GNAQ encodes G alpha q, a membrane-associated guanine-nucleotide switch in heterotrimeric G proteins. Activated receptors promote GDP/GTP exchange, allowing Gq to activate phospholipase C beta and generate inositol trisphosphate and diacylglycerol signals. Intrinsic GTP hydrolysis, accelerated by regulatory proteins and PLC beta, terminates signaling. Gq participates in diverse endocrine, vascular, platelet and neuronal responses; nuclear-membrane and Golgi pools coexist with plasma-membrane signaling in particular cells.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001664 G protein-coupled receptor binding | IEA GO_REF:0000002 | ACCEPT | Summary: Direct receptor-complex and coupling experiments establish recognition of intracellular GPCR surfaces by Gq, including serotonin and other receptor families. Reason: Direct GPCR-complex and coupling experiments establish Gq recognition of intracellular receptor surfaces. PMID:38632411 supplies receptor coupling evidence; PMID:37991948 supplies downstream PLCbeta3 effector evidence, not a receptor-bound structure. |
| GO:0001750 photoreceptor outer segment | ISS GO_REF:0000024 | UNDECIDED | Summary: Mouse retinal evidence does not resolve the precise transferred human outer-segment location. Reason: The precise human GNAQ outer-segment localization remains unresolved. PMID:12196552 reports chicken Gq/11 immunolocalization with G11-associated opsin signaling. Full PMID:24958088 adds adult mouse retinal localization, including Gnaq-selective cone-photoreceptor staining and cross-reactive Gnaq/11 staining, but the reported cone/photoreceptor-layer signal does not independently resolve this exact human subcompartment for each isoform. Its melanopsin experiments concern inner-retinal ganglion cells, not rod/cone outer segments. PMID:24870805 examines neonatal ipRGC expression and function, which likewise does not settle outer-segment residence. These limitations do not demonstrate absence. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q5F3B5 UNRESOLVED The precise human GNAQ outer-segment localization remains unresolved. PMID:12196552 reports chicken Gq/11 immunolocalization with G11-associated opsin signaling. Full PMID:24958088 adds adult mouse retinal localization, including Gnaq-selective cone-photoreceptor staining and cross-reactive Gnaq/11 staining, but the reported cone/photoreceptor-layer signal does not independently resolve this exact human subcompartment for each isoform. Its melanopsin experiments concern inner-retinal ganglion cells, not rod/cone outer segments. PMID:24870805 examines neonatal ipRGC expression and function, which likewise does not settle outer-segment residence. These limitations do not demonstrate absence. Supporting Evidence: PMID:24958088 These data confirm that Gnaq and Gna11 convey the melanopsin signal in Neuro-2A cells. PMID:24870805 Another possibility is that there is compensatory upregulation from other remaining Gq/11 family members in the tested mutant lines. |
| GO:0001750 photoreceptor outer segment | ISS GO_REF:0000024 | UNDECIDED | Summary: Mouse retinal evidence does not resolve the precise transferred human outer-segment location. Reason: The precise human GNAQ outer-segment localization remains unresolved. PMID:12196552 reports chicken Gq/11 immunolocalization with G11-associated opsin signaling. Full PMID:24958088 adds adult mouse retinal localization, including Gnaq-selective cone-photoreceptor staining and cross-reactive Gnaq/11 staining, but the reported cone/photoreceptor-layer signal does not independently resolve this exact human subcompartment for each isoform. Its melanopsin experiments concern inner-retinal ganglion cells, not rod/cone outer segments. PMID:24870805 examines neonatal ipRGC expression and function, which likewise does not settle outer-segment residence. These limitations do not demonstrate absence. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q71RI7 UNRESOLVED The precise human GNAQ outer-segment localization remains unresolved. PMID:12196552 reports chicken Gq/11 immunolocalization with G11-associated opsin signaling. Full PMID:24958088 adds adult mouse retinal localization, including Gnaq-selective cone-photoreceptor staining and cross-reactive Gnaq/11 staining, but the reported cone/photoreceptor-layer signal does not independently resolve this exact human subcompartment for each isoform. Its melanopsin experiments concern inner-retinal ganglion cells, not rod/cone outer segments. PMID:24870805 examines neonatal ipRGC expression and function, which likewise does not settle outer-segment residence. These limitations do not demonstrate absence. Supporting Evidence: PMID:24958088 These data confirm that Gnaq and Gna11 convey the melanopsin signal in Neuro-2A cells. PMID:24870805 Another possibility is that there is compensatory upregulation from other remaining Gq/11 family members in the tested mutant lines. |
