Immunoregulatory interactions between lymphoid and non-lymphoid cells (Homo sapiens)

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4, 11, 16, 27, 43...7, 40, 5936, 484528, 5522, 42, 4726, 38, 507, 40, 5921, 5713, 537, 40, 5913, 537, 40, 5941, 56323510, 1512, 17, 3325, 377, 40, 592, 6, 297, 40, 59513, 249, 34231, 8307, 40, 592020, 31184939, 52, 5814, 44, 54cellvirion membranecellcellcellHLA class Ihistocompatibilityantigen, E alphachain precursor Ig kappa chain V-IIregion MIL HLA class Ihistocompatibilityantigen, A-26 alphachain B2M(21-119) IGLV4-69(1-?) IGLC7 class I MHC B27 Ig kappa chain V-IIIregion NG9 TCR interacting withantigen-bearing MHCClass ICD96Ig lambda chain V-Iregion NEWM KLRD1HLA class Ihistocompatibilityantigen, alphachain G precursor IGLV11-55(1-?) HLA class Ihistocompatibilityantigen, A-23 alphachain Ig lambda chain V-IIregion TOG HLA class Ihistocompatibilityantigen, A-80 alphachain HLA class Ihistocompatibilityantigen, A-23 alphachain IGLC3 Ig lambda chain V-VIregion NIG-48 Ig lambda chain V-Iregion NIG-64 IGLV2-11(1-?) Ig lambda chain V-IVregion Kern class I MHC B35 HLA class Ihistocompatibilityantigen, Cw-17alpha chain HLA class Ihistocompatibilityantigen, Cw-4 alphachain precursor Ig kappa chain V-Iregion Rei Ig kappa chain V-IIIregion SIE Ig lambda chain V-IIregion MGC Ig lambda chainV-VII region MOT HLA-A3IGLV4-69(1-?) Ig kappa chain V-Iregion Daudi CD226Ig lambda chain V-IVregion Hil class I MHC B18 IFITM1 B2M(21-119) Ig lambda chain V-VIregion WLT IGLV3-27(1-?) IGLC2 class I MHC B46 HLA class Ihistocompatibilityantigen, alphachain G precursor class I MHC B13 ITGB7 Ig heavy chain V-IIregion NEWM HLA class Ihistocompatibilityantigen, A-34 alphachain CXADR bound to JAMLTYROBP Ig kappa chain V-IIIregion CLL HLA class Ihistocompatibilityantigen, A-30 alphachain IgH heavy chainV-III region VH26precursor CRTAM bound to NECL2Ig kappa chain V-IIIregion VH IGLV3-16(1-?) Ig lambda chainV-III region LOI Ig lambda chain V-IVregion MOL HLA-C Cw4 (group 2)SIGLECLFA-1:ICAM 1-4Ig heavy chain V-IIregion MCE HLA class Ihistocompatibilityantigen, A-25 alphachain Ig lambda chain V-VIregion EB4 IGKV4-1(21-?) HLA-Cgroup-I-interactingKIRsIg lambda chain V-IIregion TOG Ig kappa chain V-Iregion Gal HLA class Ihistocompatibilityantigen, alphachain G precursor Ig kappa chain V-IVregion Len HLA class Ihistocompatibilityantigen, A-36 alphachain Ig lambda chain V-Iregion HA Ig heavy chain V-IIregion DAW IGLV5-37(1-?) Ig heavy chain V-Iregion WOL CD40LG(1-261) B2M(21-119) HLA class Ihistocompatibilityantigen, A-24 alphachain HLA-C group 2interacting withKIR2DS1class I MHC B50 Ig kappa chain V-IIIregion NG9 Ig kappa chain V-IIIregion B6 HLA-Gclass I MHC B41 class I MHC B59 Ig kappa chain V-IIregion Cum HLA class Ihistocompatibilityantigen, Cw-8 alphachain CD200R1Ig heavy chain V-IIIregion TUR L-selectininteracting withknown ligandsIg kappa chain V-Iregion Lay Ig lambda chain V-IIregion BUR SLAMF6:SLAMF6VCAM1CD247-1 KLRK1 CD40-1 ITGB2 HLA class Ihistocompatibilityantigen, A-1 alphachain precursor ITGA4 Ig heavy chain V-IIIregion TIL Ig kappa chain V-Iregion EU IGHV7-81(1-?) Ig kappa chain V-IIIregion Ti TRAC Ig kappa chain V-IIIregion IARC/BL41 Ig kappa chain V-Iregion HK101 IGLV2-23(1-?) Ig kappa chain V-Iregion Hau HLA class Ihistocompatibilityantigen, A-31 alphachain C3d complexed withantigenIGLV1-44(1-?) HLA class Ihistocompatibilityantigen, Cw-4 alphachain precursor Ig kappa chain Vregion EV15 Ig kappa chain V-Iregion Gal Ig lambda chain V-IVregion Kern IGLV5-45(1-?) IGLC2 HLA class Ihistocompatibilityantigen, A-11 alphachain HLA class Ihistocompatibilityantigen, Cw-5 alphachain precursor Ig kappa chain V-Iregion Ni Ig heavy chain V-IIregion SESS IGLV4-60(1-?) IGLV5-45(1-?) CD200Ig kappa chain V-IVregion STH Ig kappa chain V-IIIregion POM TCRB KLRB1 B2M(21-119) HLA class Ihistocompatibilityantigen, A-69 alphachain Ig kappa chain V-IIIregion B6 CD40:CD40L trimerIg lambda chain V-IVregion Bau HLA class Ihistocompatibilityantigen, A-29 alphachain CXADRIg kappa chain V-Iregion Walker Ig heavy chain V-IIIregion POM Ig heavy chain V-Iregion ND class I MHC B55 IGLV(23-?) KIR2DS2 Complex of CD19,CD81, CD225 andCD21 with C3d-boundAntigenIg heavy chain V-IIregion SESS HLA Bw4 interactingwith KIR3DL1Ig kappa chain V-IVregion JI IGLV4-3(1-?) KIR2DL2 Ig lambda chain V-IVregion Bau CD34-1 CD19 Ig kappa chain V-Iregion Hau IGKV1-5(23-?) class I MHC B47 class I MHC B55 Ig heavy chain V-IIIregion JON class I MHC B8 IGKC class I MHC B44 Lymphoid-expressedFc-gamma receptorsICAM3 SLAMF7TCRA HLA class Ihistocompatibilityantigen, A-29 alphachain KLRF1 MADCAM1-1HLA class Ihistocompatibilityantigen, Cw-18alpha chain Ig kappa chain V-Iregion Wes class I MHC B59 Ig heavy chain V-IIIregion WEA Ig kappa chain V-Iregion OU Ig kappa chain V-Iregion AG Ig heavy chain V-IIIregion WAS HLA class Ihistocompatibilityantigen, Cw-16alpha chain class I MHC B56 HA class I MHC B38 Ig kappa chain V-IVregion B17 HLA class Ihistocompatibilityantigen, Cw-3 alphachain precursor HLA class Ihistocompatibilityantigen, A-74 alphachain HLA class Ihistocompatibilityantigen, Cw-15alpha chain NKG2D ligandMHC Class Iinteracting withLILRsIg heavy chain V-IIregion OU class I MHC B67 CD247-1 C3d fragment Ig kappa chain V-IIregion RPMI 6410 class I MHC B51 Ig kappa chain V-IIIregion SIE HLA class Ihistocompatibilityantigen, Cw-3 alphachain precursor IGHV(1-?) Ig lambda chain V-IIregion BOH CD3D ICAM2 Ig kappa chain V-Iregion HK101 ICAM4 HLA class Ihistocompatibilityantigen, Cw-3 alphachain precursor FCGR1A IGLV8-61(1-?) B2M(21-119) HLA class Ihistocompatibilityantigen, A-25 alphachain HN Ig kappa chain V-Iregion AG ITGA4 CD81 Ig kappa chain V-IVregion Len HLA-C group 2interacting withKIR2DL1class I MHC B35 CXADR class I MHC B7 ITGAL Ig heavy chain V-Iregion ND FCGR1A Ig lambda chain V-Iregion WAH SAP,EAT2CDH1(155-882)class I MHC B56 Ig kappa chain V-Iregion Mev IGLC6 HLA class