GNB5 encodes the atypical G protein beta subunit Gbeta5, a WD-repeat protein that binds the G gamma-like domains of R7-family RGS proteins. These complexes stabilize their partners and accelerate G alpha inactivation in neuronal, retinal and cardiac signaling. The long retinal product participates in the RGS9-1 phototransduction-regulatory complex, whereas other RGS partners support distinct neuronal and cardiac responses. Gbeta5 can bind selected conventional gamma subunits and form particular experimentally reconstituted heterotrimers, but its predominant native regulatory role is in RGS complexes rather than interchangeable participation in all conventional G protein heterotrimers.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003924 GTPase activity | NAS PMID:9606987 Cloning and tissue distribution of the human G protein beta ... | MODIFY | Summary: Gbeta5 supports the RGS GAP complex but is not itself a guanine-nucleotide-binding GTPase. Reason: The original cloning citation cannot convert a beta subunit into the G alpha catalytic component; refine to the independently demonstrated GAP contribution. Proposed replacements: GTPase activator activity Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0005096 GTPase activator activity | IDA PMID:10521509 Regulators of G protein signaling 6 and 7. Purification of c... | ACCEPT | Summary: Gbeta5 contributes to GAP activity by stabilizing and organizing its R7 RGS partner. Reason: Purified RGS6βGbeta5 complexes and functional analysis of human GNB5 variants support this complex-dependent activity; Gbeta5 is not assigned an independent GTP-hydrolyzing catalytic site. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0005096 GTPase activator activity | IDA PMID:27677260 GNB5 mutation causes a novel neuropsychiatric disorder featu... | ACCEPT | Summary: Gbeta5 contributes to GAP activity by stabilizing and organizing its R7 RGS partner. Reason: Purified RGS6βGbeta5 complexes and functional analysis of human GNB5 variants support this complex-dependent activity; Gbeta5 is not assigned an independent GTP-hydrolyzing catalytic site. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0005515 protein binding | IPI PMID:12606627 Direct interactions between the heterotrimeric G protein sub... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:19376773 Role of molecular chaperones in G protein beta5/regulator of... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:25733868 Comprehensive analysis of heterotrimeric G-protein complex d... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. Reason: The physical interactions are not denied; remove uninformative bare protein binding under the project policy while retaining the specific gamma-subunit, chaperone and GAP-complex functions. |
| GO:0005634 nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: R7BP-dependent trafficking experiments support a nuclear R7βGbeta5 pool, conditional on partner localization and palmitoylation. Reason: The mouse evidence supports a conserved contextual human assignment; it does not imply constitutive nuclear residence in every cell. Supporting Evidence: PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | IDA PMID:10521509 Regulators of G protein signaling 6 and 7. Purification of c... | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814119 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814120 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814121 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6814124 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8850529 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8850534 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8850539 | ACCEPT | Summary: Gbeta5 is an intracellular soluble protein whose RGS complexes have a cytoplasmic/cytosolic pool before or alongside recruitment to membranes. Reason: Purification and partner-dependent localization experiments support these compartments. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:15897264 R7BP binds the R7 subunit of the R7βGΞ²5 complex |
| GO:0005834 heterotrimeric G-protein complex | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the ancestral heterotrimer membership assertion as bounded biochemical capacity. Reason: PMID:9417126 reconstitutes Gbeta5βgamma2HF with Gq, whereas PMID:25733868 finds no beta5 assemblies with Gi1 or GsL in its screen. The latter is not a universal negative. Neither result makes Gbeta5 interchangeable with beta1β4 in native signaling or redefines an RGSβGbeta5 dimer as an alphaβbetaβgamma heterotrimer. Supporting Evidence: PMID:9417126 the beta5gamma2HF dimer bound only alphaq PMID:25733868 combinations consisting of Ξ±i1 or Ξ±sL |