| GO:0003924 GTPase activity | EXP PMID:37991948 The mechanism of GΞ±(q) regulation of PLCΞ²3-catalyzed PIP2 hy... | ACCEPT | Summary: GNAQ 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. |
| GO:0003924 GTPase activity | IEA GO_REF:0000002 | ACCEPT | Summary: GNAQ 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. |
| GO:0003924 GTPase activity | TAS PMID:9238049 Platelet signal transduction defect with Galpha subunit dysf... | ACCEPT | Summary: GNAQ 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. |
| GO:0003924 GTPase activity | TAS Reactome:R-HSA-167415 | ACCEPT | Summary: GNAQ 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. |
| GO:0003925 G protein activity | IBA GO_REF:0000033 | ACCEPT | Summary: GNAQ 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. |
| GO:0003925 G protein activity | IDA PMID:11024015 Identification and characterization of two G protein-coupled... | ACCEPT | Summary: GNAQ 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. |
| GO:0003925 G protein activity | IDA PMID:15331768 Signaling and ligand binding by recombinant neuromedin U rec... | ACCEPT | Summary: GNAQ 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. |
| GO:0003925 G protein activity | IDA PMID:37991948 The mechanism of GΞ±(q) regulation of PLCΞ²3-catalyzed PIP2 hy... | ACCEPT | Summary: GNAQ 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. |
| GO:0003925 G protein activity | IEA GO_REF:0000117 | ACCEPT | Summary: GNAQ 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. |
| GO:0005096 GTPase activator activity | IDA PMID:15611106 beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA an... | UNDECIDED | Summary: The original PMID:15611106 abstract reports beta-arrestin1/Gq-dependent RhoA activation and stress-fiber formation, not acceleration of GTP hydrolysis by Gq on another GTPase. Reason: Full text could not be recovered despite targeted attempts. Gq is itself a GTPase and PLCbeta can act as its GAP; neither fact resolves whether this experimental row asserts an additional GAP function. Retain uncertainty rather than invert the enzyme/regulator roles from an abstract. |
| GO:0005515 protein binding | IPI PMID:18672896 Regulation of G protein-coupled receptor activities by the p... | 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:18772143 Disease-causing mutation in GPR54 reveals the importance of ... | 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:22056876 A retinoic acid receptor RARΞ± pool present in membrane lipid... | 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:22750945 Direct inhibition of the cold-activated TRPM8 ion channel by... | 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:23353685 Ξ²-Arrestin-1 directly interacts with GΞ±s and regulates its f... | 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:23994616 A novel GΞ±s-binding protein, Gas-2 like 2, facilitates the s... | 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:27265506 ARF6 Is an Actionable Node that Orchestrates Oncogenic GNAQ ... | 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:34110646 A novel role of ADGRF1 (GPR110) in promoting cellular quiesc... | 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 | IEA GO_REF:0000117 | ACCEPT | Summary: GNAQ 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. |
| GO:0005525 GTP binding | TAS Reactome:R-HSA-167429 | ACCEPT | Summary: GNAQ 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. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The traced mouse study directly colocalizes Gq with alpha1 receptors and PLCbeta1 at the nuclear membrane and validates nuclear fractions. Reason: Retain the conserved nuclear/nuclear-membrane pool with cardiac-cell and species limits; plasma-membrane localization does not exclude it. Supporting Evidence: |
| GO:0005634 nucleus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The traced mouse study directly colocalizes Gq with alpha1 receptors and PLCbeta1 at the nuclear membrane and validates nuclear fractions. Reason: Retain the conserved nuclear/nuclear-membrane pool with cardiac-cell and species limits; plasma-membrane localization does not exclude it. Supporting Evidence: |
| 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. |
| GO:0005737 cytoplasm | TAS PMID:9175863 Interaction of the G-protein G11alpha with receptors and pho... | 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. |
| GO:0005765 lysosomal membrane | HDA PMID:17897319 Integral and associated lysosomal membrane proteins. | UNDECIDED | Summary: The placental lysosome-proteomics source is accessible only without verified target-level fraction/enrichment evidence for GNAQ in this audit. Reason: Its known plasma-membrane and Golgi pools do not disprove lysosomal association, but they cannot establish this precise membrane assignment. The specific HDA result remains unresolved. Supporting Evidence: |
