Existing Annotations Review

Core Functions

Akt1 is a protein kinase B that transduces PI3K signals to control growth, metabolism, and survival programs.

Molecular Function:

protein serine/threonine kinase activity

Directly Involved In:

insulin receptor signaling pathway

Supporting Evidence:

file:genes/DROME/Akt1/Akt1-uniprot.txt
RecName: Full=RAC serine/threonine-protein kinase
PMID:10962553
The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila.

References

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000043

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000116

Automatic Gene Ontology annotation based on Rhea mapping

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:10587646

Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB.

PMID:10962553

The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila.

PMID:11740943

Regulation of Drosophila tracheal system development by protein kinase B.

PMID:11862217

dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires dPDK1.

PMID:12172554

Akt regulates growth by directly phosphorylating Tsc2.

PMID:12893776

Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathway.

PMID:14525946

Coordinated functions of Akt/PKB and ETS1 in tubule formation.

PMID:14645523

Signaling from Akt to FRAP/TOR targets both 4E-BP and S6K in Drosophila melanogaster.

PMID:15337530

Drosophila PI3 kinase and Akt involved in insulin-stimulated proliferation and ERK pathway activation in Schneider cells.

PMID:15712201

dAkt kinase controls follicle cell size during Drosophila oogenesis.

PMID:15808505

PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth.

PMID:16611817

Requirement of Akt to mediate long-term synaptic depression in Drosophila.

PMID:17079271

Cytoplasmic activated protein kinase Akt regulates lipid-droplet accumulation in Drosophila nurse cells.

PMID:17183368

Insulin delays the progression of Drosophila cells through G2/M by activating the dTOR/dRaptor complex.

PMID:17369395

Re-evaluating AKT regulation: role of TOR complex 2 in tissue growth.

PMID:17462592

Discrete functions of rictor and raptor in cell growth regulation in Drosophila.

PMID:17895391

FOXO and insulin signaling regulate sensitivity of the circadian clock to oxidative stress.

PMID:18000865

Gliatrophic and gliatropic roles of PVF/PVR signaling during axon guidance.

PMID:18827008

The protein phosphatase PP2A-B' subunit Widerborst is a negative regulator of cytoplasmic activated Akt and lipid metabolism in Drosophila.

PMID:19216764

PDGF/VEGF signaling controls cell size in Drosophila.

PMID:19778508

The microRNA bantam functions in epithelial cells to regulate scaling growth of dendrite arbors in drosophila sensory neurons.

PMID:20585550

Dynamic switch of negative feedback regulation in Drosophila Akt-TOR signaling.

PMID:20688956

Genetic manipulation of AML1-ETO-induced expansion of hematopoietic precursors in a Drosophila model.

PMID:21464442

Drosophila insulin pathway mutants affect visual physiology and brain function besides growth, lipid, and carbohydrate metabolism.

PMID:21565616

A hormone-dependent module regulating energy balance.

PMID:22242005

MAPK/ERK signaling regulates insulin sensitivity to control glucose metabolism in Drosophila.

PMID:22759636

Regeneration of Drosophila sensory neuron axons and dendrites is regulated by the Akt pathway involving Pten and microRNA bantam.

PMID:23393158

Tuberous sclerosis complex regulates Drosophila neuromuscular junction growth via the TORC2/Akt pathway.

PMID:24068890

A Cullin1-based SCF E3 ubiquitin ligase targets the InR/PI3K/TOR pathway to regulate neuronal pruning.

PMID:24413555

The SCFSlimb E3 ligase complex regulates asymmetric division to inhibit neuroblast overgrowth.

PMID:24786828

The TORC1 inhibitors Nprl2 and Nprl3 mediate an adaptive response to amino-acid starvation in Drosophila.

PMID:24916379

Genetic dissection reveals that Akt is the critical kinase downstream of LRRK2 to phosphorylate and inhibit FOXO1, and promotes neuron survival.

PMID:25101872

A genetic strategy to measure circulating Drosophila insulin reveals genes regulating insulin production and secretion.

PMID:25749252

A systems-level interrogation identifies regulators of Drosophila blood cell number and survival.

PMID:27326933

A Drosophila Genome-Wide Screen Identifies Regulators of Steroid Hormone Production and Developmental Timing.

PMID:28829944

Spatial Activation of TORC1 Is Regulated by Hedgehog and E2F1 Signaling in the Drosophila Eye.

PMID:29045833

Intestinal Fork Head Regulates Nutrient Absorption and Promotes Longevity.

PMID:29514084

Innate Immune Signaling in Drosophila Blocks Insulin Signaling by Uncoupling PI(3,4,5)P(3) Production and Akt Activation.

PMID:29950391

Insulin signaling modulates border cell movement in Drosophila oogenesis.

PMID:31613895

The Hippo pathway integrates PI3K-Akt signals with mechanical and polarity cues to control tissue growth.

PMID:32998936

Meep, a Novel Regulator of Insulin Signaling, Supports Development and Insulin Sensitivity via Maintenance of Protein Homeostasis in Drosophila melanogaster.

PMID:34751396

Pvr and distinct downstream signaling factors are required for hemocyte spreading and epidermal wound closure at Drosophila larval wound sites.

PMID:36730473

A genetic strategy to measure insulin signaling regulation and physiology in Drosophila.

PMID:7876156

Developmental regulation of expression and activity of multiple forms of the Drosophila RAC protein kinase.

PMID:9601646

Genetic analysis of protein kinase B (AKT) in Drosophila.

Reactome:R-DME-110463

Increased PIP3 levels recruit DAkt1 to the membrane

Reactome:R-DME-110468

Activation of DAkt1 by DPDK1

Reactome:R-DME-110475

DAkt1-mediated phosphorylation inactivates DFOXO

Reactome:R-DME-169828

Activated DAkt1 phosphorylates TSC2 which inhibits the TSC1/2 complex

Deep Research

Falcon

(Akt1-deep-research-falcon.md)

this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 16 citations 2026-02-01T16:13:22.248617

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan status: We verified the Drosophila Akt identity, gathered core mechanistic evidence (domain architecture, activation sites, pathway placement), extracted quantitative data (e.g., TORC2 dependence of Ser505 phosphorylation and effects on FOXO), and synthesized these into a compact artifact for reference. Despite targeted searches, recent 2023–2024 Drosophila-specific primary studies directly on Akt (CG4006) were limited in the accessible evidence set; therefore, the report emphasizes foundational Drosophila papers with clear mechanistic data and indicates where recency is lacking.

Comprehensive research report: Drosophila melanogaster Akt (dAkt/PKB; CG4006; UniProt Q8INB9)

1) Key concepts and definitions with current understanding
- Identity and domains: Drosophila Akt (also dAkt/PKB; gene CG4006, synonyms Akt/Akt1) is an AGC-family serine/threonine kinase composed of an N‑terminal pleckstrin homology (PH) domain that binds phosphatidylinositol (3,4,5)-trisphosphate (PIP3), a central kinase domain, and a C‑terminal AGC regulatory tail that contains a hydrophobic motif (HM). These features and placement in the insulin/PI3K pathway are established in Drosophila and conserved with mammals (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3). Mammalian overviews further support the conserved PH→PIP3 recruitment, dual-site phosphorylation requirement, and AGC family architecture (publication: Jul 2009; URL: https://doi.org/10.1016/j.tem.2009.03.002) (elghazi2009aktandpten pages 11-15).
- Catalytic activity: Akt is a protein-serine/threonine kinase (EC 2.7.11.1) that phosphorylates downstream substrates to control growth, metabolism, and survival. In Drosophila, Akt lies downstream of insulin receptor and PI3K, and upstream of TSC/TOR, S6K, and 4E‑BP (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003) (miron2003signalingfromakt pages 9-10, miron2003signalingfromakt pages 11-11, miron2003signalingfromakt pages 8-9).

2) Activation mechanism and localization
- Membrane recruitment: Insulin/PI3K elevates PIP3 at the plasma membrane. The dAkt PH domain binds PIP3, recruiting dAkt to the membrane where activating kinases access it (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003) (miron2003signalingfromakt pages 9-10, miron2003signalingfromakt pages 11-11).
- Phosphorylation sites and kinases: Full activation requires phosphorylation at two conserved regulatory sites: the activation-loop threonine by PDK1 (Thr342 in Drosophila) and the C‑terminal hydrophobic-motif serine by TOR complex 2 (Ser505 in Drosophila). TORC2 (rictor/Sin1) is required for S505 HM phosphorylation and for maximal Akt activity in response to strong insulin signals (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3, hietakangas2007reevaluatingaktregulation pages 5-6).
- Subcellular localization dynamics: dAkt is predominantly cytosolic in basal conditions and translocates to the plasma membrane upon PI3K-produced PIP3 accumulation, a prerequisite step for PDK1 and TORC2 phosphorylation and activation (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003) (miron2003signalingfromakt pages 9-10).

3) Pathways, substrates, and precise roles
- Insulin/PI3K/Akt/TOR axis: Genetic and biochemical analyses in Drosophila place dAkt as the key effector linking PI3K/PTEN-regulated PIP3 signals to TSC/Rheb/TORC1. Akt phosphorylation of Tsc2 stimulates TORC1, leading to phosphorylation of S6K and 4E‑BP, which increases protein synthesis and growth (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003) (miron2003signalingfromakt pages 9-10, miron2003signalingfromakt pages 8-9).
- FOXO regulation: Akt phosphorylates FOXO, reducing its activity and nuclear localization. TORC2 loss (rictor mutants) reduces Akt S505 phosphorylation and decreases FOXO phosphorylation, increasing FOXO activity; epistasis shows TORC2 limits growth primarily when signaling is activated at or above Akt (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 4-5, hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3).
- Direct outputs to translation: Insulin-induced phosphorylation of d4E‑BP and dS6K depends on the Akt–TSC–TOR pathway. dPDK1 depletion abolishes dS6K Thr398 phosphorylation, while dAkt knockdown reduces insulin-stimulated phosphorylation of both d4E‑BP and dS6K, underscoring Akt’s upstream role (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003) (miron2003signalingfromakt pages 8-9, miron2003signalingfromakt pages 9-10).

4) Recent developments (2023–2024) and real-world implementations
- Within the accessible evidence, directly Akt-focused Drosophila primary papers from 2023–2024 were not retrieved. However, the conserved placement of Akt in insulin signaling and TOR regulation remains the conceptual framework used across recent immunometabolic and aging literature; the Drosophila pathway logic summarized above continues to be cited as canonical (e.g., recent immuno-metabolic reviews referencing Drosophila and conserved Akt/FOXO axes; publication: Mar 2023; URL: https://doi.org/10.3389/fendo.2023.1128622) — note: while located during search, this specific item was not available in the sanctioned evidence set for formal citation. Consequently, our report emphasizes rigorously established Drosophila mechanistic studies with explicit residue-level and genetic data (hietakangas2007reevaluatingaktregulation pages 4-5, hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3, miron2003signalingfromakt pages 9-10, miron2003signalingfromakt pages 11-11, miron2003signalingfromakt pages 8-9). Where needed, conserved mammalian reviews are used to support general Akt biochemistry (elghazi2009aktandpten pages 11-15).

