G alpha (q) signaling events (Homo sapiens)

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307, 14, 43910, 4110, 4125, 33, 3410, 417, 14, 431, 18, 20, 32, 3916, 3124, 38326, 4019227, 14, 4312, 3726cytosolLTC4,LTD4,LTE4 EDN1 GNA11 GNA11 GNB1 ANXA1 GTP Effects of PIP2hydrolysisGNAQ PLCB2 TRH(84-86) PIK3R3 TRH(227-229) GRK5 PLC beta:G alpha(q/11)EDN2 LTE4 NMUR1,NMUR2 MCHR1 FFAR4 GCG(53-81) AVPR1B P2RY1 P2RY6 XCL1 LPAR1,2,3,5 QRFP PGE2 GPR39 BDKRB1 LXA4 Bombesin-like receptor TRH(84-86) HTR2A-C GRPR DecS-GHRL-1(24-51) ARHGEF25 TAC1(58-68) GNRH1(24-33) NMU OPN4 GRPR GNA15 CCK GPR68 PIK3R1 AcCho KISS1(68-121) PMCH(147-165) GNG12 GNB3 GPR143 HCOOH GNA15 PI3K alphaBRS3 F2RL2(22-374) NTS(151-163) SAA1(19-122) GNB2 GNRH1(24-33) GNG5 G-protein alpha(q):GRK5CCL23-2 HCRT(70-97) P2RY1 RGS proteins activefor G alpha (q)PROKR1,PROKR2 ADRA1A TAC3 GNA14 HCRTR2 NPSR1 LTD4 ALA PLCB3 ADRA1D CASR GNA15 HTR2A 5HT GDPF2R(27-425) NPFF(69-76) GRM5 Ca2+ RGS21 GNA14 GPR132 GNA14 RGS2 PTGER1 RGS13 thrombin light chain GHSR H+ HCRT(70-97) PTGER1 EDN1 GNA15 P2RY1 PLCB4 GPRC6A RGS3 EDN2 NPSR1 HTR2B GNA14 CHRM3 G-protein beta:gammasignallingGNRH2(24-33) QRFPR P2RY2 BUT NPFF(69-76) GNG3 GNA14 GNG13 CCKAR,CCKBR LTD4 DDCX NTSR1 NMUR1 P2RY11 RGS4 ARHGEF25 GNB4 F2RL2(22-374) GNB5 CCK NTSR1,NTSR2 G-protein alpha(q):GRK2TRIO HCRTR1 TRH(114-116) NMU GNG11 GNA11 GNA14 RGS4 TRH(152-154) GNA14 RGS21 PTAFR PLCB4 STEA DTTA GNG3 OXTR GRM1 HCRTR1 GNAQ MLN(26-47) PGF2a NMS thrombin light chain PTGFR FFAR2 UTS2 TBXA2R RGZ Ca2+ Pentadecanoic acid NMUR2 H+ Valerate APP(672-713) AcCho ATP LPAR6 GPRC6A ligands GRM5 GNA14 RGZ TBXA2R G-protein alpha(q/11):PI3K alphaADP PMCH(147-165) EDN1 GPR143 EPA PLCB1 RGS1 DHA P2RY10 NPFFR2 F2RL3(18-385) P2RY1 LPAR2 GNA11 CHRM3 GNA11 GNAQ GNRHR Ligand:GPCRcomplexesthatactivateGq/11:Heterotrimeric G-protein Gq (inactive)LPAR5 NMUR1 FFAR1 ELDA QRFPR BDKRB1 LTB4R2 LTE4 LTB4R CCK GRK2 11,14,17-eicosatrienoic acid HTR2A PLCB2 GLA GNG11 DPA GNG10 H+ thrombin heavy chain NPFFR1 GNG13 ADRA1B GNG8 TRH(227-229) CCKBR HCRTR2 O-octanoyl-L-serine-GHRL-1(24-50) CYSLTR1 GNA14 GRK5G alpha (q):GTP:RGSGNAQ ADRA1A F2RL2(22-374) GPR17 RGS2 GNA15 GNG11 LTC4 HRH1 GPR17 5HT RGS19 GNA11 GAST(76-92) CCKBR PALM ANXA1 TRH(84-86) CH3COO- CYSLTR1 GNAQ GTP LPAR6 Hist NMS Active BTK P2RY6 ADR, NAd DHA GNA15 CASR UTP GTP HCRT(34-66) GNGT1 GnRH receptor APP(672-713) NPS GPR39 NPS OXT(20-28) LPAR4 GPR39 EtCOO- or C2H5COO- TACR1 DPA NMB(47-56) RGZ RGS16 F2R(27-425) GTP LPA GHSR GNG2 ADRA1B ADRA1B OPN4 TRH(152-154) AVPR1B Zn2+ NMUR1 NPS Zn2+ TACR3 HCRT(70-97) DecS-GHRL-1(24-50) GNA15 ALA NAd FFAR3 GNB5 LPAR1 TRHR UDP GNG2 G-protein alpha(q/11):GDPKISS1R CYSLTR2 GPR4 GRP(24-50) GPR17 PIK3R1 XCR1 CYSLTR2 GNA11 GNG7 LTE4 AVP(20-28) PLCB4 KISS1R HeterotrimericG-protein Gq/11(inactive)HXA LTD4 BTK FPR2 L-Glu Hist RGS18 LPAR2 GHSR PIK3CA GPR132 CHRM1 PROK2 GNB3 TRH(114-116) CCKAR DTTA FFAR2 PALM CCKBR OPN4 PLCB3 GCG(53-81) GNG10 GNB4 SAA1(19-122) RGS5 NPFFR1 PTAFR Bradykinin GNAQ DPA GNG13 GNA15 TAC3 PTAFR XCL1,XCL2 ALA F2RL1(37-397) P2RY11 thrombin heavy chain 5HT GNA11 GTP HCRTR2 LXA4 ADRA1A PROKR1 GRP(24-50) GNA15 MYSA F2RL3(18-385) GNAQ CHRM5 KALRN PAF GRM1 TACR2 GNB3 GNAQ LPAR5 HTR2B PLCB2 ATP BDKRB2 PIK3R3 thrombin light chain GNRH ligands AGTR1 GNAQ GPRC6A GNG12 DecS-GHRL-1(24-50) UDP HCOOH MLNR CCL23-2 GNA14 Bombesin-like peptide GNAQ TRH(152-154) FFAR1 ligands GNRH1(24-33) Bradykinin O-octanoyl-L-serine-GHRL-1(24-50) GNAQ GTP AVPR1B NMU Ligand:GPCRcomplexesthatactivateGq/11:Heterotrimeric G-protein Gq (active)GNGT2 GNA14 GDP EDNRB HXA TRIO family RhoGEFsAVPR1A UTS2R XCL1 RGS18 MCHR2 GNA11 NMS TACR1 GPR65 TXA2 PTGFR P2RY10 GRK2CCK PTGER1 GNRH2(24-33) HTR2C Basic L-amino acids NTSR2 EPA GPR68 GNG7 GPR4 TRH(186-188) QRFPR RGS17 TAC3 GNGT1 EDN3(97-117) UTS2R LTB4 HTR2C CCL23-2 ELDA GPR17 LTC4 PI(4,5)P2 thrombin light chain TAC3 GPR39 L-Glu F2RL3(18-385) TAC1(98-107) FFAR2 GNG4 GNA11 LPAR4 LTB4R CYSLTR1 FFAR2 EtCOO- or C2H5COO- Photon LTC4:CyslTR1,2Active