Target Name: FICD
NCBI ID: G11153
Review Report on FICD Target / Biomarker Content of Review Report on FICD Target / Biomarker
FICD
Other Name(s): Fic S-phase protein cell division homolog | adenosine monophosphate-protein transferase FICD | FIC domain containing | de-AMPylase FICD | FIC domain-containing protein | huntingtin-interacting protein 13 | huntingtin-interacting protein E | HIP13 | Huntingtin interacting protein E | FICD_HUMAN | Huntingtin yeast partner E | Huntingtin-interacting protein 13 | HIP-13 | AMPylator FICD | Protein adenylyltransferase FICD | UNQ3041 | huntingtin interactor protein E | fic S-phase protein cell division homolog | Huntingtin interacting protein 13 | FIC domain protein adenylyltransferase | De-AMPylase FICD | huntingtin yeast partner E | HYPE | Huntingtin interactor protein E | Huntingtin-interacting protein E

FICD: A Protein Involved in Cell Division and Cancer

FICD, or Fic S-phase protein cell division homolog, is a protein that plays a crucial role in the process of cell division. It is a member of the S-phase protein family, which includes several other proteins that are involved in the different stages of cell division.

One of the key functions of FICD is to regulate the timing of cell division. During the S phase, the cell prepares for cell division by producing copies of its genetic material and ensuring that all necessary changes are made to the cell's DNA. FICD helps to ensure that the S phase occurs at the right time, and that the cell is ready for cell division when it is.

FICD is also involved in the regulation of the transition from the S phase to the G1 phase. During the G1 phase, the cell grows and performs necessary functions to prepare for cell division. FICD helps to ensure that the G1 phase occurs at the right time, and that the cell is ready for cell division when it is.

In addition to its role in regulating cell division, FICD is also involved in the regulation of cell growth and the development of cancer. It has been shown to be involved in the regulation of cell cycle progression, and has been linked to the development of certain types of cancer.

Due to its involvement in cell division and its potential role in the development of cancer, FICD has been identified as a potential drug target. Researchers are currently working to develop drugs that can inhibit the activity of FICD and prevent the development of cancer. These drugs may be used to treat a variety of different types of cancer, including breast cancer, lung cancer, and colon cancer.

FICD is also of interest as a biomarker for cancer diagnosis and monitoring. Its expression has been shown to be elevated in a variety of cancer types, including breast cancer, lung cancer, and colon cancer. This makes it a potential marker for cancer diagnosis and monitoring. Researchers are currently working to develop methods for the detection and quantification of FICD expression in cancer cells, in order to improve the accuracy of cancer diagnosis and treatment.

Overall, FICD is a protein that plays a crucial role in the process of cell division and has the potential to be a drug target or biomarker for cancer. Further research is needed to fully understand its role in cell division and its potential as a drug or biomarker.

Protein Name: FIC Domain Protein Adenylyltransferase

Functions: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:25601083). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (PubMed:19362538, PubMed:25601083)

The "FICD Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about FICD comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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