5) Expert opinions and analysis from authoritative sources
- TORC2’s role in Akt regulation and tissue growth: Hietakangas & Cohen (Genes & Development, 2007) re-evaluated Akt regulation and concluded that HM phosphorylation by TORC2 (S505) is dispensable for viability but required for maximal Akt activation and for repressing FOXO under strong insulin inputs; they propose that targeting TORC2 can modulate Akt hyperactivation phenotypes (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 5-6, hietakangas2007reevaluatingaktregulation pages 4-5).
- Insulin→Akt→TOR growth control: Miron, Lasko & Sonenberg (Molecular and Cellular Biology, 2003) provide experimental RNAi evidence for the pathway from PI3K/PTEN/Akt to TSC/TOR and to 4E‑BP/S6K in Drosophila, defining Akt as a central growth-control node (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003) (miron2003signalingfromakt pages 9-10, miron2003signalingfromakt pages 8-9, miron2003signalingfromakt pages 11-11).
- Conserved activation logic: Elghazi & Bernal‑Mizrachi (Trends in Endocrinology & Metabolism, 2009) provide a mechanistic overview of Akt activation steps, PH‑domain PIP3 binding, and dual‑site phosphorylation as a general AGC‑kinase principle, aligning with Drosophila dAkt biochemistry (publication: Jul 2009; URL: https://doi.org/10.1016/j.tem.2009.03.002) (elghazi2009aktandpten pages 11-15).

6) Relevant statistics and quantitative data from Drosophila studies
- TORC2 dependence of Akt HM phosphorylation: In rictor mutants, Ser505 phosphorylation of dAkt is nearly abolished (>95% reduction), demonstrating TORC2’s essential role for this site in vivo (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 2-3).
- FOXO phosphorylation and HM site: Under rescue conditions, wild-type Akt yields ~33% FOXO in a phosphorylated (slower-migrating) form versus ~19% with Akt S505A, indicating diminished FOXO repression when the HM site is not phosphorylated (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 4-5).
- Phenotypic scope of TORC2 loss: rictor/sin1 mutants (loss of TORC2) are homozygous viable with modest growth delay; HM phosphorylation is necessary for maximal Akt activity in strong insulin signaling, but Akt retains sufficient activity for development without HM phosphorylation (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 5-6).
- Pathway epistasis: Removing rictor suppresses PI3K-hyperactivation overgrowth (e.g., PTEN loss) but not TORC1-driven overgrowth (e.g., TSC1 loss), mapping TORC2’s function to the level of Akt and above (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 4-5, hietakangas2007reevaluatingaktregulation pages 1-2).
- Translational outputs: Insulin-induced phosphorylation of d4E‑BP and dS6K requires the Akt→TSC→TOR pathway; PDK1 knockdown abolishes dS6K Thr398 phosphorylation, while Akt RNAi reduces both d4E‑BP and dS6K phosphorylation, quantitatively linking Akt to growth control via TOR substrates (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003) (miron2003signalingfromakt pages 8-9, miron2003signalingfromakt pages 9-10).

Primary function and pathway role summary (concise)
- Biochemical function: dAkt is a serine/threonine protein kinase (EC 2.7.11.1) that is activated by PIP3-dependent membrane recruitment and dual phosphorylation (activation loop Thr342 by PDK1; hydrophobic motif Ser505 by TORC2). Activated dAkt phosphorylates substrates including FOXO (inhibiting its transcriptional activity) and promotes TORC1 signaling via TSC2, leading to phosphorylation of S6K and 4E‑BP and increased translation and growth (publication URLs and dates: Dec 2003, https://doi.org/10.1128/mcb.23.24.9117-9126.2003; Mar 2007, https://doi.org/10.1101/gad.416307) (miron2003signalingfromakt pages 9-10, miron2003signalingfromakt pages 8-9, hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3).
- Cellular localization of function: Cytosolic-to-plasma membrane translocation via the PH domain upon PIP3 generation is essential for activation; downstream actions occur in the cytosol and nucleus (via FOXO regulation) and via cytosolic signaling to TORC1 at lysosomal/mTOR compartments to control translation (publication: Dec 2003; URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003; Mar 2007; URL: https://doi.org/10.1101/gad.416307) (miron2003signalingfromakt pages 9-10, hietakangas2007reevaluatingaktregulation pages 1-2).

Key facts at a glance
| Feature | Summary | Key evidence (short + DOI) |
|---|---|---|
| Domain architecture | N-terminal PH domain; central Ser/Thr kinase (AGC family); C-terminal AGC hydrophobic-motif C-tail | Hietakangas & Cohen 2007 — https://doi.org/10.1101/gad.416307 (hietakangas2007reevaluatingaktregulation pages 2-3, hietakangas2007reevaluatingaktregulation pages 1-2); Elghazi & Bernal-Mizrachi 2009 — https://doi.org/10.1016/j.tem.2009.03.002 (elghazi2009aktandpten pages 11-15) |
| Catalytic activity | Ser/Thr protein kinase (EC 2.7.11.1); phosphorylates protein Ser/Thr residues on downstream effectors | Miron et al. 2003 — https://doi.org/10.1128/mcb.23.24.9117-9126.2003 (miron2003signalingfromakt pages 9-10, miron2003signalingfromakt pages 11-11) |
| Activation mechanism | PIP3-dependent membrane recruitment via PH domain; activation-loop phosphorylation by PDK1 (T342); TORC2-mediated hydrophobic-motif phosphorylation (S505) for maximal activity | Hietakangas & Cohen 2007 — https://doi.org/10.1101/gad.416307 (hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3); Miron et al. 2003 (miron2003signalingfromakt pages 9-10) |
| Subcellular localization dynamics | Basal: cytosolic; upon insulin/PI3K → PIP3: translocates to plasma membrane via PH domain, enabling PDK1/TORC2 access and activation | Miron et al. 2003 — https://doi.org/10.1128/mcb.23.24.9117-9126.2003 (miron2003signalingfromakt pages 9-10); Hietakangas & Cohen 2007 (hietakangas2007reevaluatingaktregulation pages 4-5) |
| Pathway roles & major substrates/effects | Central effector of Insulin/PI3K → phosphorylates FOXO (inhibition/nuclear export), phosphorylates TSC2 → activates TORC1 leading to S6K and 4E-BP phosphorylation; controls cell/tissue growth and metabolism | Miron et al. 2003 — https://doi.org/10.1128/mcb.23.24.9117-9126.2003 (miron2003signalingfromakt pages 9-10); Hietakangas & Cohen 2007 (hietakangas2007reevaluatingaktregulation pages 4-5) |
| Quantitative / statistical notes | TORC2 (rictor) mutants: S505 phosphorylation reduced ≈>95%; AKT S505A shows reduced FOXO phosphorylation (WT rescue: ~33% FOXO phosphorylated vs S505A: ~19% in cited assay); HM phosphorylation required for maximal activation under strong stimulation but S505A retains partial in vivo activity | Hietakangas & Cohen 2007 — https://doi.org/10.1101/gad.416307 (hietakangas2007reevaluatingaktregulation pages 2-3, hietakangas2007reevaluatingaktregulation pages 4-5) |

Table: Compact summary of Drosophila Akt (dAkt/PKB; CG4006; UniProt Q8INB9) covering domains, catalytic activity, activation steps, localization, pathway roles, and quantitative evidence from key references (context citations provided).

Verification and symbol ambiguity
- The gene symbol “Akt” is used for Drosophila Akt/PKB encoded by CG4006 and matches UniProt Q8INB9. The organism is Drosophila melanogaster. Domain composition (PH domain, kinase domain, AGC tail) aligns with literature-corroborated features of dAkt/PKB in Drosophila (publication: Mar 2007; URL: https://doi.org/10.1101/gad.416307) (hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3). No conflicting gene symbol usage was encountered in the cited Drosophila literature.

Limitations and open needs
- While we prioritized 2023–2024 literature in searches, the accessible evidence set returned foundational Drosophila primary studies (2003–2007) and conserved mammalian analysis (2009). Recent Drosophila Akt-specific primary updates (2023–2024) were not retrievable in the sanctioned dataset; thus, claims herein are grounded in classical, high-quality Drosophila experiments and conserved mechanistic logic. Future updates should integrate newly published Drosophila Akt studies (e.g., system-specific roles in immunity or organ physiology) as they become available in accessible repositories (hietakangas2007reevaluatingaktregulation pages 1-2, hietakangas2007reevaluatingaktregulation pages 2-3, miron2003signalingfromakt pages 9-10).

References

(hietakangas2007reevaluatingaktregulation pages 1-2): Ville Hietakangas and Stephen M. Cohen. Re-evaluating akt regulation: role of tor complex 2 in tissue growth. Genes & development, 21 6:632-7, Mar 2007. URL: https://doi.org/10.1101/gad.416307, doi:10.1101/gad.416307. This article has 173 citations and is from a highest quality peer-reviewed journal.
(hietakangas2007reevaluatingaktregulation pages 2-3): Ville Hietakangas and Stephen M. Cohen. Re-evaluating akt regulation: role of tor complex 2 in tissue growth. Genes & development, 21 6:632-7, Mar 2007. URL: https://doi.org/10.1101/gad.416307, doi:10.1101/gad.416307. This article has 173 citations and is from a highest quality peer-reviewed journal.
(elghazi2009aktandpten pages 11-15): Lynda Elghazi and Ernesto Bernal-Mizrachi. Akt and pten: β-cell mass and pancreas plasticity. Trends in Endocrinology & Metabolism, 20:243-251, Jul 2009. URL: https://doi.org/10.1016/j.tem.2009.03.002, doi:10.1016/j.tem.2009.03.002. This article has 120 citations and is from a domain leading peer-reviewed journal.
(miron2003signalingfromakt pages 9-10): Mathieu Miron, Paul Lasko, and Nahum Sonenberg. Signaling from akt to frap/tor targets both 4e-bp ands6k in drosophilamelanogaster. Molecular and Cellular Biology, 23:9117-9126, Dec 2003. URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003, doi:10.1128/mcb.23.24.9117-9126.2003. This article has 170 citations and is from a domain leading peer-reviewed journal.
(miron2003signalingfromakt pages 11-11): Mathieu Miron, Paul Lasko, and Nahum Sonenberg. Signaling from akt to frap/tor targets both 4e-bp ands6k in drosophilamelanogaster. Molecular and Cellular Biology, 23:9117-9126, Dec 2003. URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003, doi:10.1128/mcb.23.24.9117-9126.2003. This article has 170 citations and is from a domain leading peer-reviewed journal.
(miron2003signalingfromakt pages 8-9): Mathieu Miron, Paul Lasko, and Nahum Sonenberg. Signaling from akt to frap/tor targets both 4e-bp ands6k in drosophilamelanogaster. Molecular and Cellular Biology, 23:9117-9126, Dec 2003. URL: https://doi.org/10.1128/mcb.23.24.9117-9126.2003, doi:10.1128/mcb.23.24.9117-9126.2003. This article has 170 citations and is from a domain leading peer-reviewed journal.
(hietakangas2007reevaluatingaktregulation pages 5-6): Ville Hietakangas and Stephen M. Cohen. Re-evaluating akt regulation: role of tor complex 2 in tissue growth. Genes & development, 21 6:632-7, Mar 2007. URL: https://doi.org/10.1101/gad.416307, doi:10.1101/gad.416307. This article has 173 citations and is from a highest quality peer-reviewed journal.
(hietakangas2007reevaluatingaktregulation pages 4-5): Ville Hietakangas and Stephen M. Cohen. Re-evaluating akt regulation: role of tor complex 2 in tissue growth. Genes & development, 21 6:632-7, Mar 2007. URL: https://doi.org/10.1101/gad.416307, doi:10.1101/gad.416307. This article has 173 citations and is from a highest quality peer-reviewed journal.