BTKPLCB1 PROK2 DAG EtCOO- or C2H5COO- PLCB1 GNA11 PLC-beta:G-alpha(q/11):DAG:IP3ADP Valerate CCKAR PTGFR TACR2 AGT(34-41) HCRT(70-97) OXT(20-28) GNB2 GNRHR2 GRPR L-Glu TAC1(98-107) CHRM3 LTC4 GPRC6A PLC-beta:G-alpha(q/11):PIP2GNB3 GPR132 NTSR2 CCKBR XCL2 Hist HCOOH GNRHR2 LTB4 TRHR GPCRs that activateGq/11LTB4R TXA2 HRH1 LPA UTS2B GNGT2 RGS4 DecS-GHRL-1(24-51) CHRM1 DTTA 5HT Ligand:GPCRcomplexes thatactivate Gq/11FFAR3 APP(672-713) GNG12 P2RY2 TRH(227-229) ADR Ligands of GPCRsthat activate Gq/11TRH(135-137) NMBR FFAR4 PTGFR TACR3 GPR68 CYSLTR2 AcCho GTP DecS-GHRL-1(24-50) PIK3R2 EDNRA GNB4 L-Dopa PROK2 Photon DDCX NTSR2 XCL2 NMBR OXTR UDP RGS2 8,11,14-Eicosatrienoic acid LTB4R2 AGT(34-41) GNA15 GAST(76-92) AcCho CYSLTR1 GTPActive Gq:Active BTKMT-RNR2 PMCH(147-165) AVP(20-28) GNA14 QRFP PiAVPR1A,B G-protein beta-gammacomplexSTEA GNG13 PROK1 LPAR5 GAST(76-92) GNG8 FFAR1 HCRTR1 OXT(20-28) PIK3CA GNA14 PGF2a TAC1(98-107) NTS(151-163) GTP LPA P2RY2 LXA4 ADP P2RY10 GCG(53-81) AGTR1 ADRA1A,B,D Ca2+ BUT GNG5 11,14,17-eicosatrienoic acid QRFP GRP(24-50) UTS2B 11,14,17-eicosatrienoic acid NPSR1 TACR2 MLN(26-47) PGF2a Bradykinin GNGT2 MT-RNR2 AGT(34-41) Pmoa RGS18 MCHR1,MCHR2 GNG3 UTS2B ANXA1 ELDA GNG2 CHRM1, 3, 5 HRH1 PLCB3 RGS17 NTS(151-163) LPAR4 RGS19 PGE2 RGS13 Zn2+ GRM1,GRM5 TRH(114-116) MLNR FPR2 TACR3 PROKR1 L-Glu XCL1 NAd LPAR4 PGF2a UTS2,UTS2B NMUR2 Basic L-amino acids CCKAR LPAR6 ATP F2RL1(37-397) O-octanoyl-L-serine-GHRL-1(24-51) PALM GNA11 PIK3R2 H+ RGS18 Pentadecanoic acid GNRHR BUT FFAR3 ligands EDN3(97-117) GDP GRM5 NTSR1 GNGT2 GNRH2(24-33) NTS(151-163) LPAR3 NMS FPR2 ligands PROK1 RGS1,2,3,4,5,13,16,17,18,19,21UTS2R KISS1(68-121) NPFFR1 pH sensing receptors LTB4R2 DecS-GHRL-1(24-51) GNG7 GNA15 PLCB3 MLNR TAC1(58-68) CHRM5 QRFPR GAST(76-92) MLN(26-47) GPR4 CYSLTR2 Photon Pmoa NMBR EDNRB TAC1(58-68) I(1,4,5)P3 XCR1 RGS3 CHRM1 F2RL1(37-397) FFAR1 TRH(135-137) UTP GCG(53-81) NMUR2 Zn2+ RGS17 GPR65 AVP(20-28) TRH(186-188) GNG4 NPFFR2 LPA PLCB2 TACR2 TRHR GPRC6A AGTR1 RGS3 NAd L-Dopa MLNR PGE2 GTP Pentadecanoic acid TACR3 RGS1 KISS1R HCRT(34-66) GNA14 L-Dopa FFAR1 EPA MCHR2 MYSA EDNRA PTGER1 RGS5 RGS21 OXTR GNB1 GLA FFAR3 EDN3(97-117) XCR1 KISS1R Pmoa BRS3 ATP NPFF(69-76) NTSR1 LTC4 TACR1 GNAQ P2RY11 GDP OLEA LPAR1 PAF GNG2 HCRT(34-66) ADRA1D GNB5 NMUR2 BDKRB2 MCHR2 NMU RGS1 LTB4 PROK1 GNA15 LPAR1 GNAQ EDNRB GNRHR GLA PAF GNG12 TRH Gastrin-CREBsignalling pathwayvia PKC and MAPKP2RY6 UDP GNAQ GNB5 LTB4 BDKRB1 PTAFR ADRA1D LPAR3 ADR FFAR2 ligands ADR GNG7 NPFFR1,NPFFR2 PGE2 NPS RGS13 Active Gq:BTKCASR PLC-betaAGT(34-41) LPAR3 Hist P2RY10 Ca2+ GNB2 GNRHR2 SAA1(19-122) GNG8 L-Dopa GNAQ STEA EDNRA UTS2 BDKRB2 TXA2 EDNRA,EDNRB GNA15 FFAR4 P2RY6 LTB4R,LTB4R2 OXT(20-28) FFAR4 GNG4 Acyl Ghrelin GNA11 NPSR1 GNB4 RGS5 BTKTRH(186-188) O-octanoyl-L-serine-GHRL-1(24-51) KALRN GNG3 XCR1 thrombin heavy chain MYSA GNA14 GNB1 GNGT1 GHSR MT-RNR2 PMCH(147-165) GNA14 LPAR2 NPFF(69-76) GNGT1 CH3COO- O-octanoyl-L-serine-GHRL-1(24-51) G-protein alpha(q/11): GTPQRFP AVPR1A KISS1(68-121) GNA11 UTP FFAR4 ligands Endothelin GNG5 GNA15 GRM1 HXA FPR2 RGS19 GPR143 TACR1 8,11,14-Eicosatrienoic acid GPR65 GNG10 HCRT(34-66) TXA2 PAF F2R(27-425) GNAQ GNG4 PROKR1 Valerate KISS1(68-121) GNG5 CH3COO- LPAR6 AGTR1 HCRTR2 P2RY11 RGS16 PLCB1 DDCX OXTR UTS2 GDP CHRM5 TRH(135-137) TAC1(98-107) PLCB4 FFAR3 FPR2 G-protein alpha(q/11):Trio familyRhoGEFsGNA15 EDN2 MCHR1 AVP(20-28) GTP GTP TBXA2R GNA15 thrombin heavy chain NMB(47-56) GNB2 HTR2B HTR2A PROKR2 OLEA OLEA 8,11,14-Eicosatrienoic acid MLN(26-47) PROKR2 RGSL1 HRH1 HCRTR1 TRHR DHA RGS21 NMB(47-56) Proteinase-activated receptors Photon GNB1 GNA11 O-octanoyl-L-serine-GHRL-1(24-50) GNA11 XCL2 RGS19 TRIO RGS2 GNG10 CYSLTR2 TBXA2R G alpha (q):GDP:RGSAVPR1A NPFFR2 TAC1(58-68) CASR BRS3 RGS3 GPR143 PROKR2 Basic L-amino acids P2RY2 GNG11 GNG8 ADP PROK1,PROK2 HTR2C RGS16 Bradykinin MCHR1 Bradykinin receptor UTS2R OPN4 GTP 13, 291113, 2921, 2313, 29213, 2913, 2913, 29355, 8, 17, 2715, 36, 424, 28213, 29313, 29


