Anti-inflammatory response favouring Leishmania parasite infection (Homo sapiens)

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771, 42, 712747, 48, 58, 67, 72...4438, 74, 8664, 81, 825518, 22, 40, 9538, 74, 86255910, 46, 65, 9313, 21, 41, 51, 62...25, 29443, 6, 28, 43, 4533, 704, 5, 23, 9235, 49, 74, 75, 8612, 39, 53, 6660, 79261, 37, 769, 3133, 70, 838516, 24, 34, 7336, 63, 79578, 50, 69, 87, 888, 11, 15, 17, 20...2, 947, 19, 528461, 891, 42, 71nucleoplasmMacrophagecytosolGolgi lumenT-cellcytosolcytosolendoplasmic reticulum lumenendoplasmic reticulum lumenLeishmania parasitenucleoplasmADAM17(215-827) Ig lambda chain V-I region HA IGLV2-18(1-?) p-Y160,Y171-CD3G IGLV11-55(1-?) Ig heavy chain V-II region NEWM Ig lambda chain V-III region SH PRKAR2B Ig kappa chain V-I region HK101 Ig lambda chain V-VI region AR IGLV5-45(1-?) IGKV2D-30 TAAR3 INSL3(106-131) DRD5 Ig heavy chain V-III region BRO IGLV3-22(1-?) ADCY7 SCT GNB5 IGKV3D-20 IGKVA18(21-?) sCD163:MYH9IGLV4-60(1-?) IGLV8-61(1-?) VIPR2 Ig heavy chain V-III region BRO p-T180,Y182-MAPK14 Ig heavy chain V-III region DOB Ig heavy chain V-II region WAH Ig heavy chain V-II region OU IGKV3D-20 Ig lambda chain V-I region VOR GNAS1 Ig kappa chain V-I region Gal Ig heavy chain V-II region ARH-77 IGLV4-3(1-?) IGLV2-33(1-?) Ig lambda chain V-II region BOH Ig kappa chain V-II region FR IGLV10-54(1-?) Ig lambda chain V-I region NEWM Ig heavy chain V-II region MCE IGLV2-11(1-?) Ig lambda chain V-IV region Bau ATPADCY7 IGHG3 IGKVA18(21-?) Protein Kinase A,catalytic subunitsIGLV2-23(1-?) FCGRIIIA:CD3G/CD3ZdimersIg lambda chain V-II region BOH IGHG1 Ig heavy chain V-I region HG3 IGLV3-25(1-?) IGHG3 IGKV1-12 GNB1 GNB5 Lma amastigotesurfaceIg kappa chain V-I region BAN PRKACA,(PRKACB,PRKACG,PRKX)VIP(125-152) Ig heavy chain V-III region TRO CRHR2 Ig lambda chain V-IV region Bau IGLV3-12(1-?) Ig kappa chain V-II region FR IGLV3-25(1-?) IGHG3 Ig heavy chain V-II region NEWM Ig kappa chain V region EV15 Ig heavy chain V-II region MCE GNGT1 PLK2, MAPK14IGLV7-46(1-?) IGKV2-28 IGLV1-36(1-?) IGLC6 Ig heavy chain V-III region BRO GNG8 Ig lambda chain V-II region TOG GNGT1 ADAM17Ig kappa chain V-I region AU IGLV11-55(1-?) ADPIg heavy chain V-I region EU IGLV2-11(1-?) Ig lambda chain V-VI region AR LPG1G2 IGLV1-40(1-?) Ig heavy chain V-II region ARH-77 IGLV7-46(1-?) GPHB5 IGLV8-61(1-?) Ig lambda chain V-IV region Bau Ig kappa chain V-I region AU IGKV3D-20 IGLV7-46(1-?) Ig kappa chain V-II region FR IL6IGKC IGLV2-18(1-?) Ig heavy chain V-III region DOB IGLV3-27(1-?) IGLV4-3(1-?) Ig kappa chain V-I region DEE Ig lambda chain V-IV region Kern Ca2+GNB3 ADCY9 Ig lambda chain V-IV region Bau IGLV4-60(1-?) IGLV1-36(1-?) IGLC3 IGKVA18(21-?) GNB2 IGLV3-16(1-?) GNG4 IGKC IGLV3-22(1-?) IGHV1-2 IGLV4-69(1-?) IgG:Lma antigensNAD+ IGLV4-60(1-?) RXFP2 Ig kappa chain V-I region HK101 iRHOM2IGLV4-69(1-?) iRHOM2LPG1G2 IGLV2-33(1-?) GNG12 Ig lambda chain V-II region TOG IGLV8-61(1-?) Ig lambda chain V-II region MGC IGHG1 RXFP1 Ig kappa chain V-III region POM IGKV2D-30 FSHB IGLV1-36(1-?) IGKV1-12 IGLC7 ADORA2B cAMP:PKA regulatorysubunitIg kappa chain V-I region AU IL10 geneIg lambda chain V-II region TOG Ig kappa chain V-II region RPMI 6410 Ig kappa chain V-III region POM Ig kappa chain V-II region FR CALCR IGLC1 Ig kappa chain V-I region HK101 Ig lambda chain V-I region HA ADCY1 GNG5 IGHG3 IGKV2-28 Ig lambda chain V-IV region Kern ADCY4 PPiIg kappa chain V-II region FR FCGR3A FCGR3A IGLC2 Ig lambda chain V-IV region Bau IGLV3-25(1-?) Ade-Rib IGLC7 Ig heavy chain V-I region HG3 TAAR8 IGLC6 p-6Y-CD247 IGLV2-33(1-?) TAAR2 IGKV3D-20 IGLV10-54(1-?) IGLV(23-?) IGHG4 IGLV7-46(1-?) ITPR1 GNAI1 IGLV3-16(1-?) I(1,4,5)P3ADCY9 G-protein alpha(i):GTP:AdenylatecyclaseIGLV4-69(1-?) IGLV3-22(1-?) IGLV3-22(1-?) IGLV2-11(1-?) Ig heavy chain V-II region WAH 5HT GNG13 GNGT1 IGLV11-55(1-?) IGLV1-40(1-?) Ig kappa chain V-I region BAN ADAM17(215-827)DPEP2 IGLV2-23(1-?) Ig lambda chain V-I region VOR IGLC3 GNG4 IGLV11-55(1-?) Ig heavy chain V-III region KOL ADORA2B:Ade-Rib:Heterotrimeric G-protein Gs:GTPIg lambda chain V-IV region Kern IGHV7-81(1-?) ADCY1 Ig heavy chain V-I region HG3 GNG7 GTP Ig kappa chain V-I region AU IGLC2 Ig kappa chain V-I region AU IGLV7-43(1-?) IgG:Lmaantigens:FCGR3A:CD3dimersp-S,T-ADAM17(215-827):Zn2+IGKV2-28 GNB5 Ig kappa chain V-I region BAN ADAM17IgGIg kappa chain V-III region B6 Ig lambda chain V-II region NEI Ig kappa chain V region EV15 Ig heavy chain V-III region DOB Ig heavy chain V-II region ARH-77 IGLC1 IGLV8-61(1-?) Ig lambda chain V-II region MGC IGLV4-3(1-?) GNB3 VIPR1 IGKV4-1(21-?) ADCY4 Ig heavy chain V-III region JON IGLV3-27(1-?) GNB2 IGLV7-46(1-?) POMC(217-234) IGHV7-81(1-?) PRKACB IGLV4-60(1-?) ADCY2 IgG:Leishmaniasurface:p-FCGR3A:p-6Y-SYK:p-3Y-PLCGTSHB Ig lambda chain V-II region TOG ITPR:I(1,4,5)P3tetramerIGHV1-2 Ig kappa chain V-II region Cum IGKVA18(21-?) IgH heavy chain V-III region VH26 precursor Ig lambda chain V-II region MGC IGKV4-1(21-?) ADCY6 PLK2 IGLV2-23(1-?) IGKV1-12 Ig heavy chain V-III region TRO IGLV4-69(1-?) IGLV3-25(1-?) IGHV(1-?) IGLV3-25(1-?) IGLV1-44(1-?) Ig heavy chain V-III region KOL IgG:Lma amastigotesurfaceIGKV3D-20 p-Y288,Y304-FCGR2A IGLC6 IGLV2-11(1-?) Ig heavy chain V-II region OU Ig lambda chain V-III region SH Ig heavy chain V-III region BUT Ig kappa chain V-I region AG Ig heavy chain V-II region OU IGLV1-40(1-?) Ig kappa chain V-III region POM Ig heavy chain V-III region TRO IGKC RLN3(26-52) p-6Y-SYK IGKC IGKV1-5(23-?) Ig kappa chain V region EV15 Ig kappa chain V-II region FR GNG10 ITPR1 Ig lambda chain V region 4A Antigen IGLC7 ADCY7 IGLV5-37(1-?) Ig kappa chain V-I region BAN GNB1 IGLV3-25(1-?) IGLV2-33(1-?) IGLV7-43(1-?) LPG1G2GNAI2 IGLV(23-?) H2OIGHG2 Ig kappa chain V-I region AU IGHV7-81(1-?) Ig lambda chain V-I region NEWM Ig heavy chain V-III region CAM Ig heavy chain V-III region BRO Ig lambda chain V-IV region Kern Ig lambda chain V-II region BOH GDP IGLV3-25(1-?) Ig heavy chain V-III region BUT Ig heavy chain V-III region TRO IGKV2-28 GGT1(1-380) Ig lambda chain V-IV region Bau Ig lambda chain V-II region NEI ADORA2B ADCY2 Ig heavy chain V-III region BUT Ig lambda chain V-I region NEW ADCYAP1(82-129) IGLC1 IGHG3 MC3R(1-360) GNGT2 GNG3 IGLV3-27(1-?) IGLV5-45(1-?) ADCY9 Ig kappa chain V region EV15 IGLV7-46(1-?) IGHG2 Ig kappa chain V-III region VG IGLV5-45(1-?) IGHV7-81(1-?) ADCY5 IL6 gene GNG4 Ig heavy chain V-II region ARH-77 IGLV4-69(1-?) GTP PLCG1 Ade-Rib IGHV(1-?) Mg2+ Ig heavy chain V-I region HG3 IGLV10-54(1-?) Ig kappa chain V-I region DEE Ig heavy chain V-II region OU FURINLma amastigote surface Ade-Rib:ADORA2B:Heterotrimeric G-protein Gs:GDPIg kappa chain V-III region B6 IGLC7 IGKV1-12 IGLV2-23(1-?) Ig heavy chain V-I region EU Ig heavy chain V-II region MCE SRC-1 IGLC3 Ig kappa chain V-III region POM IGHV7-81(1-?) Ig kappa chain V-III region VG Ig heavy chain V-I region HG3 ADCY3 CALCA(83-119) GNG5 PRKACG Ig kappa chain V-I region DEE LPG1G2 Ig lambda chain V-IV region Hil IGLV5-45(1-?) P2RY11 GNB1 IGHG2 Ig kappa chain V-II region RPMI 6410 Ig kappa chain V-II region Cum Ig heavy chain V-II region MCE IGKV2D-30 IGLV4-60(1-?) p-6Y-SYK Ig heavy chain V-III region WEA IGLV3-12(1-?) IGLV5-37(1-?) Ig kappa chain V-I region DEE IGLC2 Ig lambda chain V-II region BOH Ig kappa chain V-I region Wes MC2R CALCA(83-119) IGLV(23-?) IGKC MYH9Ig lambda chain V-IV region Hil ADORA2B IGLV1-40(1-?) sCD163 IGLV3-22(1-?) Ig heavy chain V-I region HG3 p-Y160,Y171-CD3G ADCY5 Ig heavy chain V-III region JON Ig heavy chain V-III region BUT DRD1 Ig heavy chain V-III region JON IGKV1-12 Ig lambda chain V-IV region Hil GNB1 IGHG4 RLN2(162-185) GNB4 Ig kappa chain V-III region VG IGKC IGLC1 GNAI3 IGLV7-43(1-?) Ig heavy chain V-II region NEWM IGLV4-60(1-?) PRKAR1B IGLV3-12(1-?) IGKV3D-20 Ig heavy chain V-III region WEA GNG10 GNG4 IGLV2-23(1-?) Ig heavy chain V-III region KOL Ig kappa chain V-III region VG Ig heavy chain V-III region JON PRKACA Ig heavy chain V-III region WEA Ig heavy chain V-III region TRO PRKAR1B sCD163IGLV2-18(1-?) IGLC2 Ig heavy chain V-I region HG3 Hist Ig kappa chain V-II region Cum PRKACG G-protein alpha(z):GTP:AdenylatecyclasePTGIR TAAR1 Ig kappa chain V-I region Gal Ig kappa chain V-I region HK101 IGLV4-60(1-?) IGLV4-3(1-?) Ig lambda chain V-I region NEW IGKVA18(21-?) IGLV4-3(1-?) Ig heavy chain V-II region OU p-6Y-CD247 Ig kappa chain V-I region Daudi Ig kappa chain V region EV15 Ig lambda chain V-II region BOH IGLV1-40(1-?) Ig heavy chain V-II region WAH GCG(146-178) GNG2 IGLC2 DPEP1 Ig kappa chain V-I region AG IGLC2 IGLV8-61(1-?) IGLC3 IGKV1-12 Ig heavy chain V-II region MCE Ig heavy chain V-I region HG3 p-Y753,Y759,Y1217-PLCG2 IgH heavy chain V-III region VH26 precursor IGKV4-1(21-?) IGLV4-69(1-?) NPSR1 p-4Y-PLCG1 Ig lambda chain V-II region TOG IGLV(23-?) Mg2+ ADAM17(215-827):Zn2+Ig heavy chain V-III region WEA Ig kappa chain V-I region AG MC4R IGLV1-36(1-?) IGHG1 IL6 