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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry represents the N-terminal RA domain found in the PHLPP family proteins which are are serine/threonine phosphatases that play a crucial role in the regulation of cellular signalling pathways. They are involved in the dephosphorylation of the AGC kinase family members, including AKT1, AKT2, AKT3, PRKCA, and PRKCB, which are key regulators of cell survival, apoptosis, and proliferation [ , ]. These proteins act as tumour suppressors by triggering apoptosis through the dephosphorylation of specific serine residues on these kinases [, ]. They also regulate cap-dependent translation by dephosphorylating RPS6KB1 and control the activity of STK4 and RAF1 kinases, influencing apoptosis and kinase activity, respectively. Additionally, they have roles in long-term memory formation, circadian rhythm consolidation, and T-cell development and function. PHLPP2 contains a Ras-associating (RA) domain followed by a PH domain, leucine-rich repeats and protein phosphatase 2C (PP2C) domain. The presence of a PH domain is important for interaction with some of their substrates.This domain is also found in fungal adenylate cyclases (also known as ATP pyrophosphate-lyase), which regulate developmental processes such as hyphal growth, biofilm formation, and phenotypic switching. It plays an essential role in regulation of cellular metabolism by catalysing the synthesis of a second messenger, cAMP. Fungal adenylate cyclase has at least four domains, including an N-terminal adenylate cyclase G-alpha binding domain, a Ras-associating (RA) domain, a middle leucine-rich repeat region, and a catalytic domain. The RA domain of adenylate cyclase post-translationally modifies a small GTPase called Ras, which is involved in cellular signal transduction. The activity of adenylate cyclase is stimulated directly by regulatory proteins (Ras1 and Gpa2), peptidoglycan fragments and carbon dioxide [ ]. | Name | PHLPP-like, RA domain |
| Short Name | RA_PHLPP-like | Type | Domain |
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