) is a gene that encodes a protein involved in the process of translation of RNA into proteins. Mutations in the RARS2 gene have been linked to various diseases, including cancer, neurodegenerative diseases, and developmental disorders. As a result, RARS2 has emerged as a promising drug target and biomarker for a variety of diseases. In this article, we will explore the biology of RARS2 and its potential as a drug target.

The RARS2 gene and its function

RARS2 is a member of the argineyl-tRNA synthetase (ATS) family, which is responsible for synthesizing tRNAArginine (ArG) from the amino acid Asp. The RARS2 gene is located on chromosome 16 at position 16.2 and encodes a protein with 214 amino acid residues.

The primary function of RARS2 is to synthesize ArG from Asp via a process called post-translational modification (PTM). RARS2 uses a specific set of ATP-dependent modules to initiate the synthesis reaction. These modules include: (1) the ATP-binding site, which is activated by ATP binding and provides energy for the synthesis reaction; (2) the ArG-binding site, which is activated by ArG binding and facilitates the interaction between RARS2 and ArG; and (3) the 尾-sheet, which is the binding site for various protein-protein interactions.

The RARS2 protein

RARS2 is a 214-amino acid protein that has a molecular weight of 30.1 kDa. The protein has a single transmembrane domain and a cytoplasmic tail. RARS2 is also known for having a nucleotide base composition that is highly conserved across different species, with a G-C ratio of 67.5.

RARS2 has been shown to play a role in various cellular processes, including cell signaling, DNA replication, and protein translation. One of the most significant functions of RARS2 is its role in protein translation. RARS2 is involved in the synthesis of proteins that are involved in cell signaling pathways, such as T-cell receptor signaling, and in the regulation of DNA replication and repair.

In addition to its role in protein synthesis, RARS2 has also been shown to play a role in the regulation of gene expression. Studies have shown that RARS2 can act as a negative regulator of the gene encoding the tumor suppressor protein p53. This suggests that RARS2 may be a potential drug target for cancer.

Diseases associated with RARS2 mutations

Mutations in the RARS2 gene have been linked to a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders. The most well-studied of these mutations is the R517X mutation, which is associated with the neurodegenerative disease ALS (Amyotrophic Lateral Sclerosis).

The R517X mutation is a missense mutation that results in the substitution of the amino acid Asp for Asn at position 517 in the RARS2 protein. This mutation has been shown to cause a loss of function in the RARS2 protein and to contribute to the development of neurodegenerative symptoms.

In addition to the R517X mutation, other mutations in the RARS2 gene have also been linked to various diseases, including cancer and neurodegenerative diseases. However, the full impact of these mutations on the function and regulation of RARS2 is not yet fully understood.

Drug targeting of RARS2

The potential of RARS2 as a drug target is based on its involvement in various cellular processes and its role in the regulation of gene expression. Drugs that target RARS2 have been shown to have potential therapeutic benefits in a variety of diseases.

One approach to targeting RARS2 is to use small molecules that can modulate its activity. For example, inhibitors of the R517X mutation have been shown to have therapeutic benefits in animal models of ALS. These inhibitors act by binding to the R517X mutation and preventing it from functioning as a critical regulator of the RARS2 protein.

Another approach to targeting RARS2 is to use antibodies that can specifically recognize and target the RARS2 protein. These antibodies have been shown to be effective in animal models of various diseases.

Protein Name: Arginyl-tRNA Synthetase 2, Mitochondrial

The "RARS2 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 RARS2 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

More Common Targets

Ras GTPase | Ras-Related C3 Botulinum Toxin Substrate (RAC) | Ras-related protein Ral | RASA1 | RASA2 | RASA3 | RASA4 | RASA4B | RASA4CP | RASA4DP | RASAL1 | RASAL2 | RASAL2-AS1 | RASAL3 | RASD1 | RASD2 | RASEF | RASGEF1A | RASGEF1B | RASGEF1C | RASGRF1 | RASGRF2 | RASGRP1 | RASGRP2 | RASGRP3 | RASGRP4 | RASIP1 | RASL10A | RASL10B | RASL11A | RASL11B | RASL12 | RASSF1 | RASSF10 | RASSF2 | RASSF3 | RASSF4 | RASSF5 | RASSF6 | RASSF7 | RASSF8 | RASSF8-AS1 | RASSF9 | RAVER1 | RAVER2 | RAX | RAX2 | RB1 | RB1-DT | RB1CC1 | RBAK | RBAK-RBAKDN | RBAKDN | RBBP4 | RBBP4P2 | RBBP4P6 | RBBP5 | RBBP6 | RBBP7 | RBBP8 | RBBP8NL | RBBP9 | RBCK1 | RBFA | RBFOX1 | RBFOX2 | RBFOX3 | RBIS | RBKS | RBL1 | RBL2 | RBM10 | RBM11 | RBM12 | RBM12B | RBM14 | RBM14-RBM4 | RBM15 | RBM15-AS1 | RBM15B | RBM17 | RBM17P1 | RBM18 | RBM19 | RBM20 | RBM22 | RBM22P1 | RBM23 | RBM24 | RBM25 | RBM26 | RBM26-AS1 | RBM27 | RBM28 | RBM3 | RBM33 | RBM34 | RBM38 | RBM39 | RBM4