Ihistocompatibilityantigen, alphachain G precursor CDH1(155-882) Ig heavy chain V-IIregion COR Ig heavy chain V-IIIregion GA KLRG1Ig lambda chain V-Iregion WAH Ig kappa chain V-Iregion AU Ig heavy chain V-Iregion Mot class I MHC B47 IGLC3 Ig lambda chain V-VIregion AR Ig kappa chain V-IIIregion GOL MICB E-cadherin bound toKLRG1NCR1 B2M(21-119) integrinalpha4beta1:VCAM1class I MHC B81 class I MHC B18 B2M(21-119) Ig kappa chain V-Iregion Scw IGLV3-16(1-?) CD226 HLA class Ihistocompatibilityantigen, A-24 alphachain CLEC2D dimerIGLV2-33(1-?) T-cell receptoralpha chain Vregion HPB-MLTprecursor HLA class Ihistocompatibilityantigen, A-36 alphachain IGLV8-61(1-?) KLRG1 HLA class Ihistocompatibilityantigen, Cw-16alpha chain Ig kappa chain V-IIregion TEW class I MHC B37 Ig lambda chain V-IIregion WIN Ig kappa chain V-Iregion WAT LAIR1Ig kappa chain Vregion EV15 TYROBP class I MHC B78 HLA class Ihistocompatibilityantigen, Cw-4 alphachain precursor Ig heavy chain V-Iregion SIE Ig kappa chain V-IIIregion VG CLEC2D Ig kappa chain V-IIregion Cum IGLV3-22(1-?) Ig lambda chain V-IVregion MOL Ig lambda chain V-VIregion SUT CD3G Ig heavy chain V-IIregion DAW ICAM1 Antigen-bound Ig GAntibodyKIR3DL2IGKC Ig kappa chain V-Iregion BAN SLAMF6HLA class Ihistocompatibilityantigen, Cw-12alpha chain Ig kappa chain V-IIIregion POM class I MHC B58 class I MHC B38 HLA class Ihistocompatibilityantigen, alphachain F precursor HLA-C group 1interacting withKIR2DL2/3IGLV1-36(1-?) CD200R1 IGKVA18(21-?) Ig kappa chain V-IVregion STH VCAM1 Ig lambda chain V-IIregion NIG-84 Ig heavy chain V-Iregion Mot Ig heavy chain V-IIIregion TUR HLA class Ihistocompatibilityantigen, Cw-14alpha chain Ig kappa chain V-IIregion FR SELL class I MHC B8 MADCAM1-1 IGLC6 Ig lambda chain V-Iregion VOR Ig kappa chain V-IIregion MIL T-cell receptoralpha chain Vregion PY14precursor Antigen-boundantibody bound tolymphoid Fc gammareceptorsIg heavy chain V-IIIregion BUT Ig kappa chain V-IIregion TEW Ig lambda chain V-IIregion NIG-58 Ig kappa chain V-IIIregion WOL Ig lambda chain V-IIregion TRO HLA class Ihistocompatibilityantigen, Cw-2 alphachain IGLV1-44(1-?) Ig kappa chain V-Iregion Bi class I MHC B54 Ig lambda chain V-VIregion NIG-48 IGLC1 T-cell receptoralpha chain Vregion HPB-MLTprecursor IGLV1-40(1-?) class I MHC B14 IGLV2-18(1-?) B2M(21-119) HLA-A3 interactingwith KIR3DL2PVRL2Ig kappa chain V-IVregion B17 CD40LG(1-261) KLRK1 IGLV5-37(1-?) IGLV3-12(1-?) NCR1:FCRG1A:CD3ZdimerAMICA1Ig kappa chain V-Iregion Lay KLRF1 dimer:CLEC2BdimerSLAMF6 FCGR3A CLEC2B IGLV2-33(1-?) NCR3LG1 Ig lambda chain V-Iregion NIG-64 Ig heavy chain V-IIIregion KOL HLA class Ihistocompatibilityantigen, A-68 alphachain class I MHC B15 PVRL2 HLA class Ihistocompatibilityantigen, Cw-3 alphachain precursor class I MHC B13 HLA class Ihistocompatibilityantigen, Cw-15alpha chain Ig lambda chain V-VIregion SUT Ig kappa chain V-Iregion Rei Ig kappa chain V-Iregion Scw IGLV7-46(1-?) LILR setIg heavy chain V-IIIregion WEA Ig lambda chain V-IIregion VIL Collagen type XVIIfibrilIg lambda chain V-VIregion EB4 Integrin alpha4beta1IGLV4-3(1-?) KIR3DL2 Ig lambda chain V-Iregion VOR HLA-G interactingwith KIR2DL4CD8A Ig kappa chain V-IIregion RPMI 6410 CD226:PVRSLAMF6:SLAMF6:SAP,EAT2Ig heavy chain V-IIIregion GAL Ig heavy chain V-Iregion HG3 IGLV7-46(1-?) class I MHC B78 HLA class Ihistocompatibilityantigen, A-3 alphachain precursor IGHV(1-?) B2M(21-119) Ig lambda chain V-IIregion NEI CD247-1 Ig heavy chain V-IIIregion BRO HLA class Ihistocompatibilityantigen, Cw-2 alphachain KIR2DL4 Ig lambda chain V-IIregion BOH Ig lambda chainV-III region LOI Ig heavy chain V-IIIregion NIE B2M(21-119) class I MHC B38 IGLV7-43(1-?) class I MHC B53 Ig kappa chain V-IVregion JI class I MHC B38 HCST TCRB HLA class Ihistocompatibilityantigen, Cw-18alpha chain CLEC2D KIR2DS1 Ig kappa chain V-Iregion Walker NCR1 class I MHC B15 ULBP3 Ig heavy chain V-IIIregion TRO Ig kappa chain V-Iregion CAR NCR3 CD247-1 T-cell receptoralpha chain Vregion PY14precursor B2M(21-119) TRAC KLRF1 Ig kappa chain V-Iregion Ka B2M(21-119) Ig kappa chain V-Iregion BAN HLA class Ihistocompatibilityantigen, Cw-8 alphachain class I MHC B14 HLA class Ihistocompatibilityantigen, A-66 alphachain Ig heavy chain V-IIIregion DOB class I MHC B40 CRTAMHLA-C Cw3 (group 1)KLRB1 IGLV3-27(1-?) KIR2DL1 B2M(21-119) Ig lambda chain V-VIregion AR Ig heavy chain V-IIIregion TRO Ig lambda chain V-IIregion BO TRBC1 Ig lambda chain V-IIregion TRO B2M(21-119) MHC Class Iinteracting withCD160KLRC1 HLA class Ihistocompatibilityantigen, alphachain F precursor Ig kappa chain V-Iregion DEE IGLV2-11(1-?) Ig kappa chain V-IIregion GM607 Ig kappa chain V-Iregion AU FCGR1A HLA class Ihistocompatibilityantigen, Cw-4 alphachain precursor class I MHC B42 FCGR1A Ig lambda chain V-Iregion MEM CD3D IGLV4-60(1-?) SLAMF7 Ig heavy chain V-IIIregion ZAP L-selectin ligandsCD247-1 Integrinalpha4beta7:MADCAM1T-cell receptorcomplex with CD8B2M(21-119) HLA class Ihistocompatibilityantigen, A-32 alphachain KLRB1 dimerIg heavy chain V-IIregion HE Ig kappa chain V-Iregion Wes MADCAM1-1 HLA class Ihistocompatibilityantigen, A-43 alphachain CD160 CD19 KIR3DL1HLA class Ihistocompatibilityantigen, A-69 alphachain NCR1:FCRG1A:CD3Zdimer:HemagglutininCD160KLRC1HLA class Ihistocompatibilityantigen, A-43 alphachain KIR2DS2 HLA class Ihistocompatibilityantigen, Cw-3 alphachain precursor HLA class Ihistocompatibilityantigen, A-2 alphachain class I MHC B7 class I MHC B54 CD81 Ig kappa chain V-Iregion Mev Ig kappa chain V-IIIregion HAH Ig kappa chain V-Iregion OU IFITM1 Ig kappa chain V-Iregion Kue Ig heavy chain V-IIIregion BRO PVR IGLV10-54(1-?) SH2D1A Ig kappa chain V-Iregion WAT Ig heavy chain V-IIIregion TEI CD3E Ig lambda chain V-IIregion MGC CLEC2D dimer:KLRB1dimerclass I MHC B49 class I MHC B27 class I MHC B41 Ig heavy chain V-IIIregion GAL Ig lambda chain Vregion 4A class I MHC B67 Ig kappa chain V-IIIregion IARC/BL41 Ig lambda chain