GNB1 encodes guanine nucleotide-binding protein subunit beta-1 (Gbeta1), a seven-bladed WD40 beta-propeller that forms an obligate dimer with a Ggamma subunit and, with a Galpha subunit, makes up the heterotrimeric G proteins that transduce signals from G protein-coupled receptors (GPCRs). Gbeta1 is the most widely used Gbeta, found in Gi/o, Gs, Gq/11 and rod transducin heterotrimers. Within the heterotrimer it binds the switch II region of GDP-bound Galpha and contacts the receptor, which promotes receptor-catalysed GDP/GTP exchange on Galpha; Gbeta itself has no nucleotide-binding or GTPase activity. After activation, the released, membrane-anchored (Ggamma-prenylated) Gbeta1gamma dimer directly regulates effectors, including opening G protein-gated inwardly rectifying K+ (GIRK) channels and stimulating phospholipase C-beta. Germline de novo GNB1 missense variants that disrupt the Galpha or effector interfaces cause a neurodevelopmental disorder with hypotonia and seizures (MRD42), and recurrent somatic mutations occur in myeloid and lymphoid neoplasms.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001750 photoreceptor outer segment | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GNB1 is the beta subunit of rod transducin and is present in photoreceptor outer segments. Reason: Transferred from mouse Gnb1 (Ensembl Compara). Gbeta1 is the transducin beta subunit, so this location is correct, but it is tissue-specific and not the general site of action. Supporting Evidence: PMID:3095147 This work proves for the first time that the beta-subunits of all signal-transducing G-proteins, including transducin, are the same. |
| GO:0003924 GTPase activity | IDA PMID:1543505 Diversity among the beta subunits of heterotrimeric GTP-bind... | REMOVE | Summary: GTPase activity attributed to Gbeta1. Reason: Gbeta is a seven-bladed WD40 beta-propeller with no nucleotide-binding domain. GDP/GTP exchange and GTP hydrolysis take place on the Galpha subunit of the heterotrimer. Gbetagamma is needed for receptor coupling of Galpha but does not catalyse GTP hydrolysis. The cited papers are cDNA cloning studies (PMID:3095147, human Gbeta; PMID:1543505, mouse Gbeta4) and their abstracts report no GTPase assay on Gbeta. The activity of the heterotrimer is captured on GNB1 by its complex membership (GO:0005834) and its G-protein alpha-subunit binding. The same framework is applied to GNG2; the beta and gamma chains are required for the heterotrimer's GTPase activity, which is a contributes_to relationship to the heterotrimer's nucleotide-cycling activity, not an enables claim on the subunit. Supporting Evidence: PMID:8521505 Repeated WD motifs in beta form a circularized sevenfold beta propeller. PMID:31300275 activates the G-protein transducin (GT) by catalyzing GDP-GTP exchange on its Ξ± subunit (GΞ±T) PMID:1543505 The beta and gamma subunits are thought to have a more passive role in G protein function |
| GO:0003924 GTPase activity | TAS PMID:3095147 Beta-subunits of the human liver Gs/Gi signal-transducing pr... | REMOVE | Summary: GTPase activity attributed to Gbeta1. Reason: Gbeta is a seven-bladed WD40 beta-propeller with no nucleotide-binding domain. GDP/GTP exchange and GTP hydrolysis take place on the Galpha subunit of the heterotrimer. Gbetagamma is needed for receptor coupling of Galpha but does not catalyse GTP hydrolysis. The cited papers are cDNA cloning studies (PMID:3095147, human Gbeta; PMID:1543505, mouse Gbeta4) and their abstracts report no GTPase assay on Gbeta. The activity of the heterotrimer is captured on GNB1 by its complex membership (GO:0005834) and its G-protein alpha-subunit binding. The same framework is applied to GNG2; the beta and gamma chains are required for the heterotrimer's GTPase activity, which is a contributes_to relationship to the heterotrimer's nucleotide-cycling activity, not an enables claim on the subunit. Supporting Evidence: PMID:8521505 Repeated WD motifs in beta form a circularized sevenfold beta propeller. PMID:31300275 activates the G-protein transducin (GT) by catalyzing GDP-GTP exchange on its Ξ± subunit (GΞ±T) PMID:1543505 The beta and gamma subunits are thought to have a more passive role in G protein function |
| GO:0005515 protein binding | IPI PMID:16782902 Activation state-dependent interaction between Galphai and p... | MODIFY | Summary: GNB1 binds GNAI2 (this study); Gbeta1 is the beta subunit of Gi heterotrimers. Reason: The interaction with GNAI2 is the Galpha-Gbetagamma interface of the heterotrimer, which is well established structurally (two Galpha contact regions on the Gbeta propeller). Generic protein binding is uninformative; the specific function is G-protein alpha-subunit binding. Proposed replacements: G-protein alpha-subunit binding Supporting Evidence: PMID:16782902 Indeed, FLAG-tagged GΞ²1 was found to bind to p67 phox only when GΞ±i2 was overexpressed in the cells. PMID:25733868 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:16782902 Activation state-dependent interaction between Galphai and p... | REMOVE | Summary: Interaction of GNB1 with NCF2 (p67phox) reported in this study. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. The cited study shows that the Gbetagamma-p67phox association is indirect and requires GDP-bound Galphai. Supporting Evidence: PMID:16782902 Based on these data, we concluded that the association between GΞ²Ξ³ and p67 phox is indirect and mediated through the inactive, GDP-bound GΞ±i. |