geneIg kappa chain V-I region Daudi IGKV2D-30 Ig heavy chain V-III region BUT PPiI(1,4,5)P3 IGKV1-12 IGKV1-12 Zn2+ Ig lambda chain V-II region BOH PRKAR1A IGHG1 IGLV7-46(1-?) Ig kappa chain V-III region B6 FGR IGLV10-54(1-?) GPR39 Ig lambda chain V-III region SH Ig heavy chain V-III region JON ADCY2 ITPR2 Ig kappa chain V-III region B6 IGHG2 RAMP2 GNGT1 GNAS2 IGLV10-54(1-?) Ig kappa chain V-III region B6 Ig kappa chain V-I region AU IgH heavy chain V-III region VH26 precursor Ig lambda chain V-IV region Hil IGLV3-25(1-?) Ig heavy chain V-I region EU Ig kappa chain V-III region VG ADCY7 Ig heavy chain V-II region MCE IGLC7 IGHV7-81(1-?) YES1 IGLV3-27(1-?) IGHG2 Ig lambda chain V-II region MGC p-6Y-SYK IgH heavy chain V-III region VH26 precursor IGLV1-36(1-?) Ig kappa chain V-I region AG GNAT3 IgG:Lmaantigens:FCGR3A:p-CD3 dimersIg heavy chain V-III region CAM Zn2+ Ig lambda chain V-III region LOI PRKX H2OGNGT2 Ig lambda chain V-VI region AR Ig heavy chain V-III region TRO IGLV3-27(1-?) Ig heavy chain V-III region CAM GNG8 ADCYAP1(132-158) Ig lambda chain V-I region VOR IGKV2-28 Ig kappa chain V-III region VG IGLV1-40(1-?) ITPR2 IgH heavy chain V-III region VH26 precursor ADCY2 Ig kappa chain V region EV15 IGKV3D-20 Ig heavy chain V-III region CAM IGLV3-16(1-?) IGHV(1-?) ADRB1 Ig heavy chain V-III region TRO GNB3 PTGER2 GNG3 p-PLCGIGKV4-1(21-?) IGLV1-40(1-?) IGLV2-11(1-?) HRH2 Ig lambda chain V region 4A IGHV1-2 IGKV1-12 IGLC6 G-betagammaIg kappa chain V-III region POM IGLV7-43(1-?) Ig kappa chain V-III region B6 IGKC IGHV(1-?) Ig kappa chain V-II region RPMI 6410 PGE2 PI(4,5)P2Ig lambda chain V-IV region Kern Ig kappa chain V-I region Gal Ig lambda chain V-III region LOI GNG13 Ig kappa chain V-II region RPMI 6410 Ig lambda chain V-II region MGC LPG1G2 Constitutively active orphan GPCRs p-Y160,Y171-CD3G Ig heavy chain V-II region ARH-77 IgH heavy chain V-III region VH26 precursor IGLV5-37(1-?) Ig lambda chain V-IV region Hil GNG3 IGLV1-36(1-?) Ig lambda chain V-VI region AR FCGR3A IGLC6 glucocorticoid DPEP3 PI(3,4,5)P3 IGLC1 IGLV3-12(1-?) ATPIg kappa chain V-I region Wes IGLV2-33(1-?) Ig heavy chain V-II region OU Ig heavy chain V-II region NEWM IGLV10-54(1-?) IGLV8-61(1-?) Mg2+ Ig heavy chain V-III region WEA IGLV2-18(1-?) IGKVA18(21-?) IGLV7-46(1-?) Ig lambda chain V-I region NEWM Ig heavy chain V-III region WEA PLCG1 Ig kappa chain V-II region Cum CRHR1 Ig kappa chain V-II region RPMI 6410 IGHV(1-?) IGKC Ig heavy chain V-II region MCE ADCY3 IGHV(1-?) Ig heavy chain V-III region BRO IGKV1-5(23-?) PLCG2 GNG8 GNG10 IGLV2-11(1-?) Ig heavy chain V-III region WEA ADCY1 IGKV2D-30 IGKV4-1(21-?) Ig lambda chain V-II region TOG Ig kappa chain V-I region DEE IGLV2-18(1-?) CD247-1 GNGT2 IGHG2 Ig lambda chain V-IV region Bau Ig kappa chain V-I region Wes LCHA Ig kappa chain V-I region Gal GGT1(1-380) Ig lambda chain V-I region VOR HCK Lma amastigote surface Ligand:GPCRcomplexes thatactivateGs:HeterotrimericG-protein Gs(inactive)Ig heavy chain V-III region BRO Ig heavy chain V-III region KOL IGLV(23-?) IGLV3-27(1-?) ADORA2A Ig heavy chain V-III region BUT IGLV4-3(1-?) Ig heavy chain V-I region EU PLCG2 Ig lambda chain V region 4A IGLV(23-?) Ig heavy chain V-I region EU GNG3 ADCY6 IGLV2-11(1-?) GGT1, 5 dimersIg lambda chain V-VI region AR IGLV5-45(1-?) Ig lambda chain V-II region MGC IGLV11-55(1-?) PEA IGKV1-5(23-?) Ig lambda chain V-I region VOR Ig lambda chain V-II region BOH Ig kappa chain V region EV15 FSHR Ig heavy chain V-II region OU IGLC1 IGKVA18(21-?) Ig lambda chain V-II region NEI IGLV1-44(1-?) IGLV8-61(1-?) Ig kappa chain V-I region Wes Ig lambda chain V-III region LOI Ig heavy chain V-II region OU Ig heavy chain V-II region OU IGLV7-46(1-?) IGLC6 IGHG1 Ig kappa chain V-I region Gal IGKV3D-20 Ig kappa chain V-I region Daudi G alpha(s):GTP:AdenylatecyclaseMYH9 Ig kappa chain V-III region POM IGLV3-16(1-?) Ig lambda chain V-IV region Hil Ig lambda chain V region 4A IGLV1-44(1-?) Ig heavy chain V-II region ARH-77 ITPR3 IGLV2-11(1-?) IGLC6 GNB5 LPG1G2 IGLC3 Ig kappa chain V-I region DEE GNB2 IGHV1-2 Ig lambda chain V-I region VOR CD3G IGKV2D-30 Ig kappa chain V-II region Cum IGLC1 IGLV3-16(1-?) PTGDR Ig kappa chain V-I region Gal IgH heavy chain V-III region VH26 precursor IGLV3-22(1-?) IGLV7-43(1-?) Ig kappa chain V-I region Gal Ig kappa chain V-II region Cum Ig heavy chain V-III region JON ADAM17(215-827) Ig lambda chain V-III region LOI Ig lambda chain V-I region NEWM HeterotrimericG-protein Gs(inactive)Ig lambda chain V-II region TOG p-S133-CREB1 MC1R GNAS2 GTP IGLV7-43(1-?) GDP Ig lambda chain V-I region HA Glucocorticoid, IL6,IL10RLN2(25-53) ADORA2B:Ade-RibGNB4 CYSLTR1 ADCY4 GGT5(1-387) L-GluIg lambda chain V-I region HA FCGR3A Ig heavy chain V-II region ARH-77 Ig kappa chain V-III region VG IGLV10-54(1-?) Ig kappa chain V-I region AG IGLV11-55(1-?) IGLV3-12(1-?) Ig heavy chain V-III region KOL IGHG3 Ig kappa chain V-I region Gal CD163GGT1(381-569) ADCY6 CGA IGLV3-16(1-?) Ig kappa chain V-III region B6 IGHG2 Ig lambda chain V-II region MGC Ig kappa chain V-I region HK101 CALCRL IGHG3 IGLC7 Ig kappa chain V-III region POM IGHV(1-?) Ig kappa chain V-III region B6 PTH1R GNB5 ADCY8 FCGR1A PTH2(62-100) IgH heavy chain V-III region VH26 precursor Ig kappa chain V-I region BAN AVPR2 GNG11 Ig heavy chain V-III region DOB IGLV11-55(1-?) Ig kappa chain V-III region POM IGLV2-23(1-?) Ig kappa chain V-II region FR IL10IGLV3-25(1-?) GNAS2 Ig heavy chain V-II region MCE GNB3 Lma amastigote surface Ig heavy chain V-II region WAH IGLV(23-?) Ig kappa chain V-I region DEE IGLV3-12(1-?) Ig heavy chain V-III region KOL PLCG2 FCGR3A Ig lambda chain V-III region SH PRKAR2A Ig lambda chain V-VI region AR p-Y160,Y171-CD3G RAMP1 IGLV3-12(1-?) GNAS2 GNG7 IGLV10-54(1-?) IGLV1-40(1-?) Ig heavy chain V-II region ARH-77 Ig heavy chain V-III region KOL GNB4 Ig heavy chain V-I region EU IgH heavy chain V-III region VH26 precursor Ig lambda chain V region 4A Ig kappa chain V-III region VG Lma amastigote surface ADCY7 GNAS1 Ig heavy chain V-III region TRO IGLC7 GLP2R IGLV2-33(1-?) Ig kappa chain V-I region BAN IGKV2D-30 PTH2R Zn2+ Ig heavy chain V-II region NEWM IGLV3-12(1-?) Ig lambda chain V-VI region AR Ig lambda chain V-II region MGC IGLV2-18(1-?) IGHV7-81(1-?) Ig lambda chain V-IV region Kern GNG5 GLP-1 (7-37) GNGT2 IGHV(1-?) PRKACA Ig lambda chain V-III region LOI IGKV2D-30 Ig kappa chain V-I region Daudi ADAM17(215-827):Zn2+IL6 FCGR3A IGKV4-1(21-?) IGLV2-33(1-?) p-6Y-CD247 Ig kappa chain V-I region Wes IGLV1-40(1-?) IGLV7-43(1-?) Ig heavy chain V-III region CAM Ig kappa chain V-I region AG IGLV3-22(1-?) Ig lambda chain V-I region NEWM Ig lambda chain V-II region TOG LTC4 IGLV2-33(1-?) IGLV2-23(1-?) IGKV4-1(21-?) Ig kappa chain V-I region HK101 GHRHR IGLV4-60(1-?) GGT5(388-586) Ig kappa chain V-I region HK101 GNG5 IGLV1-40(1-?) ADM2(19-153) Ig lambda chain V-I region NEW ADPIGLC1 MC5R Ig heavy chain V-II region ARH-77 Ig heavy chain V-III region JON Ig heavy chain V-II region NEWM Ig heavy chain V-III region BUT IGKV4-1(21-?) Ig lambda chain V-I region NEW ADCY5 Ig lambda chain V-I region NEW Ig kappa chain V-I region Gal Ig lambda chain V-III region LOI IGLV11-55(1-?) GNG12 IGKV1-12 GNG3 IGLV1-44(1-?) Ig lambda chain V-I region HA IGLV3-22(1-?) p-S133-CREB1 IGKV1-5(23-?) PKA tetramer:4xcAMPADCY8 Ig kappa chain V-I region HK101 Ig lambda chain V-III region SH GNG2 CCA IL10 Ig lambda chain V-II region NEI IGLV3-22(1-?) Ig lambda chain V-I region NEWM IGLV4-3(1-?) ADCY6 Ig heavy chain V-III region CAM cAMP Ig heavy chain V-III region WEA Ig kappa chain V-II region RPMI 6410 Ig heavy chain V-II region NEWM Ig lambda chain V region 4A IGLC3 Ig lambda chain V-IV region Hil Ig lambda chain V-II region NEI IGLV1-36(1-?) PRKAR1A IGHG4 Ig heavy chain V-III region BUT Ig heavy chain V-III region BUT IGHV1-2 IGLC3 IGHG3 IGLV10-54(1-?) Ca2+ Ig heavy chain V-III region JON Ig lambda chain V-I region NEW TAAR6 Ig lambda chain V-II region NEI PTGER4 GTP CYSLTR1,CYSLTR2GNAZ Ig heavy chain V-III region BUT Ig heavy chain V-III region TRO PKA catalyticsubunitIg lambda chain V-II region NEI Ig kappa chain V-II region Cum GTP IGLV1-44(1-?) ADAM17(215-827) IGKV4-1(21-?) IGLV11-55(1-?) Lma amastigote surface IGKV2D-30 IGKV3D-20 GNB4 Ig heavy chain V-II region OU IGLC2 PGI2 IGLV(23-?) GNG4 IGHV1-2 CREB1Ig kappa chain V-I region DEE p-Y753,Y759,Y1217-PLCG2 IGLV4-60(1-?) Ig kappa chain V-I region Daudi Ig heavy chain V-I region HG3 Ig lambda chain V-III region LOI Ig kappa chain V-I region AU GNG7 ATP Ig lambda chain V-I region VOR IgG:Lmaantigens:FCGR3A:p-CD3 dimers:p-6Y-SYKIGHG2 IGLV3-27(1-?) Ig lambda chain V-I region NEW IGLV1-44(1-?) IGLV1-44(1-?) IGLV5-45(1-?) Ig heavy chain V-II region MCE DPEP1,2,3 dimersPRKACA IGLV1-36(1-?) IGKV2-28 IGKV1-12 RLN3(119-142) Ig heavy chain V-III region DOB HTR7 Ig lambda chain V-I region HA IGLV2-33(1-?) IGLV3-16(1-?) IGLV5-37(1-?) IgG:Lmaantigens:FCGR3A:p-CD3 