Citations

elghazi2009aktandpten pages 11-15
miron2003signalingfromakt pages 9-10
hietakangas2007reevaluatingaktregulation pages 2-3
hietakangas2007reevaluatingaktregulation pages 4-5
hietakangas2007reevaluatingaktregulation pages 1-2
miron2003signalingfromakt pages 11-11
miron2003signalingfromakt pages 8-9
hietakangas2007reevaluatingaktregulation pages 5-6
https://doi.org/10.1101/gad.416307
https://doi.org/10.1016/j.tem.2009.03.002
https://doi.org/10.1128/mcb.23.24.9117-9126.2003
https://doi.org/10.3389/fendo.2023.1128622
https://doi.org/10.1128/mcb.23.24.9117-9126.2003;
https://doi.org/10.1101/gad.416307,
https://doi.org/10.1016/j.tem.2009.03.002,
https://doi.org/10.1128/mcb.23.24.9117-9126.2003,

📚 Additional Documentation

Bioreason Rl Predictions

(Akt1-bioreason-rl-predictions.md)

BioReason Chat Export

Exported on March 22, 2026 at 02:46 AM

Organism: Drosophila melanogaster

Sequence:

MNYLPFVLQRRSTVVASAPAPGSASRIPESPTTTGSNIINIIYSQSTHPNSSPTSGSAEKFSWQQSWPSRTSAAPTHDSGTMSINTTFDLSSPSVTSGHALTEQTQVVKEGWLMKRGEHIKNWRQRYFVLHSDGRLMGYRSKPADSASTPSDFLLNNFTVRGCQIMTVDRPKPFTFIIRGLQWTTVIERTFAVESELERQQWTEAIRNVSSRLIDVGEVAMTPSEQTDMTDVDMATIAEDELSEQFSVQGTTCNSSGVKKVTLENFEFLKVLGKGTFGKVILCREKATAKLYAIKILKKEVIIQKDEVAHTLTESRVLKSTNHPFLISLKYSFQTNDRLCFVMQYVNGGELFWHLSHERIFTEDRTRFYGAEIISALGYLHSQGIIYRDLKLENLLLDKDGHIKVADFGLCKEDITYGRTTKTFCGTPEYLAPEVLDDNDYGQAVDWWGTGVVMYEMICGRLPFYNRDHDVLFTLILVEEVKFPRNITDEAKNLLAGLLAKDPKKRLGGGKDDVKEIQAHPFFASINWTDLVLKKIPPPFKPQVTSDTDTRYFDKEFTGESVELTPPDPTGPLGSIAEEPLFPQFSYQGDMASTLGTSSHISTSTSLASMQ

Thinking Trace

I begin with the domain architecture. The N-terminal half contains a clustered PH-module core: IPR011993 (PH-like domain superfamily, residues 101–218) encompasses IPR039026 (Protein Kinase B, pleckstrin homology domain, residues 105–214) and IPR001849 (Pleckstrin homology domain, residues 106–213). This tightly overlapping trio defines a canonical PH fold specialized for binding phosphoinositide headgroups and soluble polyanions. Such PH modules target AGC-kinase pathways to membrane-associated lipid signals and can also mediate nucleic acid or protein docking; in this context, the PH architecture causally supports high-affinity interactions with acidic ligands and scaffolds that tune kinase activation.

The catalytic core is specified by IPR011009 (Protein kinase-like domain superfamily, residues 261–578), which houses IPR000719 (Protein kinase domain, residues 266–523). Within this fold, IPR017441 (Protein kinase, ATP binding site, residues 272–295) defines the P-loop and adenine pocket that coordinate ATP, while IPR008271 (Serine/threonine-protein kinase, active site, residues 385–397) marks the catalytic loop and activation segment that confer phosphotransfer to serine/threonine residues. This arrangement establishes an ATP-dependent protein kinase chemistry. C-terminal AGC-tail features—IPR000961 (AGC-kinase, C-terminal, residues 524–597) and IPR017892 (Protein kinase, C-terminal, residues 544–587)—encode the hydrophobic motif and turn motif that dock upstream activators and stabilize the active conformation. Together, the PH module plus AGC-tail create a lipid-gated serine/threonine kinase whose activity is tuned by membrane-associated cues.

From this architecture, the molecular functions resolve as follows. The conserved kinase core and ATP pocket require GO:0005524 ATP binding and drive GO:0004674 protein serine/threonine kinase activity. The PH domain’s affinity for polyanionic ligands and nucleic acids rationalizes broad binding behavior; in particular, the PH module’s electropositive surface and the AGC-tail’s regulatory role explain high-avidity interactions consistent with GO:0003674 molecular function as a kinase scaffold while executing phosphorylation.

These molecular activities feed directly into biological processes. A PH-gated AGC kinase typically transduces phosphoinositide cues to phosphorylation cascades that control metabolism, survival, and cytoskeletal dynamics. This causal chain places the protein squarely in GO:0006468 protein phosphorylation and positions it within signaling axes that regulate growth and stress responses. The PH-driven membrane targeting and AGC-tail activation situate the kinase as a signal-integrating hub that modulates downstream pathways.

Cellular location follows from the same logic. The PH module recruits the enzyme to membrane-proximal signaling zones, yet the absence of transmembrane segments and the soluble kinase fold support a cytosolic pool. This yields a dual residence: GO:0005737 cytoplasm for the soluble enzyme and GO:0005634 nucleus for a shuttling fraction that phosphorylates nuclear targets and interfaces with transcriptional control.

Mechanistically, the PH domain binds phosphoinositide-enriched membranes and soluble polyanions, positioning the kinase for activation via its AGC-tail. The ATP-binding and catalytic motifs enable phosphate transfer to serine/threonine residues on substrates that regulate metabolism and cytoskeleton. I hypothesize that upstream activators (such as 3-phosphoinositide-dependent kinases and hydrophobic-motif phosphatases/adaptors) dock on the AGC C-terminus to prime activity. Likely partners include lipid-metabolic adaptors and scaffolds that present substrates near membranes and in the nucleus. In Drosophila, this suggests transient assemblies with phosphoinositide-producing enzymes and AGC-pathway regulators to coordinate cytoplasmic and nuclear phosphorylation programs.

Functional Summary

A soluble AGC-class serine/threonine kinase in fruit fly that uses an N-terminal pleckstrin homology module to dock onto acidic lipid and polyanion-rich environments, where it becomes activated through its C-terminal regulatory tail. Once engaged, the kinase transfers phosphate from ATP to serine/threonine residues on target proteins, integrating phosphoinositide signals to control phosphorylation cascades that govern metabolism, survival, and cytoskeletal organization. It operates predominantly in the cytoplasm with a shuttling nuclear pool that likely tunes transcriptional and chromatin-associated pathways.

UniProt Summary

May bind DNA or polyanionic ligands.

InterPro Domains

PH-like domain superfamily (IPR011993, homologous_superfamily) — residues 101-218
Protein Kinase B, pleckstrin homology domain (IPR039026, domain) — residues 105-214
Pleckstrin homology domain (IPR001849, domain) — residues 106-213
Protein kinase-like domain superfamily (IPR011009, homologous_superfamily) — residues 261-578
Protein kinase domain (IPR000719, domain) — residues 266-523
Protein kinase, ATP binding site (IPR017441, binding_site) — residues 272-295
Serine/threonine-protein kinase, active site (IPR008271, active_site) — residues 385-397
AGC-kinase, C-terminal (IPR000961, domain) — residues 524-597
Protein kinase, C-terminal (IPR017892, domain) — residues 544-587

GO Terms

Molecular Function: molecular_function (GO:0003674), binding (GO:0005488), catalytic activity (GO:0003824), transferase activity (GO:0016740), catalytic activity, acting on a protein (GO:0140096), protein binding (GO:0005515), protein kinase activity (GO:0004672), transferase activity, transferring phosphorus-containing groups (GO:0016772), phosphotransferase activity, alcohol group as acceptor (GO:0016773), protein serine/threonine kinase activity (GO:0004674), kinase activity (GO:0016301)

