GNAI1 encodes G alpha i1, a heterotrimeric G protein alpha subunit that transduces signals from Gi-coupled receptors. It binds and hydrolyzes guanine nucleotides and can directly inhibit selected adenylyl cyclase isoforms, reducing cAMP production in receptor- and effector-dependent contexts. In addition to plasma-membrane signaling, Gi1 participates in cortical LGNβNuMA machinery that orients mitotic spindles and localizes to centrosomal and cytokinetic structures. Its cellular effects include neurotransmitter, endocrine and immune-cell responses.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000132 establishment of mitotic spindle orientation | NAS PMID:11781568 A mammalian Partner of inscuteable binds NuMA and regulates ... | KEEP AS NON CORE | Summary: Gi1 participates in the cortical LGNβNuMA/dynein machinery that positions the spindle; gain/loss and localization experiments support spindle organization and cortical recruitment. Reason: These are direct secondary cellular functions rather than generic proliferation associations. |
| GO:0000287 magnesium ion binding | ISS GO_REF:0000024 | ACCEPT | Summary: Magnesium coordination is integral to guanine-nucleotide binding/hydrolysis in the G alpha catalytic pocket, supported by nucleotide-state structural and biochemical studies. Reason: It is a core cofactor interaction, not peripheral simply because it is binding. |
| GO:0000922 spindle pole | IPI PMID:15537540 Mammalian Pins is a conformational switch that links NuMA to... | KEEP AS NON CORE | Summary: Imaging and biochemical studies identify Gi1 at spindle poles/centrosomes and the midbody during division. Reason: Retain these demonstrated cell-cycle-specific pools without treating plasma-membrane localization as exclusive. |
| GO:0001664 G protein-coupled receptor binding | ISS GO_REF:0000024 | ACCEPT | Summary: Direct serotonin-receptor/Gi1 complexes and coupling assays establish receptor binding, including the PAINT-supported serotonin receptor class. Reason: Preserve exact receptor and construct contexts rather than infer binding to every GPCR. |
| GO:0003924 GTPase activity | EXP PMID:33762731 Structural insights into the lipid and ligand regulation of ... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal |
| GO:0003924 GTPase activity | IDA PMID:8774883 RGS10 is a selective activator of G alpha i GTPase activity. | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal |
| GO:0003924 GTPase activity | IEA GO_REF:0000120 | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal |
| GO:0003924 GTPase activity | ISS GO_REF:0000024 | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal |
| GO:0003924 GTPase activity | TAS PMID:2834384 Presence of three distinct molecular species of Gi protein a... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal |
| GO:0003924 GTPase activity | TAS Reactome:R-HSA-170686 | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: Reactome:R-HSA-170686 G proteins can deactivate themselves via their intrinsic GTPase activity, which hydrolyzes GTP to GDP |
| GO:0003925 G protein activity | IBA GO_REF:0000033 | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Signaling by an activated GPCR promotes GDP release and GTP binding |
| GO:0003925 G protein activity | IDA PMID:15331768 Signaling and ligand binding by recombinant neuromedin U rec... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Signaling by an activated GPCR promotes GDP release and GTP binding |
| GO:0003925 G protein activity | IDA PMID:16204467 EP(4) prostanoid receptor coupling to a pertussis toxin-sens... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Signaling by an activated GPCR promotes GDP release and GTP binding |
| GO:0003925 G protein activity | IDA PMID:33762731 Structural insights into the lipid and ligand regulation of ... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Signaling by an activated GPCR promotes GDP release and GTP binding |
| GO:0003925 G protein activity | IDA PMID:35817871 Structural insight into apelin receptor-G protein stoichiome... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Signaling by an activated GPCR promotes GDP release and GTP binding |
| GO:0003925 G protein activity | IDA PMID:38428423 Structure-based design of non-hypertrophic apelin receptor m... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Signaling by an activated GPCR promotes GDP release and GTP binding |
| GO:0003925 G protein activity | IDA PMID:38503280 A gut-derived hormone regulates cholesterol metabolism. | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Signaling by an activated GPCR promotes GDP release and GTP binding |