Description

The classic signalling route for G alpha (q) is activation of phospholipase C beta thereby triggering phosphoinositide hydrolysis, calcium mobilization and protein kinase C activation. This provides a path to calcium-regulated kinases and phosphatases, GEFs, MAP kinase cassettes and other proteins that mediate cellular responses ranging from granule secretion, integrin activation, and aggregation in platelets. Gq participates in many other signalling events including direct interaction with RhoGEFs that stimulate RhoA activity and inhibition of PI3K. Both in vitro and in vivo, the G-protein Gq seems to be the predominant mediator of the activation of platelets. Moreover, G alpha (q) can stimulate the activation of Burton tyrosine kinase (Ma Y C et al. 1998). Regulator of G-protein Signalling (RGS) proteins can regulate the activity of G alpha (z) (Soundararajan M et al. 2008). View original pathway at Reactome.

Comments

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Pathway is converted from Reactome ID: 416476
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Reactome version: 74
Reactome Author 
Reactome Author: Jupe, Steve

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Bibliography

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History

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CompareRevisionActionTimeUserComment
116409view09:05, 7 May 2021EweitzModified title
113243view11:31, 2 November 2020ReactomeTeamReactome version 74
101713view14:51, 1 November 2018DeSlOntology Term : 'G protein mediated signaling pathway via Galphaq family' added !
101370view11:26, 1 November 2018ReactomeTeamreactome version 66
100908view21:01, 31 October 2018ReactomeTeamreactome version 65
100449view19:35, 31 October 2018ReactomeTeamreactome version 64
100273view16:57, 31 October 2018ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
11,14,17-eicosatrienoic acid MetaboliteCHEBI:53460 (ChEBI)
5HT MetaboliteCHEBI:28790 (ChEBI)
8,11,14-Eicosatrienoic acid MetaboliteCHEBI:53486 (ChEBI)
ADP MetaboliteCHEBI:456216 (ChEBI)
ADR MetaboliteCHEBI:28918 (ChEBI)
ADR, NAd R-ALL-390627 (Reactome)
ADRA1A ProteinP35348 (Uniprot-TrEMBL)
ADRA1A,B,D R-HSA-390684 (Reactome)
ADRA1B ProteinP35368 (Uniprot-TrEMBL)
ADRA1D ProteinP25100 (Uniprot-TrEMBL)
AGT(34-41) ProteinP01019 (Uniprot-TrEMBL)
AGTR1 ProteinP30556 (Uniprot-TrEMBL)
ALA MetaboliteCHEBI:27432 (ChEBI)
ANXA1 ProteinP04083 (Uniprot-TrEMBL)
APP(672-713) ProteinP05067 (Uniprot-TrEMBL)
ARHGEF25 ProteinQ86VW2 (Uniprot-TrEMBL)
ATP MetaboliteCHEBI:30616 (ChEBI)
AVP(20-28) ProteinP01185 (Uniprot-TrEMBL)
AVPR1A ProteinP37288 (Uniprot-TrEMBL)
AVPR1A,B R-HSA-388458 (Reactome)
AVPR1B ProteinP47901 (Uniprot-TrEMBL)
AcCho MetaboliteCHEBI:15355 (ChEBI)
Active BTK ProteinQ06187 (Uniprot-TrEMBL)
Active BTKProteinQ06187 (Uniprot-TrEMBL)
Active Gq:Active BTKComplexR-HSA-8964303 (Reactome)
Active Gq:BTKComplexR-HSA-8964296 (Reactome)
Acyl Ghrelin R-HSA-422096 (Reactome)
BDKRB1 ProteinP46663 (Uniprot-TrEMBL)
BDKRB2 ProteinP30411 (Uniprot-TrEMBL)
BRS3 ProteinP32247 (Uniprot-TrEMBL)
BTK ProteinQ06187 (Uniprot-TrEMBL)
BTKProteinQ06187 (Uniprot-TrEMBL)
BUT MetaboliteCHEBI:30772 (ChEBI)
Basic L-amino acids R-ALL-420746 (Reactome)
Bombesin-like peptide R-HSA-375360 (Reactome)
Bombesin-like receptor R-HSA-375362 (Reactome)
Bradykinin ProteinP01042 (Uniprot-TrEMBL)
Bradykinin receptor R-HSA-374323 (Reactome)
CASR ProteinP41180 (Uniprot-TrEMBL)
CCK ProteinP06307 (Uniprot-TrEMBL)
CCKAR ProteinP32238 (Uniprot-TrEMBL)
CCKAR,CCKBR R-HSA-388518 (Reactome)
CCKBR ProteinP32239 (Uniprot-TrEMBL)
CCL23-2 ProteinP55773-2 (Uniprot-TrEMBL)
CH3COO- MetaboliteCHEBI:15366 (ChEBI)
CHRM1 ProteinP11229 (Uniprot-TrEMBL)
CHRM1, 3, 5 R-HSA-390660 (Reactome)
CHRM3 ProteinP20309 (Uniprot-TrEMBL)
CHRM5 ProteinP08912 (Uniprot-TrEMBL)
CYSLTR1 ProteinQ9Y271 (Uniprot-TrEMBL)
CYSLTR2 ProteinQ9NS75 (Uniprot-TrEMBL)
Ca2+ MetaboliteCHEBI:29108 (ChEBI)
DAG MetaboliteCHEBI:17815 (ChEBI)
DDCX MetaboliteCHEBI:30805 (ChEBI)
DHA MetaboliteCHEBI:28125 (ChEBI)
DPA MetaboliteCHEBI:53488 (ChEBI)
DTTA MetaboliteCHEBI:53487 (ChEBI)
DecS-GHRL-1(24-50) ProteinQ9UBU3-1 (Uniprot-TrEMBL)
DecS-GHRL-1(24-51) ProteinQ9UBU3-1 (Uniprot-TrEMBL)
EDN1 ProteinP05305 (Uniprot-TrEMBL)
EDN2 ProteinP20800 (Uniprot-TrEMBL)
EDN3(97-117) ProteinP14138 (Uniprot-TrEMBL)
EDNRA ProteinP25101 (Uniprot-TrEMBL)
EDNRA,EDNRB R-HSA-388547 (Reactome)
EDNRB ProteinP24530 (Uniprot-TrEMBL)
ELDA MetaboliteCHEBI:27997 (ChEBI)
EPA MetaboliteCHEBI:28364 (ChEBI)
Effects of PIP2 hydrolysisPathwayR-HSA-114508 (Reactome) Hydrolysis of phosphatidyl inositol-bisphosphate (PIP2) by phospholipase C (PLC) produces diacylglycerol (DAG) and inositol triphosphate (IP3). Both are potent second messengers. IP3 diffuses into the cytosol, but as DAG is a hydrophobic lipid it remains within the plasma membrane. IP3 stimulates the release of calcium ions from the smooth endoplasmic reticulum, while DAG activates the conventional and unconventional protein kinase C (PKC) isoforms, facilitating the translocation of PKC from the cytosol to the plasma membrane. The effects of DAG are mimicked by tumor-promoting phorbol esters. DAG is also a precursor for the biosynthesis of prostaglandins, the endocannabinoid 2-arachidonoylglycerol and an activator of a subfamily of TRP-C (Transient Receptor Potential Canonical) cation channels 3, 6, and 7.
Endothelin R-HSA-388544 (Reactome)
EtCOO- or C2H5COO- MetaboliteCHEBI:30768 (ChEBI)
F2R(27-425) ProteinP25116 (Uniprot-TrEMBL) This is the inactive form of the receptor, before protease activation. Proteinase (protease) activated receptors are activated by the cleavage of an N-terminal extracellular segment by serine proteases, particularly thrombin which activates PAR1, 3 and 4. The cleaved fragment is an activating ligand for the receptor; synthetic peptide mimics of the N-terminal fragment can activate uncleaved receptors.
F2RL1(37-397) ProteinP55085 (Uniprot-TrEMBL) This is the inactive form of the receptor, before protease activation. Proteinase (protease) activated receptors are activated by the cleavage of an N-terminal extracellular segment by serine proteases, particularly thrombin which activates PAR1, 3 and 4. The cleaved fragment is an activating ligand for the receptor; synthetic peptide mimics of the N-terminal fragment can activate uncleaved receptors.
F2RL2(22-374) ProteinO00254 (Uniprot-TrEMBL) This is the inactive form of the receptor, before protease activation. Proteinase (protease) activated receptors are activated by the cleavage of an N-terminal extracellular segment by serine proteases, particularly thrombin which activates PAR1, 3 and 4. The cleaved fragment is an activating ligand for the receptor; synthetic peptide mimics of the N-terminal fragment can activate uncleaved receptors.
F2RL3(18-385) ProteinQ96RI0 (Uniprot-TrEMBL) This is the inactive form of the receptor, before protease activation. Proteinase (protease) activated receptors are activated by the cleavage of an N-terminal extracellular segment by serine proteases, particularly thrombin which activates PAR1, 3 and 4. The cleaved fragment is an activating ligand for the receptor; synthetic peptide mimics of the N-terminal fragment can activate uncleaved receptors.
FFAR1 ProteinO14842 (Uniprot-TrEMBL)
FFAR1 ligands R-ALL-400427 (Reactome)
FFAR2 ProteinO15552 (Uniprot-TrEMBL)
FFAR2 ligands R-ALL-444210 (Reactome)
FFAR3 ProteinO14843 (Uniprot-TrEMBL)
FFAR3 ligands R-ALL-444074 (Reactome)
FFAR4 ProteinQ5NUL3 (Uniprot-TrEMBL)
FFAR4 ligands R-ALL-400551 (Reactome)
FPR2 ProteinP25090 (Uniprot-TrEMBL)
FPR2 ligands R-HSA-444472 (Reactome)
G alpha (q):GDP:RGSComplexR-HSA-8982013 (Reactome)
G alpha (q):GTP:RGSComplexR-HSA-8982027 (Reactome)
G-protein alpha (q):GRK2ComplexR-HSA-416515 (Reactome)
G-protein alpha (q):GRK5ComplexR-HSA-416517 (Reactome)
G-protein alpha (q/11): GTPComplexR-HSA-114534 (Reactome)
G-protein alpha (q/11):GDPComplexR-HSA-114556 (Reactome)
G-protein alpha (q/11):PI3K alphaComplexR-HSA-416356 (Reactome)
G-protein alpha