Biological Process: biological_process (GO:0008150), positive regulation of biological process (GO:0048518), regulation of biological process (GO:0050789), signaling (GO:0023052), reproduction (GO:0000003), multicellular organismal process (GO:0032501), biological regulation (GO:0065007), rhythmic process (GO:0048511), response to stimulus (GO:0050896), developmental process (GO:0032502), cellular process (GO:0009987), metabolic process (GO:0008152), homeostatic process (GO:0042592), reproductive process (GO:0022414), growth (GO:0040007), negative regulation of biological process (GO:0048519), sexual reproduction (GO:0019953), developmental growth (GO:0048589), anatomical structure development (GO:0048856), positive regulation of lipid localization (GO:1905954), negative regulation of signaling (GO:0023057), cell motility (GO:0048870), response to chemical (GO:0042221), tissue migration (GO:0090130), regulation of reproductive process (GO:2000241), positive regulation of multicellular organismal process (GO:0051240), nitrogen compound metabolic process (GO:0006807), cellular component organization or biogenesis (GO:0071840), negative regulation of multicellular organismal process (GO:0051241), regulation of multicellular organismal process (GO:0051239), multicellular organism reproduction (GO:0032504), positive regulation of growth (GO:0045927), developmental process involved in reproduction (GO:0003006), negative regulation of metabolic process (GO:0009892), regulation of developmental process (GO:0050793), regulation of biological quality (GO:0065008), positive regulation of reproductive process (GO:2000243), cellular process involved in reproduction in multicellular organism (GO:0022412), positive regulation of cellular process (GO:0048522), response to endogenous stimulus (GO:0009719), positive regulation of locomotion (GO:0040017), regulation of cellular process (GO:0050794), regulation of response to stimulus (GO:0048583), cellular response to stimulus (GO:0051716), multicellular organism growth (GO:0035264), regulation of signaling (GO:0023051), negative regulation of developmental process (GO:0051093), negative regulation of cellular process (GO:0048523), signal transduction (GO:0007165), regulation of locomotion (GO:0040012), cellular developmental process (GO:0048869), positive regulation of signaling (GO:0023056), multicellular organism development (GO:0007275), negative regulation of transport (GO:0051051), regulation of metabolic process (GO:0019222), positive regulation of response to stimulus (GO:0048584), regulation of localization (GO:0032879), circadian rhythm (GO:0007623), regulation of immune system process (GO:0002682), organic substance metabolic process (GO:0071704), chemical homeostasis (GO:0048878), cellular metabolic process (GO:0044237), anatomical structure morphogenesis (GO:0009653), response to stress (GO:0006950), negative regulation of growth (GO:0045926), positive regulation of developmental process (GO:0051094), multicellular organismal reproductive process (GO:0048609), negative regulation of response to stimulus (GO:0048585), cell communication (GO:0007154), regulation of growth (GO:0040008), primary metabolic process (GO:0044238), regulation of border follicle cell migration (GO:1903684), negative regulation of signal transduction (GO:0009968), positive regulation of response to external stimulus (GO:0032103), regulation of neuron projection regeneration (GO:0070570), lipid homeostasis (GO:0055088), negative regulation of cellular component organization (GO:0051129), tissue morphogenesis (GO:0048729), regulation of cell motility (GO:2000145), negative regulation of cell death (GO:0060548), cell development (GO:0048468), cell differentiation (GO:0030154), negative regulation of nervous system development (GO:0051961), regulation of response to stress (GO:0080134), negative regulation of synaptic transmission (GO:0050805), system development (GO:0048731), positive regulation of neuron projection regeneration (GO:0070572), positive regulation of border follicle cell migration (GO:1903688), regulation of signal transduction (GO:0009966), cellular response to endogenous stimulus (GO:0071495), regulation of response to external stimulus (GO:0032101), regulation of organ growth (GO:0046620), regulation of synapse structure or activity (GO:0050803), regulation of lipid storage (GO:0010883), response to hormone (GO:0009725), negative regulation of secretion (GO:0051048), regulation of cellular component biogenesis (GO:0044087), phosphorus metabolic process (GO:0006793), regulation of catabolic process (GO:0009894), regulation of epithelial cell migration (GO:0010632), regulation of hemocyte proliferation (GO:0035206), cell surface receptor signaling pathway (GO:0007166), cellular component organization (GO:0016043), regulation of cellular component organization (GO:0051128), regulation of anatomical structure size (GO:0090066), negative regulation of secretion by cell (GO:1903531), regulation of developmental growth (GO:0048638), positive regulation of cell population proliferation (GO:0008284), cell migration (GO:0016477), positive regulation of developmental growth (GO:0048639), negative regulation of hormone secretion (GO:0046888), positive regulation of signal transduction (GO:0009967), regulation of dendrite development (GO:0050773), gamete generation (GO:0007276), germ cell development (GO:0007281), regulation of synaptic plasticity (GO:0048167), negative regulation of cell communication (GO:0010648), regulation of secretion by cell (GO:1903530), regulation of transport (GO:0051049), organonitrogen compound metabolic process (GO:1901564), negative regulation of lipid metabolic process (GO:0045833), intracellular signal transduction (GO:0035556), response to wounding (GO:0009611), response to oxidative stress (GO:0006979), regulation of lipid localization (GO:1905952), protein metabolic process (GO:0019538), regulation of cell growth (GO:0001558), regulation of cellular response to stress (GO:0080135), epithelium migration (GO:0090132), positive regulation of organ growth (GO:0046622), response to oxygen-containing compound (GO:1901700), positive regulation of cellular component organization (GO:0051130), positive regulation of cell growth (GO:0030307), regulation of hormone levels (GO:0010817), negative regulation of cellular metabolic process (GO:0031324), positive regulation of response to wounding (GO:1903036), macromolecule metabolic process (GO:0043170), response to organic substance (GO:0010033), positive regulation of cell motility (GO:2000147), regulation of hormone secretion (GO:0046883), regulation of multicellular organismal development (GO:2000026), regulation of cell population proliferation (GO:0042127), regulation of cell death (GO:0010941), tissue development (GO:0009888), response to nitrogen compound (GO:1901698), regulation of multicellular organism growth (GO:0040014), regulation of cell communication (GO:0010646), dendrite development (GO:0016358), cellular response to chemical stimulus (GO:0070887), cellular response to stress (GO:0033554), negative regulation of developmental growth (GO:0048640), regulation of cellular metabolic process (GO:0031323), positive regulation of cell communication (GO:0010647), negative regulation of catabolic process (GO:0009895), regulation of trans-synaptic signaling (GO:0099177), regulation of primary metabolic process (GO:0080090), positive regulation of lipid storage (GO:0010884), regeneration (GO:0031099), positive regulation of multicellular organism growth (GO:0040018), positive regulation of axon regeneration (GO:0048680), response to peptide (GO:1901652), negative regulation of synapse assembly (GO:0051964), regulation of cellular component size (GO:0032535), epithelial cell migration (GO:0010631), cell projection organization (GO:0030030), regulation of synapse organization (GO:0050807), negative regulation of programmed cell death (GO:0043069), regulation of programmed cell death (GO:0043067), negative regulation of cellular catabolic process (GO:0031330), neuron projection regeneration (GO:0031102), wound healing, spreading of cells (GO:0044319), morphogenesis of an epithelium (GO:0002009), regulation of cell migration (GO:0030334), negative regulation of peptide hormone secretion (GO:0090278), neuron development (GO:0048666), negative regulation of lipid catabolic process (GO:0050995), long-term synaptic depression (GO:0060292), macromolecule modification (GO:0043412), regulation of peptide hormone secretion (GO:0090276), nervous system development (GO:0007399), female gamete generation (GO:0007292), sterol homeostasis (GO:0055092), regulation of triglyceride metabolic process (GO:0090207), positive regulation of cell migration (GO:0030335), positive regulation of intracellular signal transduction (GO:1902533), regulation of synaptic assembly at neuromuscular junction (GO:0008582), cellular response to oxygen-containing compound (GO:1901701), cellular response to organonitrogen compound (GO:0071417), protein kinase B signaling (GO:0043491), negative regulation of neuron death (GO:1901215), enzyme-linked receptor protein signaling pathway (GO:0007167), regulation of cell projection organization (GO:0031344), regulation of response to wounding (GO:1903034), negative regulation of triglyceride metabolic process (GO:0090209), cellular response to organic substance (GO:0071310), regulation of cell junction assembly (GO:1901888), oogenesis (GO:0048477), modulation of chemical synaptic transmission (GO:0050804), cellular response to nitrogen compound (GO:1901699), negative regulation of peptide secretion (GO:0002792), regulation of neuron death (GO:1901214), phosphate-containing compound metabolic process (GO:0006796), negative regulation of intracellular signal transduction (GO:1902532), regulation of nervous system development (GO:0051960), negative regulation of cell junction assembly (GO:1901889), ameboidal-type cell migration (GO:0001667), protein modification process (GO:0036211), response to peptide hormone (GO:0043434), negative regulation of synapse organization (GO:1905809), neurogenesis (GO:0022008), regulation of axon regeneration (GO:0048679), wound healing (GO:0042060), cellular response to hormone stimulus (GO:0032870), response to organonitrogen compound (GO:0010243), regulation of peptide transport (GO:0090087), positive regulation of cell projection organization (GO:0031346), negative regulation of synaptic assembly at neuromuscular junction (GO:0045886), positive regulation of epithelial cell migration (GO:0010634), regulation of lipid catabolic process (GO:0050994), regulation of secretion (GO:0051046), epithelium development (GO:0060429), regulation of cellular catabolic process (GO:0031329), regulation of lipid metabolic process (GO:0019216), neuron differentiation (GO:0030182), regulation of intracellular signal transduction (GO:1902531), respiratory system development (GO:0060541), regulation of TOR signaling (GO:0032006), regulation of apoptotic process (GO:0042981), negative regulation of neuromuscular junction development (GO:1904397), open tracheal system development (GO:0007424), regulation of neuromuscular junction development (GO:1904396), phosphorylation (GO:0016310), epithelial cell migration, open tracheal system (GO:0007427), regulation of synapse assembly (GO:0051963), transmembrane receptor protein tyrosine kinase signaling pathway (GO:0007169), generation of neurons (GO:0048699), positive regulation of TOR signaling (GO:0032008), regulation of hippo signaling (GO:0035330), morphogenesis of an epithelial sheet (GO:0002011), negative regulation of hippo signaling (GO:0035331), regulation of plasma membrane bounded cell projection organization (GO:0120035), epiboly involved in wound healing (GO:0090505), regulation of triglyceride catabolic process (GO:0010896), cellular response to peptide hormone stimulus (GO:0071375), response to insulin (GO:0032868), negative regulation of apoptotic process (GO:0043066), positive regulation of neuron projection development (GO:0010976), protein phosphorylation (GO:0006468), plasma membrane bounded cell projection organization (GO:0120036), regulation of cell size (GO:0008361), cellular response to peptide (GO:1901653), regulation of peptide secretion (GO:0002791), neuron projection development (GO:0031175), cholesterol homeostasis (GO:0042632), positive regulation of cell size (GO:0045793), cellular response to insulin stimulus (GO:0032869), positive regulation of TORC1 signaling (GO:1904263), regulation of neuron projection development (GO:0010975), insulin receptor signaling pathway (GO:0008286), vascular endothelial growth factor receptor signaling pathway (GO:0048010), regulation of TORC1 signaling (GO:1903432), epiboly (GO:0090504)

Cellular Component: cellular_component (GO:0005575), cellular anatomical entity (GO:0110165), intracellular anatomical structure (GO:0005622), organelle (GO:0043226), membrane (GO:0016020), cell body (GO:0044297), cytosol (GO:0005829), somatodendritic compartment (GO:0036477), cytoplasm (GO:0005737), cell periphery (GO:0071944), neuronal cell body (GO:0043025), intracellular organelle (GO:0043229), cell cortex (GO:0005938), membrane-bounded organelle (GO:0043227), plasma membrane (GO:0005886), intracellular membrane-bounded organelle (GO:0043231), nucleus (GO:0005634)

Generated by BioReason

Bioreason Rl Review

(Akt1-bioreason-rl-review.md)

BioReason-Pro RL Review: Akt1 (DROME)

Source: Akt1-bioreason-rl-predictions.md

Correctness: 4/5
Completeness: 3/5

Functional Summary Review

The BioReason summary correctly identifies Akt1 as:

A soluble AGC-class serine/threonine kinase in fruit fly that uses an N-terminal pleckstrin homology module to dock onto acidic lipid and polyanion-rich environments, where it becomes activated through its C-terminal regulatory tail.

This aligns well with the curated review, which identifies Akt1 as a "protein kinase B (Akt) that transduces PI3K signals to control growth, metabolism, survival, and development." The PH domain description and AGC-class kinase identification are accurate.

The summary continues:

Once engaged, the kinase transfers phosphate from ATP to serine/threonine residues on target proteins, integrating phosphoinositide signals to control phosphorylation cascades that govern metabolism, survival, and cytoskeletal organization.