dimers:SYKIGHV(1-?) LHCGR IGKV1-5(23-?) GNB2 Ig kappa chain V-I region HK101 Ig lambda chain V-IV region Kern IGLV7-43(1-?) GNG2 IGLV11-55(1-?) IGLV(23-?) Ig kappa chain V-II region RPMI 6410 GNB1 Ig lambda chain V-II region NEI Ig kappa chain V-I region Daudi Ig kappa chain V-III region POM Ig lambda chain V-I region HA Ig lambda chain V-IV region Bau Ig kappa chain V-I region HK101 IGLV7-43(1-?) IGLV3-16(1-?) PRKAR2A GNG12 Ig lambda chain V-I region NEWM IGLV4-69(1-?) Ig kappa chain V-I region Wes AHCYL1:NAD+:ITPR1:I(1,4,5)P3 tetramerIg heavy chain V-II region MCE ATPIg lambda chain V-I region VOR Ig lambda chain V-I region HA IGLV3-27(1-?) GNAS1 Ig lambda chain V region 4A IGLV1-44(1-?) IGLV2-23(1-?) PRKAR1A Ig heavy chain V-I region EU Ig heavy chain V-II region NEWM IGHV1-2 ITPR2 Ig heavy chain V-III region TRO Ig lambda chain V-III region SH IGHG1 Ig kappa chain V region EV15 Ig lambda chain V-I region VOR Ig lambda chain V-I region VOR Ig lambda chain V-II region BOH Ig kappa chain V-I region Daudi Ig lambda chain V-III region SH IGLV1-40(1-?) IGKV2D-30 Zn2+ SYKATPZn2+Ca2+IGHG4 IGHG4 IGHV7-81(1-?) GNG13 Ig heavy chain V-III region TRO Ig lambda chain V-II region TOG IGKV1-5(23-?) Ig lambda chain V-III region LOI IGLV3-22(1-?) PRKAR1B LTC4ADCY1 CD163(1051-1156)Ig lambda chain V-IV region Hil IGLV4-69(1-?) IGLV5-37(1-?) GNB4 Ig kappa chain V-III region VG ATPIGLV2-18(1-?) Ig heavy chain V-III region JON Ig heavy chain V-II region MCE ATPIg kappa chain V-I region BAN CD247-1 Ig lambda chain V-IV region Hil Ig heavy chain V-III region BRO GPBAR1 ADCY8 Ig lambda chain V region 4A IGLC7 Ig heavy chain V-III region WEA p-4Y-PLCG1 IGHV(1-?) Ig kappa chain V-I region Daudi Ig kappa chain V-III region B6 Ig kappa chain V-I region Wes IL10 gene IGLV5-37(1-?) IGLV10-54(1-?) PRKACA GNG11 Ig heavy chain V-II region NEWM IgG:LPG1G2IGLV11-55(1-?) Ig kappa chain V-I region AG Ig heavy chain V-I region EU ADCY9 IGHG3 IGKV1-5(23-?) ADCY5 GNG8 GNG5 GNG11 GNAS2 Ig kappa chain V-I region DEE IGLV1-36(1-?) IGLV2-18(1-?) IGLV2-23(1-?) I(1,4,5)P3 Ig lambda chain V-I region NEWM Ig lambda chain V-VI region AR Src family kinases(SFKs)Ig heavy chain V-III region JON CALM1:4xCa2+TSHR Ig heavy chain V-III region DOB POMC(77-87) ADPIg kappa chain V-II region FR IGLV3-27(1-?) IGLV4-3(1-?) IGHV7-81(1-?) IGLV5-37(1-?) IGKV1-5(23-?) Ig kappa chain V-II region Cum LYN Ig heavy chain V-III region KOL IGHG4 IGHV(1-?) Ig heavy chain V-I region HG3 Ig kappa chain V-II region RPMI 6410 IGHG4 IGLV2-11(1-?) PRKAR2B LTC4:CyslTR1,2CRH IGLV5-37(1-?) Ig lambda chain V-VI region AR Ig heavy chain V-II region WAH IGLV3-27(1-?) IGKV2-28 PI(3,4,5)P3Ig kappa chain V-III region POM Ig lambda chain V-IV region Bau IGLV5-45(1-?) Ig lambda chain V-II region TOG IgH heavy chain V-III region VH26 precursor Ig kappa chain V-I region Wes IGHV1-2 IGLV3-12(1-?) IGLC2 IGHG1 NPS IGLV8-61(1-?) Ig lambda chain V-II region MGC ADCY1 AHCYL1 p-Y160,Y171-CD3G IGLV2-33(1-?) Ig lambda chain V-III region LOI IGKV4-1(21-?) Ig lambda chain V-II region NEI IGHG1 POMC(138-150) IGKC GCG(53-81) NAd Ig kappa chain V region EV15 IGLC7 Ig heavy chain V-III region DOB Ig heavy chain V-III region KOL IGLV2-23(1-?) CYSLTR2 ADCY3 IGHG4 Ig kappa chain V-III region VG IGLV3-22(1-?) IGHG4 IGLV7-46(1-?) Ig kappa chain V region EV15 IGLV1-44(1-?) Ig kappa chain V-I region Daudi Ig heavy chain V-III region BRO IGHG4 Ig lambda chain V-I region NEWM IGHV1-2 p-6Y-CD247 Ig lambda chain V-III region SH LTE4GIPR Ig kappa chain V-I region BAN Ig lambda chain V-I region NEW Ig heavy chain V-II region NEWM GNG2 Ig lambda chain V-I region HA ADR Ig kappa chain V-I region BAN IGKV4-1(21-?) IGHV7-81(1-?) IGLV7-46(1-?) Ig lambda chain V-III region LOI Ig kappa chain V-I region AG Ig kappa chain V-I region AU IGKVA18(21-?) Ig lambda chain V-II region BOH Ig lambda chain V region 4A IGLV5-45(1-?) Ade-Rib GNGT1 PRKAR2A GNG12 IGLV3-25(1-?) FCGR3A GNG13 IGHG4 GIP(52-93) IGLC1 IGLV2-18(1-?) PGD2 Ig heavy chain V-III region WEA Zn2+ PRKACB IGLV5-37(1-?) Ig kappa chain V-I region BAN ArgN-GCG(98-127) Adenylate cyclase(Mg2+ cofactor)Ig heavy chain V-III region DOB ADCY8 cAMP Ig heavy chain V-III region BRO PRKAR2B Ig lambda chain V-I region NEW G-protein beta-gammacomplexIGLC3 CDCA Ig kappa chain V-I region AU GGT1(381-569) Zn2+ PRKACB ADCY2 Ig heavy chain V-II region WAH IGLC7 AVP(20-28) p-6Y-CD247 IGLV2-18(1-?) ADCY3 ADCY5 Ig kappa chain V-II region RPMI 6410 ADAM17(1-214)IGHG3 Ig heavy chain V-II region WAH Ig lambda chain V-II region NEI p-S133-CREB1:IL6geneIg heavy chain V-II region ARH-77 ADCY4 TAAR9 IGKV3D-20 Ig kappa chain V-I region AG Ade-Rib G alpha (s):GTPGHRH IGKV1-5(23-?) Ig heavy chain V-II region WAH ITPR1 GlyIg kappa chain V-II region RPMI 6410 ADCY3 IGLV(23-?) IgH heavy chain V-III region VH26 precursor GNAS1 IGLV2-18(1-?) GNAS1 IGLV3-12(1-?) Ig lambda chain V-II region BOH ITPR3 Ig heavy chain V-III region KOL IGKV1-5(23-?) DCA SYK IGLV4-3(1-?) Ig kappa chain V-II region Cum IGLV8-61(1-?) IGLV3-16(1-?) ADPIg heavy chain V-II region OU Ig heavy chain V-I region EU IGLV10-54(1-?) cAMPGNG8 IGHG1 IGLC3 Ig lambda chain V region 4A SCTR Ig heavy chain V-III region JON Ig heavy chain V-II region NEWM PLCG1 IGLV7-43(1-?) Ig heavy chain V-III region BRO Ig lambda chain V-IV region Kern Ig kappa chain V-III region B6 IGKV3D-20 Ig kappa chain V-I region Gal Ig heavy chain V-II region WAH CYSLTR2 Ig kappa chain V-I region Daudi GGT1 dimerIGHG1 IGLV4-3(1-?) IGLV5-37(1-?) Ig heavy chain V-III region CAM Ig lambda chain V-II region MGC IGLV1-36(1-?) IgG:Leishmaniasurface:p-FCGR3As:p-6Y-SYK:PLCGIGLV4-3(1-?) Ig lambda chain V-IV region Bau Ig kappa chain V-I region Wes Ig kappa chain V-I region AG sCD163IGKVA18(21-?) Ig kappa chain V-I region DEE GNG10 ADORA2BIg heavy chain V-I region HG3 Lma amastigote surface Ig lambda chain V-IV region Hil PRKACG Ig lambda chain V-II region MGC ADCY6 Ig kappa chain V-II region Cum GNB3 IGLV2-23(1-?) CALM1 Ig lambda chain V-I region VOR PTH Adenylate cyclase(Mg2+ cofactor)CD163 geneLPG1G2 Ig kappa chain V-III region B6 IGLV4-69(1-?) IGLV2-33(1-?) IGLC6 ADCYAP1R1 Ig heavy chain V-III region BRO IGLC6 Ig lambda chain V-IV region Hil IGLV8-61(1-?) PRKACA Lma amastigote surface Ig heavy chain V-III region DOB GPHA2 Ig lambda chain V-IV region Kern Ig kappa chain V-II region FR Ig heavy chain V-III region WEA GNG7 Ig lambda chain V-IV region Kern Ig lambda chain V-VI region AR FYN p-6Y-SYK IGLC2 IGKV1-5(23-?) IGLV3-25(1-?) Ig kappa chain V-I region Wes IGHV1-2 IGLV1-44(1-?) Ig lambda chain V-I region NEW PRKACB Ade-RibIGLC2 LTD4Ig lambda chain V-IV region Bau IGLC3 Ig kappa chain V-I region AG IGLV4-69(1-?) LHB IGLC7 Mg2+ Ig lambda chain V-III region SH Ig heavy chain V-III region KOL p-S133-CREB1IGLV(23-?) IGLV3-16(1-?) Ig kappa chain V-I region AU IGLC6 PTHLH DA GNG13 Ig lambda chain V-I region HA Ig heavy chain V-I region EU ADRB3 IGLC3 IGLV1-44(1-?) IGKC ADCY4 Ig kappa chain V region EV15 Ig lambda chain V-III region SH RAMP3 Ig heavy chain V-III region BUT ADORA2B Ig kappa chain V-II region RPMI 6410 GNG11 Ig lambda chain V-III region SH FCGR3A LPG1G2 IGLV4-60(1-?) ATPLma amastigote surface Ig kappa chain V-I region Daudi Ig lambda chain V-I region NEW IGKV2-28 LPG1G2 IGLC1 Ig heavy chain V-III region CAM IGKC IGKV2-28 ADCY8 ITPR3 GNG10 IGLV3-12(1-?) Ig lambda chain V-I region NEWM IGLC6 CALCB(82-118) IGKVA18(21-?) GDP Ig lambda chain V-III region LOI Ig kappa chain V-I region HK101 CALM1CD3G INSL3(21-55) Ig kappa chain V-II region FR IGKV2-28 IGLV7-43(1-?) Ig heavy chain V-I region EU Ig heavy chain V-II region WAH IGLV5-45(1-?) HTR4 ADCY9 IGHV1-2 CYSLTR1 Ig lambda chain V-I region NEWM Ig lambda chain V-VI region AR IGLV5-45(1-?) PKA tetramerTAAR5 p-S133-CREB1:IL10geneIg heavy chain V-III region DOB Ig heavy chain V-III region DOB ADPADCYAP1(132-169) Ig lambda chain V-IV region Kern GTPIGLV5-37(1-?) IGHG1 Ig kappa chain V-I region DEE IGHG3 Ig lambda chain V region 4A Ig lambda chain V-I region HA PRKACG IGLV2-11(1-?) GNGT2 GNG2 IGLV1-36(1-?) Ig kappa chain V-I region BAN IAPP(34-70) IGHG2 IGHG2 CYSLTR2 IGHG2 GNG11 IGLV2-11(1-?) IGKV2-28 HTR6 Ig kappa chain V-II region FR IP3 receptorhomotetramerIg heavy chain V-II region ARH-77 GDPIg lambda chain V-II region NEI Ig kappa chain V-III region VG GLP1R IGHV7-81(1-?) IGLV5-45(1-?) IGKV2D-30 GNG7 PRKACB Ig heavy chain V-II region WAH GNAS2 ADM(95-146) Mg2+ Ig lambda chain V-II region TOG IGLV3-16(1-?) Ig heavy chain V-III region CAM POMC(138-176) IGLV4-60(1-?) clusteredIgG-Ag:p-FCGRs:p-6Y-SYK:PLCGPRKACG IGLV3-27(1-?) GNB2 IGLC2 DAGsIGKVA18(21-?) Ig heavy chain V-III region CAM Ig kappa chain V-I region Wes IGLV8-61(1-?) PLC gamma1,2H2OADRB2 Ig kappa chain V-III region POM GNG12 p-6Y-CD247 Ig heavy chain V-III region CAM IGLV4-69(1-?) p-Y160,Y171-CD3G GNAS1 Ig kappa chain V-II region Cum Ig kappa chain V-I region Gal IGLC1 Ig lambda chain V-II region BOH 301432145456145656, 83