| GO:0005515 protein binding | IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu... | REMOVE | Summary: Interaction of GNB1 with HTT (huntingtin) reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:23739333 X-ray structure of the mammalian GIRK2-Ξ²Ξ³ G-protein complex. | MODIFY | Summary: GNB1 binds GNG2 (this study), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG2; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:23739333 The structure was solved with Phaser52 by sequentially searching for a GIRK2 monomer (PDB id: 3SYA) and then a GΞ²1Ξ³2 dimer PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Interaction of GNB1 with PFDN5 (prefoldin subunit 5) reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. Prefoldin/CCT chaperone association reflects Gbeta folding as a chaperone client, not a Gbeta function. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: GNB1 binds GNG5 (a high-throughput interaction screen), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG5; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | MODIFY | Summary: GNB1 binds GNG2 (this study), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG2; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:25733868 G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | MODIFY | Summary: GNB1 binds GNAI1 (this study); Gbeta1 is the beta subunit of Gi heterotrimers. Reason: The interaction with GNAI1 is the Galpha-Gbetagamma interface of the heterotrimer, which is well established structurally (two Galpha contact regions on the Gbeta propeller). Generic protein binding is uninformative; the specific function is G-protein alpha-subunit binding. Proposed replacements: G-protein alpha-subunit binding Supporting Evidence: PMID:25733868 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: GNB1 binds GNG5 (this study), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG5; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:25733868 G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:28437792 Phase-plate cryo-EM structure of a class B GPCR-G-protein co... | MODIFY | Summary: GNB1 binds GNG2 (this study), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG2; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:28437792 infected with 3 separate baculovirus at a ratio of 1:2:2 for hCTR, GΞ±s and GΞ²1Ξ³2 PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MODIFY | Summary: GNB1 binds GNAI1 (a high-throughput interaction screen); Gbeta1 is the beta subunit of Gi heterotrimers. Reason: The interaction with GNAI1 is the Galpha-Gbetagamma interface of the heterotrimer, which is well established structurally (two Galpha contact regions on the Gbeta propeller). Generic protein binding is uninformative; the specific function is G-protein alpha-subunit binding. Proposed replacements: G-protein alpha-subunit binding Supporting Evidence: PMID:25733868 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: Interaction of GNB1 with VAC14 reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of GNB1 with CTNNA3 isoform 2 reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32371397 Cryo-electron microscopy structure of the glucagon receptor ... | MODIFY | Summary: GNB1 binds GNG2 (this study), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG2; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:32371397 thereby stabilizing the interaction with Ξ²Ξ³ subunits PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:32528175 Structure of a D2 dopamine receptor-G-protein complex in a l... | MODIFY | Summary: GNB1 binds GNG2 (this study), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG2; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:32528175 An additional pFastBac-Dual baculovirus was made with human GΞ²1 and human GΞ³2 genes. PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Interaction of GNB1 with P4HB reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Interaction of GNB1 with HTT (huntingtin) reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Interaction of GNB1 with DPF1 isoform 2 reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: GNB1 binds GNAI2 (a high-throughput interaction screen); Gbeta1 is the beta subunit of Gi heterotrimers. Reason: The interaction with GNAI2 is the Galpha-Gbetagamma interface of the heterotrimer, which is well established structurally (two Galpha contact regions on the Gbeta propeller). Generic protein binding is uninformative; the specific function is G-protein alpha-subunit binding. Proposed replacements: G-protein alpha-subunit binding Supporting Evidence: PMID:25733868 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:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: GNB1 binds GNG2 (a high-throughput interaction screen), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG2; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: GNB1 binds GNG5 (a high-throughput interaction screen), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG5; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction of GNB1 with PFDN5 (prefoldin subunit 5) reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. Prefoldin/CCT chaperone association reflects Gbeta folding as a chaperone client, not a Gbeta function. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: GNB1 binds GNAI2 (a high-throughput interaction screen); Gbeta1 is the beta subunit of Gi heterotrimers. Reason: The interaction with GNAI2 is the Galpha-Gbetagamma interface of the heterotrimer, which is well established structurally (two Galpha contact regions on the Gbeta propeller). Generic protein binding is uninformative; the specific function is G-protein alpha-subunit binding. Proposed replacements: G-protein alpha-subunit binding Supporting Evidence: PMID:25733868 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:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: GNB1 binds GNG2 (a high-throughput interaction screen), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG2; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: GNB1 binds GNG5 (a high-throughput interaction screen), forming the obligate Gbetagamma dimer. Reason: Gbeta1 forms an obligate dimer with Ggamma subunits including GNG5; the beta-gamma interface is extensive. Generic protein binding is uninformative; the specific function is G-protein gamma-subunit binding. Proposed replacements: G-protein gamma-subunit binding Supporting Evidence: PMID:8521505 an extended interface between beta and nearly all of gamma |
| GO:0005515 protein binding | IPI PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | MODIFY | Summary: GNB1 binds GNAI1 (this study); Gbeta1 is the beta subunit of Gi heterotrimers. Reason: The interaction with GNAI1 is the Galpha-Gbetagamma interface of the heterotrimer, which is well established structurally (two Galpha contact regions on the Gbeta propeller). Generic protein binding is uninformative; the specific function is G-protein alpha-subunit binding. Proposed replacements: G-protein alpha-subunit binding Supporting Evidence: PMID:35501348 N-terminal 6 Γ His-tagged WT human GΞ²1 and no-tag GΞ³2 were cloned into a pFastBac-Dual vector PMID:25733868 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... | MODIFY | Summary: GNB1 binds GNAI1 (a high-throughput interaction screen); Gbeta1 is the beta subunit of Gi heterotrimers. Reason: The interaction with GNAI1 is the Galpha-Gbetagamma interface of the heterotrimer, which is well established structurally (two Galpha contact regions on the Gbeta propeller). Generic protein binding is uninformative; the specific function is G-protein alpha-subunit binding. Proposed replacements: G-protein alpha-subunit binding Supporting Evidence: PMID:25733868 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: Interaction of GNB1 with PFDN5 (prefoldin subunit 5) reported in a high-throughput interaction screen. Reason: Bare protein binding is uninformative and no specific molecular function of GNB1 is established by this interaction; removal does not imply the interaction is false. Prefoldin/CCT chaperone association reflects Gbeta folding as a chaperone client, not a Gbeta function. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Gbeta is a cytoplasmic-side protein (PAINT IBA). Reason: True but broad. Gbetagamma acts at the cytoplasmic face of the plasma membrane and endomembranes. The more informative locations (plasma membrane, heterotrimeric G-protein complex) are accepted separately. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005765 lysosomal membrane | HDA PMID:17897319 Integral and associated lysosomal membrane proteins. | KEEP AS NON CORE | Summary: Detected in a lysosomal membrane proteomics study (HDA). Reason: High-throughput proteomic detection. Gbetagamma can associate with endomembranes, but lysosomal localization has no functional support and is not core. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1013012 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1013013 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1013020 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-112271 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114552 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114558 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-167408 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-167419 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-167429 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-167433 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-379044 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-379048 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380073 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392187 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392195 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392202 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392295 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392300 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392852 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392870 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3965444 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3965447 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-396996 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-397835 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-397891 