This is broadly correct. The curated review confirms Akt1 functions in insulin receptor signaling (GO:0008286), negative regulation of apoptosis (GO:0043066), and growth control. The mention of "cytoskeletal organization" is reasonable but not a primary emphasis in the curated review.

It operates predominantly in the cytoplasm with a shuttling nuclear pool that likely tunes transcriptional and chromatin-associated pathways.

The curated review does not emphasize nuclear localization, though it is plausible for Akt family kinases. This is speculative but not incorrect.

Key omission: The summary does not mention the insulin/PI3K signaling pathway, which the curated review identifies as a core function. It also lacks mention of specific biological contexts such as cell size regulation (PMID:10962553), border follicle cell migration, lipid homeostasis, and the extensive developmental roles documented in the curated review.

Comparison with interpro2go:

The ai-review.yaml includes one interpro2go (GO_REF:0000002) annotation: protein kinase activity (GO:0004672). BioReason's functional summary essentially recapitulates this interpro2go mapping -- the domain-based reasoning identifies the kinase domain and correctly infers serine/threonine kinase activity. BioReason adds biological context (membrane recruitment via PH domain, AGC-class regulation) beyond what interpro2go provides, which is a genuine value-add from the domain architecture reasoning. However, BioReason does not go beyond generic kinase biology to identify the specific insulin/PI3K pathway context that defines Akt1.

Notes on thinking trace

The thinking trace provides a detailed domain-by-domain analysis that is well-structured and mostly accurate. The progression from PH domain to kinase domain to AGC tail is logical. The trace correctly identifies the mechanistic basis of PH domain-mediated membrane recruitment and AGC-tail regulation. The hypothesized interaction partners (PDK1-like activators, phosphoinositide-producing enzymes) are reasonable but generic.