Description

Macrophages specializing in tissue repair or associated with a Th2-type immune response are more permissive to infection with leishmania, since their defense mechanisms are not very efficient in eliminating the parasite and can contribute to its persistence (Lee et al. 2018). View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 9662851
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Jassal, Bijay

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Bibliography

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  1. Buxbaum LU.; ''Leishmania mexicana infection induces IgG to parasite surface glycoinositol phospholipids that can induce IL-10 in mice and humans.''; PubMed Europe PMC Scholia
  2. Simpson RE, Ciruela A, Cooper DM.; ''The role of calmodulin recruitment in Ca2+ stimulation of adenylyl cyclase type 8.''; PubMed Europe PMC Scholia
  3. Zhang JY, Nawoschik S, Kowal D, Smith D, Spangler T, Ochalski R, Schechter L, Dunlop J.; ''Characterization of the 5-HT6 receptor coupled to Ca2+ signaling using an enabling chimeric G-protein.''; PubMed Europe PMC Scholia
  4. Asadullah K, Sterry W, Volk HD.; ''Interleukin-10 therapy--review of a new approach.''; PubMed Europe PMC Scholia
  5. Sanin DE, Prendergast CT, Mountford AP.; ''IL-10 Production in Macrophages Is Regulated by a TLR-Driven CREB-Mediated Mechanism That Is Linked to Genes Involved in Cell Metabolism.''; PubMed Europe PMC Scholia
  6. Wenzel-Seifert K, Liu HY, Seifert R.; ''Similarities and differences in the coupling of human beta1- and beta2-adrenoceptors to Gs(alpha) splice variants.''; PubMed Europe PMC Scholia
  7. Etzerodt A, Rasmussen MR, Svendsen P, Chalaris A, Schwarz J, Galea I, Møller HJ, Moestrup SK.; ''Structural basis for inflammation-driven shedding of CD163 ectodomain and tumor necrosis factor-α in macrophages.''; PubMed Europe PMC Scholia
  8. Tsang E, Giannetti AM, Shaw D, Dinh M, Tse JK, Gandhi S, Ho H, Wang S, Papp E, Bradshaw JM.; ''Molecular mechanism of the Syk activation switch.''; PubMed Europe PMC Scholia
  9. Dessauer CW, Chen-Goodspeed M, Chen J.; ''Mechanism of Galpha i-mediated inhibition of type V adenylyl cyclase.''; PubMed Europe PMC Scholia
  10. Högger P, Erpenstein U, Rohdewald P, Sorg C.; ''Biochemical characterization of a glucocorticoid-induced membrane protein (RM3/1) in human monocytes and its application as model system for ranking glucocorticoid potency.''; PubMed Europe PMC Scholia
  11. Durden DL, Liu YB.; ''Protein-tyrosine kinase p72syk in Fc gamma RI receptor signaling.''; PubMed Europe PMC Scholia
  12. Huang ZY, Barreda DR, Worth RG, Indik ZK, Kim MK, Chien P, Schreiber AD.; ''Differential kinase requirements in human and mouse Fc-gamma receptor phagocytosis and endocytosis.''; PubMed Europe PMC Scholia
  13. Fan H, Turck CW, Derynck R.; ''Characterization of growth factor-induced serine phosphorylation of tumor necrosis factor-alpha converting enzyme and of an alternatively translated polypeptide.''; PubMed Europe PMC Scholia
  14. Matsuda M, Paterson HF, Rodriguez R, Fensome AC, Ellis MV, Swann K, Katan M.; ''Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor.''; PubMed Europe PMC Scholia
  15. Crowley MT, Costello PS, Fitzer-Attas CJ, Turner M, Meng F, Lowell C, Tybulewicz VL, DeFranco AL.; ''A critical role for Syk in signal transduction and phagocytosis mediated by Fcgamma receptors on macrophages.''; PubMed Europe PMC Scholia
  16. Cooper JA, Hill SJ, Alexander SP, Rubin PC, Horn EH.; ''Adenosine receptor-induced cyclic AMP generation and inhibition of 5-hydroxytryptamine release in human platelets.''; PubMed Europe PMC Scholia
  17. Matsuda M, Park JG, Wang DC, Hunter S, Chien P, Schreiber AD.; ''Abrogation of the Fc gamma receptor IIA-mediated phagocytic signal by stem-loop Syk antisense oligonucleotides.''; PubMed Europe PMC Scholia
  18. Heise CE, O'Dowd BF, Figueroa DJ, Sawyer N, Nguyen T, Im DS, Stocco R, Bellefeuille JN, Abramovitz M, Cheng R, Williams DL, Zeng Z, Liu Q, Ma L, Clements MK, Coulombe N, Liu Y, Austin CP, George SR, O'Neill GP, Metters KM, Lynch KR, Evans JF.; ''Characterization of the human cysteinyl leukotriene 2 receptor.''; PubMed Europe PMC Scholia
  19. Droste A, Sorg C, Högger P.; ''Shedding of CD163, a novel regulatory mechanism for a member of the scavenger receptor cysteine-rich family.''; PubMed Europe PMC Scholia
  20. Kiener PA, Rankin BM, Burkhardt AL, Schieven GL, Gilliland LK, Rowley RB, Bolen JB, Ledbetter JA.; ''Cross-linking of Fc gamma receptor I (Fc gamma RI) and receptor II (Fc gamma RII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase.''; PubMed Europe PMC Scholia
  21. Gechtman Z, Alonso JL, Raab G, Ingber DE, Klagsbrun M.; ''The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading.''; PubMed Europe PMC Scholia
  22. Lynch KR, O'Neill GP, Liu Q, Im DS, Sawyer N, Metters KM, Coulombe N, Abramovitz M, Figueroa DJ, Zeng Z, Connolly BM, Bai C, Austin CP, Chateauneuf A, Stocco R, Greig GM, Kargman S, Hooks SB, Hosfield E, Williams DL, Ford-Hutchinson AW, Caskey CT, Evans JF.; ''Characterization of the human cysteinyl leukotriene CysLT1 receptor.''; PubMed Europe PMC Scholia
  23. Kelly EK, Wang L, Ivashkiv LB.; ''Calcium-activated pathways and oxidative burst mediate zymosan-induced signaling and IL-10 production in human macrophages.''; PubMed Europe PMC Scholia
  24. Linden J, Thai T, Figler H, Jin X, Robeva AS.; ''Characterization of human A(2B) adenosine receptors: radioligand binding, western blotting, and coupling to G(q) in human embryonic kidney 293 cells and HMC-1 mast cells.''; PubMed Europe PMC Scholia
  25. Timmermann M, Buck F, Sorg C, Högger P.; ''Interaction of soluble CD163 with activated T lymphocytes involves its association with non-muscle myosin heavy chain type A.''; PubMed Europe PMC Scholia
  26. Carpenter G, Ji Q.; ''Phospholipase C-gamma as a signal-transducing element.''; PubMed Europe PMC Scholia
  27. Maskos K, Fernandez-Catalan C, Huber R, Bourenkov GP, Bartunik H, Ellestad GA, Reddy P, Wolfson MF, Rauch CT, Castner BJ, Davis R, Clarke HR, Petersen M, Fitzner JN, Cerretti DP, March CJ, Paxton RJ, Black RA, Bode W.; ''Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme.''; PubMed Europe PMC Scholia
  28. Kozasa T, Itoh H, Tsukamoto T, Kaziro Y.; ''Isolation and characterization of the human Gs alpha gene.''; PubMed Europe PMC Scholia
  29. Högger P, Sorg C.; ''Soluble CD163 inhibits phorbol ester-induced lymphocyte proliferation.''; PubMed Europe PMC Scholia
  30. Martin AL, Steurer MA, Aronstam RS.; ''Constitutive Activity among Orphan Class-A G Protein Coupled Receptors.''; PubMed Europe PMC Scholia
  31. Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR.; ''Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS.''; PubMed Europe PMC Scholia
  32. Leduc R, Molloy SS, Thorne BA, Thomas G.; ''Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage.''; PubMed Europe PMC Scholia
  33. Law CL, Chandran KA, Sidorenko SP, Clark EA.; ''Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk.''; PubMed Europe PMC Scholia
  34. Peterfreund RA, MacCollin M, Gusella J, Fink JS.; ''Characterization and expression of the human A2a adenosine receptor gene.''; PubMed Europe PMC Scholia
  35. Wong E, Maretzky T, Peleg Y, Blobel CP, Sagi I.; ''The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site.''; PubMed Europe PMC Scholia
  36. Yang R, Lin Q, Gao HB, Zhang P.; ''Stress-related hormone norepinephrine induces interleukin-6 expression in GES-1 cells.''; PubMed Europe PMC Scholia
  37. Padigel UM, Farrell JP.; ''Control of infection with Leishmania major in susceptible BALB/c mice lacking the common gamma-chain for FcR is associated with reduced production of IL-10 and TGF-beta by parasitized cells.''; PubMed Europe PMC Scholia
  38. Cavadas M, Oikonomidi I, Gaspar CJ, Burbridge E, Badenes M, Félix I, Bolado A, Hu T, Bileck A, Gerner C, Domingos PM, von Kriegsheim A, Adrain C.; ''Phosphorylation of iRhom2 Controls Stimulated Proteolytic Shedding by the Metalloprotease ADAM17/TACE.''; PubMed Europe PMC Scholia
  39. Strzelecka A, Kwiatkowska K, Sobota A.; ''Tyrosine phosphorylation and Fcgamma receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  40. Sarau HM, Ames RS, Chambers J, Ellis C, Elshourbagy N, Foley JJ, Schmidt DB, Muccitelli RM, Jenkins O, Murdock PR, Herrity NC, Halsey W, Sathe G, Muir AI, Nuthulaganti P, Dytko GM, Buckley PT, Wilson S, Bergsma DJ, Hay DW.; ''Identification, molecular cloning, expression, and characterization of a cysteinyl leukotriene receptor.''; PubMed Europe PMC Scholia
  41. Schwarz J, Schmidt S, Will O, Koudelka T, Köhler K, Boss M, Rabe B, Tholey A, Scheller J, Schmidt-Arras D, Schwake M, Rose-John S, Chalaris A.; ''Polo-like kinase 2, a novel ADAM17 signaling component, regulates tumor necrosis factor α ectodomain shedding.''; PubMed Europe PMC Scholia
  42. Chu N, Thomas BN, Patel SR, Buxbaum LU.; ''IgG1 is pathogenic in Leishmania mexicana infection.''; PubMed Europe PMC Scholia
  43. Baker LP, Nielsen MD, Impey S, Metcalf MA, Poser SW, Chan G, Obrietan K, Hamblin MW, Storm DR.; ''Stimulation of type 1 and type 8 Ca2+/calmodulin-sensitive adenylyl cyclases by the Gs-coupled 5-hydroxytryptamine subtype 5-HT7A receptor.''; PubMed Europe PMC Scholia
  44. Gullingsrud J, Kim C, Taylor SS, McCammon JA.; ''Dynamic binding of PKA regulatory subunit RI alpha.''; PubMed Europe PMC Scholia
  45. Mitsuhashi M, Mitsuhashi T, Payan DG.; ''Multiple signaling pathways of histamine H2 receptors. Identification of an H2 receptor-dependent Ca2+ mobilization pathway in human HL-60 promyelocytic leukemia cells.''; PubMed Europe PMC Scholia
  46. Buechler C, Ritter M, Orsó E, Langmann T, Klucken J, Schmitz G.; ''Regulation of scavenger receptor CD163 expression in human monocytes and macrophages by pro- and antiinflammatory stimuli.''; PubMed Europe PMC Scholia
  47. James MA, Lu Y, Liu Y, Vikis HG, You M.; ''RGS17, an overexpressed gene in human lung and prostate cancer, induces tumor cell proliferation through the cyclic AMP-PKA-CREB pathway.''; PubMed Europe PMC Scholia
  48. Di Pasquale G, Stacey SN.; ''Adeno-associated virus Rep78 protein interacts with protein kinase A and its homolog PRKX and inhibits CREB-dependent transcriptional activation.''; PubMed Europe PMC Scholia
  49. Endres K, Anders A, Kojro E, Gilbert S, Fahrenholz F, Postina R.; ''Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation.''; PubMed Europe PMC Scholia
  50. Lupher ML, Rao N, Lill NL, Andoniou CE, Miyake S, Clark EA, Druker B, Band H.; ''Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323.''; PubMed Europe PMC Scholia
  51. Díaz-Rodríguez E, Montero JC, Esparís-Ogando A, Yuste L, Pandiella A.; ''Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding.''; PubMed Europe PMC Scholia
  52. Etzerodt A, Maniecki MB, Møller K, Møller HJ, Moestrup SK.; ''Tumor necrosis factor α-converting enzyme (TACE/ADAM17) mediates ectodomain shedding of the scavenger receptor CD163.''; PubMed Europe PMC Scholia
  53. Suzuki T, Kono H, Hirose N, Okada M, Yamamoto T, Yamamoto K, Honda Z.; ''Differential involvement of Src family kinases in Fc gamma receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  54. Chen TY, Illing M, Molday LL, Hsu YT, Yau KW, Molday RS.; ''Subunit 2 (or beta) of retinal rod cGMP-gated cation channel is a component of the 240-kDa channel-associated protein and mediates Ca(2+)-calmodulin modulation.''; PubMed Europe PMC Scholia
  55. Lambert NA.; ''Dissociation of heterotrimeric g proteins in cells.''; PubMed Europe PMC Scholia
  56. Kim YJ, Sekiya F, Poulin B, Bae YS, Rhee SG.; ''Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2.''; PubMed Europe PMC Scholia
  57. Kim MJ, Kim E, Ryu SH, Suh PG.; ''The mechanism of phospholipase C-gamma1 regulation.''; PubMed Europe PMC Scholia
  58. Li W, Yu ZX, Kotin RM.; ''Profiles of PrKX expression in developmental mouse embryo and human tissues.''; PubMed Europe PMC Scholia
  59. Eskdale J, Kube D, Tesch H, Gallagher G.; ''Mapping of the human IL10 gene and further characterization of the 5' flanking sequence.''; PubMed Europe PMC Scholia
  60. Burger R.; ''Impact of interleukin-6 in hematological malignancies.''; PubMed Europe PMC Scholia
  61. Wickham S, West MB, Cook PF, Hanigan MH.; ''Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes.''; PubMed Europe PMC Scholia
  62. Fan H, Derynck R.; ''Ectodomain shedding of TGF-alpha and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades.''; PubMed Europe PMC Scholia
  63. Luo Y, Zheng SG.; ''Hall of Fame among Pro-inflammatory Cytokines: Interleukin-6 Gene and Its Transcriptional Regulation Mechanisms.''; PubMed Europe PMC Scholia
  64. Raulf M, König W, Köller M, Stüning M.; ''Release and functional characterization of the leukotriene D4-metabolizing enzyme (dipeptidase) from human polymorphonuclear leucocytes.''; PubMed Europe PMC Scholia
  65. Sulahian TH, Högger P, Wahner AE, Wardwell K, Goulding NJ, Sorg C, Droste A, Stehling M, Wallace PK, Morganelli PM, Guyre PM.; ''Human monocytes express CD163, which is upregulated by IL-10 and identical to p155.''; PubMed Europe PMC Scholia
  66. Huang MM, Indik Z, Brass LF, Hoxie JA, Schreiber AD, Brugge JS.; ''Activation of Fc gamma RII induces tyrosine phosphorylation of multiple proteins including Fc gamma RII.''; PubMed Europe PMC Scholia
  67. Gonzalez GA, Montminy MR.; ''Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133.''; PubMed Europe PMC Scholia
  68. Ghazizadeh S, Bolen JB, Fleit HB.; ''Tyrosine phosphorylation and association of Syk with Fc gamma RII in monocytic THP-1 cells.''; PubMed Europe PMC Scholia
  69. Furlong MT, Mahrenholz AM, Kim KH, Ashendel CL, Harrison ML, Geahlen RL.; ''Identification of the major sites of autophosphorylation of the murine protein-tyrosine kinase Syk.''; PubMed Europe PMC Scholia
  70. Dusi S, Donini M, Della Bianca V, Rossi F.; ''Tyrosine phosphorylation of phospholipase C-gamma 2 is involved in the activation of phosphoinositide hydrolysis by Fc receptors in human neutrophils.''; PubMed Europe PMC Scholia
  71. Thomas BN, Buxbaum LU.; ''FcgammaRIII mediates immunoglobulin G-induced interleukin-10 and is required for chronic Leishmania mexicana lesions.''; PubMed Europe PMC Scholia
  72. Li X, Li HP, Amsler K, Hyink D, Wilson PD, Burrow CR.; ''PRKX, a phylogenetically and functionally distinct cAMP-dependent protein kinase, activates renal epithelial cell migration and morphogenesis.''; PubMed Europe PMC Scholia
  73. Pierce KD, Furlong TJ, Selbie LA, Shine J.; ''Molecular cloning and expression of an adenosine A2b receptor from human brain.''; PubMed Europe PMC Scholia
  74. Adrain C, Zettl M, Christova Y, Taylor N, Freeman M.; ''Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE.''; PubMed Europe PMC Scholia
  75. Srour N, Lebel A, McMahon S, Fournier I, Fugère M, Day R, Dubois CM.; ''TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity.''; PubMed Europe PMC Scholia
  76. Morehead J, Coppens I, Andrews NW.; ''Opsonization modulates Rac-1 activation during cell entry by Leishmania amazonensis.''; PubMed Europe PMC Scholia
  77. Lee SH, Charmoy M, Romano A, Paun A, Chaves MM, Cope FO, Ralph DA, Sacks DL.; ''Mannose receptor high, M2 dermal macrophages mediate nonhealing Leishmania major infection in a Th1 immune environment.''; PubMed Europe PMC Scholia
  78. Agarwal A, Salem P, Robbins KC.; ''Involvement of p72syk, a protein-tyrosine kinase, in Fc gamma receptor signaling.''; PubMed Europe PMC Scholia
  79. Dendorfer U, Oettgen P, Libermann TA.; ''Multiple regulatory elements in the interleukin-6 gene mediate induction by prostaglandins, cyclic AMP, and lipopolysaccharide.''; PubMed Europe PMC Scholia
  80. Liang Z, Liu F, Grundke-Iqbal I, Iqbal K, Gong CX.; ''Down-regulation of cAMP-dependent protein kinase by over-activated calpain in Alzheimer disease brain.''; PubMed Europe PMC Scholia
  81. Adachi H, Kubota I, Okamura N, Iwata H, Tsujimoto M, Nakazato H, Nishihara T, Noguchi T.; ''Purification and characterization of human microsomal dipeptidase.''; PubMed Europe PMC Scholia
  82. Lee CW, Lewis RA, Corey EJ, Austen KF.; ''Conversion of leukotriene D4 to leukotriene E4 by a dipeptidase released from the specific granule of human polymorphonuclear leucocytes.''; PubMed Europe PMC Scholia
  83. Sekiya F, Poulin B, Kim YJ, Rhee SG.; ''Mechanism of tyrosine phosphorylation and activation of phospholipase C-gamma 1. Tyrosine 783 phosphorylation is not sufficient for lipase activation.''; PubMed Europe PMC Scholia
  84. SUTHERLAND EW, RALL TW.; ''Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles.''; PubMed Europe PMC Scholia
  85. Feldman DS, Zamah AM, Pierce KL, Miller WE, Kelly F, Rapacciuolo A, Rockman HA, Koch WJ, Luttrell LM.; ''Selective inhibition of heterotrimeric Gs signaling. Targeting the receptor-G protein interface using a peptide minigene encoding the Galpha(s) carboxyl terminus.''; PubMed Europe PMC Scholia
  86. McIlwain DR, Lang PA, Maretzky T, Hamada K, Ohishi K, Maney SK, Berger T, Murthy A, Duncan G, Xu HC, Lang KS, Häussinger D, Wakeham A, Itie-Youten A, Khokha R, Ohashi PS, Blobel CP, Mak TW.; ''iRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS.''; PubMed Europe PMC Scholia
  87. Zhang J, Berenstein E, Siraganian RP.; ''Phosphorylation of Tyr342 in the linker region of Syk is critical for Fc epsilon RI signaling in mast cells.''; PubMed Europe PMC Scholia
  88. El-Hillal O, Kurosaki T, Yamamura H, Kinet JP, Scharenberg AM.; ''syk kinase activation by a src kinase-initiated activation loop phosphorylation chain reaction.''; PubMed Europe PMC Scholia
  89. Anderson ME, Allison RD, Meister A.; ''Interconversion of leukotrienes catalyzed by purified gamma-glutamyl transpeptidase: concomitant formation of leukotriene D4 and gamma-glutamyl amino acids.''; PubMed Europe PMC Scholia
  90. Nagakura A, Takagi N, Takeo S.; ''Impairment of cerebral cAMP-mediated signal transduction system and of spatial memory function after microsphere embolism in rats.''; PubMed Europe PMC Scholia
  91. Xu P, Derynck R.; ''Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation.''; PubMed Europe PMC Scholia
  92. Platzer C, Meisel C, Vogt K, Platzer M, Volk HD.; ''Up-regulation of monocytic IL-10 by tumor necrosis factor-alpha and cAMP elevating drugs.''; PubMed Europe PMC Scholia
  93. Wenzel I, Roth J, Sorg C.; ''Identification of a novel surface molecule, RM3/1, that contributes to the adhesion of glucocorticoid-induced human monocytes to endothelial cells.''; PubMed Europe PMC Scholia
  94. Gu C, Cooper DM.; ''Calmodulin-binding sites on adenylyl cyclase type VIII.''; PubMed Europe PMC Scholia
  95. Bandeira-Melo C, Woods LJ, Phoofolo M, Weller PF.; ''Intracrine cysteinyl leukotriene receptor-mediated signaling of eosinophil vesicular transport-mediated interleukin-4 secretion.''; PubMed Europe PMC Scholia