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-398040 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-398193 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-418576 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-420883 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-428749 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-428750 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-428752 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-428909 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-428917 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-428918 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-500717 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814119 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814120 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814121 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814124 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814418 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-744886 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-744887 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-749446 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-749448 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-749452 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-749453 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-749454 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-749456 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-750988 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-750993 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-751001 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-751013 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-751019 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-751024 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-751027 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-751029 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-751039 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-825631 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8850527 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8850560 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964241 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964271 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964317 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964599 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964604 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964605 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964614 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8964634 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8982637 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8982640 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9021600 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9021601 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9036301 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9036307 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9036308 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9660819 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9660824 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9660828 | KEEP AS NON CORE | Summary: Reactome places the Gbetagamma dimer in the cytosol compartment for this reaction. Reason: Gbetagamma acts on the cytoplasmic side of membranes. The prenylated Gbetagamma dimer is anchored to the inner face of the plasma membrane, so 'cytosol' is only approximately right for the active dimer. Newly made Gbeta is folded and assembled with Ggamma in the cytosol, so the location is not wrong. Plasma membrane / heterotrimeric G-protein complex are the core locations. Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0005834 heterotrimeric G-protein complex | IBA GO_REF:0000033 | ACCEPT | Summary: GNB1 is the beta subunit of heterotrimeric G proteins (Galpha-Gbeta1-Ggamma). Reason: Gbeta1 is the prototypical Gbeta of Gi/o, Gs, Gq and transducin heterotrimers. It is used in essentially every reconstituted GPCR-G protein structure (5-HT1B, 5-HT1F, D2, CTR, GPR88, muOR), and coIP shows it forms heterotrimers with essentially all Ggamma partners. Core cellular component. Supporting Evidence: PMID:25733868 G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex PMID:42870023 WT Gi heterotrimer (GΞ±i1Ξ²1Ξ³2) from Hi-5 cells was prepared similarly |
| GO:0005834 heterotrimeric G-protein complex | IDA PMID:1543505 Diversity among the beta subunits of heterotrimeric GTP-bind... | ACCEPT | Summary: GNB1 is the beta subunit of heterotrimeric G proteins (Galpha-Gbeta1-Ggamma). Reason: Gbeta1 is the prototypical Gbeta of Gi/o, Gs, Gq and transducin heterotrimers. It is used in essentially every reconstituted GPCR-G protein structure (5-HT1B, 5-HT1F, D2, CTR, GPR88, muOR), and coIP shows it forms heterotrimers with essentially all Ggamma partners. Core cellular component. Supporting Evidence: PMID:1543505 The beta and gamma subunits are thought to have a more passive role in G protein function |
