Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The human regulator of G-protein signaling protein 6 gene (RGS6) maps between markers WI-5202 and D14S277 on chromosome 14q24.3.
Regulators of G protein signaling 6 and 7. Purification of complexes with gbeta5 and assessment of their effects on g protein-mediated signaling pathways.
RGS6 interacts with SCG10 and promotes neuronal differentiation. Role of the G gamma subunit-like (GGL) domain of RGS6.
Human RGS6 gene structure, complex alternative splicing, and role of N terminus and G protein gamma-subunit-like (GGL) domain in subcellular localization of RGS6 splice variants.
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RGS6 splice products differ in nuclear/cytoplasmic localization and Gbeta5 association.
"RGS6 protein variants displayed
subcellular distribution patterns ranging from an exclusive cytoplasmic to
exclusive nuclear/nucleolar localization"
Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family.
RGS6/Gβ5 complex accelerates IKACh gating kinetics in atrial myocytes and modulates parasympathetic regulation of heart rate.
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition.
RGS6, but not RGS4, is the dominant regulator of G protein signaling (RGS) modulator of the parasympathetic regulation of mouse heart rate.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
GPCR downstream signalling
G alpha (i):RGS dissociates to inactive G alpha (i)–i1/i2/i3
Active G alpha (i)–i1/i2/i3 binds RGS proteins
G alpha (i)–i1/i2/i3 in G (i):RGS complex is inactivated