History

CompareRevisionActionTimeUserComment
114834view16:33, 25 January 2021ReactomeTeamReactome version 75
113280view11:35, 2 November 2020ReactomeTeamReactome version 74
112811view18:18, 9 October 2020DeSlOntology Term : 'Leishmaniasis pathway' added !
112759view16:16, 9 October 2020ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
5HT MetaboliteCHEBI:28790 (ChEBI)
ADAM17(1-214)ProteinP78536 (Uniprot-TrEMBL)
ADAM17(215-827) ProteinP78536 (Uniprot-TrEMBL)
ADAM17(215-827):Zn2+ComplexR-HSA-9662765 (Reactome)
ADAM17(215-827):Zn2+ComplexR-HSA-9662793 (Reactome)
ADAM17(215-827)ProteinP78536 (Uniprot-TrEMBL)
ADAM17ProteinP78536 (Uniprot-TrEMBL)
ADCY1 ProteinQ08828 (Uniprot-TrEMBL)
ADCY2 ProteinQ08462 (Uniprot-TrEMBL)
ADCY3 ProteinO60266 (Uniprot-TrEMBL)
ADCY4 ProteinQ8NFM4 (Uniprot-TrEMBL)
ADCY5 ProteinO95622 (Uniprot-TrEMBL)
ADCY6 ProteinO43306 (Uniprot-TrEMBL)
ADCY7 ProteinP51828 (Uniprot-TrEMBL)
ADCY8 ProteinP40145 (Uniprot-TrEMBL)
ADCY9 ProteinO60503 (Uniprot-TrEMBL)
ADCYAP1(132-158) ProteinP18509 (Uniprot-TrEMBL)
ADCYAP1(132-169) ProteinP18509 (Uniprot-TrEMBL)
ADCYAP1(82-129) ProteinP18509 (Uniprot-TrEMBL)
ADCYAP1R1 ProteinP41586 (Uniprot-TrEMBL)
ADM(95-146) ProteinP35318 (Uniprot-TrEMBL)
ADM2(19-153) ProteinQ7Z4H4 (Uniprot-TrEMBL)
ADORA2A ProteinP29274 (Uniprot-TrEMBL)
ADORA2B ProteinP29275 (Uniprot-TrEMBL)
ADORA2B:Ade-Rib:Heterotrimeric G-protein Gs:GTPComplexR-HSA-9660820 (Reactome)
ADORA2B:Ade-RibComplexR-HSA-9660818 (Reactome)
ADORA2BProteinP29275 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:456216 (ChEBI)
ADR MetaboliteCHEBI:28918 (ChEBI)
ADRB1 ProteinP08588 (Uniprot-TrEMBL)
ADRB2 ProteinP07550 (Uniprot-TrEMBL)
ADRB3 ProteinP13945 (Uniprot-TrEMBL)
AHCYL1 ProteinO43865 (Uniprot-TrEMBL)
AHCYL1:NAD+:ITPR1:I(1,4,5)P3 tetramerComplexR-HSA-5226920 (Reactome)
ATP MetaboliteCHEBI:30616 (ChEBI)
ATPMetaboliteCHEBI:30616 (ChEBI)
AVP(20-28) ProteinP01185 (Uniprot-TrEMBL)
AVPR2 ProteinP30518 (Uniprot-TrEMBL)
Ade-Rib MetaboliteCHEBI:16335 (ChEBI)
Ade-Rib:ADORA2B:Heterotrimeric G-protein Gs:GDPComplexR-HSA-9660817 (Reactome)
Ade-RibMetaboliteCHEBI:16335 (ChEBI)
Adenylate cyclase (Mg2+ cofactor)ComplexR-HSA-170665 (Reactome)
Antigen R-ALL-173548 (Reactome)
ArgN-GCG(98-127) ProteinP01275 (Uniprot-TrEMBL) The amide group at the C-terminus is not necessary for biological activity.
CALCA(83-119) ProteinP01258 (Uniprot-TrEMBL)
CALCA(83-119) ProteinP06881 (Uniprot-TrEMBL)
CALCB(82-118) ProteinP10092 (Uniprot-TrEMBL)
CALCR ProteinP30988 (Uniprot-TrEMBL)
CALCRL ProteinQ16602 (Uniprot-TrEMBL)
CALM1 ProteinP0DP23 (Uniprot-TrEMBL)
CALM1:4xCa2+ComplexR-HSA-74294 (Reactome)
CALM1ProteinP0DP23 (Uniprot-TrEMBL)
CCA MetaboliteCHEBI:16359 (ChEBI)
CD163 geneGeneProductENSG00000177575 (Ensembl)
CD163(1051-1156)ProteinQ86VB7 (Uniprot-TrEMBL)
CD163ProteinQ86VB7 (Uniprot-TrEMBL)
CD247-1 ProteinP20963-1 (Uniprot-TrEMBL)
CD3G ProteinP09693 (Uniprot-TrEMBL)
CDCA MetaboliteCHEBI:16755 (ChEBI)
CGA ProteinP01215 (Uniprot-TrEMBL)
CREB1ProteinP16220 (Uniprot-TrEMBL)
CRH ProteinP06850 (Uniprot-TrEMBL)
CRHR1 ProteinP34998 (Uniprot-TrEMBL)
CRHR2 ProteinQ13324 (Uniprot-TrEMBL)
CYSLTR1 ProteinQ9Y271 (Uniprot-TrEMBL)
CYSLTR1,CYSLTR2ComplexR-HSA-416385 (Reactome)
CYSLTR2 ProteinQ9NS75 (Uniprot-TrEMBL)
Ca2+ MetaboliteCHEBI:29108 (ChEBI)
Ca2+MetaboliteCHEBI:29108 (ChEBI)
Constitutively active orphan GPCRs R-HSA-6805225 (Reactome)
DA MetaboliteCHEBI:18243 (ChEBI)
DAGsMetaboliteCHEBI:18035 (ChEBI)
DCA MetaboliteCHEBI:28834 (ChEBI)
DPEP1 ProteinP16444 (Uniprot-TrEMBL)
DPEP1,2,3 dimersComplexR-HSA-2162149 (Reactome)
DPEP2 ProteinQ9H4A9 (Uniprot-TrEMBL)
DPEP3 ProteinQ9H4B8 (Uniprot-TrEMBL)
DRD1 ProteinP21728 (Uniprot-TrEMBL)
DRD5 ProteinP21918 (Uniprot-TrEMBL)
FCGR1A ProteinP12314 (Uniprot-TrEMBL)
FCGR3A ProteinP08637 (Uniprot-TrEMBL)
FCGRIIIA:CD3G/CD3Z dimersComplexR-HSA-2029097 (Reactome)
FGR ProteinP09769 (Uniprot-TrEMBL)
FSHB ProteinP01225 (Uniprot-TrEMBL)
FSHR ProteinP23945 (Uniprot-TrEMBL)
FURINProteinP09958 (Uniprot-TrEMBL)
FYN ProteinP06241 (Uniprot-TrEMBL)
G alpha

(s):GTP:Adenylate

cyclase		ComplexR-HSA-163622 (Reactome)
G alpha (s):GTPComplexR-HSA-164358 (Reactome)
G-betagammaR-HSA-111865 (Reactome)
G-protein alpha

(i):GTP:Adenylate

cyclase		ComplexR-HSA-396910 (Reactome)
G-protein alpha

(z):GTP:Adenylate

cyclase		ComplexR-HSA-392049 (Reactome)
G-protein beta-gamma complexComplexR-HSA-167434 (Reactome)
GCG(146-178) ProteinP01275 (Uniprot-TrEMBL)
GCG(53-81) ProteinP01275 (Uniprot-TrEMBL)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GGT1 dimerComplexR-HSA-1247898 (Reactome)
GGT1(1-380) ProteinP19440 (Uniprot-TrEMBL)
GGT1(381-569) ProteinP19440 (Uniprot-TrEMBL)
GGT1, 5 dimersComplexR-HSA-2162130 (Reactome)
GGT5(1-387) ProteinP36269 (Uniprot-TrEMBL)
GGT5(388-586) ProteinP36269 (Uniprot-TrEMBL)
GHRH ProteinP01286 (Uniprot-TrEMBL)
GHRHR ProteinQ02643 (Uniprot-TrEMBL)
GIP(52-93) ProteinP09681 (Uniprot-TrEMBL)
GIPR ProteinP48546 (Uniprot-TrEMBL)
GLP-1 (7-37) ProteinP01275 (Uniprot-TrEMBL)
GLP1R ProteinP43220 (Uniprot-TrEMBL)
GLP2R ProteinO95838 (Uniprot-TrEMBL)
GNAI1 ProteinP63096 (Uniprot-TrEMBL)
GNAI2 ProteinP04899 (Uniprot-TrEMBL)
GNAI3 ProteinP08754 (Uniprot-TrEMBL)
GNAS1 ProteinQ5JWF2 (Uniprot-TrEMBL)
GNAS2 ProteinP63092 (Uniprot-TrEMBL)
GNAT3 ProteinA8MTJ3 (Uniprot-TrEMBL)
GNAZ ProteinP19086 (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)
GPBAR1 ProteinQ8TDU6 (Uniprot-TrEMBL)
GPHA2 ProteinQ96T91 (Uniprot-TrEMBL)
GPHB5 ProteinQ86YW7 (Uniprot-TrEMBL)
GPR39 ProteinO43194 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
Glucocorticoid, IL6, IL10ComplexR-HSA-9662737 (Reactome)
GlyMetaboliteCHEBI:57305 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCK ProteinP08631 (Uniprot-TrEMBL)
HRH2 ProteinP25021 (Uniprot-TrEMBL)
HTR4 ProteinQ13639 (Uniprot-TrEMBL)
HTR6 ProteinP50406 (Uniprot-TrEMBL)
HTR7 ProteinP34969 (Uniprot-TrEMBL)
Heterotrimeric

