Proline-rich AKT1 Substrate 1: A Key Regulator of The AKT Pathway

Target Name: AKT1S1

NCBI ID: G84335

AKT1S1

Proline-rich AKT1 Substrate 1: A Key Regulator of The AKT Pathway

AKT1S1 (Proline-rich AKT1 substrate 1) is a protein that is expressed in various tissues throughout the body, including muscle, heart, and brain. It is a key regulator of the cell signaling pathway known as the AKT pathway, which is involved in a wide range of physiological processes, including muscle contractions, blood pressure, and neurotransmitter release.

The AKT pathway is a highly conserved protein that is involved in the regulation of many cellular processes that are critical for life. It is composed of three key components: the protein kinase Akt (also known as P-110), the protein inhibitor p110, and the protein adapter protein kinase substrate binding protein (also known as p21).

AKT1S1 is a key component of the AKT1 substrate, which is a protein that is targeted by the protein kinase B (PKB) to regulate the activity of the AKT pathway. The AKT1 substrate is composed of various proteins, including AKT1S1, which is known as Proline-rich AKT1 substrate 1.

Proline-rich AKT1 substrate 1 is a 21-kDa protein that is composed of 155 amino acid residues. It has a highly conserved catalytic domain, which is known as the C-terminal hypervariable region (HVR), and a unique N-terminus that is involved in protein-protein interactions.

The N-terminus of Proline-rich AKT1 substrate 1 is a 20-amino acid residue that contains a conserved putative transmembrane domain (TMD) and a conserved carboxylic acid residue (CER). The TMD is a region of the membrane that is involved in protein-protein interactions and is thought to play a role in the regulation of the AKT pathway.

The CER is a region of the membrane that is involved in the regulation of the activity of the AKT pathway. It is thought to play a role in the inhibition of the activity of the protein kinase B (PKB), which is a key regulator of the AKT pathway.

AKT1S1 has been shown to play a critical role in the regulation of the AKT pathway. It is a potent inhibitor of PKB and has been shown to inhibit the activity of the enzyme calcineurin, which is a key regulator of the PKB pathway.

In addition to its role in the regulation of the AKT pathway, Proline-rich AKT1 substrate 1 has also been shown to play a critical role in the regulation of many other cellular processes. It is involved in the regulation of muscle contractions, blood pressure, and neurotransmitter release, and is thought to play a role in the regulation of the growth and differentiation of tissues.

Overall, Proline-rich AKT1 substrate 1 is a highly conserved protein that is involved in the regulation of a wide range of cellular processes. It is a potential drug target and may be a useful biomarker for the diagnosis and treatment of a variety of diseases.

Protein Name: AKT1 Substrate 1

Functions: Subunit of mTORC1, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. Inhibits RHEB-GTP-dependent mTORC1 activation. Substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. May also play a role in nerve growth factor-mediated neuroprotection

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