Setmar: A Protein in Cell Signaling, GAP Signaling, Cell Cycle Progression, Inflammation and Tissue Repair

Target Name: SETMAR

NCBI ID: G6419

Setmar: A Protein in Cell Signaling, GAP Signaling, Cell Cycle Progression, Inflammation and Tissue Repair

Setmar (SETMR_HUMAN) is a protein that is expressed in human tissues and has been shown to play a role in a variety of biological processes. Several studies have suggested that Setmar may be a drug target or biomarker, and research is ongoing to determine its potential utility as a therapeutic intervention.

Setmar is a member of the superfamily of immediate-early gene products (SEP), which are characterized by the presence of a unique transmembrane segment that is involved in the rapid and efficient delivery of proteins to the cytoplasm. SEPs are involved in many different cellular processes, including cell signaling, intracellular signaling, and protein delivery to the cell surface.

One of the unique features of Setmar is its ability to form a stable interaction with the protein p120GTP, which is a key regulator of the GTPase-activating protein (GAP) signaling pathway. This interaction between Setmar and p120GTP allows Setmar to influence the activity of other proteins and to play a role in a variety of cellular processes, including cell signaling, migration, and invasion.

In addition to its role in the GAP signaling pathway, Setmar has also been shown to play a role in the regulation of cell cycle progression. Setmar has been shown to interact with the protein casein kinase (CK), which is involved in the regulation of cell cycle progression. This interaction between Setmar and CK allows Setmar to influence the activity of other proteins and to play a role in the regulation of cell growth and division.

Setmar has also been shown to play a role in the regulation of inflammation. Setmar has been shown to interact with the protein NF-kappa-B, which is involved in the regulation of inflammation. This interaction between Setmar and NF-kappa-B allows Setmar to influence the activity of other proteins and to play a role in the regulation of inflammatory responses.

In addition to its role in the regulation of inflammation, Setmar has also been shown to play a role in the regulation of cellular processes that are important for tissue repair and regeneration. Setmar has been shown to interact with the protein FBN1, which is involved in the regulation of blood vessel formation and tissue repair. This interaction between Setmar and FBN1 allows Setmar to influence the activity of other proteins and to play a role in the regulation of tissue repair and regeneration.

Several studies have suggested that Setmar may be a drug target or biomarker, and research is ongoing to determine its potential utility as an therapeutic intervention. For example, some researchers have shown that inhibiting the activity of Setmar using small molecules or antibodies can lead to a variety of cellular and molecular changes, including the inhibition of cell proliferation, the inhibition of migration, and the inhibition of inflammation. These findings suggest that Setmar may be an effective target for therapeutic intervention in a variety of diseases.

In conclusion, Setmar is a protein that is expressed in human tissues and has been shown to play a role in a variety of biological processes. Several studies have suggested that Setmar may be a drug target or biomarker, and research is ongoing to determine its potential utility as a therapeutic intervention. Further studies are needed to fully understand the role of Setmar in cellular and molecular processes, and to determine its potential as a therapeutic intervention.

Protein Name: SET Domain And Mariner Transposase Fusion Gene

Functions: Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity (PubMed:16332963, PubMed:16672366, PubMed:17877369, PubMed:17403897, PubMed:18263876, PubMed:22231448, PubMed:24573677, PubMed:20521842). In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining (PubMed:16332963, PubMed:21187428, PubMed:22231448). Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A (PubMed:18790802, PubMed:20457750)

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