| GO:0005515 protein binding | IPI PMID:15537540 Mammalian Pins is a conformational switch that links NuMA to... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:15537540 Mammalian Pins is a conformational switch that links NuMA to... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:18434541 Structural diversity in the RGS domain and its interaction w... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:22952234 Crystal structures of the scaffolding protein LGN reveal the... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | MODIFY | Summary: Binding to GNB1 in a systematic co-IP of GΞ±i1 with all GΞ²Ξ³ combinations. Reason: The partner is a GΞ² or GΞ³ subunit. Binding to the GΞ²Ξ³ dimer is the informative function (heterotrimer assembly), so the row is modified to GO:0031683 G-protein beta/gamma-subunit complex binding, which the gene already carries by IEA. Proposed replacements: G-protein beta/gamma-subunit complex binding Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | MODIFY | Summary: Binding to GNGT1 (GΞ³) in the same systematic GΞ±i1-Ξ²Ξ³ co-IP study. Reason: The partner is a GΞ² or GΞ³ subunit. Binding to the GΞ²Ξ³ dimer is the informative function (heterotrimer assembly), so the row is modified to GO:0031683 G-protein beta/gamma-subunit complex binding, which the gene already carries by IEA. Proposed replacements: G-protein beta/gamma-subunit complex binding Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MODIFY | Summary: Binding to GNB1 in BioPlex AP-MS. Reason: The partner is a GΞ² or GΞ³ subunit. Binding to the GΞ²Ξ³ dimer is the informative function (heterotrimer assembly), so the row is modified to GO:0031683 G-protein beta/gamma-subunit complex binding, which the gene already carries by IEA. Proposed replacements: G-protein beta/gamma-subunit complex binding Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | MODIFY | Summary: Binding to GNB1 in the GPR88-Gi1 cryo-EM complex. Reason: The partner is a GΞ² or GΞ³ subunit. Binding to the GΞ²Ξ³ dimer is the informative function (heterotrimer assembly), so the row is modified to GO:0031683 G-protein beta/gamma-subunit complex binding, which the gene already carries by IEA. Proposed replacements: G-protein beta/gamma-subunit complex binding Supporting Evidence: PMID:35501348 Here we present cryo-EM structures of the human GPR88-Gi1 signaling complex |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | MODIFY | Summary: Binding to GNB1 in multimodal cell map AP-MS. Reason: The partner is a GΞ² or GΞ³ subunit. Binding to the GΞ²Ξ³ dimer is the informative function (heterotrimer assembly), so the row is modified to GO:0031683 G-protein beta/gamma-subunit complex binding, which the gene already carries by IEA. Proposed replacements: G-protein beta/gamma-subunit complex binding Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005525 GTP binding | IDA PMID:34685729 Pediatric Encephalopathy: Clinical, Biochemical and Cellular... | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: PMID:34685729 the three mutant proteins are deficient in binding and hydrolyzing GTP, which is the fundamental function of the healthy G proteins |
| GO:0005525 GTP binding | IEA GO_REF:0000002 | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state |
| GO:0005525 GTP binding | ISS GO_REF:0000024 | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state |
| GO:0005525 GTP binding | ISS GO_REF:0000024 | ACCEPT | Summary: GNAI1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state |
| GO:0005634 nucleus | IEA GO_REF:0000044 | UNDECIDED | Summary: The inherited nuclear assignment remains plausible but was not resolved to a target-specific Gi1 nuclear-localization experiment in the accessible source chain. Reason: Spindle-pole and cortical localization do not independently prove nuclear residence, and no categorical exclusion is asserted. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB-SubCell:SL-0191 UNRESOLVED The inherited nuclear assignment remains plausible but was not resolved to a target-specific Gi1 nuclear-localization experiment in the accessible source chain. Spindle-pole and cortical localization do not independently prove nuclear residence, and no categorical exclusion is asserted. |
| GO:0005634 nucleus | ISS GO_REF:0000024 | UNDECIDED | Summary: The inherited nuclear assignment remains plausible but was not resolved to a target-specific Gi1 nuclear-localization experiment in the accessible source chain. Reason: Spindle-pole and cortical localization do not independently prove nuclear residence, and no categorical exclusion is asserted. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P10824 UNRESOLVED The inherited nuclear assignment remains plausible but was not resolved to a target-specific Gi1 nuclear-localization experiment in the accessible source chain. Spindle-pole and cortical localization do not independently prove nuclear residence, and no categorical exclusion is asserted. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: The G alpha protein is an intracellular peripheral-membrane signaling component with a cytoplasmic pool. Reason: Cytoplasm is compatible with membrane association and, where demonstrated, other intracellular pools; no exclusive localization is inferred. Supporting Evidence: PMID:17635935 A YFP fusion protein of GiΞ±1 localized at the plasma membrane and cytoplasm |
| GO:0005737 cytoplasm | IDA PMID:17635935 Localization of Gi alpha proteins in the centrosomes and at ... | ACCEPT | Summary: The G alpha protein is an intracellular peripheral-membrane signaling component with a cytoplasmic pool. Reason: Cytoplasm is compatible with membrane association and, where demonstrated, other intracellular pools; no exclusive localization is inferred. Supporting Evidence: PMID:17635935 A YFP fusion protein of GiΞ±1 localized at the plasma membrane and cytoplasm |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: The G alpha protein is an intracellular peripheral-membrane signaling component with a cytoplasmic pool. Reason: Cytoplasm is compatible with membrane association and, where demonstrated, other intracellular pools; no exclusive localization is inferred. Supporting Evidence: PMID:17635935 A YFP fusion protein of GiΞ±1 localized at the plasma membrane and cytoplasm |