| GO:0005794 Golgi apparatus | EXP PMID:19001095 Identification of G protein alpha subunit-palmitoylating enz... | KEEP AS NON CORE | Summary: PMID:19001095 directly examines Gq trafficking between Golgi and plasma membrane. Reason: Retain the root Golgi assertion independently of the main plasma-membrane activity; no finer Golgi topology is manufactured. Supporting Evidence: |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: PMID:19001095 directly examines Gq trafficking between Golgi and plasma membrane. Reason: Retain the root Golgi assertion independently of the main plasma-membrane activity; no finer Golgi topology is manufactured. 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. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | 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 |
| GO:0005886 plasma membrane | IDA PMID:19001095 Identification of G protein alpha subunit-palmitoylating enz... | 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 |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | 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-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 |
| GO:0005886 plasma membrane | TAS PMID:10633085 Interaction of folate receptor with signaling molecules lyn ... | 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 |
| GO:0005886 plasma membrane | TAS PMID:9175863 Interaction of the G-protein G11alpha with receptors and pho... | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-111879 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-112037 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-112271 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-114558 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-114688 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-167408 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-167415 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-167419 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-167429 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-167433 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-379048 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-396996 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-397835 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-400586 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-416358 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-416516 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-418576 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-418582 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-428749 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-428750 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-428752 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-428941 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-749448 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-749452 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-750993 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8850560 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8964280 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8964284 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8964340 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8982017 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8982025 | 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 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8982026 | 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 |
| 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 |
| GO:0007186 G protein-coupled receptor signaling pathway | IDA PMID:34556863 Structures of the human cholecystokinin receptors bound to a... | 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. |
| GO:0007186 G protein-coupled receptor signaling pathway | IEA GO_REF:0000002 | 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. |
| GO:0007189 adenylate cyclase-activating G protein-coupled receptor signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The PAINT assertion is placed at PTN008496048 with mouse Gnaq descendant evidence, not transferred from a generic Gs label. Reason: The original mouse transgenic source primarily measures reduced cyclase expression, but independent PMID:8390980 shows Gq-coupled receptor enhancement of AC-II through PKC; retain this contextual pathway capability while distinguishing it from direct Gs-like binding to a cyclase catalytic domain. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IDA PMID:15331768 Signaling and ligand binding by recombinant neuromedin U rec... | ACCEPT | Summary: Gq directly activates PLCbeta in receptor-dependent cellular assays and purified effector biochemistry. Reason: PLCbeta produces the second messengers; Gq regulates the enzyme rather than catalyzing phospholipid hydrolysis itself. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IDA PMID:20966218 Kinetic scaffolding mediated by a phospholipase C-beta and G... | ACCEPT | Summary: Gq directly activates PLCbeta in receptor-dependent cellular assays and purified effector biochemistry. Reason: PLCbeta produces the second messengers; Gq regulates the enzyme rather than catalyzing phospholipid hydrolysis itself. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IDA PMID:27104960 GPR142 Agonists Stimulate Glucose-Dependent Insulin Secretio... | ACCEPT | Summary: Gq directly activates PLCbeta in receptor-dependent cellular assays and purified effector biochemistry. Reason: PLCbeta produces the second messengers; Gq regulates the enzyme rather than catalyzing phospholipid hydrolysis itself. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IDA PMID:37991948 The mechanism of GΞ±(q) regulation of PLCΞ²3-catalyzed PIP2 hy... | ACCEPT | Summary: Gq directly activates PLCbeta in receptor-dependent cellular assays and purified effector biochemistry. Reason: PLCbeta produces the second messengers; Gq regulates the enzyme rather than catalyzing phospholipid hydrolysis itself. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IDA PMID:8253813 Cloning and expression of a cDNA for the human prostaglandin... | ACCEPT | Summary: Gq directly activates PLCbeta in receptor-dependent cellular assays and purified effector biochemistry. Reason: PLCbeta produces the second messengers; Gq regulates the enzyme rather than catalyzing phospholipid hydrolysis itself. |
| GO:0007200 phospholipase C-activating G protein-coupled receptor signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: Gq directly activates PLCbeta in receptor-dependent cellular assays and purified effector biochemistry. Reason: PLCbeta produces the second messengers; Gq regulates the enzyme rather than catalyzing phospholipid hydrolysis itself. |
| GO:0007208 phospholipase C-activating serotonin receptor signaling pathway | IDA PMID:37991948 The mechanism of GΞ±(q) regulation of PLCΞ²3-catalyzed PIP2 hy... | KEEP AS NON CORE | Summary: SerotoninβGq pathway supported independently of the original PLC-effector paper. Reason: Independent PMID:32946782 establishes 5-HT2A coupling to engineered Gq in a structural/cellular system, supporting this serotonin-receptor implementation. The original PMID:37991948 directly establishes GqβPLCbeta3 activation but does not itself assay serotonin receptor coupling; the pathway claim is retained from the independent evidence, not an invented serotonin experiment in that paper. |
| GO:0007209 phospholipase C-activating tachykinin receptor signaling pathway | IDA PMID:1718267 Molecular cloning, structural characterization and functiona... | KEEP AS NON CORE | Summary: Tachykinin-receptor coupling and structural work support the GqβPLC pathway in the tested receptor contexts. Reason: Preserve the specific signaling implementation without making it universal across tachykinin receptors. |
| GO:0007209 phospholipase C-activating tachykinin receptor signaling pathway | IDA PMID:37391393 Structural insights into neurokinin 3 receptor activation by... | KEEP AS NON CORE | Summary: Tachykinin-receptor coupling and structural work support the GqβPLC pathway in the tested receptor contexts. Reason: Preserve the specific signaling implementation without making it universal across tachykinin receptors. |
| GO:0007213 G protein-coupled acetylcholine receptor signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Muscarinic M1/M3 coupling assays establish Gq participation in cholinergic signaling; the mouse beta-cell Gq/G11 deletion corroborates native muscarinic signaling but does not assign every response exclusively to Gq. Reason: Muscarinic M1/M3 coupling assays establish Gq participation in cholinergic signaling; the mouse beta-cell Gq/G11 deletion corroborates native muscarinic signaling but does not assign every response exclusively to Gq. |
| GO:0007213 G protein-coupled acetylcholine receptor signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Muscarinic M1/M3 coupling assays establish Gq participation in cholinergic signaling; the mouse beta-cell Gq/G11 deletion corroborates native muscarinic signaling but does not assign every response exclusively to Gq. Reason: Muscarinic M1/M3 coupling assays establish Gq participation in cholinergic signaling; the mouse beta-cell Gq/G11 deletion corroborates native muscarinic signaling but does not assign every response exclusively to Gq. |
| GO:0007215 glutamate receptor signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The mGlu1βGqβPLC pathway and postsynaptic experiments at parallel-fiber/Purkinje-cell synapses directly support glutamate signaling and the postsynaptic intracellular pool. Reason: These are specific neuronal implementations of the general transducer function. Supporting Evidence: |
| GO:0007218 neuropeptide signaling pathway | IDA PMID:11024015 Identification and characterization of two G protein-coupled... | KEEP AS NON CORE | Summary: Neuromedin receptor activation of Gq establishes neuropeptide signaling participation. Reason: The peptide binds its receptor; Gq transduces the intracellular signal rather than binding the extracellular peptide as a hormone receptor. Supporting Evidence: |