(q/11):Trio family

RhoGEFs
ComplexR-HSA-400608 (Reactome)
G-protein beta-gamma complexComplexR-HSA-167434 (Reactome)
G-protein beta:gamma signallingPathwayR-HSA-397795 (Reactome) The classical role of the G-protein beta/gamma dimer was believed to be the inactivation of the alpha subunit, Gbeta/gamma was viewed as a negative regulator of Galpha signalling. It is now known that Gbeta/gamma subunits can directly modulate many effectors, including some also regulated by G alpha.
GAST(76-92) ProteinP01350 (Uniprot-TrEMBL)
GCG(53-81) ProteinP01275 (Uniprot-TrEMBL)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GHSR ProteinQ92847 (Uniprot-TrEMBL)
GLA MetaboliteCHEBI:28661 (ChEBI)
GNA11 ProteinP29992 (Uniprot-TrEMBL)
GNA14 ProteinO95837 (Uniprot-TrEMBL)
GNA15 ProteinP30679 (Uniprot-TrEMBL)
GNAQ ProteinP50148 (Uniprot-TrEMBL)
GNB1 ProteinP62873 (Uniprot-TrEMBL)
GNB2 ProteinP62879 (Uniprot-TrEMBL)
GNB3 ProteinP16520 (Uniprot-TrEMBL)
GNB4 ProteinQ9HAV0 (Uniprot-TrEMBL)
GNB5 ProteinO14775 (Uniprot-TrEMBL)
GNG10 ProteinP50151 (Uniprot-TrEMBL)
GNG11 ProteinP61952 (Uniprot-TrEMBL)
GNG12 ProteinQ9UBI6 (Uniprot-TrEMBL)
GNG13 ProteinQ9P2W3 (Uniprot-TrEMBL)
GNG2 ProteinP59768 (Uniprot-TrEMBL)
GNG3 ProteinP63215 (Uniprot-TrEMBL)
GNG4 ProteinP50150 (Uniprot-TrEMBL)
GNG5 ProteinP63218 (Uniprot-TrEMBL)
GNG7 ProteinO60262 (Uniprot-TrEMBL)
GNG8 ProteinQ9UK08 (Uniprot-TrEMBL)
GNGT1 ProteinP63211 (Uniprot-TrEMBL)
GNGT2 ProteinO14610 (Uniprot-TrEMBL)
GNRH ligands R-HSA-873938 (Reactome)
GNRH1(24-33) ProteinP01148 (Uniprot-TrEMBL)
GNRH2(24-33) ProteinO43555 (Uniprot-TrEMBL)
GNRHR ProteinP30968 (Uniprot-TrEMBL)
GNRHR2 ProteinQ96P88 (Uniprot-TrEMBL)
GPCRs that activate Gq/11ComplexR-HSA-791493 (Reactome)
GPR132 ProteinQ9UNW8 (Uniprot-TrEMBL)
GPR143 ProteinP51810 (Uniprot-TrEMBL)
GPR17 ProteinQ13304 (Uniprot-TrEMBL)
GPR39 ProteinO43194 (Uniprot-TrEMBL)
GPR4 ProteinP46093 (Uniprot-TrEMBL)
GPR65 ProteinQ8IYL9 (Uniprot-TrEMBL)
GPR68 ProteinQ15743 (Uniprot-TrEMBL)
GPRC6A ProteinQ5T6X5 (Uniprot-TrEMBL)
GPRC6A ligands R-ALL-420706 (Reactome)
GRK2 ProteinP25098 (Uniprot-TrEMBL)
GRK2ProteinP25098 (Uniprot-TrEMBL)
GRK5 ProteinP34947 (Uniprot-TrEMBL)
GRK5ProteinP34947 (Uniprot-TrEMBL)
GRM1 ProteinQ13255 (Uniprot-TrEMBL)
GRM1,GRM5 R-HSA-420566 (Reactome)
GRM5 ProteinP41594 (Uniprot-TrEMBL)
GRP(24-50) ProteinP07492 (Uniprot-TrEMBL)
GRPR ProteinP30550 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
Gastrin-CREB