Vregion 4A TRBC1 Ig kappa chain V-Iregion Roy Ig lambda chain V-IIregion VIL class I MHC B51 class I MHC B50 Ig heavy chain V-IIIregion HIL class I MHC B81 Ig lambda chain V-VIregion WLT Ig kappa chain V-IIIregion CLL IGLV(23-?) class I MHC B52 Ig kappa chain V-Iregion WEA IGLV3-25(1-?) IGLV11-55(1-?) Ig lambda chain V-Iregion HA PVR HLA class Ihistocompatibilityantigen, Cw-12alpha chain ITGA4 IGLV1-40(1-?) Ig heavy chain V-IIIregion CAM Ig heavy chain V-Iregion EU Ig lambda chainV-VII region MOT Ig heavy chain V-Iregion EU KIR3DL1 PVRL2 NKG2D complexed withDAP10class I MHC B82 Complex of CD19,CD81, CD225 andCD21KIR2DL1class I MHC B73 BAG6,NCR3LG1,pp65:NCR3:FCRG3A:CD3Z dimerclass I MHC B46 HLA-E interactingwith KLRC1:KLRD1Sialic acidIg lambda chainV-III region SH HLA class Ihistocompatibilityantigen, Cw-17alpha chain HLA-C group 1interacting withKIR2DS2CD8B Ig heavy chain V-IIregion ARH-77 Ig heavy chain V-IIIregion DOB HLA class Ihistocompatibilityantigen, E alphachain precursor Ig heavy chain V-IIIregion GA Ig lambda chain V-Iregion NEWM class I MHC B52 Ig heavy chain V-IIIregion LAY CLEC2B dimerB2M(21-119) BAG6,NCR3LG1,pp65HLA class Ihistocompatibilityantigen, A-30 alphachain SIGLEC:sialic acidIg heavy chain V-IIIregion NIE HLA class Ihistocompatibilityantigen, Cw-5 alphachain precursor Ig heavy chain V-IIregion ARH-77 IGLV10-54(1-?) TRBV12-3 PVRclass I MHC B58 Ig kappa chain V-Iregion DEE Ig kappa chain V-Iregion Bi CLEC2B Ig heavy chain V-IIIregion HIL B2M(21-119) MHC Class Imoleculesinteracting withCD160TYROBP LILR-interacting MHCClass I moleculesIntegrin alphaLbeta2HLA class Ihistocompatibilityantigen, E alphachain precursor NCR3:FCRG1A:CD3ZdimerFCGR2B HLA class Ihistocompatibilityantigen, Cw-1 alphachain BAG6 Ig lambda chain V-IIregion BO class I MHC B49 HLA class Ihistocompatibilityantigen, A-26 alphachain Ig heavy chain V-IIregion OU TYROBP IgH heavy chainV-III region VH26precursor KIR2DL4HLA class Ihistocompatibilityantigen, A-33 alphachain class I MHC B40 SH2D1B Ig lambda chain V-Iregion BL2 HLA class Ihistocompatibilityantigen, Cw-1 alphachain Ig lambda chain V-IVregion X cd21(1-?) HLA class Ihistocompatibilityantigen, A-3 alphachain precursor HLA class Ihistocompatibilityantigen, Cw-14alpha chain HLA class Ihistocompatibilityantigen, Cw-7 alphachain precursor class I MHC B57 ITGB1 HLA class Ihistocompatibilityantigen, Cw-6 alphachain precursor IGKV4-1(21-?) KIR2DS2 complexedwith DAP12HLA class Ihistocompatibilityantigen, A-1 alphachain precursor class I MHC B44 Ig lambda chain V-Iregion BL2 IGKV1-5(23-?) NCR3 HLA class Ihistocompatibilityantigen, A-34 alphachain LAIR1:Collagen typeXVIICD226 bound toNectin 2Ig kappa chain V-Iregion Roy class I MHC B39 HLA class Ihistocompatibilityantigen, A-33 alphachain SELLclass I MHC B57 B2M(21-119) class I MHC B39 ITGB2 IGLV3-22(1-?) Sialic acid IGLV2-23(1-?) Ig heavy chain V-IIIregion JON Ig heavy chain V-IIIregion CAM Ig heavy chain V-Iregion WOL Ig kappa chain V-IIIregion HIC Ligand interactingwith NKG2DRAET1E IGLV3-12(1-?) Antigen peptidebound class I MHCIg lambda chain V-Iregion NEW Ig lambda chain V-IIregion NEI class I MHC B37 Ig lambda chainV-III region SH Ig lambda chain V-IIregion BUR Ig lambda chain V-IIregion NIG-84 KIR2DS1 CD96 ITGAL Ig heavy chain V-IIIregion TEI IGLV1-36(1-?) KLRF1 dimerCD200 bound toCD200RITGB7 ULBP1 Ig kappa chain V-IIIregion VH CD200 Ig lambda chain V-IIregion NIG-58 KIR2DS1 complexedwith DAP12Ig heavy chain V-IIIregion TIL KIR2DL3 CD3G AMICA1 Ig heavy chain V-IIregion WAH IGLC7 HLA class Ihistocompatibilityantigen, Cw-7 alphachain precursor Ig kappa chain V-Iregion WEA TCRA CD8B TRBV12-3 CD3E CD247-1 HLA class Ihistocompatibilityantigen, A-3 alphachain precursor Ig kappa chain V-IIIregion WOL Ig heavy chain V-IIregion HE IGKVA18(21-?) IGLV3-25(1-?) HLA class Ihistocompatibilityantigen, A-3 alphachain precursor Ig heavy chain V-IIIregion WAS Ig heavy chain V-IIIregion POM CD8A HLA class Ihistocompatibilityantigen, A-2 alphachain CD96:PVRHLA class Ihistocompatibilityantigen, Cw-6 alphachain precursor IGLV2-18(1-?) Integrin alpha4beta7HLA class Ihistocompatibilityantigen, Cw-4 alphachain precursor HLA class Ihistocompatibilityantigen, E alphachain precursor Ig heavy chain V-Iregion SIE Ig heavy chain V-IIregion NEWM Ig lambda chain V-Iregion EPS ITGA4 class I MHC B73 class I MHC B45 HLA class Ihistocompatibilityantigen, A-74 alphachain HLA-Bw4Ig lambda chain V-Iregion MEM Ig lambda chain V-IVregion X IGLC1 Ig heavy chain V-IIIregion BUR pp65 CD226 SLAMF7:SLAMF7CD40 trimerIg heavy chain V-IIIregion ZAP IGHV7-81(1-?) Ig kappa chain V-IIIregion HIC class I MHC B42 Ig kappa chain V-IIIregion Ti Ig lambda chain V-IIregion WIN GLYCAM1 Ig heavy chain V-IIIregion BUR Ig kappa chain V-IIIregion GOL Ig kappa chain V-Iregion Daudi HLA class Ihistocompatibilityantigen, A-32 alphachain Ig kappa chain V-IIregion FR Ig heavy chain V-IIIregion BUT KLRD1 Ig kappa chain V-IIIregion VG HemagglutininC3d fragment HLA class Ihistocompatibilityantigen, A-80 alphachain ITGB1 Ig kappa chain V-Iregion EU Ig lambda chain V-Iregion EPS Ig heavy chain V-Iregion HG3 IGLV7-43(1-?) Ig kappa chain V-IIregion GM607 Ig lambda chain V-Vregion DEL Ig heavy chain V-IIIregion KOL HLA class Ihistocompatibilityantigen, A-68 alphachain Ig kappa chain V-IIIregion HAH cd21(1-?) class I MHC B45 Ig kappa chain V-Iregion Kue Ig heavy chain V-IIregion WAH Ig heavy chain V-IIIregion LAY class I MHC B53 HLA class Ihistocompatibilityantigen, A-31 alphachain ICAM 1-4HLA class Ihistocompatibilityantigen, A-66 alphachain CD40-1 Ig kappa chain V-Iregion Ka HLA class Ihistocompatibilityantigen, A-11 alphachain CD40LG trimerHCST LAIR1 HLA-EIg heavy chain V-IIregion MCE Ig kappa chain V-Iregion Ni class I MHC B82 Ig heavy chain V-IIregion COR CRTAM Ig lambda chain V-Vregion DEL Ig lambda chain V-Iregion NEW Ig lambda chain V-IVregion Hil Ig kappa chain V-Iregion CAR SLAMF6 19, 5919, 5919, 59519, 59