| GO:0007596 blood coagulation | TAS PMID:9238049 Platelet signal transduction defect with Galpha subunit dysf... | KEEP AS NON CORE | Summary: Native Gnaq-deficient mouse platelets fail activation by multiple physiological agonists and have prolonged bleeding. Reason: This supports a conserved signaling contribution to platelet activation and hemostasis rather than a clotting-protease function. Supporting Evidence: |
| GO:0007603 phototransduction, visible light | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Comparative mammalian experiments support a secondary phototransduction role with overlapping G-protein contributions. Reason: Retain a secondary visible-light phototransduction role for human GNAQ as comparative functional inference, not a direct human retinal assay. Full PMID:24958088 Fig. 4 isolates endogenous mouse Gnaq and Gna11 contributions in melanopsin-expressing Neuro-2A cells: either supports the calcium response, whereas joint silencing eliminates it. Fig. 5 combines native retinal knockdown with pupil measurements and supports overlapping Gnaq/Gna11/Gna14 participation without separately establishing each isoform as necessary in vivo. This mammalian evidence supplements the older chicken source PMID:12196552. PMID:24870805 preserves responses in tested single/double knockout combinations and discusses compensation or alternative signaling; this limits necessity claims, not the demonstrated participation capacity. Neither experiment establishes an exclusive human isoform assignment or every ipRGC subtype. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q5F3B5 UNRESOLVED The original chicken-source transfer is retained in light of independent mammalian functional evidence, not relabeled as a direct human experiment. Retain a secondary visible-light phototransduction role for human GNAQ as comparative functional inference, not a direct human retinal assay. Full PMID:24958088 Fig. 4 isolates endogenous mouse Gnaq and Gna11 contributions in melanopsin-expressing Neuro-2A cells: either supports the calcium response, whereas joint silencing eliminates it. Fig. 5 combines native retinal knockdown with pupil measurements and supports overlapping Gnaq/Gna11/Gna14 participation without separately establishing each isoform as necessary in vivo. This mammalian evidence supplements the older chicken source PMID:12196552. PMID:24870805 preserves responses in tested single/double knockout combinations and discusses compensation or alternative signaling; this limits necessity claims, not the demonstrated participation capacity. Neither experiment establishes an exclusive human isoform assignment or every ipRGC subtype. Supporting Evidence: PMID:24958088 These data confirm that Gnaq and Gna11 convey the melanopsin signal in Neuro-2A cells. PMID:24870805 Another possibility is that there is compensatory upregulation from other remaining Gq/11 family members in the tested mutant lines. |
| GO:0007603 phototransduction, visible light | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Comparative mammalian experiments support a secondary phototransduction role with overlapping G-protein contributions. Reason: Retain a secondary visible-light phototransduction role for human GNAQ as comparative functional inference, not a direct human retinal assay. Full PMID:24958088 Fig. 4 isolates endogenous mouse Gnaq and Gna11 contributions in melanopsin-expressing Neuro-2A cells: either supports the calcium response, whereas joint silencing eliminates it. Fig. 5 combines native retinal knockdown with pupil measurements and supports overlapping Gnaq/Gna11/Gna14 participation without separately establishing each isoform as necessary in vivo. This mammalian evidence supplements the older chicken source PMID:12196552. PMID:24870805 preserves responses in tested single/double knockout combinations and discusses compensation or alternative signaling; this limits necessity claims, not the demonstrated participation capacity. Neither experiment establishes an exclusive human isoform assignment or every ipRGC subtype. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q71RI7 UNRESOLVED The original chicken-source transfer is retained in light of independent mammalian functional evidence, not relabeled as a direct human experiment. Retain a secondary visible-light phototransduction role for human GNAQ as comparative functional inference, not a direct human retinal assay. Full PMID:24958088 Fig. 4 isolates endogenous mouse Gnaq and Gna11 contributions in melanopsin-expressing Neuro-2A cells: either supports the calcium response, whereas joint silencing eliminates it. Fig. 5 combines native retinal knockdown with pupil measurements and supports overlapping Gnaq/Gna11/Gna14 participation without separately establishing each isoform as necessary in vivo. This mammalian evidence supplements the older chicken source PMID:12196552. PMID:24870805 preserves responses in tested single/double knockout combinations and discusses compensation or alternative signaling; this limits necessity claims, not the demonstrated participation capacity. Neither experiment establishes an exclusive human isoform assignment or every ipRGC subtype. Supporting Evidence: PMID:24958088 These data confirm that Gnaq and Gna11 convey the melanopsin signal in Neuro-2A cells. PMID:24870805 Another possibility is that there is compensatory upregulation from other remaining Gq/11 family members in the tested mutant lines. |
