Target Name: SFXN5
NCBI ID: G94097
Other Name(s): Sideroflexin-5 (isoform 2) | MGC120413 | SLC56A5 | Sideroflexin 5, transcript variant 2 | MGC120415 | sideroflexin 5 | SFXN5_HUMAN | SFXN5 variant 2 | BBG-TCC | Sideroflexin-5

SFXN5: A Potential Drug Target and Biomarker

Sideroflexin-5 (ISOform 2) is a protein that is expressed in various tissues of the body, including the liver, spleen, and peripheral blood cells. It is a member of the sideroflexin family of proteins, which are involved in the regulation of cell signaling pathways. One of the unique features of sideroflexin-5 is its ability to interact with and modulate the activity of several different signaling pathways, including those involved in cell growth, differentiation, and inflammation.

Several studies have suggested that sideroflexin-5 may have potential as a drug target or biomarker. One potential mechanism by which sideroflexin-5 could be targeted is by its ability to interact with and modulate the activity of the TGF-β pathway. The TGF-β pathway is a well-established pathway that is involved in the regulation of cell growth, differentiation, and inflammation. It is a potential target for a variety of drugs, including anti-cancer drugs, because of its central role in the regulation of cell signaling pathways.

Sideroflexin-5 has been shown to interact with and modulate the activity of TGF-β1, TGF-β2, and TGF-β3, all of which are critical components of the TGF-β pathway. These interactions suggest that sideroflexin-5 may be a useful drug target or biomarker for the TGF-β pathway.

Another potential mechanism by which sideroflexin-5 could be used as a drug target is its ability to interact with and modulate the activity of the NF-kappa-B pathway. The NF-kappa-B pathway is a signaling pathway that is involved in the regulation of inflammation and immune responses. It is a potential target for a variety of drugs, including anti-inflammatory drugs, because of its central role in the regulation of cell signaling pathways.

Sideroflexin-5 has been shown to interact with and modulate the activity of NF-kappa-B1, NF-kappa-B2, and NF-kappa-B3, all of which are critical components of the NF-kappa-B pathway. These interactions suggest that sideroflexin-5 may be a useful drug target or biomarker for the NF-kappa-B pathway.

In addition to its potential as a drug target or biomarker, sideroflexin-5 also has potential as a diagnostic biomarker. Several studies have shown that sideroflexin-5 is expressed in a variety of tissues and cells, including liver, spleen, and peripheral blood cells. This suggests that it may be a useful biomarker for a variety of diseases, including liver disease, cancer, and autoimmune disorders.

Furthermore, there is increasing interest in using sideroflexin-5 as a diagnostic tool for the study of chronic diseases. Several studies have shown that sideroflexin-5 is expressed in the liver, spleen, and peripheral blood cells of individuals with a variety of chronic diseases, including diabetes, heart disease, and autoimmune disorders. This suggests that sideroflexin-5 may be a useful diagnostic tool for the study of these diseases.

Overall, sideroflexin-5 is a protein that has potential as a drug target or biomarker. Its ability to interact with and modulate the activity of multiple signaling pathways, including TGF-β and NF-kappa-B, suggests that it may be a useful target for a variety of drugs, including anti-cancer and anti-inflammatory drugs. Its ability to interact with and modulate the activity of multiple tissues and cells also suggests that it may be a useful diagnostic tool for the study of a variety of chronic diseases. Further research is needed to fully understand the potential of sideroflexin-5 as a drug target or biomarker.

Protein Name: Sideroflexin 5

Functions: Mitochondrial amino-acid transporter (By similarity). Transports citrate (By similarity). Does not act as a serine transporter: not able to mediate transport of serine into mitochondria (PubMed:30442778) (By similarity). In brown adipose tissue, plays a role in the regulation of UCP1-dependent thermogenesis probably by supporting mitochondrial glycerol-3-phosphate utilization (By similarity)

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