Description

A number of receptors and cell adhesion molecules play a key role in modifying the response of cells of lymphoid origin (such as B-, T- and NK cells) to self and tumor antigens, as well as to pathogenic organisms.

<p>Molecules such as KIRs and LILRs form part of a crucial surveillance system that looks out for any derangement, usually caused by cancer or viral infection, in MHC Class I presentation. Somatic cells are also able to report internal functional impairment by displaying surface stress markers such as MICA. The presence of these molecules on somatic cells is picked up by C-lectin NK immune receptors.<p><p>Lymphoid cells are able to regulate their location and movement in accordance to their state of activation, and home in on tissues expressing the appropriate complementary ligands. For example, lymphoid cells may fine tune the presence and concentration of adhesion molecules belonging to the IgSF, Selectin and Integrin class that interact with a number of vascular markers of inflammation.<p><p>Furthermore, there are a number of avenues through which lymphoid cells may interact with antigen. This may be presented directly to a specific T-cell receptor in the context of an MHC molecule. Antigen-antibody complexes may anchor to the cell via a small number of lymphoid-specific Fc receptors that may, in turn, influence cell function further. Activated complement factor C3d binds to both antigen and to cell surface receptor CD21. In such cases, the far-reaching influence of CD19 on B-lymphocyte function is tempered by its interaction with CD21. Source:Reactome.</div>