G-protein Gs

(inactive)		ComplexR-HSA-391179 (Reactome)
Hist MetaboliteCHEBI:18295 (ChEBI)
I(1,4,5)P3 MetaboliteCHEBI:16595 (ChEBI)
I(1,4,5)P3MetaboliteCHEBI:16595 (ChEBI)
IAPP(34-70) ProteinP10997 (Uniprot-TrEMBL)
IGHG1 ProteinP01857 (Uniprot-TrEMBL)
IGHG2 ProteinP01859 (Uniprot-TrEMBL)
IGHG3 ProteinP01860 (Uniprot-TrEMBL)
IGHG4 ProteinP01861 (Uniprot-TrEMBL)
IGHV(1-?) ProteinA2KUC3 (Uniprot-TrEMBL)
IGHV1-2 ProteinP23083 (Uniprot-TrEMBL)
IGHV7-81(1-?) ProteinQ6PIL0 (Uniprot-TrEMBL)
IGKC ProteinP01834 (Uniprot-TrEMBL)
IGKV1-12 ProteinA0A0C4DH73 (Uniprot-TrEMBL)
IGKV1-5(23-?) ProteinP01602 (Uniprot-TrEMBL)
IGKV2-28 ProteinA0A075B6P5 (Uniprot-TrEMBL)
IGKV2D-30 ProteinA0A075B6S6 (Uniprot-TrEMBL)
IGKV3D-20 ProteinA0A0C4DH25 (Uniprot-TrEMBL)
IGKV4-1(21-?) ProteinP06312 (Uniprot-TrEMBL)
IGKVA18(21-?) ProteinA2NJV5 (Uniprot-TrEMBL)
IGLC1 ProteinP0CG04 (Uniprot-TrEMBL)
IGLC2 ProteinP0DOY2 (Uniprot-TrEMBL)
IGLC3 ProteinP0DOY3 (Uniprot-TrEMBL)
IGLC6 ProteinP0CF74 (Uniprot-TrEMBL)
IGLC7 ProteinA0M8Q6 (Uniprot-TrEMBL)
IGLV(23-?) ProteinA2NXD2 (Uniprot-TrEMBL)
IGLV1-36(1-?) ProteinQ5NV67 (Uniprot-TrEMBL)
IGLV1-40(1-?) ProteinQ5NV69 (Uniprot-TrEMBL)
IGLV1-44(1-?) ProteinQ5NV81 (Uniprot-TrEMBL)
IGLV10-54(1-?) ProteinQ5NV86 (Uniprot-TrEMBL)
IGLV11-55(1-?) ProteinQ5NV87 (Uniprot-TrEMBL)
IGLV2-11(1-?) ProteinQ5NV84 (Uniprot-TrEMBL)
IGLV2-18(1-?) ProteinQ5NV65 (Uniprot-TrEMBL)
IGLV2-23(1-?) ProteinQ5NV89 (Uniprot-TrEMBL)
IGLV2-33(1-?) ProteinQ5NV66 (Uniprot-TrEMBL)
IGLV3-12(1-?) ProteinQ5NV85 (Uniprot-TrEMBL)
IGLV3-16(1-?) ProteinQ5NV64 (Uniprot-TrEMBL)
IGLV3-22(1-?) ProteinQ5NV75 (Uniprot-TrEMBL)
IGLV3-25(1-?) ProteinQ5NV90 (Uniprot-TrEMBL)
IGLV3-27(1-?) ProteinQ5NV91 (Uniprot-TrEMBL)
IGLV4-3(1-?) ProteinQ5NV61 (Uniprot-TrEMBL)
IGLV4-60(1-?) ProteinQ5NV79 (Uniprot-TrEMBL)
IGLV4-69(1-?) ProteinQ5NV92 (Uniprot-TrEMBL)
IGLV5-37(1-?) ProteinQ5NV68 (Uniprot-TrEMBL)
IGLV5-45(1-?) ProteinQ5NV82 (Uniprot-TrEMBL)
IGLV7-43(1-?) ProteinQ5NV80 (Uniprot-TrEMBL)
IGLV7-46(1-?) ProteinQ5NV83 (Uniprot-TrEMBL)
IGLV8-61(1-?) ProteinQ5NV62 (Uniprot-TrEMBL)
IL10 ProteinP22301 (Uniprot-TrEMBL)
IL10 gene ProteinENSG00000136634 (Ensembl)
IL10 geneGeneProductENSG00000136634 (Ensembl)
IL10ProteinP22301 (Uniprot-TrEMBL)
IL6 ProteinP05231 (Uniprot-TrEMBL)
IL6 gene ProteinENSG00000136244 (Ensembl)
IL6 geneGeneProductENSG00000136244 (Ensembl)
IL6ProteinP05231 (Uniprot-TrEMBL)
INSL3(106-131) ProteinP51460 (Uniprot-TrEMBL)
INSL3(21-55) ProteinP51460 (Uniprot-TrEMBL)
IP3 receptor homotetramerComplexR-HSA-169686 (Reactome)
ITPR1 ProteinQ14643 (Uniprot-TrEMBL)
ITPR2 ProteinQ14571 (Uniprot-TrEMBL)
ITPR3 ProteinQ14573 (Uniprot-TrEMBL)
ITPR:I(1,4,5)P3 tetramerComplexR-HSA-169696 (Reactome)
Ig heavy chain V-I region EU ProteinP01742 (Uniprot-TrEMBL)
Ig heavy chain V-I region HG3 ProteinP01743 (Uniprot-TrEMBL)
Ig heavy chain V-II region ARH-77 ProteinP06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region MCE ProteinP01817 (Uniprot-TrEMBL)
Ig heavy chain V-II region NEWM ProteinP01825 (Uniprot-TrEMBL)
Ig heavy chain V-II region OU ProteinP01814 (Uniprot-TrEMBL)
Ig heavy chain V-II region WAH ProteinP01824 (Uniprot-TrEMBL)
Ig heavy chain V-III region BRO ProteinP01766 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUT ProteinP01767 (Uniprot-TrEMBL)
Ig heavy chain V-III region CAM ProteinP01768 (Uniprot-TrEMBL)
Ig heavy chain V-III region DOB ProteinP01782 (Uniprot-TrEMBL)
Ig heavy chain V-III region JON ProteinP01780 (Uniprot-TrEMBL)
Ig heavy chain V-III region KOL ProteinP01772 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO ProteinP01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA ProteinP01763 (Uniprot-TrEMBL)
Ig kappa chain V region EV15 ProteinP06315 (Uniprot-TrEMBL)
Ig kappa chain V-I region AG ProteinP01593 (Uniprot-TrEMBL)
Ig kappa chain V-I region AU ProteinP01594 (Uniprot-TrEMBL)
Ig kappa chain V-I region BAN ProteinP04430 (Uniprot-TrEMBL)
Ig kappa chain V-I region DEE ProteinP01597 (Uniprot-TrEMBL)
Ig kappa chain V-I region Daudi ProteinP04432 (Uniprot-TrEMBL)
Ig kappa chain V-I region Gal ProteinP01599 (Uniprot-TrEMBL)
Ig kappa chain V-I region HK101 ProteinP01601 (Uniprot-TrEMBL)
Ig kappa chain V-I region Wes ProteinP01611 (Uniprot-TrEMBL)
Ig kappa chain V-II region Cum ProteinP01614 (Uniprot-TrEMBL)
Ig kappa chain V-II region FR ProteinP01615 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 ProteinP06310 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 ProteinP01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM ProteinP01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG ProteinP04433 (Uniprot-TrEMBL)
Ig lambda chain V region 4A ProteinP04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA ProteinP01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEW ProteinP01701 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEWM ProteinP01703 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR ProteinP01699 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH ProteinP01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region MGC ProteinP01709 (Uniprot-TrEMBL)
Ig lambda chain V-II region NEI ProteinP01705 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG ProteinP01704 (Uniprot-TrEMBL)
Ig lambda chain V-III region LOI ProteinP80748 (Uniprot-TrEMBL)
Ig lambda chain V-III region SH ProteinP01714 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Bau ProteinP01715 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Hil ProteinP01717 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Kern ProteinP01718 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR ProteinP01721 (Uniprot-TrEMBL)
IgG:LPG1G2ComplexR-HSA-9675736 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:p-3Y-PLCGComplexR-HSA-9664277 (Reactome)
IgG:Leishmania surface:p-FCGR3As:p-6Y-SYK:PLCGComplexR-HSA-9664266 (Reactome)
IgG:Lma

antigens:FCGR3A:CD3

dimers		ComplexR-HSA-9664263 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:SYKComplexR-HSA-9664272 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKComplexR-HSA-9664265 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimersComplexR-HSA-9664282 (Reactome)
IgG:Lma amastigote surfaceComplexR-HSA-9664283 (Reactome)
IgG:Lma antigensComplexR-HSA-9666422 (Reactome)
IgGComplexR-HSA-182629 (Reactome) In view of the highly variable nature of antibody proteins, this biological object is an approximate and fragmented representation of an IgM/IgD antibody, given the limitations of Ig chain enumeration in UniProt. A single mRNA transcript is alternatively spliced to give either IgM or IgD. Thus unactivated B cells contain both classes of antibody.
IgH heavy chain V-III region VH26 precursor ProteinP01764 (Uniprot-TrEMBL)
L-GluMetaboliteCHEBI:29985 (ChEBI)
LCHA MetaboliteCHEBI:16325 (ChEBI)
LHB ProteinP01229 (Uniprot-TrEMBL)
LHCGR ProteinP22888 (Uniprot-TrEMBL)
LPG1G2 ProteinQ4QD44 (Uniprot-TrEMBL)
LPG1G2ProteinQ4QD44 (Uniprot-TrEMBL)
LTC4 MetaboliteCHEBI:16978 (ChEBI)
LTC4:CyslTR1,2ComplexR-HSA-9664302 (Reactome)
LTC4MetaboliteCHEBI:16978 (ChEBI)
LTD4MetaboliteCHEBI:28666 (ChEBI)
LTE4MetaboliteCHEBI:15650 (ChEBI)
LYN ProteinP07948 (Uniprot-TrEMBL)
Ligand:GPCR

complexes that activate Gs:Heterotrimeric G-protein Gs

(inactive)		ComplexR-HSA-744885 (Reactome)
Lma amastigote surfaceR-LMA-9664274 (Reactome) This entity is intended to represent any molecule that might be at the outer cell surface of a Leishmania amastigote parasite.
Lma amastigote surface R-LMA-9664274 (Reactome) This entity is intended to represent any molecule that might be at the outer cell surface of a Leishmania amastigote parasite.
MC1R ProteinQ01726 (Uniprot-TrEMBL)
MC2R ProteinQ01718 (Uniprot-TrEMBL)
MC3R(1-360) ProteinP41968 (Uniprot-TrEMBL)
MC4R ProteinP32245 (Uniprot-TrEMBL)
MC5R ProteinP33032 (Uniprot-TrEMBL)
MYH9 ProteinP35579 (Uniprot-TrEMBL)
MYH9ProteinP35579 (Uniprot-TrEMBL)
Mg2+ MetaboliteCHEBI:18420 (ChEBI)
NAD+ MetaboliteCHEBI:57540 (ChEBI)
NAd MetaboliteCHEBI:18357 (ChEBI)
NPS ProteinP0C0P6 (Uniprot-TrEMBL)
NPSR1 ProteinQ6W5P4 (Uniprot-TrEMBL)
P2RY11 ProteinQ96G91 (Uniprot-TrEMBL)
PEA MetaboliteCHEBI:18397 (ChEBI)
PGD2 MetaboliteCHEBI:15555 (ChEBI)
PGE2 MetaboliteCHEBI:15551 (ChEBI)
PGI2 MetaboliteCHEBI:15552 (ChEBI)
PI(3,4,5)P3 MetaboliteCHEBI:16618 (ChEBI)
PI(3,4,5)P3MetaboliteCHEBI:16618 (ChEBI)
PI(4,5)P2MetaboliteCHEBI:18348 (ChEBI)
PKA catalytic subunitComplexR-HSA-111920 (Reactome)
PKA tetramer:4xcAMPComplexR-HSA-8951729 (Reactome)
PKA tetramerComplexR-HSA-111922 (Reactome)
PLC gamma1,2ComplexR-HSA-1169089 (Reactome)
PLCG1 ProteinP19174 (Uniprot-TrEMBL)
PLCG2 ProteinP16885 (Uniprot-TrEMBL)
PLK2 ProteinQ9NYY3 (Uniprot-TrEMBL)
PLK2, MAPK14ComplexR-HSA-9662745 (Reactome)
POMC(138-150) ProteinP01189 (Uniprot-TrEMBL)
POMC(138-176) ProteinP01189 (Uniprot-TrEMBL)
POMC(217-234) ProteinP01189 (Uniprot-TrEMBL)
POMC(77-87) ProteinP01189 (Uniprot-TrEMBL)
PPiMetaboliteCHEBI:29888 (ChEBI)
PRKACA ProteinP17612 (Uniprot-TrEMBL)
PRKACA,(PRKACB,PRKACG,PRKX)ComplexR-HSA-9615387 (Reactome)
PRKACB ProteinP22694 (Uniprot-TrEMBL)
PRKACG ProteinP22612 (Uniprot-TrEMBL)
PRKAR1A ProteinP10644 (Uniprot-TrEMBL)
PRKAR1B ProteinP31321 (Uniprot-TrEMBL)
PRKAR2A ProteinP13861 (Uniprot-TrEMBL)
PRKAR2B ProteinP31323 (Uniprot-TrEMBL)
PRKX ProteinP51817 (Uniprot-TrEMBL)
PTGDR ProteinQ13258 (Uniprot-TrEMBL)
PTGER2 ProteinP43116 (Uniprot-TrEMBL)
PTGER4 ProteinP35408 (Uniprot-TrEMBL)
PTGIR ProteinP43119 (Uniprot-TrEMBL)
PTH ProteinP01270 (Uniprot-TrEMBL)
PTH1R ProteinQ03431 (Uniprot-TrEMBL)
PTH2(62-100) ProteinQ96A98 (Uniprot-TrEMBL)
PTH2R ProteinP49190 (Uniprot-TrEMBL)
PTHLH ProteinP12272 (Uniprot-TrEMBL)
Protein Kinase A, catalytic subunitsComplexR-HSA-111917 (Reactome)
RAMP1 ProteinO60894 (Uniprot-TrEMBL)
RAMP2 ProteinO60895 (Uniprot-TrEMBL)
RAMP3 ProteinO60896 (Uniprot-TrEMBL)
RLN2(162-185) ProteinP04090 (Uniprot-TrEMBL)
RLN2(25-53) ProteinP04090 (Uniprot-TrEMBL)
RLN3(119-142) ProteinQ8WXF3 (Uniprot-TrEMBL)
RLN3(26-52) ProteinQ8WXF3 (Uniprot-TrEMBL)
RXFP1 ProteinQ9HBX9 (Uniprot-TrEMBL)
RXFP2 ProteinQ8WXD0 (Uniprot-TrEMBL)
SCT ProteinP09683 (Uniprot-TrEMBL)
SCTR ProteinP47872 (Uniprot-TrEMBL)
SRC-1 ProteinP12931-1 (Uniprot-TrEMBL)
SYK ProteinP43405 (Uniprot-TrEMBL)
SYKProteinP43405 (Uniprot-TrEMBL)
Src family kinases (SFKs)ComplexR-HSA-1861597 (Reactome)
TAAR1 ProteinQ96RJ0 (Uniprot-TrEMBL)
TAAR2 ProteinQ9P1P5 (Uniprot-TrEMBL)
TAAR3 ProteinQ9P1P4 (Uniprot-TrEMBL)
TAAR5 ProteinO14804 (Uniprot-TrEMBL)
TAAR6 ProteinQ96RI8 (Uniprot-TrEMBL)
TAAR8 ProteinQ969N4 (Uniprot-TrEMBL)
TAAR9 ProteinQ96RI9 (Uniprot-TrEMBL)
TSHB ProteinP01222 (Uniprot-TrEMBL)
TSHR ProteinP16473 (Uniprot-TrEMBL)
VIP(125-152) ProteinP01282 (Uniprot-TrEMBL)
VIPR1 ProteinP32241 (Uniprot-TrEMBL)
VIPR2 ProteinP41587 (Uniprot-TrEMBL)
YES1 ProteinP07947 (Uniprot-TrEMBL)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
Zn2+MetaboliteCHEBI:29105 (ChEBI)
cAMP MetaboliteCHEBI:17489 (ChEBI)
cAMP:PKA regulatory subunitComplexR-HSA-111923 (Reactome)
cAMPMetaboliteCHEBI:17489 (ChEBI)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCGComplexR-HSA-2029137 (Reactome)
glucocorticoid MetaboliteCHEBI:24261 (ChEBI)
iRHOM2ProteinQ6PJF5 (Uniprot-TrEMBL)
p-4Y-PLCG1 ProteinP19174 (Uniprot-TrEMBL)
p-6Y-CD247 ProteinP20963-1 (Uniprot-TrEMBL)
p-6Y-SYK ProteinP43405 (Uniprot-TrEMBL)
p-PLCGComplexR-HSA-2029095 (Reactome)
p-S,T-ADAM17(215-827):Zn2+ComplexR-HSA-9662806 (Reactome)
p-S133-CREB1 ProteinP16220 (Uniprot-TrEMBL)
p-S133-CREB1:IL10 geneComplexR-HSA-9664324 (Reactome)
p-S133-CREB1:IL6 geneComplexR-HSA-9662709 (Reactome)
p-S133-CREB1ProteinP16220 (Uniprot-TrEMBL)
p-T180,Y182-MAPK14 ProteinQ16539 (Uniprot-TrEMBL)
p-Y160,Y171-CD3G ProteinP09693 (Uniprot-TrEMBL)
p-Y288,Y304-FCGR2A ProteinP12318 (Uniprot-TrEMBL)
p-Y753,Y759,Y1217-PLCG2 ProteinP16885 (Uniprot-TrEMBL)
sCD163 ProteinQ86VB7 (Uniprot-TrEMBL)
sCD163:MYH9ComplexR-HSA-9663429 (Reactome)
sCD163ProteinQ86VB7 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ADAM17(1-214)ArrowR-HSA-9662786 (Reactome)
ADAM17(215-827):Zn2+ArrowR-HSA-9662773 (Reactome)
ADAM17(215-827):Zn2+ArrowR-HSA-9662818 (Reactome)
ADAM17(215-827):Zn2+R-HSA-9662818 (Reactome)
ADAM17(215-827):Zn2+R-HSA-9662823 (Reactome)
ADAM17(215-827)ArrowR-HSA-9662786 (Reactome)
ADAM17(215-827)R-HSA-9662773 (Reactome)
ADAM17ArrowR-HSA-9662747 (Reactome)
ADAM17R-HSA-9662747 (Reactome)
ADAM17R-HSA-9662786 (Reactome)
ADORA2B:Ade-Rib:Heterotrimeric G-protein Gs:GTPArrowR-HSA-9660824 (Reactome)
ADORA2B:Ade-Rib:Heterotrimeric G-protein Gs:GTPR-HSA-9660819 (Reactome)
ADORA2B:Ade-RibArrowR-HSA-9660829 (Reactome)
ADORA2B:Ade-RibR-HSA-9660828 (Reactome)
ADORA2BArrowR-HSA-9660819 (Reactome)
ADORA2BR-HSA-9660829 (Reactome)
ADPArrowR-HSA-111919 (Reactome)
ADPArrowR-HSA-9662823 (Reactome)
ADPArrowR-HSA-9664261 (Reactome)
ADPArrowR-HSA-9664275 (Reactome)
ADPArrowR-HSA-9664278 (Reactome)
AHCYL1:NAD+:ITPR1:I(1,4,5)P3 tetramerTBarR-HSA-169683 (Reactome)
ATPR-HSA-111919 (Reactome)
ATPR-HSA-111930 (Reactome)
ATPR-HSA-392129 (Reactome)
ATPR-HSA-9662823 (Reactome)
ATPR-HSA-9664261 (Reactome)
ATPR-HSA-9664275 (Reactome)
ATPR-HSA-9664278 (Reactome)
Ade-Rib:ADORA2B:Heterotrimeric G-protein Gs:GDPArrowR-HSA-9660828 (Reactome)
Ade-Rib:ADORA2B:Heterotrimeric G-protein Gs:GDPR-HSA-9660824 (Reactome)
Ade-RibArrowR-HSA-9660819 (Reactome)
Ade-RibR-HSA-9660829 (Reactome)
Adenylate cyclase (Mg2+ cofactor)R-HSA-163617 (Reactome)
Adenylate cyclase (Mg2+ cofactor)mim-catalysisR-HSA-111930 (Reactome)
CALM1:4xCa2+ArrowR-HSA-111930 (Reactome)
CALM1:4xCa2+ArrowR-HSA-74448 (Reactome)
CALM1R-HSA-74448 (Reactome)
CD163 geneR-HSA-9662781 (Reactome)
CD163(1051-1156)ArrowR-HSA-9662837 (Reactome)
CD163ArrowR-HSA-9662781 (Reactome)
CD163R-HSA-9662837 (Reactome)
CREB1R-HSA-111919 (Reactome)
CYSLTR1,CYSLTR2R-HSA-9664306 (Reactome)
Ca2+ArrowR-HSA-169683 (Reactome)
Ca2+R-HSA-169683 (Reactome)
Ca2+R-HSA-74448 (Reactome)
DAGsArrowR-HSA-202407 (Reactome)
DPEP1,2,3 dimersmim-catalysisR-HSA-266012 (Reactome)
FCGRIIIA:CD3G/CD3Z dimersR-HSA-9664268 (Reactome)
FURINmim-catalysisR-HSA-9662786 (Reactome)
G alpha