signalling pathway

via PKC and MAPK
PathwayR-HSA-881907 (Reactome) Gastrin is a hormone whose main function is to stimulate secretion of hydrochloric acid by the gastric mucosa, which results in gastrin formation inhibition. This hormone also acts as a mitogenic factor for gastrointestinal epithelial cells. Gastrin has two biologically active peptide forms, G34 and G17.Gastrin gene expression is upregulated in both a number of pre-malignant conditions and in established cancer through a variety of mechanisms. Depending on the tissue where it is expressed and the level of expression, differential processing of the polypeptide product leads to the production of different biologically active peptides. In turn, acting through the classical gastrin cholecystokinin B receptor CCK-BR, its isoforms and alternative receptors, these peptides trigger signalling pathways which influence the expression of downstream genes that affect cell survival, angiogenesis and invasion (Wank 1995, de Weerth et al. 1999, Grabowska & Watson 2007)
GnRH receptor R-HSA-391368 (Reactome)
H+ MetaboliteCHEBI:15378 (ChEBI)
HCOOH MetaboliteCHEBI:30751 (ChEBI)
HCRT(34-66) ProteinO43612 (Uniprot-TrEMBL)
HCRT(70-97) ProteinO43612 (Uniprot-TrEMBL)
HCRTR1 ProteinO43613 (Uniprot-TrEMBL)
HCRTR2 ProteinO43614 (Uniprot-TrEMBL)
HRH1 ProteinP35367 (Uniprot-TrEMBL)
HTR2A ProteinP28223 (Uniprot-TrEMBL)
HTR2A-C R-HSA-391030 (Reactome)
HTR2B ProteinP41595 (Uniprot-TrEMBL)
HTR2C ProteinP28335 (Uniprot-TrEMBL)
HXA MetaboliteCHEBI:17120 (ChEBI)
Heterotrimeric

G-protein Gq/11

(inactive)
ComplexR-HSA-114557 (Reactome)
Hist MetaboliteCHEBI:18295 (ChEBI)
I(1,4,5)P3 MetaboliteCHEBI:16595 (ChEBI)
KALRN ProteinO60229 (Uniprot-TrEMBL)
KISS1(68-121) ProteinQ15726 (Uniprot-TrEMBL)
KISS1R ProteinQ969F8 (Uniprot-TrEMBL)
L-Dopa MetaboliteCHEBI:15765 (ChEBI)
L-Glu MetaboliteCHEBI:29985 (ChEBI)
LPA MetaboliteCHEBI:52288 (ChEBI)
LPAR1 ProteinQ92633 (Uniprot-TrEMBL)
LPAR1,2,3,5 R-HSA-419369 (Reactome)
LPAR2 ProteinQ9HBW0 (Uniprot-TrEMBL)
LPAR3 ProteinQ9UBY5 (Uniprot-TrEMBL)
LPAR4 ProteinQ99677 (Uniprot-TrEMBL)
LPAR5 ProteinQ9H1C0 (Uniprot-TrEMBL)
LPAR6 ProteinP43657 (Uniprot-TrEMBL)
LTB4 MetaboliteCHEBI:15647 (ChEBI)
LTB4R ProteinQ15722 (Uniprot-TrEMBL)
LTB4R,LTB4R2 R-HSA-416401 (Reactome)
LTB4R2 ProteinQ9NPC1 (Uniprot-TrEMBL)
LTC4 MetaboliteCHEBI:16978 (ChEBI)
LTC4,LTD4,LTE4 R-ALL-416372 (Reactome)
LTC4:CyslTR1,2ComplexR-HSA-9664302 (Reactome)
LTD4 MetaboliteCHEBI:28666 (ChEBI)
LTE4 MetaboliteCHEBI:15650 (ChEBI)
LXA4 MetaboliteCHEBI:6498 (ChEBI)
Ligand:GPCR

complexes that activate

Gq/11:Heterotrimeric G-protein Gq (active)
ComplexR-HSA-749447 (Reactome)
Ligand:GPCR

complexes that activate

Gq/11:Heterotrimeric G-protein Gq (inactive)
ComplexR-HSA-749451 (Reactome)
Ligand:GPCR

