Target Name: OGFOD1
NCBI ID: G55239
Other Name(s): uS12 prolyl 3-hydroxylase | 2-oxoglutarate and iron dependent oxygenase domain containing 1, transcript variant 1 | 2-oxoglutarate and iron dependent oxygenase domain containing 1 | OGFOD1 variant 1 | OGFD1_HUMAN | termination and polyadenylation 1 homolog | 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 | Prolyl 3-hydroxylase OGFOD1 | TPA1 | KIAA1612 | TPA1, termination and polyadenylation 1, homolog | Prolyl 3-hydroxylase OGFOD1 (isoform 1) | Termination and polyadenylation 1 homolog

uS12 Prolyl 3-Hydroxylase: A Potential Drug Target Or Biomarker

OGFOD1 (uS12 prolyl 3-hydroxylase) is a gene that encodes a protein known as uS12p3H, which is a critical enzyme involved in the metabolism of prolyl hydroxylation. Prolyl hydroxylation is a post-translational modification that involves the addition of a hydroxyl group to specific amino acid residues, such as lysine or arginine. This modification is important for the regulation of protein stability, localization, and interactions with other molecules.

The uS12p3H protein is a member of the S12 family of enzymes, which are involved in a variety of cellular processes, including cell signaling, DNA replication, and metabolism. The uS12p3H protein is specifically involved in the regulation of prolyl hydroxylation and is a key player in the pathway that converts prolyl amino acids to their hydrated forms.

One of the unique features of uS12p3H is its specificity for the hydroxyl group. While other enzymes in the S12 family are capable of adding a variety of different post-translational modifications, uS12p3H is specifically designed to add a hydroxyl group to only lysine and arginine residues. This specificity makes uS12p3H a valuable tool for the study of prolyl hydroxylation and the regulation of protein stability.

In addition to its specificity for lysine and arginine, uS12p3H also has several other unique features that make it a potential drug target or biomarker. One of the most significant is its expression pattern. uS12p3H is primarily expressed in the brain, which suggests that it may be involved in the regulation of important brain functions. Additionally, uS12p3H has been shown to play a role in the development and progression of a variety of neurological diseases, including Alzheimer's disease and Parkinson's disease.

Another potential mechanism by which uS12p3H may be involved in the regulation of protein stability is its role in the regulation of protein localization. Prolyl hydroxylation is a critical step in the regulation of protein localization, as it can alter the properties of proteins and influence their interactions with other molecules. By modifying the hydroxyl groups on lysine and arginine residues, uS12p3H can alter the stability and localization of these proteins, which may have important implications for their function and stability.

Finally, uS12p3H may also be a potential biomarker for certain diseases. The expression and activity of uS12p3H have been shown to be altered in a variety of diseases, including Alzheimer's disease, Parkinson's disease, and multiple sclerosis. These changes in uS12p3H expression and activity may be associated with the development and progression of these diseases, and may be potential targets for therapeutic intervention.

In conclusion, OGFOD1 (uS12 prolyl 3-hydroxylase) is a protein that plays a critical role in the regulation of prolyl hydroxylation and may be a valuable drug target or biomarker for the treatment of a variety of neurological diseases. Its specificity for the hydroxyl group and its role in the regulation of protein stability and localization make it a promising target for therapeutic intervention. Further research is needed to fully understand the mechanisms of uS12p3H and its potential as a therapeutic agent.

Protein Name: 2-oxoglutarate And Iron Dependent Oxygenase Domain Containing 1

Functions: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein translation termination efficiency. Involved in stress granule formation

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