(s):GTP:Adenylate

cyclase		ArrowR-HSA-163617 (Reactome)
G alpha

(s):GTP:Adenylate

cyclase		mim-catalysisR-HSA-392129 (Reactome)
G alpha (s):GTPArrowR-HSA-9660819 (Reactome)
G alpha (s):GTPR-HSA-163617 (Reactome)
G-betagammaTBarR-HSA-111930 (Reactome)
G-protein alpha

(i):GTP:Adenylate

cyclase		TBarR-HSA-392129 (Reactome)
G-protein alpha

(z):GTP:Adenylate

cyclase		TBarR-HSA-392129 (Reactome)
G-protein beta-gamma complexArrowR-HSA-9660819 (Reactome)
GDPArrowR-HSA-9660824 (Reactome)
GGT1 dimerTBarR-HSA-9664306 (Reactome)
GGT1, 5 dimersmim-catalysisR-HSA-266046 (Reactome)
GTPR-HSA-9660824 (Reactome)
Glucocorticoid, IL6, IL10ArrowR-HSA-9662781 (Reactome)
GlyArrowR-HSA-266012 (Reactome)
H2OR-HSA-202407 (Reactome)
H2OR-HSA-266012 (Reactome)
H2OR-HSA-266046 (Reactome)
Heterotrimeric

G-protein Gs

(inactive)		R-HSA-9660828 (Reactome)
I(1,4,5)P3ArrowR-HSA-169683 (Reactome)
I(1,4,5)P3ArrowR-HSA-202407 (Reactome)
I(1,4,5)P3R-HSA-169680 (Reactome)
IL10 geneR-HSA-9664332 (Reactome)
IL10 geneR-HSA-9664346 (Reactome)
IL10ArrowR-HSA-9664346 (Reactome)
IL6 geneR-HSA-9662708 (Reactome)
IL6 geneR-HSA-9662710 (Reactome)
IL6ArrowR-HSA-9662710 (Reactome)
IP3 receptor homotetramerR-HSA-169680 (Reactome)
ITPR:I(1,4,5)P3 tetramerArrowR-HSA-169680 (Reactome)
ITPR:I(1,4,5)P3 tetramermim-catalysisR-HSA-169683 (Reactome)
IgG:LPG1G2ArrowR-HSA-9664397 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:p-3Y-PLCGArrowR-HSA-9664278 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:p-3Y-PLCGR-HSA-9664271 (Reactome)
IgG:Leishmania surface:p-FCGR3As:p-6Y-SYK:PLCGArrowR-HSA-9664270 (Reactome)
IgG:Leishmania surface:p-FCGR3As:p-6Y-SYK:PLCGR-HSA-9664278 (Reactome)
IgG:Lma

antigens:FCGR3A:CD3

dimers		ArrowR-HSA-9664268 (Reactome)
IgG:Lma

antigens:FCGR3A:CD3

dimers		R-HSA-9664275 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:SYKArrowR-HSA-9664273 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:SYKR-HSA-9664261 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKArrowR-HSA-9664261 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKArrowR-HSA-9664271 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKR-HSA-9664270 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimersArrowR-HSA-9664275 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimersR-HSA-9664273 (Reactome)
IgG:Lma amastigote surfaceArrowR-HSA-9664285 (Reactome)
IgG:Lma antigensR-HSA-9664268 (Reactome)
IgGR-HSA-9664285 (Reactome)
IgGR-HSA-9664397 (Reactome)
L-GluArrowR-HSA-266046 (Reactome)
LPG1G2R-HSA-9664397 (Reactome)
LTC4:CyslTR1,2ArrowR-HSA-9664306 (Reactome)
LTC4R-HSA-266046 (Reactome)
LTC4R-HSA-9664306 (Reactome)
LTD4ArrowR-HSA-266046 (Reactome)
LTD4R-HSA-266012 (Reactome)
LTE4ArrowR-HSA-266012 (Reactome)
Ligand:GPCR

complexes that activate Gs:Heterotrimeric G-protein Gs

(inactive)		mim-catalysisR-HSA-9660824 (Reactome)
Lma amastigote surfaceR-HSA-9664285 (Reactome)
MYH9R-HSA-9663426 (Reactome)
PI(3,4,5)P3ArrowR-HSA-9664271 (Reactome)
PI(3,4,5)P3R-HSA-9664278 (Reactome)
PI(4,5)P2R-HSA-202407 (Reactome)
PKA catalytic subunitArrowR-HSA-111925 (Reactome)
PKA catalytic subunitR-HSA-111924 (Reactome)
PKA tetramer:4xcAMPArrowR-HSA-8951727 (Reactome)
PKA tetramer:4xcAMPR-HSA-111925 (Reactome)
PKA tetramerR-HSA-8951727 (Reactome)
PLC gamma1,2R-HSA-9664270 (Reactome)
PLK2, MAPK14mim-catalysisR-HSA-9662823 (Reactome)
PPiArrowR-HSA-111930 (Reactome)
PPiArrowR-HSA-392129 (Reactome)
PRKACA,(PRKACB,PRKACG,PRKX)mim-catalysisR-HSA-111919 (Reactome)
Protein Kinase A, catalytic subunitsArrowR-HSA-111924 (Reactome)
R-HSA-111919 (Reactome) Protein kinase A (PKA) has two regulatory subunits and two catalytic subunits which are held together to form the holoenzyme and is activated upon binding of cAMP to the regulatory subunits. Once cAMP binds the regulatory subunits, the catalytic subunits are released to carry out phosphorylation of CREB1 at serine residue S133. Only the PKA catalytic subunit alpha, PRKACA, was directly demonstrated to phosphorylate CREB1 at S133, using recombinant mouse and rat proteins, respectively (Gonzalez and Montminy 1989). PKA catalytic subunits beta and gamma (PRKACB and PRKACG) are candidate CREB1 kinases based on indirect evidence and sequence similarity (Nagakura et al. 2002, Liang et al. 2007, James et al. 2009). PRKX is the catalytic subunit of the cAMP dependent protein kinase X, which shares the regulatory subunits and functional properties with the PKA. PRKX is highly expressed in the mouse fetal brain (Li et al. 2005) and is implicated in CREB1 phosphorylation through indirect evidence (Di Pasquale and Stacey 1998, Li et al. 2002).
R-HSA-111924 (Reactome) When cAMP level rises, the PKA catalytic subunit (C subunit) released from the holoenzyme enters the nucleus by passive diffusion whereas termination of signaling to the nucleus involves an active mechanism. In the nucleus, the C subunit binds to the heat-stable protein kinase inhibitor (PKI), and this binding not only inactivates the C subunit but also by conformational change unveils a nuclear export signal in PKI which leads to export of the C-PKI complex from the nucleus.
R-HSA-111925 (Reactome) The protein kinase A (PKA) regulatory subunit isoforms differ in their tissue specificity and functional characteristics. The specific isoform activated in response to glucagon signaling is not known. The PKA kinase is a tetramer of two regulatory and two catalytic subunits. The regulatory subunits block the catalytic subunits. Binding of cAMP to the regulatory subunit triggers dissociation of the tetramer into two active dimers made up of a regulatory and a catalytic subunit.
R-HSA-111930 (Reactome) Adenylate cyclase is responsive to calcium and calmodulin and produces cAMP. One important physiological role for Calmodulin is the regulation of adenylylcyclases. Four of the ten known adenylylcyclases are calcium sensitive, in particular type 8 (AC8).
R-HSA-163617 (Reactome) G(s)-alpha:GTP binds to inactive adenylate cyclase, causing a conformational transition in adenylate cyclase exposing the catalytic site and activating it.
R-HSA-169680 (Reactome) The IP3 receptor (IP3R) is an IP3-gated calcium channel. It is a large, homotetrameric protein, similar to other calcium channel proteins such as ryanodine. The four subunits form a 'four-leafed clover' structure arranged around the central calcium channel. Binding of ligands such as IP3 results in conformational changes in the receptor's structure that leads to channel opening.
R-HSA-169683 (Reactome) IP3 promotes the release of intracellular calcium.
R-HSA-202407 (Reactome) On recruitment to plasma membrane PLC-gamma1 then hydrolyses PIP2 producing two second messengers, diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). IP3 induces a transient increase in intracellular free Ca++, while DAG is a direct activator of protein kinase C (PKC theta). These process have been implicated in many cellular physiological functions like cell proliferation, cell growth and differentiation.
R-HSA-266012 (Reactome) Another outer surface membrane-bound, homodimeric enzyme, dipeptidase, existing in two forms DPEP1 (Adachi et al. 1989) and DPEP2 (Lee et al. 1983, Raulf et al. 1987), further hydrolyses leukotriene D4 (LTD4) to leukotriene E4 (LTE4), cleaving a glycine residue in the process.
R-HSA-266046 (Reactome) The reversible conversion of leukotriene C4 (LTC4) to leukotriene D4 (LTD4) is catalysed by gamma-glutamyl transferases 1 (GGT1) and 5 (GGT5). GGTs are present on the outer surface of plasma membranes and are a heterodimer of a heavy and a light chain. Its action involves the hydrolysis of the gamma-glutamyl peptide bond of glutathione and glutathione conjugates, releasing glutamate. In this example, LTC4 is a glutathione conjugate that is hydrolysed to LTD4 (Anderson et al. 1982, Wickham et al. 2011).
R-HSA-392129 (Reactome) The activation of adenylyl (adenylate) cyclase (AC) results in the production of adenosine-3',5'-monophosphate i.e. cyclic AMP. Humans have 9 genes encoding membrane-associated AC and one encoding a soluble AC. Two of the classes of heterotrimeric G-proteins are named according to their effect on AC; G(s) stimulates all membrane-bound ACs (the s in G(s) denotes AC stimulatory); the G(i) class inhibits some AC isoforms, particularly 5 and 6. Beta-gamma subunits of heterotrimeric G-proteins can also regulate AC. Ca2+/Calmodulin activates some AC isoforms (1, 8 and 3) but is inhibitory to others (5 and 6).
R-HSA-74448 (Reactome) Upon increase in calcium concentration, calmodulin (CaM) is activated by binding to four calcium ions (Crouch and Klee 1980).
R-HSA-8951727 (Reactome) Protein kinase A (PKA) regulatory subunit isoforms differ in their tissue specificity and functional characteristics. The isoform activated in response to glucagon signaling is not known.

PKA kinase is a tetramer of two regulatory and two catalytic subunits. The regulatory subunits block the activity of the catalytic subunits.