complexes that

activate Gq/11
ComplexR-HSA-380110 (Reactome)
Ligands of GPCRs that activate Gq/11ComplexR-HSA-791492 (Reactome)
MCHR1 ProteinQ99705 (Uniprot-TrEMBL)
MCHR1,MCHR2 R-HSA-947667 (Reactome)
MCHR2 ProteinQ969V1 (Uniprot-TrEMBL)
MLN(26-47) ProteinP12872 (Uniprot-TrEMBL)
MLNR ProteinO43193 (Uniprot-TrEMBL)
MT-RNR2 ProteinQ8IVG9 (Uniprot-TrEMBL)
MYSA MetaboliteCHEBI:28875 (ChEBI)
NAd MetaboliteCHEBI:18357 (ChEBI)
NMB(47-56) ProteinP08949 (Uniprot-TrEMBL)
NMBR ProteinP28336 (Uniprot-TrEMBL)
NMS ProteinQ5H8A3 (Uniprot-TrEMBL)
NMU ProteinP48645 (Uniprot-TrEMBL)
NMUR1 ProteinQ9HB89 (Uniprot-TrEMBL)
NMUR1,NMUR2 R-HSA-964805 (Reactome)
NMUR2 ProteinQ9GZQ4 (Uniprot-TrEMBL)
NPFF(69-76) ProteinO15130 (Uniprot-TrEMBL)
NPFFR1 ProteinQ9GZQ6 (Uniprot-TrEMBL)
NPFFR1,NPFFR2 R-HSA-389406 (Reactome)
NPFFR2 ProteinQ9Y5X5 (Uniprot-TrEMBL)
NPS ProteinP0C0P6 (Uniprot-TrEMBL)
NPSR1 ProteinQ6W5P4 (Uniprot-TrEMBL)
NTS(151-163) ProteinP30990 (Uniprot-TrEMBL)
NTSR1 ProteinP30989 (Uniprot-TrEMBL)
NTSR1,NTSR2 R-HSA-388917 (Reactome)
NTSR2 ProteinO95665 (Uniprot-TrEMBL)
O-octanoyl-L-serine-GHRL-1(24-50) ProteinQ9UBU3-1 (Uniprot-TrEMBL)
O-octanoyl-L-serine-GHRL-1(24-51) ProteinQ9UBU3-1 (Uniprot-TrEMBL)
OLEA MetaboliteCHEBI:16196 (ChEBI)
OPN4 ProteinQ9UHM6 (Uniprot-TrEMBL)
OXT(20-28) ProteinP01178 (Uniprot-TrEMBL)
OXTR ProteinP30559 (Uniprot-TrEMBL)
P2RY1 ProteinP47900 (Uniprot-TrEMBL)
P2RY10 ProteinO00398 (Uniprot-TrEMBL)
P2RY11 ProteinQ96G91 (Uniprot-TrEMBL)
P2RY2 ProteinP41231 (Uniprot-TrEMBL)
P2RY6 ProteinQ15077 (Uniprot-TrEMBL)
PAF MetaboliteCHEBI:52450 (ChEBI)
PALM MetaboliteCHEBI:15756 (ChEBI)
PGE2 MetaboliteCHEBI:15551 (ChEBI)
PGF2a MetaboliteCHEBI:15553 (ChEBI)
PI(4,5)P2 MetaboliteCHEBI:18348 (ChEBI)
PI3K alphaComplexR-HSA-198379 (Reactome)
PIK3CA ProteinP42336 (Uniprot-TrEMBL)
PIK3R1 ProteinP27986 (Uniprot-TrEMBL)
PIK3R2 ProteinO00459 (Uniprot-TrEMBL)
PIK3R3 ProteinQ92569 (Uniprot-TrEMBL)
PLC beta:G alpha (q/11)ComplexR-HSA-398158 (Reactome)
PLC-beta:G-alpha(q/11):DAG:IP3ComplexR-HSA-8983509 (Reactome)
PLC-beta:G-alpha(q/11):PIP2ComplexR-HSA-8983508 (Reactome)
PLC-betaComplexR-HSA-111854 (Reactome)
PLCB1 ProteinQ9NQ66 (Uniprot-TrEMBL)
PLCB2 ProteinQ00722 (Uniprot-TrEMBL)
PLCB3 ProteinQ01970 (Uniprot-TrEMBL)
PLCB4 ProteinQ15147 (Uniprot-TrEMBL)
PMCH(147-165) ProteinP20382 (Uniprot-TrEMBL)
PROK1 ProteinP58294 (Uniprot-TrEMBL)
PROK1,PROK2 R-HSA-444692 (Reactome)
PROK2 ProteinQ9HC23 (Uniprot-TrEMBL)
PROKR1 ProteinQ8TCW9 (Uniprot-TrEMBL)
PROKR1,PROKR2 R-HSA-444628 (Reactome)
PROKR2 ProteinQ8NFJ6 (Uniprot-TrEMBL)
PTAFR ProteinP25105 (Uniprot-TrEMBL)
PTGER1 ProteinP34995 (Uniprot-TrEMBL)
PTGFR ProteinP43088 (Uniprot-TrEMBL)
Pentadecanoic acid MetaboliteCHEBI:42504 (ChEBI)
Photon MetaboliteCHEBI:30212 (ChEBI)
PiMetaboliteCHEBI:43474 (ChEBI)
Pmoa MetaboliteCHEBI:28716 (ChEBI)
Proteinase-activated receptors R-HSA-389458 (Reactome)
QRFP ProteinP83859 (Uniprot-TrEMBL)
QRFPR ProteinQ96P65 (Uniprot-TrEMBL)
RGS proteins active for G alpha (q)ComplexR-HSA-921123 (Reactome)
RGS1 ProteinQ08116 (Uniprot-TrEMBL)
RGS1,2,3,4,5,13,16,17,18,19,21ComplexR-HSA-8982302 (Reactome)
RGS13 ProteinO14921 (Uniprot-TrEMBL)
RGS16 ProteinO15492 (Uniprot-TrEMBL)
RGS17 ProteinQ9UGC6 (Uniprot-TrEMBL)
RGS18 ProteinQ9NS28 (Uniprot-TrEMBL)
RGS19 ProteinP49795 (Uniprot-TrEMBL)
RGS2 ProteinP41220 (Uniprot-TrEMBL)
RGS21 ProteinQ2M5E4 (Uniprot-TrEMBL)
RGS3 ProteinP49796 (Uniprot-TrEMBL)
RGS4 ProteinP49798 (Uniprot-TrEMBL)
RGS5 ProteinO15539 (Uniprot-TrEMBL)
RGSL1 ProteinA5PLK6 (Uniprot-TrEMBL)
RGZ MetaboliteCHEBI:50122 (ChEBI)
SAA1(19-122) ProteinP0DJI8 (Uniprot-TrEMBL)
STEA MetaboliteCHEBI:9254 (ChEBI)
TAC1(58-68) ProteinP20366 (Uniprot-TrEMBL)
TAC1(98-107) ProteinP20366 (Uniprot-TrEMBL)
TAC3 ProteinQ9UHF0 (Uniprot-TrEMBL)
TACR1 ProteinP25103 (Uniprot-TrEMBL)
TACR2 ProteinP21452 (Uniprot-TrEMBL)
TACR3 ProteinP29371 (Uniprot-TrEMBL)
TBXA2R ProteinP21731 (Uniprot-TrEMBL)
TRH R-HSA-444529 (Reactome)
TRH(114-116) ProteinP20396 (Uniprot-TrEMBL)
TRH(135-137) ProteinP20396 (Uniprot-TrEMBL)
TRH(152-154) ProteinP20396 (Uniprot-TrEMBL)
TRH(186-188) ProteinP20396 (Uniprot-TrEMBL)
TRH(227-229) ProteinP20396 (Uniprot-TrEMBL)
TRH(84-86) ProteinP20396 (Uniprot-TrEMBL)
TRHR ProteinP34981 (Uniprot-TrEMBL)
TRIO ProteinO75962 (Uniprot-TrEMBL)
TRIO family RhoGEFsComplexR-HSA-399963 (Reactome)
TXA2 MetaboliteCHEBI:15627 (ChEBI)
UDP MetaboliteCHEBI:17659 (ChEBI)
UTP MetaboliteCHEBI:15713 (ChEBI)
UTS2 ProteinO95399 (Uniprot-TrEMBL)
UTS2,UTS2B R-HSA-445115 (Reactome)
UTS2B ProteinQ765I0 (Uniprot-TrEMBL)
UTS2R ProteinQ9UKP6 (Uniprot-TrEMBL)
Valerate MetaboliteCHEBI:31011 (ChEBI)
XCL1 ProteinP47992 (Uniprot-TrEMBL)
XCL1,XCL2 R-HSA-373356 (Reactome)
XCL2 ProteinQ9UBD3 (Uniprot-TrEMBL)
XCR1 ProteinP46094 (Uniprot-TrEMBL)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
pH sensing receptors R-HSA-444736 (Reactome)
thrombin heavy chain ProteinP00734 (Uniprot-TrEMBL)
thrombin light chain ProteinP00734 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
Active BTKArrowR-HSA-8964340 (Reactome)
Active Gq:Active BTKArrowR-HSA-8964284 (Reactome)
Active Gq:Active BTKR-HSA-8964340 (Reactome)
Active Gq:BTKArrowR-HSA-8964280 (Reactome)
Active Gq:BTKR-HSA-8964284 (Reactome)
BTKR-HSA-8964280 (Reactome)
G alpha (q):GDP:RGSArrowR-HSA-8982025 (Reactome)
G alpha (q):GDP:RGSR-HSA-8982026 (Reactome)
G alpha (q):GTP:RGSArrowR-HSA-8982017 (Reactome)
G alpha (q):GTP:RGSR-HSA-8982025 (Reactome)
G alpha (q):GTP:RGSmim-catalysisR-HSA-8982025 (Reactome)
G-protein alpha (q):GRK2ArrowR-HSA-416516 (Reactome)
G-protein alpha (q):GRK5ArrowR-HSA-416510 (Reactome)
G-protein alpha (q/11): GTPArrowR-HSA-749452 (Reactome)
G-protein alpha (q/11): GTPArrowR-HSA-8964340 (Reactome)
G-protein alpha (q/11): GTPR-HSA-398188 (Reactome)
G-protein alpha (q/11): GTPR-HSA-400586 (Reactome)
G-protein alpha (q/11): GTPR-HSA-416358 (Reactome)
G-protein alpha (q/11): GTPR-HSA-416510 (Reactome)
G-protein alpha (q/11): GTPR-HSA-416516 (Reactome)
G-protein alpha (q/11): GTPR-HSA-418582 (Reactome)
G-protein alpha (q/11): GTPR-HSA-8964280 (Reactome)
G-protein alpha (q/11): GTPR-HSA-8982017 (Reactome)
G-protein alpha (q/11): GTPmim-catalysisR-HSA-418582 (Reactome)
G-protein alpha (q/11):GDPArrowR-HSA-418582 (Reactome)
G-protein alpha (q/11):GDPArrowR-HSA-8982026 (Reactome)
G-protein alpha (q/11):GDPR-HSA-750993 (Reactome)
G-protein alpha (q/11):PI3K alphaArrowR-HSA-416358 (Reactome)
G-protein alpha