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  1. Fuchs A, Colonna M.; ''The role of NK cell recognition of nectin and nectin-like proteins in tumor immunosurveillance.''; PubMed Europe PMC Scholia
  2. Lenting PJ, Westerlaken GH, Denis CV, Akkerman JW, Meyaard L.; ''Efficient inhibition of collagen-induced platelet activation and adhesion by LAIR-2, a soluble Ig-like receptor family member.''; PubMed Europe PMC Scholia
  3. Tabata S, Kuroki K, Wang J, Kajikawa M, Shiratori I, Kohda D, Arase H, Maenaka K.; ''Biophysical characterization of O-glycosylated CD99 recognition by paired Ig-like type 2 receptors.''; PubMed Europe PMC Scholia
  4. Rosen DB, Bettadapura J, Alsharifi M, Mathew PA, Warren HS, Lanier LL.; ''Cutting edge: lectin-like transcript-1 is a ligand for the inhibitory human NKR-P1A receptor.''; PubMed Europe PMC Scholia
  5. Kaifu T, Escalière B, Gastinel LN, Vivier E, Baratin M.; ''B7-H6/NKp30 interaction: a mechanism of alerting NK cells against tumors.''; PubMed Europe PMC Scholia
  6. Binici J, Koch J.; ''BAG-6, a jack of all trades in health and disease.''; PubMed Europe PMC Scholia
  7. Welte S, Kuttruff S, Waldhauer I, Steinle A.; ''Mutual activation of natural killer cells and monocytes mediated by NKp80-AICL interaction.''; PubMed Europe PMC Scholia
  8. Fuchs A, Cella M, Giurisato E, Shaw AS, Colonna M.; ''Cutting edge: CD96 (tactile) promotes NK cell-target cell adhesion by interacting with the poliovirus receptor (CD155).''; PubMed Europe PMC Scholia
  9. Zajonc DM, Crispin MD, Bowden TA, Young DC, Cheng TY, Hu J, Costello CE, Rudd PM, Dwek RA, Miller MJ, Brenner MB, Moody DB, Wilson IA.; ''Molecular mechanism of lipopeptide presentation by CD1a.''; PubMed Europe PMC Scholia
  10. Latour S, Veillette A.; ''The SAP family of adaptors in immune regulation.''; PubMed Europe PMC Scholia
  11. Merck E, Gaillard C, Gorman DM, Montero-Julian F, Durand I, Zurawski SM, Menetrier-Caux C, Carra G, Lebecque S, Trinchieri G, Bates EE.; ''OSCAR is an FcRgamma-associated receptor that is expressed by myeloid cells and is involved in antigen presentation and activation of human dendritic cells.''; PubMed Europe PMC Scholia
  12. Mizuno T, Yoshihara Y, Inazawa J, Kagamiyama H, Mori K.; ''cDNA cloning and chromosomal localization of the human telencephalin and its distinctive interaction with lymphocyte function-associated antigen-1.''; PubMed Europe PMC Scholia
  13. Sawicki MW, Dimasi N, Natarajan K, Wang J, Margulies DH, Mariuzza RA.; ''Structural basis of MHC class I recognition by natural killer cell receptors.''; PubMed Europe PMC Scholia
  14. Cao E, Ramagopal UA, Fedorov A, Fedorov E, Yan Q, Lary JW, Cole JL, Nathenson SG, Almo SC.; ''NTB-A receptor crystal structure: insights into homophilic interactions in the signaling lymphocytic activation molecule receptor family.''; PubMed Europe PMC Scholia
  15. Rabot M, Tabiasco J, Polgar B, Aguerre-Girr M, Berrebi A, Bensussan A, Strbo N, Rukavina D, Le Bouteiller P.; ''HLA class I/NK cell receptor interaction in early human decidua basalis: possible functional consequences.''; PubMed Europe PMC Scholia
  16. de Jong A.; ''Activation of human T cells by CD1 and self-lipids.''; PubMed Europe PMC Scholia
  17. Wang J, Springer TA.; ''Structural specializations of immunoglobulin superfamily members for adhesion to integrins and viruses.''; PubMed Europe PMC Scholia
  18. Brown D, Trowsdale J, Allen R.; ''The LILR family: modulators of innate and adaptive immune pathways in health and disease.''; PubMed Europe PMC Scholia
  19. Molloy EJ.; ''Triggering Receptor Expressed on Myeloid Cells (TREM) family and the application of its antagonists.''; PubMed Europe PMC Scholia
  20. Kim JR, Horton NC, Mathew SO, Mathew PA.; ''CS1 (SLAMF7) inhibits production of proinflammatory cytokines by activated monocytes.''; PubMed Europe PMC Scholia
  21. Barrow AD, Raynal N, Andersen TL, Slatter DA, Bihan D, Pugh N, Cella M, Kim T, Rho J, Negishi-Koga T, Delaisse JM, Takayanagi H, Lorenzo J, Colonna M, Farndale RW, Choi Y, Trowsdale J.; ''OSCAR is a collagen receptor that costimulates osteoclastogenesis in DAP12-deficient humans and mice.''; PubMed Europe PMC Scholia
  22. Galibert L, Diemer GS, Liu Z, Johnson RS, Smith JL, Walzer T, Comeau MR, Rauch CT, Wolfson MF, Sorensen RA, Van der Vuurst de Vries AR, Branstetter DG, Koelling RM, Scholler J, Fanslow WC, Baum PR, Derry JM, Yan W.; ''Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and is a ligand for class-I-restricted T-cell-associated molecule.''; PubMed Europe PMC Scholia
  23. Boyington JC, Sun PD.; ''A structural perspective on MHC class I recognition by killer cell immunoglobulin-like receptors.''; PubMed Europe PMC Scholia
  24. Shiratori I, Ogasawara K, Saito T, Lanier LL, Arase H.; ''Activation of natural killer cells and dendritic cells upon recognition of a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor.''; PubMed Europe PMC Scholia
  25. Vivier E, Tomasello E, Baratin M, Walzer T, Ugolini S.; ''Functions of natural killer cells.''; PubMed Europe PMC Scholia
  26. Van Rhijn I, Moody DB.; ''CD1 and mycobacterial lipids activate human T cells.''; PubMed Europe PMC Scholia
  27. Rudolph MG, Stanfield RL, Wilson IA.; ''How TCRs bind MHCs, peptides, and coreceptors.''; PubMed Europe PMC Scholia
  28. Arase N, Takeuchi A, Unno M, Hirano S, Yokosuka T, Arase H, Saito T.; ''Heterotypic interaction of CRTAM with Necl2 induces cell adhesion on activated NK cells and CD8+ T cells.''; PubMed Europe PMC Scholia
  29. Cannon JP, O'Driscoll M, Litman GW.; ''Specific lipid recognition is a general feature of CD300 and TREM molecules.''; PubMed Europe PMC Scholia
  30. Giustiniani J, Marie-Cardine A, Bensussan A.; ''A soluble form of the MHC class I-specific CD160 receptor is released from human activated NK lymphocytes and inhibits cell-mediated cytotoxicity.''; PubMed Europe PMC Scholia
  31. Minas K, Liversidge J.; ''Is the CD200/CD200 receptor interaction more than just a myeloid cell inhibitory signal?''; PubMed Europe PMC Scholia
  32. Zajonc DM, Girardi E.; ''Recognition of Microbial Glycolipids by Natural Killer T Cells.''; PubMed Europe PMC Scholia
  33. Cohen-Solal JF, Cassard L, Fridman WH, Sautès-Fridman C.; ''Fc gamma receptors.''; PubMed Europe PMC Scholia
  34. Biassoni R, Falco M, Cambiaggi A, Costa P, Verdiani S, Pende D, Conte R, Di Donato C, Parham P, Moretta L.; ''Amino acid substitutions can influence the natural killer (NK)-mediated recognition of HLA-C molecules. Role of serine-77 and lysine-80 in the target cell protection from lysis mediated by "group 2" or "group 1" NK clones.''; PubMed Europe PMC Scholia
  35. Radaev S, Sun P.; ''Recognition of immunoglobulins by Fcgamma receptors.''; PubMed Europe PMC Scholia
  36. Strong RK.; ''Asymmetric ligand recognition by the activating natural killer cell receptor NKG2D, a symmetric homodimer.''; PubMed Europe PMC Scholia
  37. Pessino A, Sivori S, Bottino C, Malaspina A, Morelli L, Moretta L, Biassoni R, Moretta A.; ''Molecular cloning of NKp46: a novel member of the immunoglobulin superfamily involved in triggering of natural cytotoxicity.''; PubMed Europe PMC Scholia
  38. Carrasco YR, Batista FD.; ''B cell recognition of membrane-bound antigen: an exquisite way of sensing ligands.''; PubMed Europe PMC Scholia
  39. Speckman RA, Wright Daw JA, Helms C, Duan S, Cao L, Taillon-Miller P, Kwok PY, Menter A, Bowcock AM.; ''Novel immunoglobulin superfamily gene cluster, mapping to a region of human chromosome 17q25, linked to psoriasis susceptibility.''; PubMed Europe PMC Scholia
  40. Bottino C, Falco M, Parolini S, Marcenaro E, Augugliaro R, Sivori S, Landi E, Biassoni R, Notarangelo LD, Moretta L, Moretta A.; ''NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface molecule contributing to the inability of natural killer cells to kill Epstein-Barr virus-infected B cells in X-linked lymphoproliferative disease.''; PubMed Europe PMC Scholia
  41. Dando J, Wilkinson KW, Ortlepp S, King DJ, Brady RL.; ''A reassessment of the MAdCAM-1 structure and its role in integrin recognition.''; PubMed Europe PMC Scholia
  42. Clark GJ, Cooper B, Fitzpatrick S, Green BJ, Hart DN.; ''The gene encoding the immunoregulatory signaling molecule CMRF-35A localized to human chromosome 17 in close proximity to other members of the CMRF-35 family.''; PubMed Europe PMC Scholia
  43. Sun Y, Senger K, Baginski TK, Mazloom A, Chinn Y, Pantua H, Hamidzadeh K, Ramani SR, Luis E, Tom I, Sebrell A, Quinones G, Ma Y, Mukhyala K, Sai T, Ding J, Haley B, Shadnia H, Kapadia SB, Gonzalez LC, Hass PE, Zarrin AA.; ''Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands.''; PubMed Europe PMC Scholia
  44. Gorczynski R, Chen Z, Kai Y, Lee L, Wong S, Marsden PA.; ''CD200 is a ligand for all members of the CD200R family of immunoregulatory molecules.''; PubMed Europe PMC Scholia
  45. Pogge von Strandmann E, Simhadri VR, von Tresckow B, Sasse S, Reiners KS, Hansen HP, Rothe A, Böll B, Simhadri VL, Borchmann P, McKinnon PJ, Hallek M, Engert A.; ''Human leukocyte antigen-B-associated transcript 3 is released from tumor cells and engages the NKp30 receptor on natural killer cells.''; PubMed Europe PMC Scholia
  46. Scharf L, Li NS, Hawk AJ, Garzón D, Zhang T, Fox LM, Kazen AR, Shah S, Haddadian EJ, Gumperz JE, Saghatelian A, Faraldo-Gómez JD, Meredith SC, Piccirilli JA, Adams EJ.; ''The 2.5 Å structure of CD1c in complex with a mycobacterial lipid reveals an open groove ideally suited for diverse antigen presentation.''; PubMed Europe PMC Scholia
  47. Falco M, Biassoni R, Bottino C, Vitale M, Sivori S, Augugliaro R, Moretta L, Moretta A.; ''Identification and molecular cloning of p75/AIRM1, a novel member of the sialoadhesin family that functions as an inhibitory receptor in human natural killer cells.''; PubMed Europe PMC Scholia
  48. Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY.; ''The crystal structure of human CD1b with a bound bacterial glycolipid.''; PubMed Europe PMC Scholia
