Summary: cytoplasm is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling. The AKT1 kinase domain has been crystallized with small-molecule ATP-competitive inhibitors (PDB 3CQU, 3CQW; 3CQW also contains Mn), confirming the kinase active site/ATP pocket.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: intracellular signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: negative regulation of apoptotic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: insulin receptor signaling pathway is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of blood vessel endothelial cell migration is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein kinase activity is directionally correct but less specific than AKT1's established kinase activity.

Reason: AKT1 is specifically a protein serine/threonine kinase; the broader kinase term should be replaced with the more precise GO term.

Proposed replacements: protein serine/threonine kinase activity

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: ATP binding is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling. The AKT1 kinase domain has been crystallized with small-molecule ATP-competitive inhibitors bound in the ATP pocket (PDB 3CQU, 3CQW; 3CQW also contains Mn), structurally confirming the nucleotide-binding site of the kinase domain.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: nucleus is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cytoplasm is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: mitochondrial intermembrane space is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: plasma membrane is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of cell migration is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: postsynapse is retained as a weak database-supported localization/context annotation, but it is not AKT1's core molecular function.

Reason: UniProt carries a postsynapse GO cross-reference for AKT1, but the central curatable function remains PI3K-regulated protein serine/threonine phosphorylation rather than a postsynaptic localization claim.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: identical protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: identical protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: identical protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: mitochondrion is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: spindle is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cytosol is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cell-cell junction is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: insulin receptor signaling pathway is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: response to heat is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: response to hormone is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of gene expression is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of gene expression is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: regulation of neuron projection development is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: kinase activity is directionally correct but less specific than AKT1's established kinase activity.

Reason: AKT1 is specifically a protein serine/threonine kinase; the broader kinase term should be replaced with the more precise GO term.

Proposed replacements: protein serine/threonine kinase activity

Summary: protein kinase binding is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: ciliary basal body is retained as a database-supported localization/context annotation, but it is not AKT1's core molecular function.

Reason: UniProt carries an HPA-supported ciliary basal body GO cross-reference for AKT1. This should be non-core because AKT1's principal function is PI3K-regulated protein serine/threonine kinase activity.

Summary: regulation of apoptotic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of apoptotic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: insulin-like growth factor receptor signaling pathway is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: behavioral response to pain is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cellular response to epidermal growth factor stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of release of cytochrome c from mitochondria is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: glutamatergic synapse is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: regulation of postsynapse organization is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: negative regulation of PERK-mediated unfolded protein response is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of TORC2 signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of protein localization to cell surface is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of intrinsic apoptotic signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of protein import into nucleus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: nucleoplasm is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cytokine-mediated signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: T cell costimulation is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cellular response to stress is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: regulation of mRNA stability is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: regulation of mRNA stability is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: negative regulation of Notch signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: nitric oxide metabolic process is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: vascular endothelial cell response to laminar fluid shear stress is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: regulation of signal transduction by p53 class mediator is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: regulation of signal transduction by p53 class mediator is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: regulation of type B pancreatic cell development is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: plasma membrane is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: insulin receptor signaling pathway is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: beta-arrestin-dependent dopamine receptor signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: complement receptor mediated signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine/tyrosine kinase activity is directionally correct but less specific than AKT1's established kinase activity.

Reason: AKT1 is specifically a protein serine/threonine kinase; the broader kinase term should be replaced with the more precise GO term.

Proposed replacements: protein serine/threonine kinase activity

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of anaphase-promoting complex-dependent catabolic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: epidermal growth factor receptor signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: kinase binding is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of cell migration is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of transcription by RNA polymerase II is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of G1/S transition of mitotic cell cycle is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: TORC2 complex binding is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of cGAS/STING signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of PERK-mediated unfolded protein response is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: osteoblast differentiation is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein-containing complex is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: mitochondrial intermembrane space is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cellular response to rapamycin is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of protein maturation is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of cell migration is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cytosol is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cytosol is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: negative regulation of cGAS/STING signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein kinase activity is directionally correct but less specific than AKT1's established kinase activity.

Reason: AKT1 is specifically a protein serine/threonine kinase; the broader kinase term should be replaced with the more precise GO term.