| GO:0005765 lysosomal membrane | HDA PMID:17897319 Integral and associated lysosomal membrane proteins. | UNDECIDED | Summary: The placental lysosome-proteomics source has not been independently resolved to Gi1-specific enrichment or membrane topology. Reason: Other locations do not negate the curator assertion, but the precise HDA claim remains uncertain. Supporting Evidence: |
| GO:0005813 centrosome | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Imaging and biochemical studies identify Gi1 at spindle poles/centrosomes and the midbody during division. Reason: Retain these demonstrated cell-cycle-specific pools without treating plasma-membrane localization as exclusive. |
| GO:0005813 centrosome | IDA PMID:17635935 Localization of Gi alpha proteins in the centrosomes and at ... | KEEP AS NON CORE | Summary: Imaging and biochemical studies identify Gi1 at spindle poles/centrosomes and the midbody during division. Reason: Retain these demonstrated cell-cycle-specific pools without treating plasma-membrane localization as exclusive. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Imaging and biochemical studies identify Gi1 at spindle poles/centrosomes and the midbody during division. Reason: Retain these demonstrated cell-cycle-specific pools without treating plasma-membrane localization as exclusive. |
| GO:0005813 centrosome | IPI PMID:17635935 Localization of Gi alpha proteins in the centrosomes and at ... | KEEP AS NON CORE | Summary: Imaging and biochemical studies identify Gi1 at spindle poles/centrosomes and the midbody during division. Reason: Retain these demonstrated cell-cycle-specific pools without treating plasma-membrane localization as exclusive. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Gi1 has a soluble cytosolic pool in addition to its peripheral-membrane and mitotic pools. Reason: Cellular localization and cell-cycle experiments independently support this intracellular distribution. Supporting Evidence: |
| GO:0005834 heterotrimeric G-protein complex | IBA GO_REF:0000033 | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005834 heterotrimeric G-protein complex | IDA PMID:33762731 Structural insights into the lipid and ligand regulation of ... | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005834 heterotrimeric G-protein complex | IDA PMID:34239069 Structural basis for recognition of anti-migraine drug lasmi... | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005834 heterotrimeric G-protein complex | IPI PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. Supporting Evidence: PMID:35501348 Here we present cryo-EM structures of the human GPR88-Gi1 signaling complex |
| GO:0005834 heterotrimeric G-protein complex | TAS PMID:3110783 Human cDNA clones for an alpha subunit of Gi signal-transduc... | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0005886 plasma membrane | EXP PMID:17635935 Localization of Gi alpha proteins in the centrosomes and at ... | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:17635935 A YFP fusion protein of GiΞ±1 localized at the plasma membrane and cytoplasm |
| GO:0005886 plasma membrane | EXP PMID:26766442 SAPCD2 Controls Spindle Orientation and Asymmetric Divisions... | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | IDA GO_REF:0000054 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | IDA PMID:23027904 Cortical dynein is critical for proper spindle positioning i... | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:23027904 GΞ±i1-YFP, which is enriched at the plasma membrane |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB:B2RSH2 SUPPORTS TRANSFER The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. UniProtKB-SubCell:SL-0039 SUPPORTS TRANSFER The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | IPI PMID:11976690 Structural determinants for GoLoco-induced inhibition of nuc... | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | IPI PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS PMID:3139448 GTP-binding proteins in human platelet membranes serving as ... | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:3139448 Two GTP-binding proteins serving as the specific substrate of islet-activating protein (IAP), pertussis toxin, were purified from human platelet membranes as heterotrimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-170666 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-170671 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-170674 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-170686 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-380073 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-392187 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-392195 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-392202 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-749454 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-749456 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-751001 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8964242 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8964329 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8982012 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8982019 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8982020 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9021600 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9021601 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor |
| GO:0005938 cell cortex | IDA PMID:22327364 Chromosome- and spindle-pole-derived signals generate an int... | KEEP AS NON CORE | Summary: Gi1 participates directly in the cortical machinery positioning NuMA/LGN and spindle forces. Reason: The cortex location is supported independently of generic membrane annotation. |
| GO:0005938 cell cortex | IDA PMID:23870127 Cortical dynein and asymmetric membrane elongation coordinat... | KEEP AS NON CORE | Summary: Gi1 participates directly in the cortical machinery positioning NuMA/LGN and spindle forces. Reason: The cortex location is supported independently of generic membrane annotation. |
| GO:0005938 cell cortex | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Gi1 participates directly in the cortical machinery positioning NuMA/LGN and spindle forces. Reason: The cortex location is supported independently of generic membrane annotation. |
| GO:0005938 cell cortex | IPI PMID:15537540 Mammalian Pins is a conformational switch that links NuMA to... | KEEP AS NON CORE | Summary: Gi1 participates directly in the cortical machinery positioning NuMA/LGN and spindle forces. Reason: The cortex location is supported independently of generic membrane annotation. |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: The protein directly transduces signals through heterotrimeric G protein-coupled receptor signaling. Reason: Refine generic signal transduction to the established receptor pathway without excluding additional receptor-independent functions. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: InterPro:IPR011025 SUPPORTS TRANSFER The protein directly transduces signals through heterotrimeric G protein-coupled receptor signaling. Refine generic signal transduction to the established receptor pathway without excluding additional receptor-independent functions. Proposed replacements: G protein-coupled receptor signaling pathway Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades |
| GO:0007186 G protein-coupled receptor signaling pathway | IDA PMID:34239069 Structural basis for recognition of anti-migraine drug lasmi... | ACCEPT | Summary: Receptor-dependent nucleotide exchange and effector coupling establish direct participation in GPCR signaling. Reason: Individual receptor preferences and physiological contexts must be established separately rather than inferred from the whole G protein family. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades |
| GO:0007186 G protein-coupled receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: Receptor-dependent nucleotide exchange and effector coupling establish direct participation in GPCR signaling. Reason: Individual receptor preferences and physiological contexts must be established separately rather than inferred from the whole G protein family. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades |
| GO:0007186 G protein-coupled receptor signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: Receptor-dependent nucleotide exchange and effector coupling establish direct participation in GPCR signaling. Reason: Individual receptor preferences and physiological contexts must be established separately rather than inferred from the whole G protein family. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades |
| GO:0007186 G protein-coupled receptor signaling pathway | NAS PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | ACCEPT | Summary: Receptor-dependent nucleotide exchange and effector coupling establish direct participation in GPCR signaling. Reason: Individual receptor preferences and physiological contexts must be established separately rather than inferred from the whole G protein family. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades |
| GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Gi1 modulates cyclase output in an isoform-dependent manner: purified Gi1 inhibits several cyclases, while high concentrations can stimulate certain isoforms in reconstituted assays. Reason: Retain the unsigned process because this documented biochemical breadth is not adequately represented by an unconditional inhibitory-only statement. Supporting Evidence: PMID:8119955 Type II adenylyl cyclase appears to be immune to inhibition by these proteins PMID:8119955 High concentrations of Gi alpha can interact with site 1 on types I and II adenylyl cyclase and activate the enzymes. |
| GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: Gi1 modulates cyclase output in an isoform-dependent manner: purified Gi1 inhibits several cyclases, while high concentrations can stimulate certain isoforms in reconstituted assays. Reason: Retain the unsigned process because this documented biochemical breadth is not adequately represented by an unconditional inhibitory-only statement. Supporting Evidence: PMID:8119955 Type II adenylyl cyclase appears to be immune to inhibition by these proteins PMID:8119955 High concentrations of Gi alpha can interact with site 1 on types I and II adenylyl cyclase and activate the enzymes. |
| GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: Gi1 modulates cyclase output in an isoform-dependent manner: purified Gi1 inhibits several cyclases, while high concentrations can stimulate certain isoforms in reconstituted assays. Reason: Retain the unsigned process because this documented biochemical breadth is not adequately represented by an unconditional inhibitory-only statement. Supporting Evidence: PMID:8119955 Type II adenylyl cyclase appears to be immune to inhibition by these proteins PMID:8119955 High concentrations of Gi alpha can interact with site 1 on types I and II adenylyl cyclase and activate the enzymes. |
| GO:0007189 adenylate cyclase-activating G protein-coupled receptor signaling pathway | ISS GO_REF:0000024 | REMOVE | Summary: The ISS donor P30804 resolves in the source chain to an adenylyl-cyclase family protein, not a Gi1 ortholog, and the term has the opposite sign to Gi1's in vivo role. Reason: Gi1 mediates the adenylate cyclase-inhibiting arm of GPCR signaling (GO:0007193, retained here). Stimulation of some purified cyclases by high concentrations of Gi alpha (PMID:8119955) is an in vitro observation; GO annotates the gene's in vivo role, and no native Gi1-mediated cyclase-activating pathway has been shown. The transfer itself is unsound, because the donor is an adenylyl cyclase rather than a Galpha ortholog. An electronic inference that is both wrongly sourced and contradicted on biological grounds is removed. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG REGULATORY SIGN INVERSION Sources checked: UniProtKB:P30804 SUPPORTS SOURCE BUT NOT TARGET The ISS donor P30804 resolves in the source chain to an adenylyl-cyclase family protein, not a Gi1 ortholog. The transferred term is the activating arm of adenylate cyclase signaling, the opposite of Gi1's in vivo inhibitory role; high-concentration stimulation of purified cyclases in vitro (PMID:8119955) does not establish an in vivo pathway. Supporting Evidence: PMID:8119955 High concentrations of Gi alpha can interact with site 1 on types I and II adenylyl cyclase and activate the enzymes. |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:15331768 Signaling and ligand binding by recombinant neuromedin U rec... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:16204467 EP(4) prostanoid receptor coupling to a pertussis toxin-sens... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:19047060 Lactate inhibits lipolysis in fat cells through activation o... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:23841650 Dynamics of GΞ±i1 interaction with type 5 adenylate cyclase r... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:23841650 Gi1-protein-mediated attenuation of AC5-dependent increases in cAMP occurred at comparable low concentrations of agonist |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:34239069 Structural basis for recognition of anti-migraine drug lasmi... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:35817871 Structural insight into apelin receptor-G protein stoichiome... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:37221270 Structural genomics of the human dopamine receptor system. | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:38428423 Structure-based design of non-hypertrophic apelin receptor m... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:38503280 A gut-derived hormone regulates cholesterol metabolism. | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | TAS Reactome:R-HSA-170670 | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: Reactome:R-HSA-170670 Guanine nucleotide-binding protein G(i) alpha (Gi-alpha) inhibits adenylate cyclase, thus inhibiting the production of cAMP from ATP |
| GO:0007195 adenylate cyclase-inhibiting dopamine receptor signaling pathway | IDA PMID:33548201 Structures of the human dopamine D3 receptor-G(i) complexes. | KEEP AS NON CORE | Summary: D2-family receptor structural/coupling studies demonstrate Gi1 receptor binding and inhibitory cAMP signaling in the tested complexes. Reason: Retain this specific neurotransmitter implementation with the experimental construct scope. |
| GO:0007195 adenylate cyclase-inhibiting dopamine receptor signaling pathway | IDA PMID:33571431 Structural insights into the human D1 and D2 dopamine recept... | KEEP AS NON CORE | Summary: D2-family receptor structural/coupling studies demonstrate Gi1 receptor binding and inhibitory cAMP signaling in the tested complexes. Reason: Retain this specific neurotransmitter implementation with the experimental construct scope. |
| GO:0007195 adenylate cyclase-inhibiting dopamine receptor signaling pathway | IDA PMID:37221270 Structural genomics of the human dopamine receptor system. | KEEP AS NON CORE | Summary: D2-family receptor structural/coupling studies demonstrate Gi1 receptor binding and inhibitory cAMP signaling in the tested complexes. Reason: Retain this specific neurotransmitter implementation with the experimental construct scope. |
| GO:0007198 adenylate cyclase-inhibiting serotonin receptor signaling pathway | IDA PMID:33762731 Structural insights into the lipid and ligand regulation of ... | KEEP AS NON CORE | Summary: Serotonin-receptor/Gi1 structures and coupling assays establish a specific cyclase-inhibitory signaling implementation. Reason: Receptor subtype specificity is retained; this does not apply to every serotonin receptor. |