| GO:0009649 entrainment of circadian clock | ISS GO_REF:0000024 | UNDECIDED | Summary: Mammalian circadian assays limit necessity claims but do not independently resolve this human entrainment assignment. Reason: The precise human GNAQ contribution to circadian entrainment remains unresolved after mammalian source review. Chicken pineal phase shifting in PMID:12196552 is a different photoreceptive implementation. PMID:24958088 measures cellular phototransduction and pupillary responses, not circadian entrainment. Full PMID:24870805 actually tests mouse wheel-running rhythms: the tested mutant combinations retain light-dark entrainment and light-pulse phase shifting; Gnaq/Gna11 double mutants show a small reduction of period lengthening in constant light. That combined-genotype effect does not separately establish human GNAQ entrainment, and normal entrainment does not demonstrate absence of a redundant contribution. Do not equate melanopsin participation with proof of every downstream circadian role. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q5F3B5 UNRESOLVED The precise human GNAQ contribution to circadian entrainment remains unresolved after mammalian source review. Chicken pineal phase shifting in PMID:12196552 is a different photoreceptive implementation. PMID:24958088 measures cellular phototransduction and pupillary responses, not circadian entrainment. Full PMID:24870805 actually tests mouse wheel-running rhythms: the tested mutant combinations retain light-dark entrainment and light-pulse phase shifting; Gnaq/Gna11 double mutants show a small reduction of period lengthening in constant light. That combined-genotype effect does not separately establish human GNAQ entrainment, and normal entrainment does not demonstrate absence of a redundant contribution. Do not equate melanopsin participation with proof of every downstream circadian role. Supporting Evidence: PMID:24958088 These data confirm that Gnaq and Gna11 convey the melanopsin signal in Neuro-2A cells. PMID:24870805 Another possibility is that there is compensatory upregulation from other remaining Gq/11 family members in the tested mutant lines. |
| GO:0009649 entrainment of circadian clock | ISS GO_REF:0000024 | UNDECIDED | Summary: Mammalian circadian assays limit necessity claims but do not independently resolve this human entrainment assignment. Reason: The precise human GNAQ contribution to circadian entrainment remains unresolved after mammalian source review. Chicken pineal phase shifting in PMID:12196552 is a different photoreceptive implementation. PMID:24958088 measures cellular phototransduction and pupillary responses, not circadian entrainment. Full PMID:24870805 actually tests mouse wheel-running rhythms: the tested mutant combinations retain light-dark entrainment and light-pulse phase shifting; Gnaq/Gna11 double mutants show a small reduction of period lengthening in constant light. That combined-genotype effect does not separately establish human GNAQ entrainment, and normal entrainment does not demonstrate absence of a redundant contribution. Do not equate melanopsin participation with proof of every downstream circadian role. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q71RI7 UNRESOLVED The precise human GNAQ contribution to circadian entrainment remains unresolved after mammalian source review. Chicken pineal phase shifting in PMID:12196552 is a different photoreceptive implementation. PMID:24958088 measures cellular phototransduction and pupillary responses, not circadian entrainment. Full PMID:24870805 actually tests mouse wheel-running rhythms: the tested mutant combinations retain light-dark entrainment and light-pulse phase shifting; Gnaq/Gna11 double mutants show a small reduction of period lengthening in constant light. That combined-genotype effect does not separately establish human GNAQ entrainment, and normal entrainment does not demonstrate absence of a redundant contribution. Do not equate melanopsin participation with proof of every downstream circadian role. Supporting Evidence: PMID:24958088 These data confirm that Gnaq and Gna11 convey the melanopsin signal in Neuro-2A cells. PMID:24870805 Another possibility is that there is compensatory upregulation from other remaining Gq/11 family members in the tested mutant lines. |