Proposed replacements: protein serine/threonine kinase activity

Summary: negative regulation of cilium assembly is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cellular response to epidermal growth factor stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of TORC1 signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cellular response to insulin stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of protein localization to lysosome is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of TORC1 signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: membrane is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: cellular response to insulin stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of TORC1 signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cellular response to insulin stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of TORC1 signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of TORC1 signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: AKT1 phosphorylation of Rac1 promotes FBXL19-mediated Rac1 ubiquitination and degradation, supporting this proteasomal catabolic context but not making proteasome regulation a core AKT1 function.

Reason: Keep as non-core because the evidence is substrate-specific regulation downstream of AKT1 kinase activity, not a general role as proteasome machinery.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: regulation of tRNA methylation is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cell cortex is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: negative regulation of long-chain fatty acid import across plasma membrane is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of glucose metabolic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase inhibitor activity is not a supported direct molecular activity for AKT1.

Reason: AKT1 acts as a protein serine/threonine kinase and signaling effector; this annotation reverses or overextends the direction of regulation.

Summary: protein serine/threonine kinase inhibitor activity is not a supported direct molecular activity for AKT1.

Reason: AKT1 acts as a protein serine/threonine kinase and signaling effector; this annotation reverses or overextends the direction of regulation.

Summary: negative regulation of fatty acid beta-oxidation is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cellular response to insulin stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of glycogen biosynthetic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of D-glucose import across plasma membrane is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cytoplasm is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of TORC1 signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of protein localization to endoplasmic reticulum is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: response to growth factor is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: potassium channel activator activity is supported as a direct but non-core AKT1 molecular activity involving TMEM175.

Reason: UniProt explicitly describes AKT1 as an activator of TMEM175 potassium channel activity in response to growth factors, independently of AKT1 kinase activity. This should be retained as a non-core molecular activity rather than removed.

Summary: sphingosine-1-phosphate receptor signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of endothelial cell migration is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: lamellipodium is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: fibroblast migration is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of lipid biosynthetic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: calmodulin binding is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cell migration involved in sprouting angiogenesis is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of gene expression is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: phosphatidylinositol 3-kinase/protein kinase B signal transduction is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: cellular response to oxidised low-density lipoprotein particle stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of leukocyte cell-cell adhesion is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: negative regulation of lymphocyte migration is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of gene expression is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: AKT1 can prevent CHIP-mediated tau ubiquitination and degradation, supporting a substrate-specific protein quality-control context but not a core AKT1 function.

Reason: Keep as non-core because the evidence concerns tau/CHIP regulation downstream of AKT1 signaling rather than a general ubiquitination or proteostasis role.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: excitatory postsynaptic potential is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein serine/threonine kinase activity is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein homodimerization activity is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: epidermal growth factor receptor signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein-containing complex is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: regulation of apoptotic process is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: PI3K-AKT-MTORC1 signaling can suppress autophagy in some contexts, but this paper emphasizes that detachment-induced macroautophagy is cell-context dependent.

Reason: Keep as non-core because macroautophagy regulation is a downstream pathway context of AKT1 signaling and not its direct molecular function.

Summary: TOR signaling is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: anoikis is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: interleukin-18-mediated signaling pathway is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: positive regulation of smooth muscle cell proliferation is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cytosol is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: positive regulation of protein localization to nucleus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: positive regulation of endodeoxyribonuclease activity is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: cellular response to nerve growth factor stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: peptidyl-threonine phosphorylation is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: vesicle is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein localization to mitochondrion is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: maintenance of protein location in mitochondrion is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: response to growth hormone is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: response to insulin-like growth factor stimulus is a supported pathway, substrate, interaction, localization, or phenotype context for AKT1 but not its core molecular function.

Reason: AKT1 has broad downstream effects; this annotation should be retained as context while the core function remains PI3K-regulated protein serine/threonine phosphorylation.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: protein binding is too generic or indirect for AKT1.

Reason: The annotation should not be treated as a core function when the supported molecular activity is phosphoinositide-regulated protein serine/threonine kinase activity.

Summary: cytoplasm is consistent with AKT1 as a phosphoinositide-regulated serine/threonine kinase in PI3K-AKT signaling.

Reason: Falcon research and UniProt support AKT1 activation downstream of PI3K and phosphorylation of serine/threonine substrates in growth, metabolic, survival, and mTOR-linked signaling.