NRBP1's Role in Myeloid Leukemia Development (G29959)

Target Name: NRBP1

NCBI ID: G29959

NRBP1

NRBP1's Role in Myeloid Leukemia Development

Myeloid leukemia factor 1 (MLL-1) adaptor protein, also known as NRBP1, is a protein that plays a crucial role in the development and progression of myeloid leukemias, one of the most common types of cancer in the United States.NRBP1 is a transmembrane protein that is expressed in a variety of tissues, including blood cells, nervous system cells, and epithelial cells. It is known for its ability to interact with and regulate the activity of several key signaling pathways that are involved in the development and progression of cancer.

NRBP1 functions as an adaptor protein, which means it can interact with and transfer a phosphate group from one protein to another. In the context of myeloid leukemias, NRBP1 is involved in the regulation of several key signaling pathways, including the PI3K/Akt signaling pathway, the TGF-β signaling pathway, and the NF-kappa-B signaling pathway.

NRBP1 and the PI3K/Akt signaling pathway

The PI3K/Akt signaling pathway is a key signaling pathway that is involved in the regulation of cell growth, survival, and angiogenesis. This pathway is the target of several anti-cancer drugs, including some that are currently in use to treat myeloid leukemias.

NRBP1 is known to play a role in the regulation of PI3K/Akt signaling pathway. It has been shown to interact with the protein Pyk2, which is a key regulator of the PI3K/Akt pathway. Pyk2 is a protein that is involved in the regulation of several different signaling pathways, including cell growth, survival, and angiogenesis.

NRBP1 has been shown to play a role in the regulation of Pyk2 activity by interacting with its tyrosine residue. This interaction between NRBP1 and Pyk2 allows Pyk2 to modulate the activity of other proteins that are involved in the PI3K/Akt pathway.

NRBP1 and the TGF-β signaling pathway

The TGF-β signaling pathway is another key signaling pathway that is involved in the regulation of cell growth, survival, and angiogenesis. This pathway is the target of several anti-cancer drugs, including some that are currently in use to treat myeloid leukemias.

NRBP1 is also known to play a role in the regulation of TGF-β signaling pathway. It has been shown to interact with the protein Fyn, which is a key regulator of the TGF-β pathway. Fyn is a protein that is involved in the regulation of several different signaling pathways, including cell growth, survival, and angiogenesis.

NRBP1 has been shown to play a role in the regulation of Fyn activity by interacting with its tyrosine residue. This interaction between NRBP1 and Fyn allows Fyn to modulate the activity of other proteins that are involved in the TGF-β pathway.

NRBP1 and the NF-kappa-B signaling pathway

The NF-kappa-B signaling pathway is a third key signaling pathway that is involved in the regulation of cell growth, survival, and angiogenesis. This pathway is the target of several anti-cancer drugs, including some that are currently in use to treat myeloid leukemias.

NRBP1 is also known to play a role in the regulation of NF-kappa-B signaling pathway. It has been shown to interact with the protein IKK尾, which is a key regulator of the NF-kappa-B pathway. IKK尾 is a protein that is involved in the regulation of several different signaling pathways, including cell growth, survival, and angiogenesis.

NRBP1 has been shown to play a role in the regulation of IKK尾 activity by interacting with its tyrosine residue. This interaction between NRBP1 and IKK尾 allows IKK尾 to

Protein Name: Nuclear Receptor Binding Protein 1

Functions: Required for embryonic development (By similarity). Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (By similarity). May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases (PubMed:11956649). Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication (PubMed:15084397)

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