| GO:0005834 heterotrimeric G-protein complex | IDA PMID:29925951 Cryo-EM structure of the serotonin 5-HT(1B) receptor coupled... | ACCEPT | Summary: GNB1 is the beta subunit of heterotrimeric G proteins (Galpha-Gbeta1-Ggamma). Reason: Gbeta1 is the prototypical Gbeta of Gi/o, Gs, Gq and transducin heterotrimers. It is used in essentially every reconstituted GPCR-G protein structure (5-HT1B, 5-HT1F, D2, CTR, GPR88, muOR), and coIP shows it forms heterotrimers with essentially all Ggamma partners. Core cellular component. Supporting Evidence: PMID:29925951 assembled into a complex containing 5-HT1BR, donitriptan, mini-GO, Ξ²1 and Ξ³2 subunits PMID:42870023 WT Gi heterotrimer (GΞ±i1Ξ²1Ξ³2) from Hi-5 cells was prepared similarly |
| GO:0005834 heterotrimeric G-protein complex | IDA PMID:33762731 Structural insights into the lipid and ligand regulation of ... | ACCEPT | Summary: GNB1 is the beta subunit of heterotrimeric G proteins (Galpha-Gbeta1-Ggamma). Reason: Gbeta1 is the prototypical Gbeta of Gi/o, Gs, Gq and transducin heterotrimers. It is used in essentially every reconstituted GPCR-G protein structure (5-HT1B, 5-HT1F, D2, CTR, GPR88, muOR), and coIP shows it forms heterotrimers with essentially all Ggamma partners. Core cellular component. Supporting Evidence: PMID:33762731 Here we report five structures of 5-HT receptor-G-protein PMID:42870023 WT Gi heterotrimer (GΞ±i1Ξ²1Ξ³2) from Hi-5 cells was prepared similarly |
| GO:0005834 heterotrimeric G-protein complex | IDA PMID:34239069 Structural basis for recognition of anti-migraine drug lasmi... | ACCEPT | Summary: GNB1 is the beta subunit of heterotrimeric G proteins (Galpha-Gbeta1-Ggamma). Reason: Gbeta1 is the prototypical Gbeta of Gi/o, Gs, Gq and transducin heterotrimers. It is used in essentially every reconstituted GPCR-G protein structure (5-HT1B, 5-HT1F, D2, CTR, GPR88, muOR), and coIP shows it forms heterotrimers with essentially all Ggamma partners. Core cellular component. Supporting Evidence: PMID:34239069 Although the conformations of the main interfaces between receptor and G protein are similar, the G protein conformation shows observable changes. PMID:42870023 WT Gi heterotrimer (GΞ±i1Ξ²1Ξ³2) from Hi-5 cells was prepared similarly |
| GO:0005834 heterotrimeric G-protein complex | IEA GO_REF:0000107 | ACCEPT | Summary: GNB1 is the beta subunit of heterotrimeric G proteins (Galpha-Gbeta1-Ggamma). Reason: Gbeta1 is the prototypical Gbeta of Gi/o, Gs, Gq and transducin heterotrimers. It is used in essentially every reconstituted GPCR-G protein structure (5-HT1B, 5-HT1F, D2, CTR, GPR88, muOR), and coIP shows it forms heterotrimers with essentially all Ggamma partners. Core cellular component. Supporting Evidence: PMID:25733868 G-protein combinations consisting of Ξ±i1 or Ξ±sL and all possible Ξ²Ξ³-dimers to form a heterotrimeric complex PMID:42870023 WT Gi heterotrimer (GΞ±i1Ξ²1Ξ³2) from Hi-5 cells was prepared similarly |
| GO:0005834 heterotrimeric G-protein complex | IPI PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | ACCEPT | Summary: GNB1 is the beta subunit of heterotrimeric G proteins (Galpha-Gbeta1-Ggamma). Reason: Gbeta1 is the prototypical Gbeta of Gi/o, Gs, Gq and transducin heterotrimers. It is used in essentially every reconstituted GPCR-G protein structure (5-HT1B, 5-HT1F, D2, CTR, GPR88, muOR), and coIP shows it forms heterotrimers with essentially all Ggamma partners. Core cellular component. Supporting Evidence: PMID:35501348 N-terminal 6 Γ His-tagged WT human GΞ²1 and no-tag GΞ³2 were cloned into a pFastBac-Dual vector PMID:42870023 WT Gi heterotrimer (GΞ±i1Ξ²1Ξ³2) from Hi-5 cells was prepared similarly |
| GO:0005886 plasma membrane | IPI PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | MODIFY | Summary: Gbetagamma (and the heterotrimer) is located at the cytoplasmic face of the plasma membrane. Reason: Ggamma prenylation anchors Gbetagamma to the inner leaflet of the plasma membrane, where it couples to GPCRs and activates membrane effectors such as GIRK channels. Core location. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-167419 | MODIFY | Summary: Gbetagamma (and the heterotrimer) is located at the cytoplasmic face of the plasma membrane. Reason: Ggamma prenylation anchors Gbetagamma to the inner leaflet of the plasma membrane, where it couples to GPCRs and activates membrane effectors such as GIRK channels. Core location. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-167429 | MODIFY | Summary: Gbetagamma (and the heterotrimer) is located at the cytoplasmic face of the plasma membrane. Reason: Ggamma prenylation anchors Gbetagamma to the inner leaflet of the plasma membrane, where it couples to GPCRs and activates membrane effectors such as GIRK channels. Core location. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9712210 | MODIFY | Summary: Gbetagamma (and the heterotrimer) is located at the cytoplasmic face of the plasma membrane. Reason: Ggamma prenylation anchors Gbetagamma to the inner leaflet of the plasma membrane, where it couples to GPCRs and activates membrane effectors such as GIRK channels. Core location. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9717206 | MODIFY | Summary: Gbetagamma (and the heterotrimer) is located at the cytoplasmic face of the plasma membrane. Reason: Ggamma prenylation anchors Gbetagamma to the inner leaflet of the plasma membrane, where it couples to GPCRs and activates membrane effectors such as GIRK channels. Core location. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9728723 | MODIFY | Summary: Gbetagamma (and the heterotrimer) is located at the cytoplasmic face of the plasma membrane. Reason: Ggamma prenylation anchors Gbetagamma to the inner leaflet of the plasma membrane, where it couples to GPCRs and activates membrane effectors such as GIRK channels. Core location. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9728748 | MODIFY | Summary: Gbetagamma (and the heterotrimer) is located at the cytoplasmic face of the plasma membrane. Reason: Ggamma prenylation anchors Gbetagamma to the inner leaflet of the plasma membrane, where it couples to GPCRs and activates membrane effectors such as GIRK channels. Core location. The more specific supported term is cytoplasmic side of plasma membrane (GO:0009898), supported by the inner-leaflet anchoring/recruitment evidence though not yet a separate GOA row -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: Gbetagamma participates in signal transduction. Reason: Correct but too general. Gbeta1 acts in GPCR signaling, as the beta subunit that couples Galpha to activated receptors and, once released, as an effector-regulating Gbetagamma dimer. The specific supported term is G protein-coupled receptor signaling pathway (GO:0007186), which the gene already carries (IBA). Proposed replacements: G protein-coupled receptor signaling pathway Supporting Evidence: PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0007165 signal transduction | TAS PMID:7649993 Mitogen-activated protein kinase activation requires two sig... | MODIFY | Summary: Gbetagamma participates in signal transduction. Reason: Correct but too general. Gbeta1 acts in GPCR signaling, as the beta subunit that couples Galpha to activated receptors and, once released, as an effector-regulating Gbetagamma dimer. The specific supported term is G protein-coupled receptor signaling pathway (GO:0007186), which the gene already carries (IBA). Proposed replacements: G protein-coupled receptor signaling pathway Supporting Evidence: PMID:7649993 two independent signals are required for the maximal activation of MAP kinase by G protein-coupled receptors PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0007165 signal transduction | TAS PMID:8717044 Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm ... | MODIFY | Summary: Gbetagamma participates in signal transduction. Reason: Correct but too general. Gbeta1 acts in GPCR signaling, as the beta subunit that couples Galpha to activated receptors and, once released, as an effector-regulating Gbetagamma dimer. The specific supported term is G protein-coupled receptor signaling pathway (GO:0007186), which the gene already carries (IBA). Proposed replacements: G protein-coupled receptor signaling pathway Supporting Evidence: PMID:8717044 cotransfection with G-protein beta gamma subunits caused a constitutive activation that was sensitive to PP1 PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0007186 G protein-coupled receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Gbeta1 is a core component of GPCR signaling via heterotrimeric G proteins. Reason: Gbeta1gamma is required for receptor coupling of Galpha and, when released, directly regulates effectors (GIRK channels, PLC-beta). The PAINT IBA placement over the Gbeta family is sound, and GPCR-Gi1 structures with Gbeta1 support the NAS row. Supporting Evidence: PMID:35501348 N-terminal 6 Γ His-tagged WT human GΞ²1 and no-tag GΞ³2 were cloned into a pFastBac-Dual vector PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open PMID:1606965 beta gamma subunits, purified from bovine retinal transducin (beta gamma t), markedly stimulated the hydrolysis of phosphatidylinositol 4,5-bisphosphate by this phospholipase C preparation |
| GO:0007186 G protein-coupled receptor signaling pathway | NAS PMID:35501348 Activation and allosteric regulation of the orphan GPR88-Gi1... | ACCEPT | Summary: Gbeta1 is a core component of GPCR signaling via heterotrimeric G proteins. Reason: Gbeta1gamma is required for receptor coupling of Galpha and, when released, directly regulates effectors (GIRK channels, PLC-beta). The PAINT IBA placement over the Gbeta family is sound, and GPCR-Gi1 structures with Gbeta1 support the NAS row. Supporting Evidence: PMID:35501348 N-terminal 6 Γ His-tagged WT human GΞ²1 and no-tag GΞ³2 were cloned into a pFastBac-Dual vector PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open PMID:1606965 beta gamma subunits, purified from bovine retinal transducin (beta gamma t), markedly stimulated the hydrolysis of phosphatidylinositol 4,5-bisphosphate by this phospholipase C preparation |
| GO:0007191 adenylate cyclase-activating dopamine receptor signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS from bovine Gnb1 (P62871), based on reconstitution of D1 receptor-Gs-adenylyl cyclase signaling with Gbeta1gamma2. Reason: Gbeta1gamma2 supported D1-receptor-Galphas-ACVI coupling in a reconstituted system. This is true but is one of many GPCR pathways Gbeta1 serves, and is non-core. Supporting Evidence: PMID:18403039 BV co-expressing DR-D1, Galpha(s), Gbeta(1)gamma(2), and ACVI also responded to dopamine agonists and an antagonist. |