  49. Kumaresan PR, Lai WC, Chuang SS, Bennett M, Mathew PA.; ''CS1, a novel member of the CD2 family, is homophilic and regulates NK cell function.''; PubMed Europe PMC Scholia
  50. Bromley SK, Burack WR, Johnson KG, Somersalo K, Sims TN, Sumen C, Davis MM, Shaw AS, Allen PM, Dustin ML.; ''The immunological synapse.''; PubMed Europe PMC Scholia
  51. Toapanta FR, Ross TM.; ''Complement-mediated activation of the adaptive immune responses: role of C3d in linking the innate and adaptive immunity.''; PubMed Europe PMC Scholia
  52. Moody DB, Zajonc DM, Wilson IA.; ''Anatomy of CD1-lipid antigen complexes.''; PubMed Europe PMC Scholia
  53. Cemerski S, Shaw A.; ''Immune synapses in T-cell activation.''; PubMed Europe PMC Scholia
  54. Sivori S, Vitale M, Morelli L, Sanseverino L, Augugliaro R, Bottino C, Moretta L, Moretta A.; ''p46, a novel natural killer cell-specific surface molecule that mediates cell activation.''; PubMed Europe PMC Scholia
  55. Yusuf-Makagiansar H, Anderson ME, Yakovleva TV, Murray JS, Siahaan TJ.; ''Inhibition of LFA-1/ICAM-1 and VLA-4/VCAM-1 as a therapeutic approach to inflammation and autoimmune diseases.''; PubMed Europe PMC Scholia
  56. Barral DC, Brenner MB.; ''CD1 antigen presentation: how it works.''; PubMed Europe PMC Scholia
  57. Silk JD, Salio M, Brown J, Jones EY, Cerundolo V.; ''Structural and functional aspects of lipid binding by CD1 molecules.''; PubMed Europe PMC Scholia
  58. Kelley J, Walter L, Trowsdale J.; ''Comparative genomics of natural killer cell receptor gene clusters.''; PubMed Europe PMC Scholia
  59. Vilches C, Parham P.; ''KIR: diverse, rapidly evolving receptors of innate and adaptive immunity.''; PubMed Europe PMC Scholia
  60. Lebbink RJ, de Ruiter T, Adelmeijer J, Brenkman AB, van Helvoort JM, Koch M, Farndale RW, Lisman T, Sonnenberg A, Lenting PJ, Meyaard L.; ''Collagens are functional, high affinity ligands for the inhibitory immune receptor LAIR-1.''; PubMed Europe PMC Scholia
  61. Barrow AD, Palarasah Y, Bugatti M, Holehouse AS, Byers DE, Holtzman MJ, Vermi W, Skjødt K, Crouch E, Colonna M.; ''OSCAR is a receptor for surfactant protein D that activates TNF-α release from human CCR2+ inflammatory monocytes.''; PubMed Europe PMC Scholia
  62. Lebbink RJ, van den Berg MC, de Ruiter T, Raynal N, van Roon JA, Lenting PJ, Jin B, Meyaard L.; ''The soluble leukocyte-associated Ig-like receptor (LAIR)-2 antagonizes the collagen/LAIR-1 inhibitory immune interaction.''; PubMed Europe PMC Scholia
  63. Zen K, Liu Y, McCall IC, Wu T, Lee W, Babbin BA, Nusrat A, Parkos CA.; ''Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils.''; PubMed Europe PMC Scholia
  64. Arnett KL, Harrison SC, Wiley DC.; ''Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment.''; PubMed Europe PMC Scholia
  65. Clark GJ, Green BJ, Hart DN.; ''The CMRF-35H gene structure predicts for an independently expressed member of an ITIM/ITAM pair of molecules localized to human chromosome 17.''; PubMed Europe PMC Scholia
  66. Carter RH, Barrington RA.; ''Signaling by the CD19/CD21 complex on B cells.''; PubMed Europe PMC Scholia
  67. Nishimura T.; ''Expression of potential lymphocyte trafficking mediator molecules in the mammary gland.''; PubMed Europe PMC Scholia
  68. Vitale M, Falco M, Castriconi R, Parolini S, Zambello R, Semenzato G, Biassoni R, Bottino C, Moretta L, Moretta A.; ''Identification of NKp80, a novel triggering molecule expressed by human NK cells.''; PubMed Europe PMC Scholia
  69. Chen K, Huang J, Gong W, Zhang L, Yu P, Wang JM.; ''CD40/CD40L dyad in the inflammatory and immune responses in the central nervous system.''; PubMed Europe PMC Scholia
  70. Sieling PA, Chatterjee D, Porcelli SA, Prigozy TI, Mazzaccaro RJ, Soriano T, Bloom BR, Brenner MB, Kronenberg M, Brennan PJ.; ''CD1-restricted T cell recognition of microbial lipoglycan antigens.''; PubMed Europe PMC Scholia
  71. Garcia-Alles LF, Collmann A, Versluis C, Lindner B, Guiard J, Maveyraud L, Huc E, Im JS, Sansano S, Brando T, Julien S, Prandi J, Gilleron M, Porcelli SA, de la Salle H, Heck AJ, Mori L, Puzo G, Mourey L, De Libero G.; ''Structural reorganization of the antigen-binding groove of human CD1b for presentation of mycobacterial sulfoglycolipids.''; PubMed Europe PMC Scholia
  72. Deng L, Mariuzza RA.; ''Structural basis for recognition of MHC and MHC-like ligands by natural killer cell receptors.''; PubMed Europe PMC Scholia
  73. Klimosch SN, Bartel Y, Wiemann S, Steinle A.; ''Genetically coupled receptor-ligand pair NKp80-AICL enables autonomous control of human NK cell responses.''; PubMed Europe PMC Scholia
  74. Tomfohrde J, Silverman A, Barnes R, Fernandez-Vina MA, Young M, Lory D, Morris L, Wuepper KD, Stastny P, Menter A.; ''Gene for familial psoriasis susceptibility mapped to the distal end of human chromosome 17q.''; PubMed Europe PMC Scholia
  75. Kjer-Nielsen L, Dunstone MA, Kostenko L, Ely LK, Beddoe T, Mifsud NA, Purcell AW, Brooks AG, McCluskey J, Rossjohn J.; ''Crystal structure of the human T cell receptor CD3 epsilon gamma heterodimer complexed to the therapeutic mAb OKT3.''; PubMed Europe PMC Scholia
  76. Clark GJ, Ju X, Tate C, Hart DN.; ''The CD300 family of molecules are evolutionarily significant regulators of leukocyte functions.''; PubMed Europe PMC Scholia
  77. Nakamura K, Funakoshi H, Miyamoto K, Tokunaga F, Nakamura T.; ''Molecular cloning and functional characterization of a human scavenger receptor with C-type lectin (SRCL), a novel member of a scavenger receptor family.''; PubMed Europe PMC Scholia
  78. Jones EY, Harlos K, Bottomley MJ, Robinson RC, Driscoll PC, Edwards RM, Clements JM, Dudgeon TJ, Stuart DI.; ''Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution.''; PubMed Europe PMC Scholia
  79. Griewank K, Borowski C, Rietdijk S, Wang N, Julien A, Wei DG, Mamchak AA, Terhorst C, Bendelac A.; ''Homotypic interactions mediated by Slamf1 and Slamf6 receptors control NKT cell lineage development.''; PubMed Europe PMC Scholia
  80. Meyaard L, Adema GJ, Chang C, Woollatt E, Sutherland GR, Lanier LL, Phillips JH.; ''LAIR-1, a novel inhibitory receptor expressed on human mononuclear leukocytes.''; PubMed Europe PMC Scholia
  81. Uhrberg M.; ''The KIR gene family: life in the fast lane of evolution.''; PubMed Europe PMC Scholia
  82. Varki A, Angata T.; ''Siglecs--the major subfamily of I-type lectins.''; PubMed Europe PMC Scholia
  83. Clark GJ, Ju X, Azlan M, Tate C, Ding Y, Hart DN.; ''The CD300 molecules regulate monocyte and dendritic cell functions.''; PubMed Europe PMC Scholia
  84. Wang J, Li Y, Kinjo Y, Mac TT, Gibson D, Painter GF, Kronenberg M, Zajonc DM.; ''Lipid binding orientation within CD1d affects recognition of Borrelia burgorferi antigens by NKT cells.''; PubMed Europe PMC Scholia
  85. Borrego F, Kabat J, Kim DK, Lieto L, Maasho K, Peña J, Solana R, Coligan JE.; ''Structure and function of major histocompatibility complex (MHC) class I specific receptors expressed on human natural killer (NK) cells.''; PubMed Europe PMC Scholia
  86. Nedvetzki S, Sowinski S, Eagle RA, Harris J, Vély F, Pende D, Trowsdale J, Vivier E, Gordon S, Davis DM.; ''Reciprocal regulation of human natural killer cells and macrophages associated with distinct immune synapses.''; PubMed Europe PMC Scholia
  87. Pende D, Bottino C, Castriconi R, Cantoni C, Marcenaro S, Rivera P, Spaggiari GM, Dondero A, Carnemolla B, Reymond N, Mingari MC, Lopez M, Moretta L, Moretta A.; ''PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1 (CD226) activating receptor: involvement in tumor cell lysis.''; PubMed Europe PMC Scholia
  88. Del Nagro CJ, Otero DC, Anzelon AN, Omori SA, Kolla RV, Rickert RC.; ''CD19 function in central and peripheral B-cell development.''; PubMed Europe PMC Scholia
  89. Kogure A, Shiratori I, Wang J, Lanier LL, Arase H.; ''PANP is a novel O-glycosylated PILRα ligand expressed in neural tissues.''; PubMed Europe PMC Scholia
  90. Hernández-Caselles T, Martínez-Esparza M, Pérez-Oliva AB, Quintanilla-Cecconi AM, García-Alonso A, Alvarez-López DM, García-Peñarrubia P.; ''A study of CD33 (SIGLEC-3) antigen expression and function on activated human T and NK cells: two isoforms of CD33 are generated by alternative splicing.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
117760view12:54, 22 May 2021EweitzModified title
112459view15:41, 9 October 2020ReactomeTeamReactome version 73
101366view11:25, 1 November 2018ReactomeTeamreactome version 66
100904view21:00, 31 October 2018ReactomeTeamreactome version 65
100445view19:35, 31 October 2018ReactomeTeamreactome version 64
99994view16:18, 31 October 2018ReactomeTeamreactome version 63
99548view14:53, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99181view12:42, 31 October 2018ReactomeTeamreactome version 62
96981view18:21, 24 April 2018AlexanderPicoReverted to version '06:43, 16 August 2017' by AlexanderPico
96973view15:45, 24 April 2018WpblockedModified title
93898view13:43, 16 August 2017ReactomeTeamreactome version 61
93471view11:24, 9 August 2017ReactomeTeamreactome version 61
86567view09:21, 11 July 2016ReactomeTeamreactome version 56
83164view10:14, 18 November 2015ReactomeTeamVersion54
81523view13:03, 21 August 2015ReactomeTeamVersion53
76993view08:28, 17 July 2014ReactomeTeamFixed remaining interactions
76698view12:06, 16 July 2014ReactomeTeamFixed remaining interactions
76024view10:08, 11 June 2014ReactomeTeamRe-fixing comment source
75733view11:21, 10 June 2014ReactomeTeamReactome 48 Update
75083view14:03, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74730view08:48, 30 April 2014ReactomeTeamReactome46
68927view17:33, 8 July 2013MaintBotUpdated to 2013 gpml schema
44851view09:50, 6 October 2011MartijnVanIerselOntology Term : 'signaling pathway pertinent to immunity' added !
42000view21:22, 4 March 2011MaintBotAutomatic update
39855view05:53, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
AMICA1 ProteinQ86YT9 (Uniprot-TrEMBL)
AMICA1ProteinQ86YT9 (Uniprot-TrEMBL)
Antigen peptide bound class I MHCComplexR-HSA-198904 (Reactome)
Antigen-bound

