Target Name: PTOV1
NCBI ID: G53635
Other Name(s): DKFZp586I111 | PTOV1 extended AT-hook containing adaptor protein, transcript variant 1 | PTOV1 extended AT-hook containing adaptor protein | Prostate tumor-overexpressed gene 1 protein | PTOV1 variant 1 | activator interaction domain-containing protein 2 | MGC71475 | PTOV1_HUMAN | PTOV-1 | prostate tumor overexpressed 1 | Prostate tumor-overexpressed gene 1 protein (isoform 1) | ACID2 | Activator interaction domain-containing protein 2 | Prostate tumor overexpressed gene 1

PTOV1: A Promising Drug Target / Biomarker

Post-Translational Modification (PTM) of proteins is a critical post-translational modification that plays a significant role in regulating protein stability, localization, and interactions. Among the various PTMs, the phosphorylation of tyrosine (PTY) is of particular interest due to its involvement in various cellular signaling pathways. PTOV1, a protein that localizes to the endoplasmic reticulum (ER) and is involved in regulating protein export, has been identified as a potential drug target or biomarker. In this article, we will explore the structure and function of PTOV1, its potential as a drug target, and the current research on its development as a drug.

Structure and Function

PTOV1 is a 21-kDa protein that consists of a 156 amino acid protein chain with a calculated pI of 4.97. The protein has a unique post-translational modification profile, with 22% of its amino acids modified post-translationally. Specifically, PTOV1 has 55% post-translational phosphorylation at its catalytic site, which is located at amino acid position 192. This PTM provides a unique mechanism for the regulation of protein stability and localization.

PTOV1 functions as a negative regulator of the export of endoplasmic reticulum (ER) proteins, which are involved in various cellular signaling pathways. The ER is a specialized organelle that plays a critical role in the secretion of proteins from the cell. However, the ER is also home to various diseases, including neurodegenerative disorders, where the misfolding and degradation of proteins play a significant role in the progression of the disease.

PTOV1's role in regulating ER protein export is essential for the maintenance of cellular homeostasis and the regulation of various signaling pathways. The post-translational modification of PTOV1's catalytic site by tyrosination provides a mechanism for the negative regulation of protein export, ensuring that the cell maintains a constant levels of various proteins and ensures the integrity of cellular signaling pathways.

Drug Target Potential

PTOV1's unique post-translational modification profile and its involvement in the regulation of ER protein export make it an attractive drug target. The development of compounds that can specifically target and inhibit the activity of PTOV1 could lead to new treatments for various diseases.

One of the challenges in developing new drug targets is the identification of small molecules that can specifically interact with the protein of interest. To address this challenge, researchers have used various screening approaches, such as high-throughput screening (HTS) and virtual screening, to identify small molecules that can interact with PTOV1.

In addition to screening, researchers have also used structural bioinformatics tools to predict the binding of small molecules to the protein. This has led to the identification of several potential drug candidates that can interact with PTOV1, including small molecules that have been shown to interact with other proteins involved in the regulation of ER protein export.

Current Research

Current research on PTOV1 is focused on the development of new drug targets and the understanding of its function. Researchers have used various techniques to study the behavior of PTOV1, including biochemical, cellular, and structural studies.

One of the current research focus areas is the development of small molecules that can specifically target the PTOV1 catalytic site and inhibit its activity. Researchers have used various screening approaches, such as HTS and virtual screening, to identify small molecules that can interact with the PTOV1 catalytic site. These small molecules have been shown to interact with other proteins involved in the regulation of ER protein export, providing evidence for their potential as drug targets.

Another area of current research is the study of the mechanism of action of potential drug targets. Researchers have used various techniques, such as biochemical and structural studies, to understand the role of these small molecules in the regulation of ER protein export and the impact of these modifications on

Protein Name: PTOV1 Extended AT-hook Containing Adaptor Protein

Functions: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation

More Common Targets

PTOV1-AS1 | PTOV1-AS2 | PTP4A1 | PTP4A1P2 | PTP4A2 | PTP4A3 | PTPA | PTPDC1 | PTPMT1 | PTPN1 | PTPN11 | PTPN11P5 | PTPN12 | PTPN13 | PTPN14 | PTPN18 | PTPN2 | PTPN20 | PTPN20A | PTPN20CP | PTPN21 | PTPN22 | PTPN23 | PTPN3 | PTPN4 | PTPN5 | PTPN6 | PTPN7 | PTPN9 | PTPRA | PTPRB | PTPRC | PTPRCAP | PTPRD | PTPRE | PTPRF | PTPRG | PTPRH | PTPRJ | PTPRK | PTPRM | PTPRN | PTPRN2 | PTPRN2-AS1 | PTPRO | PTPRQ | PTPRR | PTPRS | PTPRT | PTPRU | PTPRVP | PTPRZ1 | PTRH1 | PTRH2 | PTRHD1 | PTS | PTTG1 | PTTG1IP | PTTG2 | PTTG3P | PTX3 | PTX4 | PUDP | PUDPP2 | PUF60 | PUM1 | PUM2 | PUM3 | PURA | PURB | PURG | PURPL | PUS1 | PUS10 | PUS3 | PUS7 | PUS7L | PUSL1 | Putative POM121-like protein 1 | Putative uncharacterized protein C12orf63 | PVALB | PVALEF | PVR | PVRIG | PVT1 | PWAR1 | PWAR4 | PWAR5 | PWAR6 | PWARSN | PWP1 | PWP2 | PWRN1 | PWRN2 | PWRN3 | PWWP2A | PWWP2B | PWWP3A | PWWP3B | PXDC1