| GO:0007213 G protein-coupled acetylcholine receptor signaling pathway | TAS PMID:8717044 Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm ... | KEEP AS NON CORE | Summary: Muscarinic receptor signaling via Gbetagamma to Ras-GRF. Reason: Gbetagamma mediates muscarinic receptor activation of Ras-GRF. This is a valid GPCR context, and Gbeta1 is part of the Gi/Gq heterotrimers that muscarinic receptors use. Specific receptor context, non-core. Supporting Evidence: PMID:8717044 cotransfection with G-protein beta gamma subunits caused a constitutive activation that was sensitive to PP1 |
| GO:0007265 Ras protein signal transduction | TAS PMID:8717044 Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm ... | MARK AS OVER ANNOTATED | Summary: Gbetagamma activates the Ras exchange factor Ras-GRF. Reason: Gbetagamma acts upstream of Ras by stimulating Ras-GRF exchange activity through a phosphorylation-dependent mechanism. It is not a component of the Ras-initiated signaling cascade itself, so 'Ras protein signal transduction' over-states its role. The upstream contribution is covered by GPCR signaling. Supporting Evidence: PMID:8717044 cotransfection with G-protein beta gamma subunits caused a constitutive activation that was sensitive to PP1 |
| GO:0016004 phospholipase activator activity | ISS GO_REF:0000024 | ACCEPT | Summary: Gbetagamma directly stimulates phospholipase C-beta. Reason: Purified transducin betagamma (Gbeta1gamma1) and brain betagamma stimulate PIP2 hydrolysis by PLC-beta. This is a canonical Gbetagamma effector activity, and the ISS from bovine Gnb1 is well founded. Supporting Evidence: PMID:1606965 beta gamma subunits, purified from bovine retinal transducin (beta gamma t), markedly stimulated the hydrolysis of phosphatidylinositol 4,5-bisphosphate by this phospholipase C preparation |
| GO:0016020 membrane | ISS GO_REF:0000024 | MODIFY | Summary: Gbetagamma is membrane-associated. Reason: Correct but general. Gbeta1gamma is anchored to the cytoplasmic face of the plasma membrane via Ggamma prenylation, so it faces the cytosol rather than the cell exterior. Replace with cytoplasmic side of plasma membrane (GO:0009898), the specific inner-leaflet descendant. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:42870023 The main peak containing prenylated GΞ²Ξ³ was dialyzed |
| GO:0030159 signaling receptor complex adaptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT/ISS term for the Gbeta scaffolding role within receptor-G protein complexes. Reason: Gbeta1 is a structural WD40 scaffold that holds Galpha and Ggamma together and contacts the receptor (ICL1/helix 8) in GPCR-G protein complexes. GO represents this role across the Gbeta family as signaling receptor complex adaptor activity, and the PAINT node placement is sound. Supporting Evidence: PMID:8521505 Repeated WD motifs in beta form a circularized sevenfold beta propeller. PMID:35501348 N-terminal 6 Γ His-tagged WT human GΞ²1 and no-tag GΞ³2 were cloned into a pFastBac-Dual vector |
| GO:0030159 signaling receptor complex adaptor activity | ISS GO_REF:0000024 | ACCEPT | Summary: PAINT/ISS term for the Gbeta scaffolding role within receptor-G protein complexes. Reason: Gbeta1 is a structural WD40 scaffold that holds Galpha and Ggamma together and contacts the receptor (ICL1/helix 8) in GPCR-G protein complexes. GO represents this role across the Gbeta family as signaling receptor complex adaptor activity, and the PAINT node placement is sound. Supporting Evidence: PMID:8521505 Repeated WD motifs in beta form a circularized sevenfold beta propeller. PMID:35501348 N-terminal 6 Γ His-tagged WT human GΞ²1 and no-tag GΞ³2 were cloned into a pFastBac-Dual vector |
| GO:0044877 protein-containing complex binding | IDA PMID:23209302 KIF14 negatively regulates Rap1a-Radil signaling during brea... | KEEP AS NON CORE | Summary: Gbetagamma associates with Radil-Rap1 complexes. Reason: Gbetagamma co-purifies with the Rap1 effector Radil and promotes Rap1-dependent integrin activation. The interaction is real, but 'protein-containing complex binding' is uninformative and peripheral to core function. Supporting Evidence: PMID:23209302 We previously identified the Rap1 effector Radil as a protein associating with GΞ²Ξ³ subunits of heterotrimeric G-proteins |
| GO:0045202 synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Synapse localization transferred from mouse Gnb1. Reason: Gbetagamma acts at synapses, for example in GIRK activation and presynaptic inhibition, but synapse is a tissue-context location. Non-core. Supporting Evidence: PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:0051020 GTPase binding | IPI PMID:19255495 The cationic region of Rhes mediates its interactions with s... | KEEP AS NON CORE | Summary: Gbeta1 binds the small GTPase Rhes (RASD2) in yeast two-hybrid. Reason: Rhes binds Gbeta1, Gbeta2 and Gbeta3 via its cationic region. This is a plausible regulatory interaction but has no clear role in Gbeta1 function. Non-core. Supporting Evidence: PMID:19255495 we have used yeast two-hybrid studies to show that Rhes binds selectively to Gbeta1, Gbeta2 and Gbeta3 subunits |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Detected in exosome proteomics (HDA). Reason: Gbeta1 is an abundant, ubiquitous membrane-associated protein that is commonly found in vesicle proteomes. The finding is accepted at face value but has no known functional significance. |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | KEEP AS NON CORE | Summary: Detected in exosome proteomics (HDA). Reason: Gbeta1 is an abundant, ubiquitous membrane-associated protein that is commonly found in vesicle proteomes. The finding is accepted at face value but has no known functional significance. