HECTD1: A Protein Role in Mitosis and Many Diseases (G25831)

Target Name: HECTD1

NCBI ID: G25831

HECTD1

HECTD1: A Protein Role in Mitosis and Many Diseases

HECTD1 (KIAA1131) is a protein that is expressed in nearly all human tissue cells, and it plays an important role in the cell cycle. HECTD1 plays a spindle role in mitosis, helps cells undergo mitosis, and regulates many important processes in the cell cycle.

HECTD1 is a non-histone protein with a molecular weight of approximately 42 kDa. HECTD1 exists in two forms in cells: ribosome-bound form and free form. During the cell cycle, HECTD1 mainly exists in the spindle and is responsible for assembling and maintaining the structure of the spindle. The ribosome-bound form of HECTD1 is a dimer formed by the non-covalent interaction of two HECTD1 molecules.

HECTD1 is closely associated with mitotic progression. During prophase of mitosis, HECTD1 forms the spindle head complex together with histone H1 to help spindle assembly. In mid-mitosis, HECTD1 forms the spindle centrosome together with histone H2 and participates in the formation of the spindle. During late mitosis, HECTD1 forms a spindle tail complex with histone H3 to help the spindle separate chromosomes.

HECTD1 is also related to the rate of mitotic progression. The larger the molecular weight of HECTD1, the slower the spindle assembly and separation. Therefore, the levels of HECTD1 reflect the progression rate of mitosis and are a potential drug target.

HECTD1 is also associated with many diseases. For example, elevated levels of HECTD1 are associated with many tumors, including breast, colon, and ovarian cancer. Reduced levels of HECTD1 are also associated with many neurodegenerative diseases, such as Parkinson's disease and Alzheimer's disease.

HECTD1's biological function also makes it an ideal molecule for studying the cell cycle. Researchers have used HECTD1 to study spindle assembly and separation, the rate of mitosis progression, and the role of other molecules during mitosis. For example, researchers used HECTD1 to study the role of histone H1 and histone H2 in spindle assembly and found that the binding of HECTD1 to histone H1 and histone H2 is a key step in the formation of HECTD1 in the spindle.

HECTD1 is a molecule that plays an important role in mitosis. The levels of HECTD1 reflect the progression rate of mitosis and can be used as a drug target to treat many diseases. Future research will continue to further investigate the role of HECTD1 in mitosis and discover the potential of HECTD1 as a drug target.

Protein Name: HECT Domain E3 Ubiquitin Protein Ligase 1

Functions: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:33711283). Mediates 'Lys-63'-linked polyubiquitination of HSP90AA1 which leads to its intracellular localization and reduced secretion (By similarity). Negatively regulating HSP90AA1 secretion in cranial mesenchyme cells may impair their emigration and may be essential for the correct development of the cranial neural folds and neural tube closure (By similarity). Catalyzes ubiquitination and degradation of ZNF622, an assembly factor for the ribosomal 60S subunit, in hematopoietic cells, thereby promoting hematopoietic stem cell renewal (PubMed:33711283)

The "HECTD1 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 HECTD1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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