| GO:0007198 adenylate cyclase-inhibiting serotonin receptor signaling pathway | IDA PMID:34239069 Structural basis for recognition of anti-migraine drug lasmi... | KEEP AS NON CORE | Summary: Serotonin-receptor/Gi1 structures and coupling assays establish a specific cyclase-inhibitory signaling implementation. Reason: Receptor subtype specificity is retained; this does not apply to every serotonin receptor. |
| GO:0007218 neuropeptide signaling pathway | IDA PMID:15331768 Signaling and ligand binding by recombinant neuromedin U rec... | KEEP AS NON CORE | Summary: Neuromedin receptor assays establish Gi1-mediated neuropeptide signaling as one receptor context. Reason: The G protein transduces the response rather than binding the extracellular peptide as its primary receptor. Supporting Evidence: |
| GO:0007218 neuropeptide signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Neuromedin receptor assays establish Gi1-mediated neuropeptide signaling as one receptor context. Reason: The G protein transduces the response rather than binding the extracellular peptide as its primary receptor. Supporting Evidence: |
| GO:0008277 regulation of G protein-coupled receptor signaling pathway | NAS PMID:11976690 Structural determinants for GoLoco-induced inhibition of nuc... | KEEP AS NON CORE | Summary: Gi1 interactions with regulatory proteins can alter receptor signaling alongside its direct transducer function. Reason: Retain the demonstrated regulatory process without calling Gi1 an RGS-like GAP for another alpha subunit. Supporting Evidence: |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:12135370 Activation-induced subcellular redistribution of G alpha(s) ... | ACCEPT | Summary: The intracellular G alphaβbeta/gamma complex contacts the cytoplasmic receptor surface and intracellular effectors. Reason: Receptor-complex structures, membrane targeting and signaling experiments support the cytoplasmic plasma-membrane face. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor file:human/GNAI1/GNAI1-uniprot.txt Peripheral membrane protein {ECO:0000305|PubMed:12135370}; Cytoplasmic side |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:17635935 Localization of Gi alpha proteins in the centrosomes and at ... | ACCEPT | Summary: The intracellular G alphaβbeta/gamma complex contacts the cytoplasmic receptor surface and intracellular effectors. Reason: Receptor-complex structures, membrane targeting and signaling experiments support the cytoplasmic plasma-membrane face. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor file:human/GNAI1/GNAI1-uniprot.txt Peripheral membrane protein {ECO:0000305|PubMed:12135370}; Cytoplasmic side |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:26766442 SAPCD2 Controls Spindle Orientation and Asymmetric Divisions... | ACCEPT | Summary: The intracellular G alphaβbeta/gamma complex contacts the cytoplasmic receptor surface and intracellular effectors. Reason: Receptor-complex structures, membrane targeting and signaling experiments support the cytoplasmic plasma-membrane face. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor file:human/GNAI1/GNAI1-uniprot.txt Peripheral membrane protein {ECO:0000305|PubMed:12135370}; Cytoplasmic side |
| GO:0009898 cytoplasmic side of plasma membrane | IEA GO_REF:0000117 | ACCEPT | Summary: The intracellular G alphaβbeta/gamma complex contacts the cytoplasmic receptor surface and intracellular effectors. Reason: Receptor-complex structures, membrane targeting and signaling experiments support the cytoplasmic plasma-membrane face. Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt Associated to the plasma membrane via lipid-anchor file:human/GNAI1/GNAI1-uniprot.txt Peripheral membrane protein {ECO:0000305|PubMed:12135370}; Cytoplasmic side |
| GO:0010855 adenylate cyclase inhibitor activity | IDA PMID:8119955 Distinct patterns of bidirectional regulation of mammalian a... | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0010855 adenylate cyclase inhibitor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Purified reconstitution directly establishes Gi1 inhibition of selected cyclases, and receptor-dependent assays show Gi1-mediated suppression of cAMP. Reason: The inhibitory MF is isoform/context dependent, not inhibition of every adenylyl cyclase under every condition. Supporting Evidence: PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:0016020 membrane | ISS GO_REF:0000024 | MODIFY | Summary: The conserved membrane-associated pool is specifically on the cytoplasmic plasma-membrane surface, independently annotated here. Reason: Refine the generic membrane assertion without excluding centrosomal, cortical or soluble pools. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB:P10824 SUPPORTS TRANSFER The conserved membrane-associated pool is specifically on the cytoplasmic plasma-membrane surface, independently annotated here. Refine the generic membrane assertion without excluding centrosomal, cortical or soluble pools. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: |