| GO:0009755 hormone-mediated signaling pathway | IDA PMID:31911434 The GPCR accessory protein MRAP2 regulates both biased signa... | KEEP AS NON CORE | Summary: The hormone-receptor/Gq coupling experiments establish direct intracellular transduction of hormonal stimulation. Reason: This broad hormone-response role is contextual rather than a distinct catalytic hormone activity. 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. |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:18703424 RGS22, a novel testis-specific regulator of G-protein signal... | 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. |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:19001095 Identification of G protein alpha subunit-palmitoylating enz... | 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. |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:27276689 mGlu1 receptor canonical signaling pathway contributes to th... | 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. |
| 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. |
| GO:0010543 regulation of platelet activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Native Gnaq-deficient mouse platelets fail activation by multiple physiological agonists and have prolonged bleeding. Reason: This supports a conserved signaling contribution to platelet activation and hemostasis rather than a clotting-protease function. 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 |
| 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. |
| GO:0031965 nuclear membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The traced mouse study directly colocalizes Gq with alpha1 receptors and PLCbeta1 at the nuclear membrane and validates nuclear fractions. Reason: Retain the conserved nuclear/nuclear-membrane pool with cardiac-cell and species limits; plasma-membrane localization does not exclude it. Supporting Evidence: |
| GO:0031965 nuclear membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The traced mouse study directly colocalizes Gq with alpha1 receptors and PLCbeta1 at the nuclear membrane and validates nuclear fractions. Reason: Retain the conserved nuclear/nuclear-membrane pool with cardiac-cell and species limits; plasma-membrane localization does not exclude it. Supporting Evidence: |
| GO:0032278 positive regulation of gonadotropin secretion | IDA PMID:18772143 Disease-causing mutation in GPR54 reveals the importance of ... | KEEP AS NON CORE | Summary: GPR54 signaling and gonadotrope-specific mouse Gq/G11 genetics support participation in gonadotropin synthesis/secretion through receptor signaling. Reason: The combined knockout establishes a Gq/G11 requirement, not that each paralog is individually indispensable or that Gq directly synthesizes hormone. |
| GO:0032278 positive regulation of gonadotropin secretion | IMP PMID:14573733 The GPR54 gene as a regulator of puberty. | KEEP AS NON CORE | Summary: GPR54 signaling and gonadotrope-specific mouse Gq/G11 genetics support participation in gonadotropin synthesis/secretion through receptor signaling. Reason: The combined knockout establishes a Gq/G11 requirement, not that each paralog is individually indispensable or that Gq directly synthesizes hormone. |
| GO:0034695 response to prostaglandin E | IDA PMID:8253813 Cloning and expression of a cDNA for the human prostaglandin... | KEEP AS NON CORE | Summary: The prostaglandin-receptor coupling study supports a specific Gq signaling response to prostaglandin E. Reason: This does not assign prostaglandin synthesis or direct ligand binding to Gq. Supporting Evidence: |
| GO:0042446 hormone biosynthetic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: GPR54 signaling and gonadotrope-specific mouse Gq/G11 genetics support participation in gonadotropin synthesis/secretion through receptor signaling. Reason: The combined knockout establishes a Gq/G11 requirement, not that each paralog is individually indispensable or that Gq directly synthesizes hormone. |
| GO:0042593 glucose homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Beta-cell-specific mouse Gq/G11 inactivation impairs glucose tolerance and insulin secretion. Reason: Retain the conserved endocrine signaling role with combined-paralog and native-mouse scope; Gq is not a glucose transporter or metabolic enzyme. Supporting Evidence: |
| GO:0043303 mast cell degranulation | IDA PMID:28288109 In silico design of novel probes for the atypical opioid rec... | KEEP AS NON CORE | Summary: Mast-cell receptor activation studies support Gq-linked signaling contributing to degranulation. Reason: Preserve the receptor/cell-specific signaling contribution without assigning Gq as the vesicle fusion machinery. |
| GO:0043303 mast cell degranulation | IDA PMID:34789875 Structure, function and pharmacology of human itch receptor ... | KEEP AS NON CORE | Summary: Mast-cell receptor activation studies support Gq-linked signaling contributing to degranulation. Reason: Preserve the receptor/cell-specific signaling contribution without assigning Gq as the vesicle fusion machinery. |
| GO:0045202 synapse | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The mGlu1βGqβPLC pathway and postsynaptic experiments at parallel-fiber/Purkinje-cell synapses directly support glutamate signaling and the postsynaptic intracellular pool. Reason: These are specific neuronal implementations of the general transducer function. Supporting Evidence: |
