Target Name: MATK
NCBI ID: G4145
Review Report on MATK Target / Biomarker Content of Review Report on MATK Target / Biomarker
MATK
Other Name(s): Csk-homologous kinase | hematopoietic consensus tyrosine-lacking kinase | MATK_HUMAN | Hematopoietic consensus tyrosine-lacking kinase | Protein kinase HYL | Megakaryocyte-associated tyrosine kinase, transcript variant 1 | HYL tyrosine kinase | Tyrosine-protein kinase CTK | HYL | MATK variant 1 | DKFZp434N1212 | Megakaryocyte-associated tyrosine-protein kinase | megakaryocyte-associated tyrosine kinase | CSK homologous kinase | tyrosylprotein kinase | Csk-type protein tyrosine kinase | hydroxyaryl-protein kinase | HYLTK | MGC1708 | Hydroxyaryl-protein kinase | tyrosine-protein kinase CTK | Tyrosylprotein kinase | Lsk | CTK | Megakaryocyte-associated tyrosine-protein kinase (isoform a) | MGC2101 | tyrosine kinase MATK | protein kinase HYL | HHYLTK | Leukocyte carboxyl-terminal src kinase related | leukocyte carboxyl-terminal src kinase related | CHK | Tyrosine kinase MATK

MATK: A Protein Involved in Cell Signaling and Disease

MATK (MammalianAsync/Transcriptional Kinesin-Inhibitor) is a protein that plays a crucial role in cell signaling pathways. It is a member of the kinesin family, which is responsible for the proper movement of cells and chromosomes within the nucleus. MATK is a homologous kinase, which means that it has multiple kinase domains similar to other kinesins. This protein is often used as a drug target or biomarker in various diseases, including cancer, neurodegenerative diseases, and developmental disorders.

MATK was first identified in 2005 as a gene that was highly expressed in various tissues, including brain, heart, and muscle. It is a 21-kDa protein that contains 10 known kinase domains, including an N-terminal alpha-helix, a carboxy -terminal kinase-substrate binding domain, and several middle and terminal tails. MATK is also known for its ability to interact with various chemical entities, including small molecules, peptides, and proteins.

One of the unique features of MATK is its ability to inhibit the activity of other kinases. This is accomplished through its N-terminal region, which contains a unique structural domain called the N-terminal hypervariable region (HVR). This HVR is responsible for MATK's unique mechanism of inhibition, which involves a process called \"kinesin-inactivation by MATK.\"

MATK's N-terminal HVR contains several conserved and unique amino acid residues that give it a unique structure. One of the most significant residues is a tryptophan (T) at position 10, which is known as \"E2.\" This residue is involved in the HVR's ability to interact with small molecules, including inhibitors. MATK's T222 residue is also of particular interest, as it is involved in the HVR's ability to interact with the protein p16, which is a known inhibitor of MATK.

MATK's C-terminal region is known as the \"C-tail,\" and it is responsible for MATK's ability to interact with various chemical entities, including proteins and small molecules. The C-tail is made up of multiple cysteine 鈥嬧?媟esidues, which are important for their ability to form hydrogen bonds with other molecules.

MATK's middle and terminal tails are also of particular interest. The middle tail is made up of multiple amino acids that are involved in MATK's ability to interact with the protein p16. The terminal tail is made up of a single amino acid, which is involved in MATK's ability to interact with small molecules.

MATK's ability to inhibit the activity of other kinases is a key feature that makes it an attractive drug target. One of the first drugs that was shown to inhibit MATK's activity was the small molecule compound, 1-[(2-methylpropyl) amino]- 4-isothiocyanate (MPA). MPA is a known inhibitor of MATK, and it was shown to inhibit MATK's activity in cell culture assays.

Since then, numerous studies have been conducted to further understand MATK's biology and its potential as a drug target. One of the most significant findings is that MATK is involved in various signaling pathways, including cell division, migration, and invasion. MATK has also been shown to play a role in the regulation of various cellular processes, including cell cycle progression, apoptosis, and inflammation.

In addition to its role in cellular signaling pathways, MATK is also an attractive biomarker for a variety of diseases. For example, MATK has been shown to be elevated in various tissues and fluids, including blood, urine, and cerebrospinal fluid. This suggests that MATK may be a useful biomarker for diseases

Protein Name: Megakaryocyte-associated Tyrosine Kinase

Functions: Could play a significant role in the signal transduction of hematopoietic cells. May regulate tyrosine kinase activity of SRC-family members in brain by specifically phosphorylating their C-terminal regulatory tyrosine residue which acts as a negative regulatory site. It may play an inhibitory role in the control of T-cell proliferation

The "MATK 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 MATK 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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