DDHD2: A Potential Drug Target and Biomarker (G23259)
DDHD2: A Potential Drug Target and Biomarker
Double cysteine-containing domains (DDHDs) are a class of protein structures that have been identified in a variety of organisms, including humans. These domains are characterized by the presence of two cysteine residues, which are often linked by a disulfide bond. One of the most well-studied DDHDs is DDHD2, which has been identified as a potential drug target and biomarker for various diseases.
The Importance of DDHD2 as a Drug Target
DDHD2 has been shown to play a role in a variety of cellular processes, including cell signaling, DNA replication, and metabolism. It is also involved in the regulation of cellular interactions with the extracellular matrix (ECM), which is important for tissue repair and regeneration.
One of the key reasons for the potential of DDHD2 as a drug target is its involvement in cell signaling pathways. The DAD (DNA-protein-DNA) domain in DDHD2 is known to play a role in the regulation of DNA replication and repair, while the second cysteine-containing domain (CCSD) is involved in the regulation of cellular interactions with ECM. These domains have been shown to interact with a variety of proteins, including the transcription factor, p53, which is a key regulator of DNA replication and repair.
Additionally, the N-terminal region of DDHD2 contains a unique farnesylated cysteine residue, which is known to play a role in the regulation of cellular processes such as cell signaling and metabolism. This cysteine residue is also involved in the regulation of the activity of the protein kinase, which is a key regulator of cellular processes that are important for the development and maintenance of tissues.
The Potential of DDHD2 as a Biomarker
DDHD2 has also been shown to be a potential biomarker for various diseases. For example, it has been shown to be involved in the regulation of the development and progression of cancer, and it has been shown to be involved in the regulation of neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.
In addition to its potential as a drug target, DDHD2 has also been shown to be a potential biomarker for a variety of diseases. For example, it has been shown to be involved in the regulation of the development and progression of cancer, and it has been shown to be involved in the regulation of neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.
Conclusion
In conclusion, DDHD2 is a protein structure that has been identified in a variety of organisms, including humans. It is characterized by the presence of two cysteine residues, which are often linked by a disulfide bond. The N-terminal region of DDHD2 contains a unique farnesylated cysteine residue, which is involved in the regulation of cellular processes such as cell signaling and metabolism. Additionally, the DAD (DNA-protein-DNA) domain in DDHD2 is known to play a role in the regulation of DNA replication and repair, while the second cysteine-containing domain (CCSD) is involved in the regulation of cellular interactions with ECM. These domains have been shown to interact with a variety of proteins, including the transcription factor, p53. Therefore, DDHD2 is a potential drug target and biomarker for various diseases.
Protein Name: DDHD Domain Containing 2
Functions: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane
More Common Targets
DDI1 | DDI2 | DDIAS | DDIT3 | DDIT4 | DDIT4L | DDN | DDO | DDOST | DDR1 | DDR2 | DDRGK1 | DDT | DDTL | DDX1 | DDX10 | DDX11 | DDX11-AS1 | DDX11L1 | DDX11L10 | DDX11L2 | DDX11L8 | DDX11L9 | DDX12P | DDX17 | DDX18 | DDX18P1 | DDX19A | DDX19A-DT | DDX19B | DDX20 | DDX21 | DDX23 | DDX24 | DDX25 | DDX27 | DDX28 | DDX31 | DDX39A | DDX39B | DDX39B-AS1 | DDX3P1 | DDX3X | DDX3Y | DDX4 | DDX41 | DDX42 | DDX43 | DDX46 | DDX47 | DDX49 | DDX5 | DDX50 | DDX50P1 | DDX51 | DDX52 | DDX53 | DDX54 | DDX55 | DDX56 | DDX59 | DDX59-AS1 | DDX6 | DDX60 | DDX60L | DDX6P1 | DEAF1 | Death-associated protein kinase | Decapping Complex | DECR1 | DECR2 | DEDD | DEDD2 | Dedicator of cytokinesis protein | DEF6 | DEF8 | DEFA1 | DEFA10P | DEFA11P | DEFA1B | DEFA3 | DEFA4 | DEFA5 | DEFA6 | DEFA7P | DEFA8P | DEFA9P | DEFB1 | DEFB103A | DEFB103B | DEFB104A | DEFB104B | DEFB105A | DEFB105B | DEFB106A | DEFB106B | DEFB107A | DEFB108B | DEFB108F | DEFB109A