antibody bound to lymphoid Fc gamma

receptors		ComplexR-HSA-198877 (Reactome)
Antigen-bound Ig G AntibodyComplexR-HSA-199174 (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.
B2M(21-119) ProteinP61769 (Uniprot-TrEMBL)
BAG6 ProteinP46379 (Uniprot-TrEMBL)
BAG6,NCR3LG1,pp65:NCR3:FCRG3A:CD3Z dimerComplexR-NUL-5685590 (Reactome)
BAG6,NCR3LG1,pp65R-HSA-5685586 (Reactome)
C3d complexed with antigenComplexR-HSA-199000 (Reactome)
C3d fragment ProteinP01024 (Uniprot-TrEMBL)
CD160 ProteinO95971 (Uniprot-TrEMBL)
CD160ProteinO95971 (Uniprot-TrEMBL)
CD19 ProteinP15391 (Uniprot-TrEMBL)
CD200 ProteinP41217 (Uniprot-TrEMBL)
CD200 bound to CD200RComplexR-HSA-198191 (Reactome)
CD200ProteinP41217 (Uniprot-TrEMBL)
CD200R1 ProteinQ8TD46 (Uniprot-TrEMBL)
CD200R1ProteinQ8TD46 (Uniprot-TrEMBL)
CD226 ProteinQ15762 (Uniprot-TrEMBL)
CD226 bound to Nectin 2ComplexR-HSA-198190 (Reactome)
CD226:PVRComplexR-HSA-198197 (Reactome)
CD226ProteinQ15762 (Uniprot-TrEMBL)
CD247-1 ProteinP20963-1 (Uniprot-TrEMBL)
CD34-1 ProteinP28906-1 (Uniprot-TrEMBL)
CD3D ProteinP04234 (Uniprot-TrEMBL)
CD3E ProteinP07766 (Uniprot-TrEMBL)
CD3G ProteinP09693 (Uniprot-TrEMBL)
CD40 trimerComplexR-HSA-5672850 (Reactome)
CD40-1 ProteinP25942-1 (Uniprot-TrEMBL)
CD40:CD40L trimerComplexR-HSA-199402 (Reactome)
CD40LG trimerComplexR-HSA-5672851 (Reactome)
CD40LG(1-261) ProteinP29965 (Uniprot-TrEMBL)
CD81 ProteinP60033 (Uniprot-TrEMBL)
CD8A ProteinP01732 (Uniprot-TrEMBL)
CD8B ProteinP10966 (Uniprot-TrEMBL)
CD96 ProteinP40200 (Uniprot-TrEMBL)
CD96:PVRComplexR-HSA-198194 (Reactome)
CD96ProteinP40200 (Uniprot-TrEMBL)
CDH1(155-882) ProteinP12830 (Uniprot-TrEMBL)
CDH1(155-882)ProteinP12830 (Uniprot-TrEMBL)
CLEC2B ProteinQ92478 (Uniprot-TrEMBL)
CLEC2B dimerComplexR-HSA-5685596 (Reactome)
CLEC2D ProteinQ9UHP7 (Uniprot-TrEMBL)
CLEC2D dimer:KLRB1 dimerComplexR-HSA-5685592 (Reactome)
CLEC2D dimerComplexR-HSA-5685598 (Reactome)
CRTAM ProteinO95727 (Uniprot-TrEMBL)
CRTAM bound to NECL2ComplexR-HSA-198195 (Reactome)
CRTAMProteinO95727 (Uniprot-TrEMBL)
CXADR ProteinP78310 (Uniprot-TrEMBL)
CXADR bound to JAMLComplexR-HSA-198198 (Reactome)
CXADRProteinP78310 (Uniprot-TrEMBL)
Collagen type XVII fibrilR-HSA-2172656 (Reactome)
Complex of CD19,

CD81, CD225 and CD21 with C3d-bound

Antigen		ComplexR-HSA-198991 (Reactome)
Complex of CD19,

CD81, CD225 and

CD21		ComplexR-HSA-198931 (Reactome)
E-cadherin bound to KLRG1ComplexR-HSA-198192 (Reactome)
FCGR1A ProteinP12314 (Uniprot-TrEMBL)
FCGR2B ProteinP31994 (Uniprot-TrEMBL)
FCGR3A ProteinP08637 (Uniprot-TrEMBL)
GLYCAM1 ProteinQ8IVK1 (Uniprot-TrEMBL)
HA ProteinP03452 (Uniprot-TrEMBL)
HCST ProteinQ9UBK5 (Uniprot-TrEMBL)
HLA Bw4 interacting with KIR3DL1ComplexR-HSA-199565 (Reactome)
HLA class I

histocompatibility antigen, A-1 alpha

chain precursor 		ProteinP30443 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-11 alpha

chain 		ProteinP13746 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-2 alpha

chain 		ProteinP01892 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-23 alpha

chain 		ProteinP30447 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-24 alpha

chain 		ProteinP05534 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-25 alpha

chain 		ProteinP18462 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-26 alpha

chain 		ProteinP30450 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-29 alpha

chain 		ProteinP30512 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-3 alpha

chain precursor 		ProteinP04439 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-30 alpha

chain 		ProteinP16188 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-31 alpha

chain 		ProteinP16189 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-32 alpha

chain 		ProteinP10314 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-33 alpha

chain 		ProteinP16190 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-34 alpha

chain 		ProteinP30453 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-36 alpha

chain 		ProteinP30455 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-43 alpha

chain 		ProteinP30456 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-66 alpha

chain 		ProteinP30457 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-68 alpha

chain 		ProteinP01891 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-69 alpha

chain 		ProteinP10316 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-74 alpha

chain 		ProteinP30459 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, A-80 alpha

chain 		ProteinQ09160 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-1 alpha

chain 		ProteinP30499 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-12

alpha chain 		ProteinP30508 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-14

alpha chain 		ProteinP30510 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-15

alpha chain 		ProteinQ07000 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-16

alpha chain 		ProteinQ29960 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-17

alpha chain 		ProteinQ95604 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-18

alpha chain 		ProteinQ29865 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-2 alpha

chain 		ProteinP30501 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-3 alpha

chain precursor 		ProteinP04222 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-4 alpha

chain precursor 		ProteinP30504 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-5 alpha

chain precursor 		ProteinQ9TNN7 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-6 alpha

chain precursor 		ProteinQ29963 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-7 alpha

chain precursor 		ProteinP10321 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, Cw-8 alpha

chain 		ProteinP30505 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, E alpha

chain precursor 		ProteinP13747 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, alpha

chain F precursor 		ProteinP30511 (Uniprot-TrEMBL)
HLA class I

histocompatibility antigen, alpha

chain G precursor 		ProteinP17693 (Uniprot-TrEMBL)
HLA-A3 interacting with KIR3DL2ComplexR-HSA-199573 (Reactome)
HLA-A3ComplexR-HSA-199571 (Reactome)
HLA-Bw4ComplexR-HSA-199567 (Reactome)
HLA-C

group-I-interacting

KIRs		R-HSA-199540 (Reactome)
HLA-C Cw3 (group 1)ComplexR-HSA-199562 (Reactome)
HLA-C Cw4 (group 2)ComplexR-HSA-198911 (Reactome)
HLA-C group 1

