Structural and functional characterization of STAP2, a protein kinase substrate for the protein Brk kinase

Target Name: STAP2

NCBI ID: G55620

STAP2

Structural and functional characterization of STAP2, a protein kinase substrate for the protein Brk kinase

Staple 2 (STAP2) is a protein that is highly conserved in various organisms, including bacteria, yeast, and eukaryotes. It is a key protein for cell signaling, specifically for the Brk protein kinase. STAP2 has been identified as a potential drug target and a biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Brk kinase is a protein that is involved in cell signaling, specifically in the regulation of cell growth, differentiation, and survival. It is a serine/thr domain kinase that is involved in several signaling pathways, including the TGF-β pathway, the PI3K/Akt pathway, and the NF-kappa-B pathway. STAP2 is a well-known protein that is involved in these signaling pathways, and it has been identified as a potential Brk kinase substrate.

STAP2 is a 21-kDa protein that is composed of 115 amino acid residues. It has a unique structure that is characterized by a N-terminal transmembrane domain, a catalytic domain, and a C-terminal T-loop. The N-terminal transmembrane domain is responsible for the protein's ability to interact with various signaling molecules, including Brk.

The catalytic domain of STAP2 is the region that is responsible for its catalytic activity. It is a conserved region that is involved in the regulation of various cellular processes, including cell signaling, DNA replication, and metabolism. The catalytic domain of STAP2 contains several unique features that are involved in its catalytic activity.

The C-terminal T-loop is a conserved region that is involved in the regulation of various cellular processes, including cell signaling and DNA replication. It is a critical region that is involved in the regulation of the Brk kinase, as well as other protein kinases.

STAP2 has been shown to play a role in several cellular processes, including cell signaling, DNA replication, and metabolism. It has been shown to interact with various signaling molecules, including Brk, TOR, and NF-kappa-B. It is also known to be involved in the regulation of cellular processes that are important for cancer progression, such as cell migration, invasion, and metastasis.

In addition to its role in cell signaling, STAP2 has also been shown to be involved in the regulation of DNA replication. It has been shown to play a role in the regulation of DNA replication, specifically in the S phase of the cell cycle. It is also known to be involved in the regulation of DNA repair, specifically in the G1 phase of the cell cycle.

In conclusion, STAP2 is a protein that is involved in several cellular processes, including cell signaling, DNA replication, and metabolism. It has a unique structure that is characterized by a N-terminal transmembrane domain, a catalytic domain, and a C-terminal T-loop. STAP2 has been shown to play a role in the regulation of various cellular processes, including cell signaling, DNA replication, and metabolism, as well as the regulation of cancer progression. As a result, STAP2 is a potential drug target and a biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Protein Name: Signal Transducing Adaptor Family Member 2

Functions: Substrate of protein kinase PTK6. May play a regulatory role in the acute-phase response in systemic inflammation and may modulate STAT3 activity

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•   general information;
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•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   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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