| GO:0045453 bone resorption | NAS PMID:23516330 Parathyroid hormone (PTH) and PTH-related peptide domains co... | UNDECIDED | Summary: The cited PTH-receptor biased-agonist study links signaling profiles to bone effects, but the available source does not isolate a GNAQ-specific resorptive mechanism. Reason: Broad PTH physiology or Gq pathway engagement alone is insufficient to assign this precise outcome; full target-level support remains unresolved. 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: CaSR coupling to Gq contributes to calcium-dependent control of hormone secretion. Reason: Retain this contextual pathway participation; the receptorβG protein structure is direct coupling evidence, whereas the secretion outcome draws on the known CaSR endocrine mechanism and is not itself measured by a structure. Supporting Evidence: |
| GO:0050821 protein stabilization | IMP PMID:20399743 Regulation of GSK-3beta and beta-Catenin by Galphaq in HEK29... | KEEP AS NON CORE | Summary: Activated Gq stabilizes beta-catenin through signaling that inhibits GSK3 in the studied cells, supporting the protein-stabilization and Wnt-regulatory outcomes. Reason: Retain these secondary signaling effects without assigning Gq direct ubiquitin-ligase or Wnt-receptor activity. Supporting Evidence: |
| GO:0060828 regulation of canonical Wnt signaling pathway | IMP PMID:20399743 Regulation of GSK-3beta and beta-Catenin by Galphaq in HEK29... | KEEP AS NON CORE | Summary: Activated Gq stabilizes beta-catenin through signaling that inhibits GSK3 in the studied cells, supporting the protein-stabilization and Wnt-regulatory outcomes. Reason: Retain these secondary signaling effects without assigning Gq direct ubiquitin-ligase or Wnt-receptor activity. Supporting Evidence: |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | UNDECIDED | Summary: The original urinary, parotid and prostate vesicle-proteomics citations are retained, but target-specific detection and vesicle enrichment could not be independently resolved here. Reason: Intracellular membrane association neither proves nor excludes released-vesicle localization; the precise HDA claim remains open. |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | UNDECIDED | Summary: The original urinary, parotid and prostate vesicle-proteomics citations are retained, but target-specific detection and vesicle enrichment could not be independently resolved here. Reason: Intracellular membrane association neither proves nor excludes released-vesicle localization; the precise HDA claim remains open. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | UNDECIDED | Summary: The original urinary, parotid and prostate vesicle-proteomics citations are retained, but target-specific detection and vesicle enrichment could not be independently resolved here. Reason: Intracellular membrane association neither proves nor excludes released-vesicle localization; the precise HDA claim remains open. |
| GO:0071468 cellular response to acidic pH | IDA PMID:39753132 Molecular basis of proton sensing by G protein-coupled recep... | KEEP AS NON CORE | Summary: The acid-sensing receptor study establishes Gq coupling in response to extracellular acidity. Reason: The G protein transduces the receptor response rather than acting as the primary proton sensor. Supporting Evidence: |
| GO:0099524 postsynaptic cytosol | IDA PMID:27276689 mGlu1 receptor canonical signaling pathway contributes to th... | KEEP AS NON CORE | Summary: The mGlu1βGqβPLC pathway and postsynaptic experiments at parallel-fiber/Purkinje-cell synapses directly support glutamate signaling and the postsynaptic intracellular pool. Reason: These are specific neuronal implementations of the general transducer function. Supporting Evidence: |
| GO:0160025 sensory perception of itch | IDA PMID:31500698 MRGPRX4 is a bile acid receptor for human cholestatic itch. | KEEP AS NON CORE | Summary: MRGPRX4 activation and Gq coupling provide a signaling route relevant to human itch. Reason: The receptor/neuronal experiments support a sensory implementation, not an assertion that every Gq-containing cell mediates itch. |
| GO:0160025 sensory perception of itch | IDA PMID:39476841 Structure-guided discovery of bile acid derivatives for trea... | KEEP AS NON CORE | Summary: MRGPRX4 activation and Gq coupling provide a signaling route relevant to human itch. Reason: The receptor/neuronal experiments support a sensory implementation, not an assertion that every Gq-containing cell mediates itch. |
| GO:1904181 positive regulation of membrane depolarization | TAS PMID:34939256 The electrophysiologic properties of gonadotropin-releasing ... | KEEP AS NON CORE | Summary: The cited receptor-driven depolarization pathway implicates Gq-mediated intracellular signaling. Reason: Retain the contextual regulatory role, distinguishing signal transduction from direct ion-channel pore activity. Supporting Evidence: |
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