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6VU5

Structure of G-alpha-q bound to its chaperone Ric-8A

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0001664molecular_functionG protein-coupled receptor binding
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005096molecular_functionGTPase activator activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005794cellular_componentGolgi apparatus
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007206biological_processphospholipase C-activating G protein-coupled glutamate receptor signaling pathway
B0007208biological_processphospholipase C-activating serotonin receptor signaling pathway
B0007209biological_processphospholipase C-activating tachykinin receptor signaling pathway
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007215biological_processglutamate receptor signaling pathway
B0007218biological_processneuropeptide signaling pathway
B0007596biological_processblood coagulation
B0007603biological_processphototransduction, visible light
B0009649biological_processentrainment of circadian clock
B0009755biological_processhormone-mediated signaling pathway
B0009898cellular_componentcytoplasmic side of plasma membrane
B0010543biological_processregulation of platelet activation
B0016787molecular_functionhydrolase activity
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0031965cellular_componentnuclear membrane
B0032278biological_processpositive regulation of gonadotropin secretion
B0034695biological_processresponse to prostaglandin E
B0042593biological_processglucose homeostasis
B0043303biological_processmast cell degranulation
B0046872molecular_functionmetal ion binding
B0050821biological_processprotein stabilization
B0060828biological_processregulation of canonical Wnt signaling pathway
B0070062cellular_componentextracellular exosome
B0071468biological_processcellular response to acidic pH
B0099524cellular_componentpostsynaptic cytosol
B0160025biological_processsensory perception of itch
B1904181biological_processpositive regulation of membrane depolarization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"29844055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32103024","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32126208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CK2","evidences":[{"source":"PubMed","id":"29844055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32103024","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32126208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3TIR3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P21279","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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