📄 View Raw YAML

id: Q8INB9
gene_symbol: Akt1
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:7227
  label: Drosophila melanogaster
description: 'Protein kinase B (Akt) that transduces PI3K signals to control growth,
  metabolism, survival, and development.'
alternative_products:
- name: C (PK85)
  id: Q8INB9-1
- name: A (PK66)
  id: Q8INB9-2
  sequence_note: VSP_018833
existing_annotations:
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: file:genes/DROME/Akt1/Akt1-deep-research-falcon.md
      supporting_text: 'RecName: Full=RAC serine/threonine-protein kinase'
- term:
    id: GO:0035556
    label: intracellular signal transduction
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Akt1 participates in intracellular signal transduction.
    action: KEEP_AS_NON_CORE
    reason: Akt1 is a core kinase in insulin/PI3K signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
- term:
    id: GO:0043066
    label: negative regulation of apoptotic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Akt1 negatively regulates apoptosis.
    action: KEEP_AS_NON_CORE
    reason: Akt1 is described as a survival protein and dephosphorylation 
      triggers apoptosis.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: During early embryogenesis, acts as a survival protein
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Dephosphorylation of 'Ser-586' by Phlpp triggers 
        apoptosis and suppression of tumor growth
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
- term:
    id: GO:0043536
    label: positive regulation of blood vessel endothelial cell migration
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Blood vessel endothelial cell migration is not applicable to 
      Drosophila Akt1.
    action: MARK_AS_OVER_ANNOTATED
    reason: Drosophila lacks vascular endothelium; this term is too specific for
      fly Akt1.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
- term:
    id: GO:0000166
    label: nucleotide binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Akt1 binds nucleotides as part of its kinase reaction.
    action: KEEP_AS_NON_CORE
    reason: The catalytic reaction uses ATP, indicating nucleotide binding.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + 
        ADP + H(+)
- term:
    id: GO:0004672
    label: protein kinase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: Akt1 has protein kinase activity.
    action: KEEP_AS_NON_CORE
    reason: Catalytic activity confirms protein kinase function.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + 
        ADP + H(+)
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
- term:
    id: GO:0005524
    label: ATP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: Akt1 uses ATP in its catalytic reaction.
    action: KEEP_AS_NON_CORE
    reason: The kinase reaction explicitly consumes ATP.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + 
        ADP + H(+)
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: Akt1 localizes to the cytosol/cytoplasm.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports cytosolic and cytoplasmic localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: Akt1 can localize to the plasma membrane upon activation.
    action: KEEP_AS_NON_CORE
    reason: UniProt notes membrane recruitment upon activation.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0006915
    label: apoptotic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Akt1 regulates apoptosis rather than executing apoptotic processes.
    action: MODIFY
    reason: Akt1 functions as a survival protein and opposes apoptosis; use 
      regulation term.
    proposed_replacement_terms:
    - id: GO:0043066
      label: negative regulation of apoptotic process
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: During early embryogenesis, acts as a survival protein
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
- term:
    id: GO:0008582
    label: regulation of synaptic assembly at neuromuscular junction
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: Regulation of synaptic assembly at the NMJ is not clearly supported
      for Akt1.
    action: UNDECIDED
    reason: No direct NMJ synaptic assembly evidence for Akt1 was found in 
      accessible sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
- term:
    id: GO:0016301
    label: kinase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Akt1 has kinase activity.
    action: KEEP_AS_NON_CORE
    reason: Catalytic activity confirms kinase function.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + 
        ADP + H(+)
- term:
    id: GO:0016740
    label: transferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Akt1 is a transferase (kinase) enzyme.
    action: KEEP_AS_NON_CORE
    reason: Kinases transfer phosphate groups from ATP.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + 
        ADP + H(+)
- term:
    id: GO:0106310
    label: protein serine kinase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000116
  review:
    summary: Akt1 has protein serine kinase activity.
    action: KEEP_AS_NON_CORE
    reason: Akt1 is a serine/threonine kinase.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24068890
  review:
    summary: Akt1 interacts with protein partners such as Trbl.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports interaction with Trbl, supporting protein binding.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Interacts with trbl.
    - reference_id: PMID:24068890
      supporting_text: A Cullin1-based SCF E3 ubiquitin ligase targets the 
        InR/PI3K/TOR pathway to regulate neuronal pruning.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24413555
  review:
    summary: Akt1 interacts with protein partners such as Trbl.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports interaction with Trbl, supporting protein binding.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Interacts with trbl.
    - reference_id: PMID:24413555
      supporting_text: The SCFSlimb E3 ligase complex regulates asymmetric 
        division to inhibit neuroblast overgrowth.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-110475
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-169828
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:20585550
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:20585550
      supporting_text: Dynamic switch of negative feedback regulation in 
        Drosophila Akt-TOR signaling.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:36730473
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:36730473
      supporting_text: A genetic strategy to measure insulin signaling 
        regulation and physiology in Drosophila.
- term:
    id: GO:0043524
    label: negative regulation of neuron apoptotic process
  evidence_type: IGI
  original_reference_id: PMID:24916379
  review:
    summary: Akt1 promotes neuron survival.
    action: KEEP_AS_NON_CORE
    reason: Akt is described as promoting neuron survival downstream of LRRK2.
    supported_by:
    - reference_id: PMID:24916379
      supporting_text: Genetic dissection reveals that Akt is the critical 
        kinase downstream of LRRK2 to phosphorylate and inhibit FOXO1, and 
        promotes neuron survival.
- term:
    id: GO:0048010
    label: vascular endothelial growth factor receptor signaling pathway
  evidence_type: IGI
  original_reference_id: PMID:34751396
  review:
    summary: VEGF receptor signaling pathway is not directly supported for 
      Drosophila Akt1.
    action: MARK_AS_OVER_ANNOTATED
    reason: No direct VEGF receptor signaling evidence was identified for Akt1 
      in available sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:34751396
      supporting_text: Pvr and distinct downstream signaling factors are 
        required for hemocyte spreading and epidermal wound closure at 
        Drosophila larval wound sites.
- term:
    id: GO:0044319
    label: wound healing, spreading of cells
  evidence_type: IGI
  original_reference_id: PMID:34751396
  review:
    summary: Wound healing, spreading of cells is not directly supported by 
      accessible Akt1 evidence.
    action: UNDECIDED
    reason: No direct evidence for wound healing roles of Akt1 was identified in
      accessible sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:34751396
      supporting_text: Pvr and distinct downstream signaling factors are 
        required for hemocyte spreading and epidermal wound closure at 
        Drosophila larval wound sites.
- term:
    id: GO:0030307
    label: positive regulation of cell growth
  evidence_type: IMP
  original_reference_id: PMID:12172554
  review:
    summary: Akt1 promotes cell growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls cell growth.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:12172554
      supporting_text: Akt regulates growth by directly phosphorylating Tsc2.
- term:
    id: GO:0008284
    label: positive regulation of cell population proliferation
  evidence_type: IGI
  original_reference_id: PMID:12893776
  review:
    summary: Akt1 promotes cell population proliferation through growth 
      signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 promotes growth and 
      organ size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:12893776
      supporting_text: 'Control of cell number by Drosophila FOXO: downstream and
        feedback regulation of the insulin receptor pathway.'
- term:
    id: GO:0030307
    label: positive regulation of cell growth
  evidence_type: IMP
  original_reference_id: PMID:17462592
  review:
    summary: Akt1 promotes cell growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls cell growth.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:17462592
      supporting_text: Discrete functions of rictor and raptor in cell growth 
        regulation in Drosophila.
- term:
    id: GO:0030307
    label: positive regulation of cell growth
  evidence_type: IMP
  original_reference_id: PMID:29514084
  review:
    summary: Akt1 promotes cell growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls cell growth.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:29514084
      supporting_text: Innate Immune Signaling in Drosophila Blocks Insulin 
        Signaling by Uncoupling PI(3,4,5)P(3) Production and Akt Activation.
- term:
    id: GO:0035206
    label: regulation of hemocyte proliferation
  evidence_type: IMP
  original_reference_id: PMID:20688956
  review:
    summary: Hemocyte proliferation regulation is not supported by accessible 
      Akt-specific evidence.
    action: UNDECIDED
    reason: The cited study does not directly mention Akt in hemocyte 
      proliferation in the abstract.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:20688956
      supporting_text: Genetic manipulation of AML1-ETO-induced expansion of 
        hematopoietic precursors in a Drosophila model.
- term:
    id: GO:0035264
    label: multicellular organism growth
  evidence_type: IMP
  original_reference_id: PMID:21464442
  review:
    summary: Akt1 contributes to multicellular organism growth.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls growth and 
      organ size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:21464442
      supporting_text: Drosophila insulin pathway mutants affect visual 
        physiology and brain function besides growth, lipid, and carbohydrate 
        metabolism.
- term:
    id: GO:0040014
    label: regulation of multicellular organism growth
  evidence_type: IMP
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 regulates multicellular organism growth via insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls growth and 
      organ size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:0040018
    label: positive regulation of multicellular organism growth
  evidence_type: IGI
  original_reference_id: PMID:29514084
  review:
    summary: Akt1 positively regulates multicellular organism growth.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls growth and 
      organ size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:29514084
      supporting_text: Innate Immune Signaling in Drosophila Blocks Insulin 
        Signaling by Uncoupling PI(3,4,5)P(3) Production and Akt Activation.
- term:
    id: GO:0043066
    label: negative regulation of apoptotic process
  evidence_type: IMP
  original_reference_id: PMID:9601646
  review:
    summary: Akt1 negatively regulates apoptosis.
    action: KEEP_AS_NON_CORE
    reason: Akt1 is described as a survival protein and dephosphorylation 
      triggers apoptosis.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: During early embryogenesis, acts as a survival protein
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Dephosphorylation of 'Ser-586' by Phlpp triggers 
        apoptosis and suppression of tumor growth
    - reference_id: PMID:9601646
      supporting_text: Genetic analysis of protein kinase B (AKT) in Drosophila.
- term:
    id: GO:0045793
    label: positive regulation of cell size
  evidence_type: IMP
  original_reference_id: PMID:10587646
  review:
    summary: Akt1 promotes cell size via insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls growth and 
      size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10587646
      supporting_text: Cell-autonomous regulation of cell and organ growth in 
        Drosophila by Akt/PKB.
- term:
    id: GO:0045793
    label: positive regulation of cell size
  evidence_type: IMP
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 promotes cell size via insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls growth and 
      size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:0045793
    label: positive regulation of cell size
  evidence_type: IMP
  original_reference_id: PMID:19216764
  review:
    summary: Akt1 promotes cell size via insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls growth and 
      size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:19216764
      supporting_text: PDGF/VEGF signaling controls cell size in Drosophila.
- term:
    id: GO:0046622
    label: positive regulation of organ growth
  evidence_type: IMP
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 promotes organ growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls organ size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:1904263
    label: positive regulation of TORC1 signaling
  evidence_type: IMP
  original_reference_id: PMID:28829944
  review:
    summary: Akt1 can promote TORC1 signaling via Tsc2 inhibition.
    action: KEEP_AS_NON_CORE
    reason: UniProt notes Akt1 may stimulate growth by inactivating the Tsc 
      complex.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: May also stimulate cell growth by phosphorylating 
        Gig/Tsc2 and inactivating the Tsc complex
    - reference_id: PMID:28829944
      supporting_text: Spatial Activation of TORC1 Is Regulated by Hedgehog and 
        E2F1 Signaling in the Drosophila Eye.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:32998936
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:32998936
      supporting_text: Meep, a Novel Regulator of Insulin Signaling, Supports 
        Development and Insulin Sensitivity via Maintenance of Protein 
        Homeostasis in Drosophila melanogaster.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IMP
  original_reference_id: PMID:31613895
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:31613895
      supporting_text: The Hippo pathway integrates PI3K-Akt signals with 
        mechanical and polarity cues to control tissue growth.
- term:
    id: GO:0035331
    label: negative regulation of hippo signaling
  evidence_type: IMP
  original_reference_id: PMID:31613895
  review:
    summary: Negative regulation of Hippo signaling is not directly supported 
      for Akt1.
    action: MARK_AS_OVER_ANNOTATED
    reason: The cited Hippo study shows IIS/PI3K/PDK1/Akt inputs but not 
      specific negative regulation by Akt.
    supported_by:
    - reference_id: PMID:31613895
      supporting_text: via phosphatidyl inositol-3-kinase (PI3K), 
        phosphoinositide-dependent kinase 1 (PDK1 or PDPK1), and protein kinase 
        B (Akt or PKB)
- term:
    id: GO:0048010
    label: vascular endothelial growth factor receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:18000865
  review:
    summary: VEGF receptor signaling pathway is not directly supported for 
      Drosophila Akt1.
    action: MARK_AS_OVER_ANNOTATED
    reason: No direct VEGF receptor signaling evidence was identified for Akt1 
      in available sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:18000865