| GO:0005886 plasma membrane | IEA GO_REF:0000107 | ACCEPT | Summary: R7-complex recruitment and immunolocalization establish a plasma-membrane-associated Gbeta5 pool. Reason: Its association depends on partners and does not require Gbeta5 itself to have a membrane-spanning domain. |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: Gbeta5 has a defined role in GPCR signal regulation through R7 RGS complexes. Reason: Refine the generic signal-transduction term to the existing GPCR process rather than retain it merely because it is broad. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: InterPro:IPR016346 SUPPORTS TRANSFER Gbeta5 has a defined role in GPCR signal regulation through R7 RGS complexes. Refine the generic signal-transduction term to the existing GPCR process rather than retain it merely because it is broad. Proposed replacements: G protein-coupled receptor signaling pathway Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0007165 signal transduction | NAS PMID:9606987 Cloning and tissue distribution of the human G protein beta ... | MODIFY | Summary: Gbeta5 has a defined role in GPCR signal regulation through R7 RGS complexes. Reason: Refine the generic signal-transduction term to the existing GPCR process rather than retain it merely because it is broad. Proposed replacements: G protein-coupled receptor signaling pathway Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0007186 G protein-coupled receptor signaling pathway | IDA PMID:10521509 Regulators of G protein signaling 6 and 7. Purification of c... | ACCEPT | Summary: Gbeta5 contributes structural and regulatory work to R7 GAP complexes that terminate GPCR signaling. Reason: This is direct participation despite not itself being the guanine-nucleotide-hydrolyzing subunit. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0007212 G protein-coupled dopamine receptor signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The RGS9/Gbeta5 dopamine-receptor assay in PMID:27677260 demonstrates defective termination with a human disease-associated GNB5 variant. Reason: Retain dopamine signaling as a specific implementation of the broader R7-complex function; the target itself among PAINT descendant evidence is legitimate experimental grounding. Supporting Evidence: PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0007212 G protein-coupled dopamine receptor signaling pathway | IDA PMID:27677260 GNB5 mutation causes a novel neuropsychiatric disorder featu... | KEEP AS NON CORE | Summary: The RGS9/Gbeta5 dopamine-receptor assay in PMID:27677260 demonstrates defective termination with a human disease-associated GNB5 variant. Reason: Retain dopamine signaling as a specific implementation of the broader R7-complex function; the target itself among PAINT descendant evidence is legitimate experimental grounding. Supporting Evidence: PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
| GO:0016020 membrane | IEA GO_REF:0000044 | MODIFY | Summary: Partner-mediated plasma-membrane recruitment is experimentally established and already annotated. Reason: Refine the broad membrane term to plasma membrane; this does not assert that all Gbeta5 is membrane-bound or that other membrane pools are absent. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB-SubCell:SL-0162 SUPPORTS TRANSFER Partner-mediated plasma-membrane recruitment is experimentally established and already annotated. Refine the broad membrane term to plasma membrane; this does not assert that all Gbeta5 is membrane-bound or that other membrane pools are absent. Proposed replacements: plasma membrane |
| GO:0016020 membrane | ISS GO_REF:0000024 | MODIFY | Summary: Partner-mediated plasma-membrane recruitment is experimentally established and already annotated. Reason: Refine the broad membrane term to plasma membrane; this does not assert that all Gbeta5 is membrane-bound or that other membrane pools are absent. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB:P62881 SUPPORTS TRANSFER Partner-mediated plasma-membrane recruitment is experimentally established and already annotated. Refine the broad membrane term to plasma membrane; this does not assert that all Gbeta5 is membrane-bound or that other membrane pools are absent. Proposed replacements: plasma membrane |
| GO:0030159 signaling receptor complex adaptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: Gbeta5 supports assembly and stabilization of R7 RGS signaling complexes. Reason: Structural and biochemical evidence for receptor-associated RGS7βGbeta5 supports the adaptor/scaffold role without claiming Gbeta5 is an autonomous receptor or enzymatic G alpha subunit. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) |
| GO:0030425 dendrite | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse retinal immunofluorescence in PMID:25997951 localizes Gbeta5-containing signaling machinery to ON-bipolar dendritic tips, with cell-type-dependent loss in Lrit3 mutants. Reason: Retain this specific neuronal localization and its conserved human inference; it is not cone-photoreceptor outer-segment evidence. Supporting Evidence: |
| GO:0031682 G-protein gamma-subunit binding | IPI PMID:12606627 Direct interactions between the heterotrimeric G protein sub... | KEEP AS NON CORE | Summary: Direct FRET experiments support Gbeta5 association with gamma2 and gamma13. Reason: The same study finds that a CFP tag creates gamma3 binding absent for untagged gamma3, so retain gamma-subunit binding as a selective capability rather than universal affinity for every gamma isoform. Supporting Evidence: PMID:12606627 Ggamma2 and Ggamma13 |
