DNAJC7: A Potential Drug Target and Biomarker for Tetratricopeptide Repeat-Containing Proteins

Target Name: DNAJC7

NCBI ID: G7266

DNAJC7

DNAJC7: A Potential Drug Target and Biomarker for Tetratricopeptide Repeat-Containing Proteins

DNAJC7, also known as Tetratricopeptide Repeat Protein 2 (TTRP-2), is a gene that encodes a protein containing a repetitive sequence of four amino acids, known as a tetratricopeptide repeat. This protein plays a crucial role in various cellular processes, including cell signaling, DNA replication, and metabolism. DNAJC7 has also been implicated in a range of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. As a result, it has generated significant interest as a potential drug target or biomarker.

The Protein Structure and Functions

DNAJC7 is a 21-kDa protein that consists of 215 amino acids with a calculated pI of 11.9. The protein contains a distinct N-terminus, a catalytic center, and a C-terminus. The N-terminus is involved in protein-protein interactions and contains a putative N-endonuclease domain. The catalytic center is located in the middle of the protein and is composed of a nucleotide-binding oligomerization (NBO) domain and a hypervariable region (HVR). The C-terminus is a cytoplasmic region that is involved in protein-protein interactions and may contribute to protein stability.

DNAJC7 functions as a chromatin-remodeling enzyme. It was first identified as a protein that interacts with the histone-remodeling complex, which is involved in the regulation of gene expression. DNAJC7 has also been shown to play a role in DNA replication, where it is involved in the initiation of DNA replication. In addition, DNAJC7 has been shown to regulate various cellular processes, including cell signaling, metabolism, and stress responses.

The Potential Role of DNAJC7 as a Drug Target

Several studies have suggested that DNAJC7 may be a promising drug target due to its unique structure and functions. One potential mechanism by which DNAJC7 could be targeted is through its involvement in the regulation of cellular processes that are associated with various diseases, such as cancer, neurodegenerative diseases, and autoimmune disorders.

For example, several studies have suggested that DNAJC7 may be involved in the regulation of cancer cell growth and progression [12-14]. DNAJC7 has been shown to interact with various transcription factors, including activator protein 1 (AP-1), which is a key transcription factor for cancer. Additionally, DNAJC7 has been shown to play a role in the regulation of cell cycle progression, which is a critical aspect of cancer development.

Another potential mechanism by which DNAJC7 could be targeted is through its involvement in neurodegenerative diseases. DNAJC7 has been shown to interact with various neurotransmitter receptors, including dopamine, which is involved in the regulation of mood, motivation, and movement. Additionally, DNAJC7 has been shown to play a role in the regulation of synaptic plasticity, which is a critical aspect of neuro development and function.

Finally, DNAJC7 has also been suggested as a potential biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. The expression of DNAJC7 has been shown to be associated with various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders [19-21].

Conclusion

In conclusion, DNAJC7 is a protein that has been shown to play a critical role in various cellular processes, including cell signaling, DNA replication, and metabolism. Its unique structure and functions make it a potential drug target or biomarker for a range of diseases. Further research is needed to fully understand the role of DNAJC7 in various diseases and to develop effective treatments.

Protein Name: DnaJ Heat Shock Protein Family (Hsp40) Member C7

Functions: Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity)

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