      supporting_text: Gliatrophic and gliatropic roles of PVF/PVR signaling 
        during axon guidance.
- term:
    id: GO:0043491
    label: phosphatidylinositol 3-kinase/protein kinase B signal transduction
  evidence_type: IDA
  original_reference_id: PMID:12172554
  review:
    summary: Akt1 is a central kinase in PI3K/PKB signal transduction.
    action: KEEP_AS_NON_CORE
    reason: Akt1 operates downstream of PI3K in insulin signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:12172554
      supporting_text: Akt regulates growth by directly phosphorylating Tsc2.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:29514084
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:29514084
      supporting_text: Innate Immune Signaling in Drosophila Blocks Insulin 
        Signaling by Uncoupling PI(3,4,5)P(3) Production and Akt Activation.
- term:
    id: GO:1903688
    label: positive regulation of border follicle cell migration
  evidence_type: IGI
  original_reference_id: PMID:29950391
  review:
    summary: Insulin signaling modulates border cell migration in oogenesis.
    action: KEEP_AS_NON_CORE
    reason: Insulin signaling regulates border cell movement during oogenesis.
    supported_by:
    - reference_id: PMID:29950391
      supporting_text: insulin signaling modulates collective BC movement during
        Drosophila oogenesis
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:11862217
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:11862217
      supporting_text: dS6K-regulated cell growth is dPKB/dPI(3)K-independent, 
        but requires dPDK1.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:11862217
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:11862217
      supporting_text: dS6K-regulated cell growth is dPKB/dPI(3)K-independent, 
        but requires dPDK1.
- term:
    id: GO:0032869
    label: cellular response to insulin stimulus
  evidence_type: IDA
  original_reference_id: PMID:11862217
  review:
    summary: Akt1 mediates cellular responses to insulin.
    action: KEEP_AS_NON_CORE
    reason: Akt1 acts downstream of insulin receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:11862217
      supporting_text: dS6K-regulated cell growth is dPKB/dPI(3)K-independent, 
        but requires dPDK1.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:29045833
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:29045833
      supporting_text: Intestinal Fork Head Regulates Nutrient Absorption and 
        Promotes Longevity.
- term:
    id: GO:0055088
    label: lipid homeostasis
  evidence_type: IMP
  original_reference_id: PMID:21464442
  review:
    summary: Lipid homeostasis involvement is supported through Akt-dependent 
      lipid storage regulation.
    action: KEEP_AS_NON_CORE
    reason: Activated Akt affects lipid droplet accumulation in nurse cells.
    supported_by:
    - reference_id: PMID:17079271
      supporting_text: accumulation of activated Akt in the cytoplasm is 
        responsible for this phenotype and leads to a much higher expression of 
        LSD2
    - reference_id: PMID:21464442
      supporting_text: Drosophila insulin pathway mutants affect visual 
        physiology and brain function besides growth, lipid, and carbohydrate 
        metabolism.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:22242005
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:22242005
      supporting_text: MAPK/ERK signaling regulates insulin sensitivity to 
        control glucose metabolism in Drosophila.
- term:
    id: GO:0048010
    label: vascular endothelial growth factor receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:25749252
  review:
    summary: VEGF receptor signaling pathway is not directly supported for 
      Drosophila Akt1.
    action: MARK_AS_OVER_ANNOTATED
    reason: No direct VEGF receptor signaling evidence was identified for Akt1 
      in available sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:25749252
      supporting_text: A systems-level interrogation identifies regulators of 
        Drosophila blood cell number and survival.
- term:
    id: GO:0048010
    label: vascular endothelial growth factor receptor signaling pathway
  evidence_type: IGI
  original_reference_id: PMID:19216764
  review:
    summary: VEGF receptor signaling pathway is not directly supported for 
      Drosophila Akt1.
    action: MARK_AS_OVER_ANNOTATED
    reason: No direct VEGF receptor signaling evidence was identified for Akt1 
      in available sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:19216764
      supporting_text: PDGF/VEGF signaling controls cell size in Drosophila.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:21565616
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:21565616
      supporting_text: A hormone-dependent module regulating energy balance.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IDA
  original_reference_id: PMID:18827008
  review:
    summary: Akt1 localizes to the cytosol/cytoplasm.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports cytosolic and cytoplasmic localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
    - reference_id: PMID:18827008
      supporting_text: The protein phosphatase PP2A-B' subunit Widerborst is a 
        negative regulator of cytoplasmic activated Akt and lipid metabolism in 
        Drosophila.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:14645523
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:14645523
      supporting_text: Signaling from Akt to FRAP/TOR targets both 4E-BP and S6K
        in Drosophila melanogaster.
- term:
    id: GO:0010884
    label: positive regulation of lipid storage
  evidence_type: IMP
  original_reference_id: PMID:18827008
  review:
    summary: Activated Akt promotes lipid storage in nurse cells.
    action: KEEP_AS_NON_CORE
    reason: Activated Akt increases LSD2 expression linked to lipid droplet 
      accumulation.
    supported_by:
    - reference_id: PMID:17079271
      supporting_text: accumulation of activated Akt in the cytoplasm is 
        responsible for this phenotype and leads to a much higher expression of 
        LSD2
    - reference_id: PMID:18827008
      supporting_text: The protein phosphatase PP2A-B' subunit Widerborst is a 
        negative regulator of cytoplasmic activated Akt and lipid metabolism in 
        Drosophila.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:17183368
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:17183368
      supporting_text: Insulin delays the progression of Drosophila cells 
        through G2/M by activating the dTOR/dRaptor complex.
- term:
    id: GO:0010897
    label: negative regulation of triglyceride catabolic process
  evidence_type: IMP
  original_reference_id: PMID:21565616
  review:
    summary: Akt1 promotes lipid storage, consistent with reduced triglyceride 
      catabolism.
    action: KEEP_AS_NON_CORE
    reason: Activated Akt increases lipid storage markers.
    supported_by:
    - reference_id: PMID:17079271
      supporting_text: accumulation of activated Akt in the cytoplasm is 
        responsible for this phenotype and leads to a much higher expression of 
        LSD2
    - reference_id: PMID:21565616
      supporting_text: A hormone-dependent module regulating energy balance.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:17369395
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:17369395
      supporting_text: 'Re-evaluating AKT regulation: role of TOR complex 2 in tissue
        growth.'
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:17369395
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:17369395
      supporting_text: 'Re-evaluating AKT regulation: role of TOR complex 2 in tissue
        growth.'
- term:
    id: GO:0032869
    label: cellular response to insulin stimulus
  evidence_type: IDA
  original_reference_id: PMID:17369395
  review:
    summary: Akt1 mediates cellular responses to insulin.
    action: KEEP_AS_NON_CORE
    reason: Akt1 acts downstream of insulin receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:17369395
      supporting_text: 'Re-evaluating AKT regulation: role of TOR complex 2 in tissue
        growth.'
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IMP
  original_reference_id: PMID:12893776
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:12893776
      supporting_text: 'Control of cell number by Drosophila FOXO: downstream and
        feedback regulation of the insulin receptor pathway.'
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:15337530
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:15337530
      supporting_text: Drosophila PI3 kinase and Akt involved in 
        insulin-stimulated proliferation and ERK pathway activation in Schneider
        cells.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:12172554
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:12172554
      supporting_text: Akt regulates growth by directly phosphorylating Tsc2.
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:7876156
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:7876156
      supporting_text: Developmental regulation of expression and activity of 
        multiple forms of the Drosophila RAC protein kinase.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IDA
  original_reference_id: PMID:17079271
  review:
    summary: Nuclear localization is not supported by the UniProt subcellular 
      location statement.
    action: UNDECIDED
    reason: UniProt lists cytosol/cell membrane, not nuclear localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
    - reference_id: PMID:17079271
      supporting_text: Cytoplasmic activated protein kinase Akt regulates 
        lipid-droplet accumulation in Drosophila nurse cells.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IDA
  original_reference_id: PMID:17079271
  review:
    summary: Akt1 localizes to the cytosol/cytoplasm.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports cytosolic and cytoplasmic localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
    - reference_id: PMID:17079271
      supporting_text: Cytoplasmic activated protein kinase Akt regulates 
        lipid-droplet accumulation in Drosophila nurse cells.
- term:
    id: GO:0005938
    label: cell cortex
  evidence_type: IDA
  original_reference_id: PMID:17079271
  review:
    summary: Cell cortex localization is not supported by available sources for 
      Akt1.
    action: UNDECIDED
    reason: No direct evidence for cortical localization was identified in 
      accessible sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
    - reference_id: PMID:17079271
      supporting_text: Cytoplasmic activated protein kinase Akt regulates 
        lipid-droplet accumulation in Drosophila nurse cells.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:12172554
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:12172554
      supporting_text: Akt regulates growth by directly phosphorylating Tsc2.
- term:
    id: GO:0010884
    label: positive regulation of lipid storage
  evidence_type: IGI
  original_reference_id: PMID:17079271
  review:
    summary: Activated Akt promotes lipid storage in nurse cells.
    action: KEEP_AS_NON_CORE
    reason: Activated Akt increases LSD2 expression linked to lipid droplet 
      accumulation.
    supported_by:
    - reference_id: PMID:17079271
      supporting_text: accumulation of activated Akt in the cytoplasm is 
        responsible for this phenotype and leads to a much higher expression of 
        LSD2
- term:
    id: GO:0042632
    label: cholesterol homeostasis
  evidence_type: IMP
  original_reference_id: PMID:27326933
  review:
    summary: Cholesterol homeostasis is not directly supported by accessible 
      evidence.
    action: UNDECIDED
    reason: Available sources focus on insulin signaling and lipid storage 
      rather than cholesterol homeostasis.
    supported_by:
    - reference_id: PMID:17079271
      supporting_text: accumulation of activated Akt in the cytoplasm is 
        responsible for this phenotype and leads to a much higher expression of 
        LSD2
    - reference_id: PMID:27326933
      supporting_text: A Drosophila Genome-Wide Screen Identifies Regulators of 
        Steroid Hormone Production and Developmental Timing.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-110463
  review:
    summary: Akt1 localizes to the cytosol/cytoplasm.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports cytosolic and cytoplasmic localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-110468
  review:
    summary: Akt1 localizes to the cytosol/cytoplasm.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports cytosolic and cytoplasmic localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-110475
  review:
    summary: Akt1 localizes to the cytosol/cytoplasm.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports cytosolic and cytoplasmic localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-169828
  review:
    summary: Akt1 localizes to the cytosol/cytoplasm.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports cytosolic and cytoplasmic localization.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-110463
  review:
    summary: Akt1 can localize to the plasma membrane upon activation.
    action: KEEP_AS_NON_CORE
    reason: UniProt notes membrane recruitment upon activation.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-DME-110468
  review:
    summary: Akt1 can localize to the plasma membrane upon activation.
    action: KEEP_AS_NON_CORE
    reason: UniProt notes membrane recruitment upon activation.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
- term:
    id: GO:0090278
    label: negative regulation of peptide hormone secretion
  evidence_type: IMP
  original_reference_id: PMID:25101872
  review:
    summary: Negative regulation of peptide hormone secretion is not supported 
      by accessible Akt1 evidence.
    action: UNDECIDED
    reason: No direct evidence for Akt1 in peptide hormone secretion was 
      identified in accessible sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:25101872
      supporting_text: A genetic strategy to measure circulating Drosophila 
        insulin reveals genes regulating insulin production and secretion.
- term:
    id: GO:0048477
    label: oogenesis
  evidence_type: IMP
  original_reference_id: PMID:24786828
  review:
    summary: Akt1 functions in oogenesis by controlling follicle cell size.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports control of follicle cell size during oogenesis.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Controls follicle cell size during oogenesis
    - reference_id: PMID:24786828
      supporting_text: The TORC1 inhibitors Nprl2 and Nprl3 mediate an adaptive 
        response to amino-acid starvation in Drosophila.
- term:
    id: GO:0043025
    label: neuronal cell body
  evidence_type: IDA
  original_reference_id: PMID:24068890
  review:
    summary: Neuronal cell body localization is not supported by accessible 
      sources.
    action: UNDECIDED
    reason: No direct neuronal cell body localization evidence was identified in
      accessible sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
        to plasma membrane upon activation.'
    - reference_id: PMID:24068890
      supporting_text: A Cullin1-based SCF E3 ubiquitin ligase targets the 
        InR/PI3K/TOR pathway to regulate neuronal pruning.
- term:
    id: GO:0045886
    label: negative regulation of synaptic assembly at neuromuscular junction
  evidence_type: IMP
  original_reference_id: PMID:23393158
  review:
    summary: Negative regulation of synaptic assembly at the NMJ is not clearly 
      supported for Akt1.
    action: UNDECIDED
    reason: No direct NMJ synaptic assembly evidence for Akt1 was found in 
      accessible sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:23393158
      supporting_text: Tuberous sclerosis complex regulates Drosophila 
        neuromuscular junction growth via the TORC2/Akt pathway.
- term:
    id: GO:0031104
    label: dendrite regeneration
  evidence_type: IMP
  original_reference_id: PMID:22759636
  review:
    summary: Akt pathway promotes dendrite regeneration.
    action: KEEP_AS_NON_CORE
    reason: Akt pathway activity affects dendrite regeneration in sensory 
      neurons.
    supported_by:
    - reference_id: PMID:22759636
      supporting_text: dendrite regeneration is restrained via inhibition of the
        Akt pathway
- term:
    id: GO:0048680
    label: positive regulation of axon regeneration
  evidence_type: IMP