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: Detected in exosome proteomics (HDA). Reason: Gbeta1 is an abundant, ubiquitous membrane-associated protein that is commonly found in vesicle proteomes. The finding is accepted at face value but has no known functional significance. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: Detected in exosome proteomics (HDA). Reason: Gbeta1 is an abundant, ubiquitous membrane-associated protein that is commonly found in vesicle proteomes. The finding is accepted at face value but has no known functional significance. |
| GO:0071380 cellular response to prostaglandin E stimulus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS from bovine Gnb1, based on the same reconstitution study of Gs-coupled receptors. Reason: Gbeta1gamma2 supports Gs-coupled receptor signaling in reconstitution, which plausibly includes prostaglandin E receptors. As a subunit of the heterotrimer Gbeta1 does take part. This is one receptor context among many, so it is non-core. Supporting Evidence: PMID:18403039 Furthermore, BV expressing two other Galpha(s)-coupled receptors together with Galpha(s), Gbeta(1)gamma(2), and ACVI also produced cAMP in response to their specific ligands. |
| GO:0071870 cellular response to catecholamine stimulus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS from bovine Gnb1, based on the same reconstitution study of Gs-coupled receptors. Reason: As for prostaglandin E: Gbeta1gamma2 supports Gs-coupled (for example beta-adrenergic) receptor signaling. This is one receptor context among many, so it is non-core. Supporting Evidence: PMID:18403039 Furthermore, BV expressing two other Galpha(s)-coupled receptors together with Galpha(s), Gbeta(1)gamma(2), and ACVI also produced cAMP in response to their specific ligands. |
| GO:0097381 photoreceptor disc membrane | TAS Reactome:R-HSA-2485182 | KEEP AS NON CORE | Summary: Reactome places transducin Gbeta1gamma1 on the rod photoreceptor disc membrane. Reason: Gbeta1 is the transducin beta subunit, so the location is correct in rods. It is tissue-specific and not core. Supporting Evidence: PMID:3095147 This work proves for the first time that the beta-subunits of all signal-transducing G-proteins, including transducin, are the same. |
| GO:0099104 potassium channel activator activity | IDA PMID:23739333 X-ray structure of the mammalian GIRK2-Ξ²Ξ³ G-protein complex. | ACCEPT | Summary: Gbeta1gamma2 directly activates GIRK2 potassium channels. Reason: The GIRK2-Gbeta1gamma2 crystal structure and reconstitution with purified components show that Gbetagamma alone, in PIP2-containing membranes, is sufficient to open GIRK channels. This is a canonical Gbetagamma effector activity. Supporting Evidence: PMID:23739333 GΞ²Ξ³ by itself is sufficient to activate the GIRK channel PMID:23739333 The GΞ²Ξ³ subunits activate G protein-gated Inward Rectifier K+ (GIRK) channels, causing them to open |
| GO:1903561 extracellular vesicle | HDA PMID:24769233 Proteomic analysis of cerebrospinal fluid extracellular vesi... | KEEP AS NON CORE | Summary: Detected in cerebrospinal fluid extracellular vesicle proteomics (HDA). Reason: Proteomic detection with no known functional significance. Non-core. |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Does Gbeta1 actively hold the open Galpha alpha-helical domain during receptor-catalysed nucleotide exchange? The smFRET study of muOR-Gi suggests the open AHD is affixed against Gbeta, and rhodopsin-transducin structures show the AHD contacting Gbetagamma. If so, is a GO MF term needed for this role beyond 'G-protein alpha-subunit binding'?
Q: Do MRD42 GNB1 variants act mainly by weakening the Galpha interface (giving constitutive Gbetagamma signaling) or by impairing effector binding, and does this differ by residue?
Q: Is 'signaling receptor complex adaptor activity' the best GO MF representation of Gbeta's scaffolding role in the heterotrimer, or would 'G-protein alpha-subunit binding' plus 'G-protein gamma-subunit binding' be more accurate?
Experiment: Mutate the predicted AHD-contacting residues on Gbeta1. In reconstituted muOR-Gi with labelled Galphai AHD, measure smFRET dwell times in the open state and GTPgammaS binding kinetics, comparing wild type and mutant Gbeta1gamma2.
Hypothesis: Gbeta1 surface residues that contact the open Galphai alpha-helical domain stabilise the open AHD state and speed GDP release.
Type: single-molecule FRET
Experiment: Express patient GNB1 variants with Ggamma2 and measure Galphai binding (BRET), basal and agonist-evoked GIRK currents, and PLC-beta activation in heterologous cells and iPSC-derived neurons.
Hypothesis: MRD42-associated GNB1 variants differentially affect Galpha binding versus GIRK/PLC-beta activation.
Type: electrophysiology and BRET
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)