(q/11):Trio family

RhoGEFs
ArrowR-HSA-400586 (Reactome)
G-protein beta-gamma complexArrowR-HSA-749452 (Reactome)
G-protein beta-gamma complexR-HSA-750993 (Reactome)
GDPArrowR-HSA-379048 (Reactome)
GPCRs that activate Gq/11ArrowR-HSA-749452 (Reactome)
GRK2R-HSA-416516 (Reactome)
GRK5R-HSA-416510 (Reactome)
GTPR-HSA-379048 (Reactome)
Heterotrimeric

G-protein Gq/11

(inactive)
ArrowR-HSA-750993 (Reactome)
Heterotrimeric

G-protein Gq/11

(inactive)
R-HSA-749448 (Reactome)
LTC4:CyslTR1,2mim-catalysisR-HSA-379048 (Reactome)
Ligand:GPCR

complexes that activate

Gq/11:Heterotrimeric G-protein Gq (active)
ArrowR-HSA-379048 (Reactome)
Ligand:GPCR

complexes that activate

Gq/11:Heterotrimeric G-protein Gq (active)
R-HSA-749452 (Reactome)
Ligand:GPCR

complexes that activate

Gq/11:Heterotrimeric G-protein Gq (inactive)
ArrowR-HSA-749448 (Reactome)
Ligand:GPCR