cAMP binds the regulatory subunits, which leads to dissociation of the tetramer into two active dimers made up of a regulatory and a catalytic subunit.
R-HSA-9660819 (Reactome) The classical view of G-protein signalling is that the G-protein alpha subunit dissociates from the beta:gamma dimer. Activated G alpha (s) 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-9660824 (Reactome) The liganded receptor undergoes a conformational change, generating a signal that is propagated in a manner that is not completely understood to the the G-protein. This stimulates the exchange of GDP for GTP in the G-protein alpha subunit, activating the G-protein. This event is negatively regulated by some Activators of G protein signaling (AGS) proteins, a class of proteins identified in yeast functional screens for proteins able to activate G protein signaling in the absence of a G protein–coupled receptor (GPCR) (Cismowski et al. 1999, Takesono et al. 1999). AGS proteins contain G protein regulatory (GPR) motifs (also referred to as the GoLoco motif) that bind and stabilize the Galpha subunit in its GDP-bound conformation (Mochizuki et al. 1996, Peterson et al. 2000, Cao et al. 2004, Blumer & Lanier 2014). Some RGS proteins similarly bind to Galpha preventing the exchange of GDP for GTP (Soundararajan et al. 2008).
R-HSA-9660828 (Reactome) The role of the guanine nucleotide-binding protein G alpha-s subunit (G alpha-s) (Kozasa T et al, 1988) is to activate adenylate cyclase, which, in turn, produces cAMP, which, in turn, activates cAMP-dependent protein kinase.
R-HSA-9660829 (Reactome) Adenosine receptors A2a and A2b (ADORA2A and ADORA2B) bind extracellular adenosine (Ado-Rib) and are believed to play a role in regulating myocardial oxygen consumption and coronary blood flow (Peterfreund 1996). The A2A receptor is responsible for regulating myocardial blood flow by vasodilation of the coronary arteries, which increases blood flow to the myocardium, but may lead to hypotension. Just as in A1 receptors, this normally serves as a protective mechanism. A2B receptor work (Pierce KD et al, 1992) has lagged behind research in the other adenosine receptors.
Both ADORA receptors mediate their actions by coupling with the G protein alpha s subunit which activates adenylyl cyclase and increases intracellular cAMP concentrations. In surfactant physiology, the receptor:adenosine complex positively regulates surfactant export from lamellar bodies. (Cooper JA et al, 1995; Linden J et al, 1999). Adenosine deaminase (CECR1, ADA2) degrades extracellular adenosine (Ade-Rib), reducing or neutralising the positive regulatory effect of adenosine in surfactant export.
R-HSA-9662708 (Reactome) The IL-6 promoter contains several transcription factor-responsive elements (Luo and Zheng 2016). CREB, a classical cAMP-inducible CRE-binding factor interacts with a region of the IL-6 promoter that is known as CRE-like sequence (Dendorfer et al. 1994). Moreover, IL-6 is a pleiotropic cytokine produced by a wide variety of cells including macrophages, T cells, B cells, fibroblasts, and endothelial cells (Yang et al. 2014).
R-HSA-9662710 (Reactome) The gene for IL-6 is located at chromosome 7 whose unit transcription consists of 5 exons and 4 introns. The promoter region contains several transcription start sites with response elements for nuclear factor (NF)-κB, enhancer-binding protein beta (C/EPBβ; formerly NF-IL6), activator protein (AP)-1 (Burger 2013) and CREB transcription factor (Dendorfer et al. 1994). The protein form of human IL-6 is a glycoprotein composed of 184 amino acids with a molecular weight of 21-28 kDa, depending on its degree of glycosylation. It has a 4-helix bundle structure made up of 4 long α-helices arranged in an up-up-down-down topology (Burger 2013).
R-HSA-9662747 (Reactome) In mice, inactive rhomboid protein 2 (iRHOM2) has been shown to be required for disintegrin and metalloproteinase domain-containing protein 17's (ADAM17) exit from the ER (Cavadas et al. 2017), through the trans-Golgi network and on to the plasma membrane (Adrain et al. 2012, McIlwain et al. 2012, Issuree et al. 2013, Cavadas et al. 2017).
R-HSA-9662773 (Reactome) A crystallography study revealed that disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) requires Zinc as a cofactor to function properly (Maskos et al. 1998).
R-HSA-9662781 (Reactome) The CD163 gene encodes scavenger receptor cysteine-rich type 1 protein M130 (CD163) which functions at the plasma membrane of macrophages (Etzerodt & Moestrup 2013). Glucocorticoid, interleukin (IL)-6 and IL-10 are some of the most potent stimulators of CD163 expression (Petra Högger et al. 1998, P Högger et al. 1998, Van den Heuvel et al. 1999, Buechler et al. 2000 & Sulahian et al. 2000, ). For simplicity, the steps involed in transcription and translation have been omitted.
R-HSA-9662786 (Reactome) Disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) is a type I transmembrane protein that consist of an N-terminal signal sequence followed by a prodomain, a metalloproteinase (catalytic) domain, a disintegrin domain, an EGF-like (cysteine-rich) domain, a single transmembrane domain and a cytoplasmic domain (Scheller et al. 2011, Lambrecht et al. 2018). While ADAM17 is being transported through the trans-Golgi network, FURIN cleaves the prodomain region of ADAM17 releasing the inhibitory part (Milla et al. 1999, Gonzales et al. 2004, Wong et al. 2015) and leaving the catalytically-active form (ADAM17(215-827) (Srour et al. 2003, Endres et al. 2003, Adrain et al. 2012, McIlwain et al. 2012, Wong et al. 2015).
R-HSA-9662818 (Reactome) In mice, inactive rhomboid protein 2 (iRHOM2) has been shown to be required for disintegrin and metalloproteinase domain-containing protein 17's (ADAM17) exit from the ER (Cavadas et al. 2017), through the trans-Golgi network and on to the plasma membrane (Adrain et al. 2012, McIlwain et al. 2012, Issuree et al. 2013, Cavadas et al. 2017).
R-HSA-9662823 (Reactome) The phosphorylation of disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) by PLK2 and MAPKs has been determined by direct and indirect experiments (Müllberg et al. 1993, Schwarz et al. 2014, Fan and Derynck 1999; Gechtman et al. 1999; Díaz-Rodríguez et al. 2002; Fan, Turck, and Derynck 2003 & Xu and Derynck 2010). Specifically, the phosphorylation at residues Thr735 (Díaz-Rodríguez et al. 2002 & Xu and Derynck 2010) and Ser819 is required for ectodomains shedding.
R-HSA-9662837 (Reactome) The scavenger receptor cysteine-rich type 1 (CD163) is a transmembrane macrophage protein which upon cleavage, leads to the release of a soluble form (sCD163, CD163(42-1050)) (Droste, Sorg, and Högger 1999 and Hintz et al. 2002). The inflammation-responsive protease ADAM17 can mediate the cleavage of CD163 to release sCD163 (Etzerodt et al. 2010 & Etzerodt et al. 2014).
R-HSA-9663426 (Reactome) The soluble form of CD163 (sCD163) has been suggested to inhibit activated T-lymphocyte proliferation (P Högger & Sorg 2001) by potentially binding to a non-muscle myosin heavy chain type a (MYH9) (Timmermann et al. 2004, Hou et al. 2019).
R-HSA-9664261 (Reactome) Multiple sites of phosphorylation are known to exist in SYK, which both regulate its activity and also serve as docking sites for other proteins. Some of these sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, and Y525 and Y526 within the activation loop of the kinase domain and Y630 in the C-terminus (Zhang et al. 2002, Lupher et al. 1998, Furlong et al. 1997). Phosphorylation of these tyrosine residues disrupts autoinhibitory interactions and results in kinase activation even in the absence of phosphorylated ITAM tyrosines (Tsang et al. 2008). SYK is primarily phosphorylated by Src family kinases and this acts as an initiating trigger by generating few molecules of activated SYK which are then involved in major SYK autophosphorylation (Hillal et al. 1997).
R-HSA-9664268 (Reactome) Leishmania amastigotes parasites opsonized by IgG are more susceptible to be phagocytosed through FcγRs. Nevertheless, besides the phagocytosis induction, the interaction IgG-FcγRs has been implicated in the synthesis induction, of several cytokines (Buxbaum 2013; Chu et al. 2010; Thomas and Buxbaum 2008). In particular, Buxbaum et al. in 2008 showed that IgGs bound glycoinositol phospholipids (GIPLs) of L. Mexicana and that IgG:GIPLs induces the synthesis of IL-10 through FcγRIII.
R-HSA-9664270 (Reactome) PLCgamma (PLCG) is recruited to FCGR and the phosphorylated Y342 and Y346 in SYK have been reported to be involved in the interaction of PLCG (Law et al. 1996). PLCG accumulates at the phagocytic cup during FCGR, but the exact role of PLCG in the regulation of phagocytosis is not clear. It may be involved in FCGR signaling by activating PKC through DAG production (Garcia-Garcia & Rosales 2002 )
R-HSA-9664271 (Reactome) Activated PLCG translocates to the plasmamembrane and interacts with the inositol ring of the membrane bound phosphatidylinositol 4,5-bisphosphate (PIP2) with its PH domain. The active enzyme promotes intracelllular signaling by catalysing the hydrolysis of PIP2 to generate the second messengers IP3 and DAG.
R-HSA-9664273 (Reactome) SYK is a tyrosine kinase related to ZAP70 that is expressed in all hematopoietic cells and coimmunoprecipitates with the gamma chain associated with FCGRIIIA in macrophages and with FCERI in mast cells. SYK is very important for FCGR phagocytosis and is recruited to these phosphorylated ITAM residues through its two SRC homology 2 (SH2) domains (Agarwal et al. 1993). When SYK kinase expression is inhibited with antisense oligonucleotides both in vitro and in vivo, phagocytosis and inflammation are abolished (Matsuda et al. 1997). The domain structure of SYK comprises a regulatory region at the N-terminus consisting of a pair of SH2 domains separated by an inter-SH2 linker called interdomain A, an SH2-domain-kinase linker termed interdomain B, and a C-terminal kinase domain (Arias-Palomo et al. 2009). In resting state SYK exists in an auto-inhibited conformation by the interactions between the SH2-SH2 regulatory region and the inter-SH2 linker and the catalytic domain. This interdomain interaction reduces the conformational flexibility required by the kinase domain for catalysis (Arias-Palomo et al. 2007). Changes in the orientation of the SH2 domains could control the disruption of the auto inhibitory interactions and the activation of SYK. These movements could be totally or partially induced by the binding to phosphorylated ITAMs and/or phosphorylation of tyrosine residues in interdomain A or B (Arias-Palomo et al. 2009). Tsang et al. suggested that SYK functions as an OR-gate switch with respect to phosphorylation and ITAM binding, as either one stimulus OR the other is sufficient to cause full activation (Tsang et al. 2008).
R-HSA-9664275 (Reactome) After cross linking, Fc gamma receptors are sequestered to lipid rafts where they are complexed with some of the tyrosine kinases of Src family and undergo phosphorylation on the tyrosine residues contained in conserved ITAM sequences. At least six out of nine members of the Src family kinases (SRC, FYN, FGR, HCK, YES and LYN ) have been identified in the phagocytic cells and are implicated in the initiation of Fc gamma mediated signaling. (Suzuki et al. 2000, Majeed et al. 2001, Kwiatkowska et al. 2003). Some of these kinases have been found associated with specific receptors. In monocytes HCK and LYN have been found associated with FCGRI (Durden et al. 1995), whereas only HCK with FCGRIIA (Ghazizadeh et al. 1994) while FGR in neutrophils (Hamada et al. 1993) and LCK in NK cells with FCGRIIIA (Pignata et al. 1993)
The implication of Src kinases in phosphorylation was first supported by pharmacological findings that herbimycin A, a tyrosine kinase inhibitor relatively specific for Src-family kinases, potently suppressed Fc receptor mediated functions (Greenberg et al. 1993, Suzuki et al. 2000). However, their particular involvement in phagocytosis remains unclear, as targeted disruption of single or multiple Src family genes did not result in significant alterations in phagocytosis (Hunter et al. 1993, Fitzer Attas et al. 2000, Suzuki et al. 2000). HCK, FGR and LYN triple-deficient (-/-) macrophages have shown significant delays in FCGR mediated phagocytosis, but these deficiencies do not completly disrupt the process (Fitzer Attas et al. 2000).
Tyrosine residues Y288 and Y304 (Y282 and Y298 according to the literature reference, it is 6 residues shorter compared to uniprot entry due to an alternate initiation codon usage), within ITAM sequence in the cytoplasmic domain of FCGRIIA are the key target sites that are phosphorylated by Src family kinases (Mitchell et al, 1994). In case of FCGRIA and FCGRIIIA the specific tyrosine residues within ITAMs of the associated gamma/zeta chains are phosphorylated by activated Src family kinases (SFKs) (Park et al. 1993).
R-HSA-9664278 (Reactome) PLCG is tyrosine phosphorylated by either SYK or Src kinases on three tyrosine residues and this phosphorylation enhances the activity of PLCG. Although maximal activation requires binding of PLCG to PIP3 with its plecstrin homology (PH) domain.
R-HSA-9664285 (Reactome) The internalization of Leishmania amastigotes by macrophages is thought to be mediated mainly through opsonization with immunoglobulins (Igs) which bind Fc gamma receptors (FCGRs), stimulating their uptake (Morehead et al 2002 & Padigel et al. 2005). Glycoinositol phospholipids (GIPLs) are the most abundant glycolipids on the surface of the amastigote form of Leishmania parasites and Buxbaum and colleagues showed that IgG1 in mice binds GIPL molecules on the amastigote stage of L. mexicana to subsequently induce phagocytosis through FCGRs (Buxbaum 2013).
R-HSA-9664306 (Reactome) The cysteinyl-leukotrienes (cys-LTs) are potent smooth muscle contractile agents mediating bronchoconstriction. Examples are LTC4, LTD4 and LTE4. There are two human cys-LT receptors, 1 (Lynch KR et al, 1999) and 2 (Heise CE et al, 2000). They mediate their effects via coupling to the G protein alpha q/11 subunit (Sarau HM et al, 1999). However, signalling downstream LTC4-cysLTR binding has been associated with the production of IL4, independent of the GPCR associated heterotrimeric protein Gq (Bandeira Melo et al. 2002).
R-HSA-9664332 (Reactome) The IL-10 promoter contains several transcription factor-responsive elements. (Asadullah et al 2003). In macrophages, the major source of IL-10, several receptor-mediated cytokine transcription end up in the activation of IL10 transcription factors, such as CREB (Platzer et al. 1995, Kelly et al 2010 & Sanin et al 2015)
R-HSA-9664346 (Reactome) The Interleukin 10 (IL10) gene is located at chromosome 1q31-32. It encodes for a protein with the same name that acts as a pleiotropic cytokine expressed primarily by monocytes and to a smaller degree by lymphocytes. IL10 down-regulates the expression of Th1 cytokines, MHC class II and costimulatory molecules on macrophages (Eskdale et al. 1997).
R-HSA-9664397 (Reactome) The internalization of Leishmania amastigotes by macrophages is thought to be mediated mainly through opsonization with immunoglobulins (Igs) which bind FcγRs, stimulating the uptake (Morehead et al 2002 & Padigel et al. 2005). Glycoinositol phospholipids (GIPLs) are the most abundant glycolipids on the surface of the amastigote form of Leishmania parasites and Buxbaum and colleagues showed that IgG1 in mice, binds the GIPL molecules on the amastigote stage of L. mexicana to subsequently induced the phagocytosis through FcγRs (Buxbaum 2013).
R-HSA-9665525 (Reactome) Solube CD163 (sCD163) is taken up by T-cells from the circulation by an unknown mechanism (Timmermann et al. 2004).
SYKR-HSA-9664273 (Reactome)
Src family kinases (SFKs)mim-catalysisR-HSA-9664261 (Reactome)
Src family kinases (SFKs)mim-catalysisR-HSA-9664275 (Reactome)
Zn2+R-HSA-9662773 (Reactome)
cAMP:PKA regulatory subunitArrowR-HSA-111925 (Reactome)
cAMPArrowR-HSA-111930 (Reactome)
cAMPArrowR-HSA-392129 (Reactome)
cAMPR-HSA-8951727 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCGmim-catalysisR-HSA-9664278 (Reactome)
iRHOM2mim-catalysisR-HSA-9662747 (Reactome)
iRHOM2mim-catalysisR-HSA-9662818 (Reactome)
p-PLCGArrowR-HSA-9664271 (Reactome)
p-PLCGmim-catalysisR-HSA-202407 (Reactome)
p-S,T-ADAM17(215-827):Zn2+ArrowR-HSA-9662823 (Reactome)
p-S,T-ADAM17(215-827):Zn2+mim-catalysisR-HSA-9662837 (Reactome)
p-S133-CREB1:IL10 geneArrowR-HSA-9664332 (Reactome)
p-S133-CREB1:IL10 geneArrowR-HSA-9664346 (Reactome)
p-S133-CREB1:IL6 geneArrowR-HSA-9662708 (Reactome)
p-S133-CREB1:IL6 geneArrowR-HSA-9662710 (Reactome)
p-S133-CREB1ArrowR-HSA-111919 (Reactome)
p-S133-CREB1R-HSA-9662708 (Reactome)
p-S133-CREB1R-HSA-9664332 (Reactome)
sCD163:MYH9ArrowR-HSA-9663426 (Reactome)
sCD163ArrowR-HSA-9662837 (Reactome)
sCD163ArrowR-HSA-9665525 (Reactome)
sCD163R-HSA-9663426 (Reactome)
sCD163R-HSA-9665525 (Reactome)
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