  original_reference_id: PMID:22759636
  review:
    summary: Akt pathway activation enhances axon regeneration.
    action: KEEP_AS_NON_CORE
    reason: Akt activation enhances axon regeneration in the CNS.
    supported_by:
    - reference_id: PMID:22759636
      supporting_text: activating the Akt pathway enhances axon regeneration in 
        the CNS
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15808505
  review:
    summary: Akt1 interacts with protein partners such as Trbl.
    action: KEEP_AS_NON_CORE
    reason: UniProt reports interaction with Trbl, supporting protein binding.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Interacts with trbl.
    - reference_id: PMID:15808505
      supporting_text: 'PHLPP: a phosphatase that directly dephosphorylates Akt, promotes
        apoptosis, and suppresses tumor growth.'
- term:
    id: GO:0006979
    label: response to oxidative stress
  evidence_type: IMP
  original_reference_id: PMID:17895391
  review:
    summary: Akt influences circadian clock sensitivity to oxidative stress.
    action: KEEP_AS_NON_CORE
    reason: Akt overexpression increases susceptibility of the central clock to 
      oxidative stress.
    supported_by:
    - reference_id: PMID:17895391
      supporting_text: such as the insulin receptor or Akt, in the fat body also
        increased susceptibility of the central clock to oxidative stress.
- term:
    id: GO:0007623
    label: circadian rhythm
  evidence_type: IMP
  original_reference_id: PMID:17895391
  review:
    summary: Akt impacts circadian rhythm via insulin/FOXO signaling.
    action: KEEP_AS_NON_CORE
    reason: Akt overexpression affects central clock function under oxidative 
      stress.
    supported_by:
    - reference_id: PMID:17895391
      supporting_text: such as the insulin receptor or Akt, in the fat body also
        increased susceptibility of the central clock to oxidative stress.
- term:
    id: GO:0060292
    label: long-term synaptic depression
  evidence_type: IMP
  original_reference_id: PMID:16611817
  review:
    summary: Long-term synaptic depression is not supported by accessible 
      Akt1-specific evidence.
    action: UNDECIDED
    reason: No direct evidence for Akt1 in long-term synaptic depression was 
      identified in accessible sources.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:16611817
      supporting_text: Requirement of Akt to mediate long-term synaptic 
        depression in Drosophila.
- term:
    id: GO:0050773
    label: regulation of dendrite development
  evidence_type: IMP
  original_reference_id: PMID:19778508
  review:
    summary: Akt activity influences dendrite development.
    action: KEEP_AS_NON_CORE
    reason: Akt kinase activity in neurons influences dendrite growth.
    supported_by:
    - reference_id: PMID:19778508
      supporting_text: ban in epithelial cells dampens Akt kinase activity in 
        adjacent neurons to influence dendrite growth
- term:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  evidence_type: IMP
  original_reference_id: PMID:9601646
  review:
    summary: Akt1 is a serine/threonine protein kinase.
    action: ACCEPT
    reason: UniProt describes Akt1 as a serine/threonine kinase involved in 
      developmental processes.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Serine/threonine kinase involved in various developmental
        processes
    - reference_id: PMID:9601646
      supporting_text: Genetic analysis of protein kinase B (AKT) in Drosophila.
- term:
    id: GO:0007424
    label: open tracheal system development
  evidence_type: IMP
  original_reference_id: PMID:11740943
  review:
    summary: Akt1 regulates tracheal development by activating Trh.
    action: KEEP_AS_NON_CORE
    reason: Akt1 phosphorylates Trh required for tracheal cell fate.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: phosphorylates and activates trh, a transcription factor 
        required for tracheal cell fate determination
    - reference_id: PMID:11740943
      supporting_text: Regulation of Drosophila tracheal system development by 
        protein kinase B.
- term:
    id: GO:0007427
    label: epithelial cell migration, open tracheal system
  evidence_type: IMP
  original_reference_id: PMID:14525946
  review:
    summary: Akt1 regulates tracheal cell migration.
    action: KEEP_AS_NON_CORE
    reason: UniProt notes Akt1 regulates tracheal cell migration.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: Also regulates tracheal cell migration
    - reference_id: PMID:14525946
      supporting_text: Coordinated functions of Akt/PKB and ETS1 in tubule 
        formation.
- term:
    id: GO:0008284
    label: positive regulation of cell population proliferation
  evidence_type: IMP
  original_reference_id: PMID:10587646
  negated: true
  review:
    summary: Akt1 promotes cell population proliferation through growth 
      signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 promotes growth and 
      organ size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10587646
      supporting_text: Cell-autonomous regulation of cell and organ growth in 
        Drosophila by Akt/PKB.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IDA
  original_reference_id: PMID:10587646
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:10587646
      supporting_text: Cell-autonomous regulation of cell and organ growth in 
        Drosophila by Akt/PKB.
- term:
    id: GO:0008286
    label: insulin receptor signaling pathway
  evidence_type: IGI
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 acts in the insulin receptor signaling pathway.
    action: ACCEPT
    reason: UniProt states Akt1 functions downstream of PI3K/PDK1 in insulin 
      receptor signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:0030307
    label: positive regulation of cell growth
  evidence_type: IMP
  original_reference_id: PMID:10587646
  review:
    summary: Akt1 promotes cell growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls cell growth.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10587646
      supporting_text: Cell-autonomous regulation of cell and organ growth in 
        Drosophila by Akt/PKB.
- term:
    id: GO:0030307
    label: positive regulation of cell growth
  evidence_type: IMP
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 promotes cell growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls cell growth.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:0030307
    label: positive regulation of cell growth
  evidence_type: IMP
  original_reference_id: PMID:15712201
  review:
    summary: Akt1 promotes cell growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls cell growth.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:15712201
      supporting_text: dAkt kinase controls follicle cell size during Drosophila
        oogenesis.
- term:
    id: GO:0035556
    label: intracellular signal transduction
  evidence_type: IGI
  original_reference_id: PMID:10962553
  review:
    summary: Akt1 participates in intracellular signal transduction.
    action: KEEP_AS_NON_CORE
    reason: Akt1 is a core kinase in insulin/PI3K signaling.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: acts downstream of PI3K and Pk61C/PDK1 in the insulin 
        receptor transduction pathway
    - reference_id: PMID:10962553
      supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
        both cell size and survival in Drosophila.
- term:
    id: GO:0046622
    label: positive regulation of organ growth
  evidence_type: IMP
  original_reference_id: PMID:10587646
  review:
    summary: Akt1 promotes organ growth downstream of insulin signaling.
    action: KEEP_AS_NON_CORE
    reason: Insulin receptor signaling regulated by Akt1 controls organ size.
    supported_by:
    - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
      supporting_text: insulin receptor transduction pathway which regulates 
        cell growth and organ size
    - reference_id: PMID:10587646
      supporting_text: Cell-autonomous regulation of cell and organ growth in 
        Drosophila by Akt/PKB.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with 
    GO terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000043
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular 
    Location vocabulary mapping, accompanied by conservative changes to GO terms
    applied by UniProt
  findings: []
- id: GO_REF:0000116
  title: Automatic Gene Ontology annotation based on Rhea mapping
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning 
    models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:10587646
  title: Cell-autonomous regulation of cell and organ growth in Drosophila by 
    Akt/PKB.
  findings: []
- id: PMID:10962553
  title: The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size
    and survival in Drosophila.
  findings: []
- id: PMID:11740943
  title: Regulation of Drosophila tracheal system development by protein kinase 
    B.
  findings: []
- id: PMID:11862217
  title: dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires 
    dPDK1.
  findings: []
- id: PMID:12172554
  title: Akt regulates growth by directly phosphorylating Tsc2.
  findings: []
- id: PMID:12893776
  title: 'Control of cell number by Drosophila FOXO: downstream and feedback regulation
    of the insulin receptor pathway.'
  findings: []
- id: PMID:14525946
  title: Coordinated functions of Akt/PKB and ETS1 in tubule formation.
  findings: []
- id: PMID:14645523
  title: Signaling from Akt to FRAP/TOR targets both 4E-BP and S6K in Drosophila
    melanogaster.
  findings: []
- id: PMID:15337530
  title: Drosophila PI3 kinase and Akt involved in insulin-stimulated 
    proliferation and ERK pathway activation in Schneider cells.
  findings: []
- id: PMID:15712201
  title: dAkt kinase controls follicle cell size during Drosophila oogenesis.
  findings: []
- id: PMID:15808505
  title: 'PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis,
    and suppresses tumor growth.'
  findings: []
- id: PMID:16611817
  title: Requirement of Akt to mediate long-term synaptic depression in 
    Drosophila.
  findings: []
- id: PMID:17079271
  title: Cytoplasmic activated protein kinase Akt regulates lipid-droplet 
    accumulation in Drosophila nurse cells.
  findings: []
- id: PMID:17183368
  title: Insulin delays the progression of Drosophila cells through G2/M by 
    activating the dTOR/dRaptor complex.
  findings: []
- id: PMID:17369395
  title: 'Re-evaluating AKT regulation: role of TOR complex 2 in tissue growth.'
  findings: []
- id: PMID:17462592
  title: Discrete functions of rictor and raptor in cell growth regulation in 
    Drosophila.
  findings: []
- id: PMID:17895391
  title: FOXO and insulin signaling regulate sensitivity of the circadian clock 
    to oxidative stress.
  findings: []
- id: PMID:18000865
  title: Gliatrophic and gliatropic roles of PVF/PVR signaling during axon 
    guidance.
  findings: []
- id: PMID:18827008
  title: The protein phosphatase PP2A-B' subunit Widerborst is a negative 
    regulator of cytoplasmic activated Akt and lipid metabolism in Drosophila.
  findings: []
- id: PMID:19216764
  title: PDGF/VEGF signaling controls cell size in Drosophila.
  findings: []
- id: PMID:19778508
  title: The microRNA bantam functions in epithelial cells to regulate scaling 
    growth of dendrite arbors in drosophila sensory neurons.
  findings: []
- id: PMID:20585550
  title: Dynamic switch of negative feedback regulation in Drosophila Akt-TOR 
    signaling.
  findings: []
- id: PMID:20688956
  title: Genetic manipulation of AML1-ETO-induced expansion of hematopoietic 
    precursors in a Drosophila model.
  findings: []
- id: PMID:21464442
  title: Drosophila insulin pathway mutants affect visual physiology and brain 
    function besides growth, lipid, and carbohydrate metabolism.
  findings: []
- id: PMID:21565616
  title: A hormone-dependent module regulating energy balance.
  findings: []
- id: PMID:22242005
  title: MAPK/ERK signaling regulates insulin sensitivity to control glucose 
    metabolism in Drosophila.
  findings: []
- id: PMID:22759636
  title: Regeneration of Drosophila sensory neuron axons and dendrites is 
    regulated by the Akt pathway involving Pten and microRNA bantam.
  findings: []
- id: PMID:23393158
  title: Tuberous sclerosis complex regulates Drosophila neuromuscular junction 
    growth via the TORC2/Akt pathway.
  findings: []
- id: PMID:24068890
  title: A Cullin1-based SCF E3 ubiquitin ligase targets the InR/PI3K/TOR 
    pathway to regulate neuronal pruning.
  findings: []
- id: PMID:24413555
  title: The SCFSlimb E3 ligase complex regulates asymmetric division to inhibit
    neuroblast overgrowth.
  findings: []
- id: PMID:24786828
  title: The TORC1 inhibitors Nprl2 and Nprl3 mediate an adaptive response to 
    amino-acid starvation in Drosophila.
  findings: []
- id: PMID:24916379
  title: Genetic dissection reveals that Akt is the critical kinase downstream 
    of LRRK2 to phosphorylate and inhibit FOXO1, and promotes neuron survival.
  findings: []
- id: PMID:25101872
  title: A genetic strategy to measure circulating Drosophila insulin reveals 
    genes regulating insulin production and secretion.
  findings: []
- id: PMID:25749252
  title: A systems-level interrogation identifies regulators of Drosophila blood
    cell number and survival.
  findings: []
- id: PMID:27326933
  title: A Drosophila Genome-Wide Screen Identifies Regulators of Steroid 
    Hormone Production and Developmental Timing.
  findings: []
- id: PMID:28829944
  title: Spatial Activation of TORC1 Is Regulated by Hedgehog and E2F1 Signaling
    in the Drosophila Eye.
  findings: []
- id: PMID:29045833
  title: Intestinal Fork Head Regulates Nutrient Absorption and Promotes 
    Longevity.
  findings: []
- id: PMID:29514084
  title: Innate Immune Signaling in Drosophila Blocks Insulin Signaling by 
    Uncoupling PI(3,4,5)P(3) Production and Akt Activation.
  findings: []
- id: PMID:29950391
  title: Insulin signaling modulates border cell movement in Drosophila 
    oogenesis.
  findings: []
- id: PMID:31613895
  title: The Hippo pathway integrates PI3K-Akt signals with mechanical and 
    polarity cues to control tissue growth.
  findings: []
- id: PMID:32998936
  title: Meep, a Novel Regulator of Insulin Signaling, Supports Development and 
    Insulin Sensitivity via Maintenance of Protein Homeostasis in Drosophila 
    melanogaster.
  findings: []
- id: PMID:34751396
  title: Pvr and distinct downstream signaling factors are required for hemocyte
    spreading and epidermal wound closure at Drosophila larval wound sites.
  findings: []
- id: PMID:36730473
  title: A genetic strategy to measure insulin signaling regulation and 
    physiology in Drosophila.
  findings: []
- id: PMID:7876156
  title: Developmental regulation of expression and activity of multiple forms 
    of the Drosophila RAC protein kinase.
  findings: []
- id: PMID:9601646
  title: Genetic analysis of protein kinase B (AKT) in Drosophila.
  findings: []
- id: Reactome:R-DME-110463
  title: Increased PIP3 levels recruit DAkt1 to the membrane
  findings: []
- id: Reactome:R-DME-110468
  title: Activation of DAkt1 by DPDK1
  findings: []
- id: Reactome:R-DME-110475
  title: DAkt1-mediated phosphorylation inactivates DFOXO
  findings: []
- id: Reactome:R-DME-169828
  title: Activated DAkt1 phosphorylates TSC2 which inhibits the TSC1/2 complex
  findings: []
core_functions:
- description: Akt1 is a protein kinase B that transduces PI3K signals to 
    control growth, metabolism, and survival programs.
  supported_by:
  - reference_id: file:genes/DROME/Akt1/Akt1-uniprot.txt
    supporting_text: 'RecName: Full=RAC serine/threonine-protein kinase'
  - reference_id: PMID:10962553
    supporting_text: The conserved PI3'K/PTEN/Akt signaling pathway regulates 
      both cell size and survival in Drosophila.
  molecular_function:
    id: GO:0004674
    label: protein serine/threonine kinase activity
  directly_involved_in:
  - id: GO:0008286
    label: insulin receptor signaling pathway

Akt1

Gene Description

Existing Annotations Review

Core Functions

Akt1 is a protein kinase B that transduces PI3K signals to control growth, metabolism, and survival programs.

References

Deep Research

Falcon

Citations

📚 Additional Documentation

Bioreason Rl Predictions

BioReason Chat Export

Thinking Trace

Functional Summary

UniProt Summary

InterPro Domains

GO Terms

Bioreason Rl Review

BioReason-Pro RL Review: Akt1 (DROME)

Functional Summary Review

Notes on thinking trace

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