| GO:0019001 guanyl nucleotide binding | IEA GO_REF:0000002 | MODIFY | Summary: The conserved guanine-nucleotide pocket binds GTP during activation and GDP in the inactive state. Reason: Refine the generic nucleotide-binding term to these two chemically defined ligands, preserving both halves of the switch. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: InterPro:IPR001019 SUPPORTS TRANSFER The conserved guanine-nucleotide pocket binds GTP during activation and GDP in the inactive state. Refine the generic nucleotide-binding term to these two chemically defined ligands, preserving both halves of the switch. Proposed replacements: GTP binding GDP binding Supporting Evidence: file:human/GNAI1/GNAI1-uniprot.txt The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state |
| GO:0019003 GDP binding | ISS GO_REF:0000024 | ACCEPT | Summary: GDP is the physiological ligand of the inactive G alpha nucleotide pocket. Reason: Structural and nucleotide-exchange experiments support GDP binding as an integral part of the switch. |
| GO:0030496 midbody | IDA PMID:17635935 Localization of Gi alpha proteins in the centrosomes and at ... | KEEP AS NON CORE | Summary: Imaging and biochemical studies identify Gi1 at spindle poles/centrosomes and the midbody during division. Reason: Retain these demonstrated cell-cycle-specific pools without treating plasma-membrane localization as exclusive. |
| GO:0030496 midbody | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Imaging and biochemical studies identify Gi1 at spindle poles/centrosomes and the midbody during division. Reason: Retain these demonstrated cell-cycle-specific pools without treating plasma-membrane localization as exclusive. |
| GO:0031683 G-protein beta/gamma-subunit complex binding | IEA GO_REF:0000002 | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. Supporting Evidence: PMID:25733868 capability of 120 different G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex |
| GO:0031749 D2 dopamine receptor binding | IPI PMID:33571431 Structural insights into the human D1 and D2 dopamine recept... | KEEP AS NON CORE | Summary: D2-family receptor structural/coupling studies demonstrate Gi1 receptor binding and inhibitory cAMP signaling in the tested complexes. Reason: Retain this specific neurotransmitter implementation with the experimental construct scope. |
| GO:0031821 G protein-coupled serotonin receptor binding | IBA GO_REF:0000033 | ACCEPT | Summary: Direct serotonin-receptor/Gi1 complexes and coupling assays establish receptor binding, including the PAINT-supported serotonin receptor class. Reason: Preserve exact receptor and construct contexts rather than infer binding to every GPCR. |
| GO:0034695 response to prostaglandin E | IDA PMID:16204467 EP(4) prostanoid receptor coupling to a pertussis toxin-sens... | KEEP AS NON CORE | Summary: The prostaglandin receptor-coupling study directly tests Gi1 signaling, supporting a contextual response to prostaglandin E rather than prostaglandin metabolism. Reason: The prostaglandin receptor-coupling study directly tests Gi1 signaling, supporting a contextual response to prostaglandin E rather than prostaglandin metabolism. Supporting Evidence: |
| GO:0038112 interleukin-8-mediated signaling pathway | IDA PMID:15331768 Signaling and ligand binding by recombinant neuromedin U rec... | UNDECIDED | Summary: The accessible original PMID:15331768 source foregrounds neuromedin U receptor coupling. Reason: That alone cannot establish or refute additional IL-8 receptor experiments in uninspected full text. No independently verified Gi1-specific IL-8 signaling result was recovered, so retain uncertainty rather than assert a wrong-gene or wrong-receptor error. Supporting Evidence: |
| GO:0043303 mast cell degranulation | IDA PMID:34789875 Structure, function and pharmacology of human itch receptor ... | KEEP AS NON CORE | Summary: The receptorβGi signaling study supports a mast-cell degranulation implementation. Reason: Retain the specific downstream response while distinguishing receptor-transducer participation from direct vesicle-fusion activity. Supporting Evidence: |
| GO:0043434 response to peptide hormone | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Gi1 responds to peptide-receptor activation in direct coupling experiments, supporting the conserved peptide-hormone response annotation independently of the unresolved details of the transferred donor. Reason: Gi1 responds to peptide-receptor activation in direct coupling experiments, supporting the conserved peptide-hormone response annotation independently of the unresolved details of the transferred donor. |
| GO:0045542 positive regulation of cholesterol biosynthetic process | IDA PMID:38503280 A gut-derived hormone regulates cholesterol metabolism. | UNDECIDED | Summary: The cholesinβGPR146 paper describes suppression of cholesterol synthesis through Gi signaling in its accessible abstract, whereas this row asserts a positive sign. Reason: The complete target-specific experiment was not recovered here; whether another context supports a positive role remains unresolved. Do not silently invert the experimental annotation from its abstract. Supporting Evidence: |
| GO:0046888 negative regulation of hormone secretion | IDA PMID:38632411 Promiscuous G-protein activation by the calcium-sensing rece... | KEEP AS NON CORE | Summary: CaSRβGi coupling supports signaling that suppresses endocrine secretion in the receptor physiological context. Reason: The structure establishes receptorβtransducer compatibility; it is not itself an assay of hormone output or proof that Gi1 is uniquely required. Supporting Evidence: |
