Target Name: PTPN23
NCBI ID: G25930
Review Report on PTPN23 Target / Biomarker Content of Review Report on PTPN23 Target / Biomarker
PTPN23
Other Name(s): DKFZp564F0923 | HDPTP | PTPN23 variant 2 | protein tyrosine phosphatase non-receptor type 23 | NEDBASS | protein tyrosine phosphatase TD14 | Protein tyrosine phosphatase TD14 | Protein tyrosine phosphatase non-receptor type 23, transcript variant 1 | PTP-TD14 | PTPN23 variant 1 | his domain-containing protein tyrosine phosphatase | HD-PTP | Tyrosine-protein phosphatase non-receptor type 23 (isoform 2) | Protein tyrosine phosphatase non-receptor type 23, transcript variant 2 | PTN23_HUMAN | Tyrosine-protein phosphatase non-receptor type 23 | Tyrosine-protein phosphatase non-receptor type 23 (isoform 1) | KIAA1471 | His domain-containing protein tyrosine phosphatase

Introduction To PTPN23: Structure, Function and Potential Drug Targets

Post-Translational Modification (PTM) modification is a way to modify proteins, which can affect the structure, function and interaction of proteins. In living organisms, PTM modification is a ubiquitous phenomenon, and the regulation of protein function often involves PTM modification. PTPN23 is a protein whose function plays an important role in a variety of physiological processes. In this article, we will introduce relevant information of PTPN23, including its structure, function and PTM modification, and explore its potential as a potential drug target or biomarker.

structure

PTPN23 is a protein containing 23 amino acids with a molecular weight of approximately 40 kDa. The protein is composed of a single polypeptide chain, and its light chain and heavy chain are composed of 伪-helices and 尾-sheet structures. Observed from the molecular level, PTPN23 has a single 伪-helical structure, consisting of three 伪-helical units, including an alanine residue, and its pI is approximately 21.5. In addition, PTPN23 also has a 尾-sheet structure, consisting of 2 尾-sheet units, including an asparagine residue, and its pI is approximately 19.5.

Function

PTPN23 plays an important role in a variety of physiological processes, including cell proliferation, differentiation and tumor formation. During tumorigenesis, the expression of PTPN23 is often inhibited, which may lead to the growth and spread of tumor cells. In cell proliferation, PTPN23 can participate in the S phase of the cell cycle and play an important role in the transition from S phase to G1 phase.

In addition, PTPN23 is also involved in regulating the differentiation and function of immune cells. During the differentiation process of immune cells, PTPN23 can participate in antigen presentation and T cell differentiation. In addition, PTPN23 can also participate in the apoptosis of immune cells, which helps immune cells maintain homeostasis in the body.

PTM modification

In living organisms, PTM modification is a ubiquitous phenomenon, and the regulation of protein function often involves PTM modification. PTPN23 is no exception. PTPN23 plays an important role in a variety of physiological processes, and these physiological processes also involve PTM modification.

There are PTM modifications in both the light and heavy chains of PTPN23. The sixth amino acid residue on the light chain of PTPN23 is an alanine, and its modified form is cysteine 鈥嬧?媘ethylation. The seventh amino acid residue on the light chain of PTPN23 is an asparagine, and its modified form is asparagine carboxamide. The sixth amino acid residue on the heavy chain of PTPN23 is an alanine, and its modified form is cysteine 鈥嬧?媘ethylation. The seventh amino acid residue on the heavy chain of PTPN23 is an asparagine, and its modified form is asparagine carboxamide.

PTM modifications can affect protein structure, function, and interactions. The PTM modification of PTPN23 has an important impact on its function.

As a drug target or biomarker

As a protein, PTPN23 has great potential as a drug target or biomarker. Since PTPN23 plays an important role in a variety of physiological processes, studying the structure, function and PTM modification of PTPN23 can provide an important theoretical basis for our understanding of these physiological processes and provide an important reference for the development of new drugs.

in conclusion

PTPN23 is a protein that plays an important role in various physiological processes. Its function is mainly regulated by PTM modification. Studying the structure, function and PTM modification of PTPN23 can provide an important theoretical basis for our understanding of these physiological processes and provide an important reference for the development of new drugs.

Protein Name: Protein Tyrosine Phosphatase Non-receptor Type 23

Functions: Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes (PubMed:18434552, PubMed:21757351). May act as a negative regulator of Ras-mediated mitogenic activity (PubMed:18434552). Plays a role in ciliogenesis (PubMed:20393563)

The "PTPN23 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 PTPN23 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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