complexes that activate

Gq/11:Heterotrimeric G-protein Gq (inactive)
R-HSA-379048 (Reactome)
Ligand:GPCR

complexes that

activate Gq/11
R-HSA-749448 (Reactome)
Ligands of GPCRs that activate Gq/11ArrowR-HSA-749452 (Reactome)
PI3K alphaR-HSA-416358 (Reactome)
PLC beta:G alpha (q/11)ArrowR-HSA-398188 (Reactome)
PLC beta:G alpha (q/11)mim-catalysisR-HSA-114688 (Reactome)
PLC-beta:G-alpha(q/11):DAG:IP3ArrowR-HSA-114688 (Reactome)
PLC-beta:G-alpha(q/11):PIP2R-HSA-114688 (Reactome)
PLC-betaR-HSA-398188 (Reactome)
PiArrowR-HSA-8982025 (Reactome)
R-HSA-114688 (Reactome) Phospholipase C (PLC) isozymes are a group of related proteins that cleave the polar head group from inositol phospholipids, typically in response to signals from cell surface receptors. They hydrolyze the highly phosphorylated lipid phosphatidylinositol 4,5-bisphosphate (PIP2) generating two products: inositol 1,4,5-trisphosphate (IP3), a universal calcium-mobilizing second messenger, and diacylglycerol (DAG), an activator of protein kinase C. PLC-beta isoforms are regulated by heterotrimeric GTP-binding proteins. PLC-beta 1 and 3 are widely expressed, with the highest concentrations found in (differing) specific regions of the brain. PLC-beta 2 is expressed at highest levels in cells of hematopoeitic origin; it is involved in leukocyte signaling and host defense. PLC-beta 4 is highly concentrated in cerebellar Purkinje and granule cells, the median geniculate body, whose axons terminate in the auditory cortex, and the lateral geniculate nucleus, where most retinal axons terminate in a visuotopic representation of each half of the visual field.
R-HSA-379048 (Reactome) G alpha q protein (or Gq/11) consists of four family members (G-alpha 11, -alpha 14, -alpha 15 and -alpha q). It activates phospholipase C (PLC) (Dowal L et al, 2006). PLC hydrolyzes phosphatidylinositol (PIP2) to diacyl glycerol (DAG) and inositol triphosphate (IP3). DAG acts as a second messenger that activates protein kinase C (PKC) and IP3 can bind to IP3 receptors, particular calcium channels in the endoplasmic reticulum (ER). Calcium flow causes the cytosolic concentration of calcium to increase, causing a cascade of intracellular changes and activity.
R-HSA-398188 (Reactome) The active form of G protein alpha subunit q (Gq-alpha) was found to activate phospholipase C beta-1 (PLC-beta1), in investigations using bovine membranes. Subsequently, all 4 human isoforms have been shown to be activated by Gq, though activation of PLCbeta-4 is limited. In recombinant assays, several activated rat G alpha q family members were found to stimulate human PLC-beta isoforms with the same rank order of decreasing potency. PLC-beta1 stimulation was slightly more than for PLC-beta3; PLC-beta3 stimulation was 10-fold greater than for beta-2. PLC-beta2 is expressed specifically in hematopoietic cells. PLC-beta acts directly on Gq to accelerate hydrolysis of bound GTP, thus PLC-betas are GTPase activating proteins (GAPs). The crystal structure of the C-terminal region from Turkey PLC-beta, revealed a novel fold composed almost entirely of three long helices forming a coiled-coil that dimerizes along its long axis in an antiparallel orientation. The extent of the dimer interface and gel exclusion chromatography data suggest that PLC-betas are functionally dimeric.
R-HSA-400586 (Reactome) The Trio family of RhoA guanine nucleotide exchange factors (RhoGEFs) are directly activated by G alpha (q), possibly within a Gq:Trio:RhoA signalling complex, thereby linking Gq to RhoA-mediated processes such as cell migration, proliferation, and contraction. Like most other RhoGEFs, they have a tandem motif consisting of a Dbl homology (DH) and a pleckstrin homology (PH) domain. Trio and Duet have a number of other domains including an immunoglobin domains that may be involved in interacting with Rho, but the considerably smaller GEFT (p63RhoGEF) does not have any identifiable additional domains yet appears to be sufficient to mediate the activation of RhoA by G alpha (q). The structure represented by GEFT is proposed to represent the core of an ancient signal transduction pathway.
R-HSA-416358 (Reactome) Phospholipase C activation is the classical signalling route for G alpha (q) but an additional mechanism is an inhibitory interaction between G alpha (q) and phosphatidylinositol 3-kinase alpha (PI3K alpha). There are several PI3K subtypes but only the p85 alpha/p110 alpha subtype (PI3K alpha) is a G alpha (q) effector (PMID: 18515384). Activated G alpha (q) inhibits PI3K alpha directly, in a GTP-dependent manner. G alpha(q) binding of PI3K competes with Ras, a PI3K activator (PMID: 16268778).
R-HSA-416510 (Reactome) GRKs are serine/threonine kinases that phosphorylate GPCRs leading to receptor desensitization. GRK5 appears to be the predominant regulator of PAR1 desensitization in endothelial cells.
R-HSA-416516 (Reactome) GRK2 can inhibit GPCR signaling via phosphorylation-independent sequestration of Gq/11/14 subunits utilising its RGS homology (RH) domain. GRK2 may be an effector of activated Gq, initiating signalling cascades other than the classical PLC beta signalling associated with Gq.
R-HSA-418582 (Reactome) When a ligand activates a G protein-coupled receptor, it induces a conformational change in the receptor (a change in shape) that allows the receptor to function as a guanine nucleotide exchange factor (GEF), stimulating the exchange of GDP for GTP on the G alpha subunit. In the traditional view of heterotrimeric protein activation, this exchange triggers the dissociation of the now active G alpha subunit from the beta:gamma dimer, initiating downstream signalling events. The G alpha subunit has intrinsic GTPase activity and will eventually hydrolyze the attached GTP to GDP, allowing reassociation with G beta:gamma. Additional GTPase-activating proteins (GAPs) stimulate the GTPase activity of G alpha, leading to more rapid termination of the transduced signal. In some cases the downstream effector may have GAP activity, helping to deactivate the pathway. This is the case for phospholipase C beta, which possesses GAP activity within its C-terminal region (Kleuss et al. 1994).
R-HSA-749448 (Reactome) Numerous functionally unrelated GPCRs couple with the Gq G-protein subtype.
R-HSA-749452 (Reactome) The classical view of G-protein signalling is that the G-protein alpha subunit dissociates from the beta:gamma dimer. Activated G alpha (q) and the beta:gamma dimer then participate in separate signaling cascades. Although G protein dissociation has been contested (e.g. Bassi et al. 1996), recent in vivo experiments have demonstrated that dissociation does occur, though possibly not to completion (Lambert 2008).
R-HSA-750993 (Reactome) The classical model of G-protein signaling suggests that the G-protein dissociates upon GPCR activation. The active G alpha (q) subunit then participates in signaling, until its intrinsic GTPase activity degrades the bound GTP to GDP. The inactive G alpha (q):GDP complex has much higher affinity for the G beta:gamma complex and consequently reassociates.
R-HSA-8964280 (Reactome) G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15) can bind directly to the THSH3 domain of the non-receptor Tyrosine-protein kinase BTK in vitro and in vivo. This binding results in a conformational change in BTK, which leads to its activation. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.
R-HSA-8964284 (Reactome) G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15) can bind directly to the non-receptor Tyrosine-protein kinase BTK. This binding breaks intramolecular interactions in BTK thereby making the kinase domain available for substrates. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.
R-HSA-8964340 (Reactome) G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15) can bind to the non-receptor Tyrosine-protein kinase BTK. This binding results in a conformational change in BTK. Subsequently, the structurally modified BTK is released from GNAQ and is now catalytically active. Active BTK can trigger the downstream MAPK p38 pathway. Physiologically, BTK plays a key role in B lymphocyte development, differentiation and signalling.
R-HSA-8982017 (Reactome) G Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins (G proteins). Upon activation, GPCRs can replace the GDP with GTP in the alpha subunit of G proteins. GTP binding modifies the conformation of G alpha proteins and activates them. The Regulator of G protein Signalling (RGS) are GTPase Accelerating Proteins (GAPs) that can directly inhibit the G alpha subunit activity. There are at least 25 different types of RGS proteins known. Several of these RGS proteins (1, 2, 3, 4, 5, 8, 13, 16, 17, 18, 19, 21) can bind and stabilize the transition state for GTP hydrolysis of Guanine nucleotide binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15). Subsequently, this leads to GTP hydrolysis and inactivation of G alpha (q) and terminating downstream signalling (Neubig RR and Siderovski DP et al. 2002, Kach J et al., 2012). The primary function of G alpha (q) is activation of phospholipase C beta thereby triggering phosphoinositide hydrolysis, calcium mobilization and protein kinase C activation.
R-HSA-8982025 (Reactome) G Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins (G proteins). Upon activation, GPCRs can replace the GDP with GTP in the alpha subunit of G proteins. GTP binding modifies the conformation of G alpha proteins and activates them. The Regulator of G protein Signalling (RGS) are GTPase Accelerating Proteins (GAPs) that can directly inhibit the G alpha subunit activity. There are at least 25 different types of RGS proteins known. Several of these RGS proteins (1, 2, 3, 4, 5, 8, 13, 16, 17, 18, 19, 21) can bind and stabilize the transition state of Guanine nucleotide binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15). Following this, the RGS domain of the proteins exert GAP activity on G alpha (q) and allosterically modulate residues within G-alpha subunit to accelerate the intrinsic GTPase activity that hydrolyses GTP to GDP. This inactivates G alpha (q) and terminates downstream signalling (Neubig & Siderovski 2002, Kach et al. 2012). The primary function of G alpha (q) is activation of phospholipase C beta thereby triggering phosphoinositide hydrolysis, calcium mobilization and protein kinase C activation.
R-HSA-8982026 (Reactome) G Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins (G proteins). Upon activation, GPCRs can replace the GDP with GTP in the alpha subunit of G proteins. GTP binding modifies the conformation of G alpha proteins and activates them. The Regulator of G protein Signalling (RGS) are GTPase Accelerating Proteins (GAPs) that can directly inhibit the G alpha subunit activity. There are at least 25 different types of RGS proteins known. Several of these RGS proteins (1, 2, 3, 4, 5, 8, 13, 16, 17, 18, 19, 21) can bind and stabilize the transition state of Guanine nucleotide binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15). Subsequently, the RGS domain in the complex facilitates the hydrolyses of G alpha (q):GTP to G alpha (q):GDP. Following this, the complex dissociates releasing inactive G alpha (q) (Neubig & Siderovski 2002, Kach et al. 2012). The primary function of G alpha (q) is activation of phospholipase C beta thereby triggering phosphoinositide hydrolysis, calcium mobilization and protein kinase C activation.
RGS proteins active for G alpha (q)ArrowR-HSA-418582 (Reactome)
RGS1,2,3,4,5,13,16,17,18,19,21ArrowR-HSA-8982026 (Reactome)
RGS1,2,3,4,5,13,16,17,18,19,21R-HSA-8982017 (Reactome)
TRIO family RhoGEFsR-HSA-400586 (Reactome)
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