| GO:0051301 cell division | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Gi1 localization and perturbation during cytokinesis support direct regulatory participation in division. Reason: This secondary role is supported by cell-cycle machinery experiments, not inferred solely from cancer proliferation. Supporting Evidence: |
| GO:0051301 cell division | IMP PMID:17635935 Localization of Gi alpha proteins in the centrosomes and at ... | KEEP AS NON CORE | Summary: Gi1 localization and perturbation during cytokinesis support direct regulatory participation in division. Reason: This secondary role is supported by cell-cycle machinery experiments, not inferred solely from cancer proliferation. Supporting Evidence: |
| GO:0060236 regulation of mitotic spindle organization | IMP PMID:23027904 Cortical dynein is critical for proper spindle positioning i... | KEEP AS NON CORE | Summary: Gi1 participates in the cortical LGNβNuMA/dynein machinery that positions the spindle; gain/loss and localization experiments support spindle organization and cortical recruitment. Reason: These are direct secondary cellular functions rather than generic proliferation associations. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | UNDECIDED | Summary: The urinary exosome-proteomics citation is retained, but the Gi1-specific peptide/enrichment result could not be independently inspected. Reason: Membrane association alone is insufficient evidence for released-vesicle localization and does not disprove it. Supporting Evidence: |
| GO:0070098 chemokine-mediated signaling pathway | IDA PMID:35570218 Molecular insights into ligand recognition and activation of... | KEEP AS NON CORE | Summary: Chemokine-receptor/Gi1 structures and coupling establish a chemokine-transduction implementation. Reason: This is distinct from asserting a particular native tissue response solely from structural occupancy. Supporting Evidence: |
| GO:0072678 T cell migration | IDA PMID:20829352 Differentiation of human T cells alters their repertoire of ... | KEEP AS NON CORE | Summary: Native human CD4 T-cell experiments identify a Gi1 contribution to naive-cell migration, distinct from the Go-dominant memory-cell context. Reason: Retain that cell-state-specific migration function. Supporting Evidence: |
| GO:1901082 positive regulation of relaxation of smooth muscle | ISS PMID:9843699 G protein-dependent activation of smooth muscle eNOS via nat... | KEEP AS NON CORE | Summary: The comparative gastric smooth-muscle study implicates Gi1/Gi2-dependent signaling in nitric-oxide-linked relaxation. Reason: Retain this contextual conserved regulatory role, not direct contractile structural activity. Supporting Evidence: |
| GO:1903998 regulation of eating behavior | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The traced mouse source connects Gi1-dependent signaling with feeding regulation. Reason: Retain the comparative behavioral role with native-mouse rather than direct human behavioral evidence. Supporting Evidence: |
| GO:1904322 cellular response to forskolin | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The source tests the Gi1 T329A GDP-release mutant and reports decreased forskolin-stimulated cAMP accumulation. Reason: Retain the contextual response inference with the mutant limitation, corroborated by wild-type Gi1 cyclase inhibition; forskolin is not asserted to bind Gi1. Supporting Evidence: PMID:19703466 when expressed in culture, it causes a significant decrease in forskolin-stimulated cAMP accumulation PMID:8119955 Types V and VI adenylyl cyclase are most sensitive to inhibition by Gi alpha 1, Gi alpha 2, and Gi alpha 3 |
| GO:1904778 positive regulation of protein localization to cell cortex | IMP PMID:22327364 Chromosome- and spindle-pole-derived signals generate an int... | KEEP AS NON CORE | Summary: Gi1 participates in the cortical LGNβNuMA/dynein machinery that positions the spindle; gain/loss and localization experiments support spindle organization and cortical recruitment. Reason: These are direct secondary cellular functions rather than generic proliferation associations. |
| GO:1904778 positive regulation of protein localization to cell cortex | IMP PMID:23027904 Cortical dynein is critical for proper spindle positioning i... | KEEP AS NON CORE | Summary: Gi1 participates in the cortical LGNβNuMA/dynein machinery that positions the spindle; gain/loss and localization experiments support spindle organization and cortical recruitment. Reason: These are direct secondary cellular functions rather than generic proliferation associations. |
| GO:1904778 positive regulation of protein localization to cell cortex | IMP PMID:26766442 SAPCD2 Controls Spindle Orientation and Asymmetric Divisions... | KEEP AS NON CORE | Summary: Gi1 participates in the cortical LGNβNuMA/dynein machinery that positions the spindle; gain/loss and localization experiments support spindle organization and cortical recruitment. Reason: These are direct secondary cellular functions rather than generic proliferation associations. |
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