| GO:0031682 G-protein gamma-subunit binding | IPI PMID:12606627 Direct interactions between the heterotrimeric G protein sub... | KEEP AS NON CORE | Summary: Direct FRET experiments support Gbeta5 association with gamma2 and gamma13. Reason: The same study finds that a CFP tag creates gamma3 binding absent for untagged gamma3, so retain gamma-subunit binding as a selective capability rather than universal affinity for every gamma isoform. Supporting Evidence: PMID:12606627 Ggamma2 and Ggamma13 |
| GO:0042734 presynaptic membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse immunoelectron microscopy localizes RGS7βGbeta5 complexes to peri/extrasynaptic neuronal membranes and to a smaller presynaptic pool; cerebellar work includes parallel-fiber/Purkinje sites. Reason: Retain the anatomical assignments with their native mouse/comparative human scope, not as proof of exclusive active-zone residence. |
| GO:0045202 synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Independent immunolocalization studies place Gbeta5 complexes at neuronal synaptic sites. Reason: This supports synapse localization even though the abstract of the separate SNARE proteomics paper does not identify Gbeta5-specific results; no specific SNARE-binding mechanism is inferred from that abstract. |
| GO:0045211 postsynaptic membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse immunoelectron microscopy localizes RGS7βGbeta5 complexes to peri/extrasynaptic neuronal membranes and to a smaller presynaptic pool; cerebellar work includes parallel-fiber/Purkinje sites. Reason: Retain the anatomical assignments with their native mouse/comparative human scope, not as proof of exclusive active-zone residence. |
| GO:0051087 protein-folding chaperone binding | IPI PMID:19376773 Role of molecular chaperones in G protein beta5/regulator of... | KEEP AS NON CORE | Summary: Gbeta5 interacts with the folding/assembly machinery during RGS-complex biogenesis. Reason: The chaperone-binding assignment describes Gbeta5 as a client/assembly partner, not as a chaperone that catalyzes folding itself. Supporting Evidence: |
| GO:0051286 cell tip | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse retinal immunofluorescence in PMID:25997951 localizes Gbeta5-containing signaling machinery to ON-bipolar dendritic tips, with cell-type-dependent loss in Lrit3 mutants. Reason: Retain this specific neuronal localization and its conserved human inference; it is not cone-photoreceptor outer-segment evidence. Supporting Evidence: |
| GO:0098688 parallel fiber to Purkinje cell synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse immunoelectron microscopy localizes RGS7βGbeta5 complexes to peri/extrasynaptic neuronal membranes and to a smaller presynaptic pool; cerebellar work includes parallel-fiber/Purkinje sites. Reason: Retain the anatomical assignments with their native mouse/comparative human scope, not as proof of exclusive active-zone residence. |
| GO:0098793 presynapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse immunoelectron microscopy localizes RGS7βGbeta5 complexes to peri/extrasynaptic neuronal membranes and to a smaller presynaptic pool; cerebellar work includes parallel-fiber/Purkinje sites. Reason: Retain the anatomical assignments with their native mouse/comparative human scope, not as proof of exclusive active-zone residence. |
| GO:0120199 cone photoreceptor outer segment | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Publisher full text of PMID:11262419 was recovered and inspected. Reason: Methods explicitly stain Gb5 with an antibody recognizing the long/short products, and Fig. 2 compares Gb5 in PNA-labeled cones of wild-type and Rgs9-null mouse retina. This directly supports the mouse cone outer-segment assignment and a qualified conserved human inference; it is not inferred solely from rod or RGS9 localization. Supporting Evidence: url:https://www.molvis.org/molvis/v7/a11/ To stain Gb5, a polyclonal antibody directed against a peptide epitope |
| GO:0120199 cone photoreceptor outer segment | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Publisher full text of PMID:11262419 was recovered and inspected. Reason: Methods explicitly stain Gb5 with an antibody recognizing the long/short products, and Fig. 2 compares Gb5 in PNA-labeled cones of wild-type and Rgs9-null mouse retina. This directly supports the mouse cone outer-segment assignment and a qualified conserved human inference; it is not inferred solely from rod or RGS9 localization. Supporting Evidence: url:https://www.molvis.org/molvis/v7/a11/ To stain Gb5, a polyclonal antibody directed against a peptide epitope |
| GO:1902773 GTPase activator complex | TAS PMID:27677260 GNB5 mutation causes a novel neuropsychiatric disorder featu... | ACCEPT | Summary: Gbeta5 is a physical and functional component of R7 RGS GAP complexes, including the RGS9 complex tested in the human variant study. Reason: This specific complex role is central to its molecular biology. Supporting Evidence: PMID:10521509 act as GTPase-activating proteins specifically toward Galpha(o) PMID:27677260 the S81L mutant form of GΞ²5 has significantly impaired activity in terminating responses that are elicited by dopamine |
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