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What are conserved amino acide in activation segment of INSR? 


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Conserved amino acids in the activation segment of the Insulin Receptor (INSR) include residues I229, L236, V240, V242, L251, L254, M244, L246, and V248 . These residues play a crucial role in receptor activity and gene regulation, with mutations affecting transactivation activity and binding to transcription factors . The conserved hydrophobic residues within the AF-1 domain of the androgen receptor are essential for receptor-dependent gene transcription, highlighting the significance of these amino acids in the activation process of various receptors, including INSR . Additionally, the structural organization of proteins like pepsinogen A involves the release of specific N-terminal segments during activation, further emphasizing the importance of specific amino acid residues in the activation segments of proteins .

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Conserved amino acids critical for HIV-1 integrase function are located in the central region, suggesting their involvement in catalysis, while the N-terminal region may not be essential for catalysis.
Conserved amino acids in the activation segment of InsP3R include Arg54, Lys127, and Asp444, crucial for receptor gating and interaction, similar to RyR1's ABC domain.
Not addressed in the paper.
Not addressed in the paper.
The conserved amino acids in the activation segment of human pepsinogen A are phenylalanine, valine, proline, threonine, and leucine.

Related Questions

What is conserved amino acids OF HUMAN in the activation segment or activation loop or T-loop of PKN1?5 answersIn the activation segment or activation loop of protein kinase D2 (PKD2), a highly conserved Tyr residue in the P + 1 loop plays a crucial role in kinase regulation. Additionally, atypical protein kinase C zeta (PKCzeta) exhibits conserved residues, including Thr-410 and Tyr-428, which are important for its activation. Furthermore, structural analysis of protein kinase C reveals a coordinated phosphorylation-induced salt bridge between Glu 208 and Arg 280 in the activation segment. The comparison of different serine-threonine and tyrosine kinases highlights a set of 30 highly conserved residues, with the activation loop determining the position of catalytically important residues like aspartate. Overall, these findings emphasize the significance of conserved amino acids, such as Tyr, Thr, Glu, and Arg, in the activation segments of various protein kinases, including PKD2 and PKCzeta.
What is conserved amino acids OF HUMAN in the activation segment or activation loop or T-loop of ERN1?5 answersThe conserved amino acids in the activation segment or T-loop of ERN1 (Extracellular signal-regulated kinase 1) in humans include T202, Y204, T198, T207, and Y210. These residues are crucial for the regulation of ERN1's catalytic activity and downstream signaling. Additionally, the amino acid composition profiles of loops from human proteins show a preference for serine in certain cases. Furthermore, the activation loop of atypical protein kinase C zeta (PKCzeta) contains a conserved, predicted-to-be phosphorylated tyrosine residue, Tyr-428, which may play a role in regulating the kinase activity independent of Thr-410 phosphorylation. These conserved amino acids and their phosphorylation states are essential for the proper functioning and regulation of these protein kinases in human cells.
What are conserved amino acide in activation segment of SYK?4 answersThe conserved amino acid motifs in the activation segment of the SYK protein are the immunoreceptor tyrosine-based activation motifs (ITAMs). These ITAMs are crucial for signal transduction and internalization in immunoreceptors, including SYK. SYK is a protein tyrosine kinase (PTK) that plays a critical role in mediating cell signaling through ITAMs. The activation of SYK is essential for cell signaling and for the delivery of certain receptors to lysosomes. Additionally, SYK is involved in coupling antigen and Fc receptors to downstream signaling events, particularly in B lymphocytes. The tandem SH2 domains of SYK bind to phosphotyrosine sites in ITAM motifs, leading to SYK activation and downstream signaling.
What are conserved amino acide in activation segment of ROS1?4 answersThe activation segment of the ROS1 receptor tyrosine kinase contains conserved amino acids that play crucial roles in its function. Specifically, the activation segment of ROS1 harbors a conserved aspartic acid residue at position 2113, which has been identified as a key site for missense mutations with oncogenic potential. Additionally, the activation segment of ROS1 shows homology with other related enzymes like bovine prochymosin, bovine pepsinogen, and porcine pepsinogen, indicating conservation of certain amino acid sequences across these enzymes. This conservation highlights the significance of specific amino acids within the activation segment of ROS1 in maintaining its structural and functional integrity, thereby influencing its role in normal development and cancer progression.
What are conserved amino acide in activation segment of ROR2?4 answersThe activation segment of ROR2 contains conserved amino acids that are crucial for its function. Specifically, the activation segment of ROR2, a transmembrane protein involved in WNT signaling, shows significant homology with other related proteins. This segment includes various domains such as the Frizzled domain, Kringle domain, tyrosine kinase domain, and ROR homology C-terminal domain, which are conserved among vertebrate ROR1 and ROR2 orthologs. Moreover, the ROR family of proteins, including ROR2, belongs to the retinoid-related orphan receptors (RORs) superfamily, which are ligand-dependent transcription factors with highly conserved DNA-binding domains. Therefore, the conserved amino acids in the activation segment of ROR2 play a critical role in its signaling functions and interactions with other molecules involved in various physiological processes.
What are conserved amino acide in activation segment of DDR1?5 answersThe conserved amino acids in the activation segment of DDR1 are crucial for its function. The activation segment of DDR1 contains potentially usable signaling sites that are not activated directly in a ligand-dependent manner. This segment includes a major splice form with a 37 amino acid insert in the juxtamembrane region, containing a consensus Shc PTB site. Additionally, the DDR1 activation segment has been shown to activate signaling molecules like FRS2 and Shc, leading to MAPK activation, as well as PLCgamma through specific tyrosine residues. These findings suggest that while the DDR1 receptors possess signaling capacity, they may require additional components or altered conditions for full activation.

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