interacting with

KIR2DL2/3		ComplexR-HSA-198909 (Reactome)
HLA-C group 1

interacting with

KIR2DS2		ComplexR-HSA-199588 (Reactome)
HLA-C group 2

interacting with

KIR2DL1		ComplexR-HSA-199560 (Reactome)
HLA-C group 2

interacting with

KIR2DS1		ComplexR-HSA-199585 (Reactome)
HLA-E interacting with KLRC1:KLRD1ComplexR-HSA-198914 (Reactome)
HLA-EComplexR-HSA-198912 (Reactome)
HLA-G interacting with KIR2DL4ComplexR-HSA-199578 (Reactome)
HLA-GComplexR-HSA-199581 (Reactome)
HN ProteinP04853 (Uniprot-TrEMBL)
HemagglutininR-FLU-5685588 (Reactome)
ICAM 1-4R-HSA-198193 (Reactome)
ICAM1 ProteinP05362 (Uniprot-TrEMBL)
ICAM2 ProteinP13598 (Uniprot-TrEMBL)
ICAM3 ProteinP32942 (Uniprot-TrEMBL)
ICAM4 ProteinQ14773 (Uniprot-TrEMBL)
IFITM1 ProteinP13164 (Uniprot-TrEMBL)
IGHV(1-?) ProteinA2KUC3 (Uniprot-TrEMBL)
IGHV7-81(1-?) ProteinQ6PIL0 (Uniprot-TrEMBL)
IGKC ProteinP01834 (Uniprot-TrEMBL)
IGKV1-5(23-?) ProteinP01602 (Uniprot-TrEMBL)
IGKV4-1(21-?) ProteinP06312 (Uniprot-TrEMBL)
IGKVA18(21-?) ProteinA2NJV5 (Uniprot-TrEMBL)
IGLC1 ProteinP0CG04 (Uniprot-TrEMBL)
IGLC2 ProteinP0CG05 (Uniprot-TrEMBL)
IGLC3 ProteinP0CG06 (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)
ITGA4 ProteinP13612 (Uniprot-TrEMBL)
ITGAL ProteinP20701 (Uniprot-TrEMBL)
ITGB1 ProteinP05556 (Uniprot-TrEMBL)
ITGB2 ProteinP05107 (Uniprot-TrEMBL)
ITGB7 ProteinP26010 (Uniprot-TrEMBL)
Ig heavy chain V-I region EU ProteinP01742 (Uniprot-TrEMBL)
Ig heavy chain V-I region HG3 ProteinP01743 (Uniprot-TrEMBL)
Ig heavy chain V-I region Mot ProteinP06326 (Uniprot-TrEMBL)
Ig heavy chain V-I region ND ProteinP01744 (Uniprot-TrEMBL)
Ig heavy chain V-I region SIE ProteinP01761 (Uniprot-TrEMBL)
Ig heavy chain V-I region WOL ProteinP01760 (Uniprot-TrEMBL)
Ig heavy chain V-II region ARH-77 ProteinP06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region COR ProteinP01815 (Uniprot-TrEMBL)
Ig heavy chain V-II region DAW ProteinP01816 (Uniprot-TrEMBL)
Ig heavy chain V-II region HE ProteinP01818 (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 SESS ProteinP04438 (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 BUR ProteinP01773 (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 GA ProteinP01769 (Uniprot-TrEMBL)
Ig heavy chain V-III region GAL ProteinP01781 (Uniprot-TrEMBL)
Ig heavy chain V-III region HIL ProteinP01771 (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 LAY ProteinP01775 (Uniprot-TrEMBL)
Ig heavy chain V-III region NIE ProteinP01770 (Uniprot-TrEMBL)
Ig heavy chain V-III region POM ProteinP01774 (Uniprot-TrEMBL)
Ig heavy chain V-III region TEI ProteinP01777 (Uniprot-TrEMBL)
Ig heavy chain V-III region TIL ProteinP01765 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO ProteinP01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region TUR ProteinP01779 (Uniprot-TrEMBL)
Ig heavy chain V-III region WAS ProteinP01776 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA ProteinP01763 (Uniprot-TrEMBL)
Ig heavy chain V-III region ZAP ProteinP01778 (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 Bi ProteinP01595 (Uniprot-TrEMBL)
Ig kappa chain V-I region CAR ProteinP01596 (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 EU ProteinP01598 (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 Hau ProteinP01600 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ka ProteinP01603 (Uniprot-TrEMBL)
Ig kappa chain V-I region Kue ProteinP01604 (Uniprot-TrEMBL)
Ig kappa chain V-I region Lay ProteinP01605 (Uniprot-TrEMBL)
Ig kappa chain V-I region Mev ProteinP01612 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ni ProteinP01613 (Uniprot-TrEMBL)
Ig kappa chain V-I region OU ProteinP01606 (Uniprot-TrEMBL)
Ig kappa chain V-I region Rei ProteinP01607 (Uniprot-TrEMBL)
Ig kappa chain V-I region Roy ProteinP01608 (Uniprot-TrEMBL)
Ig kappa chain V-I region Scw ProteinP01609 (Uniprot-TrEMBL)
Ig kappa chain V-I region WAT ProteinP80362 (Uniprot-TrEMBL)
Ig kappa chain V-I region WEA ProteinP01610 (Uniprot-TrEMBL)
Ig kappa chain V-I region Walker ProteinP04431 (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 GM607 ProteinP06309 (Uniprot-TrEMBL)
Ig kappa chain V-II region MIL ProteinP01616 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 ProteinP06310 (Uniprot-TrEMBL)
Ig kappa chain V-II region TEW ProteinP01617 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 ProteinP01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region CLL ProteinP04207 (Uniprot-TrEMBL)
Ig kappa chain V-III region GOL ProteinP04206 (Uniprot-TrEMBL)
Ig kappa chain V-III region HAH ProteinP18135 (Uniprot-TrEMBL)
Ig kappa chain V-III region HIC ProteinP18136 (Uniprot-TrEMBL)
Ig kappa chain V-III region IARC/BL41 ProteinP06311 (Uniprot-TrEMBL)
Ig kappa chain V-III region NG9 ProteinP01621 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM ProteinP01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region SIE ProteinP01620 (Uniprot-TrEMBL)
Ig kappa chain V-III region Ti ProteinP01622 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG ProteinP04433 (Uniprot-TrEMBL)
Ig kappa chain V-III region VH ProteinP04434 (Uniprot-TrEMBL)
Ig kappa chain V-III region WOL ProteinP01623 (Uniprot-TrEMBL)
Ig kappa chain V-IV region B17 ProteinP06314 (Uniprot-TrEMBL)
Ig kappa chain V-IV region JI ProteinP06313 (Uniprot-TrEMBL)
Ig kappa chain V-IV region Len ProteinP01625 (Uniprot-TrEMBL)
Ig kappa chain V-IV region STH ProteinP83593 (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-VII region MOT ProteinP01720 (Uniprot-TrEMBL)
Ig lambda chain V region 4A ProteinP04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region BL2 ProteinP06316 (Uniprot-TrEMBL)
Ig lambda chain V-I region EPS ProteinP06888 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA ProteinP01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region MEM ProteinP06887 (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 NIG-64 ProteinP01702 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR ProteinP01699 (Uniprot-TrEMBL)
Ig lambda chain V-I region WAH ProteinP04208 (Uniprot-TrEMBL)
Ig lambda chain V-II region BO ProteinP01710 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH ProteinP01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region BUR ProteinP01708 (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 NIG-58 ProteinP01713 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-84 ProteinP04209 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG ProteinP01704 (Uniprot-TrEMBL)
Ig lambda chain V-II region TRO ProteinP01707 (Uniprot-TrEMBL)
Ig lambda chain V-II region VIL ProteinP01711 (Uniprot-TrEMBL)
Ig lambda chain V-II region WIN ProteinP01712 (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-IV region MOL ProteinP06889 (Uniprot-TrEMBL)
Ig lambda chain V-IV region X ProteinP01716 (Uniprot-TrEMBL)
Ig lambda chain V-V region DEL ProteinP01719 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR ProteinP01721 (Uniprot-TrEMBL)
Ig lambda chain V-VI region EB4 ProteinP06319 (Uniprot-TrEMBL)
Ig lambda chain V-VI region NIG-48 ProteinP01722 (Uniprot-TrEMBL)
Ig lambda chain V-VI region SUT ProteinP06317 (Uniprot-TrEMBL)
Ig lambda chain V-VI region WLT ProteinP06318 (Uniprot-TrEMBL)
IgH heavy chain

V-III region VH26

precursor 		ProteinP01764 (Uniprot-TrEMBL)
Integrin alpha4beta7:MADCAM1ComplexR-HSA-198925 (Reactome)
Integrin alpha4beta1ComplexR-HSA-198201 (Reactome)
Integrin alpha4beta7ComplexR-HSA-198927 (Reactome)
Integrin alphaLbeta2ComplexR-HSA-198196 (Reactome)
KIR2DL1 ProteinP43626 (Uniprot-TrEMBL)
KIR2DL1ProteinP43626 (Uniprot-TrEMBL)
KIR2DL2 ProteinP43627 (Uniprot-TrEMBL)
KIR2DL3 ProteinP43628 (Uniprot-TrEMBL)
KIR2DL4 ProteinQ99706 (Uniprot-TrEMBL)
KIR2DL4ProteinQ99706 (Uniprot-TrEMBL)
KIR2DS1 ProteinQ14954 (Uniprot-TrEMBL)
KIR2DS1 complexed with DAP12ComplexR-HSA-199586 (Reactome)
KIR2DS2 ProteinP43631 (Uniprot-TrEMBL)
KIR2DS2 complexed with DAP12ComplexR-HSA-199584 (Reactome)
KIR3DL1 ProteinP43629 (Uniprot-TrEMBL)
KIR3DL1ProteinP43629 (Uniprot-TrEMBL)
KIR3DL2 ProteinP43630 (Uniprot-TrEMBL)
KIR3DL2ProteinP43630 (Uniprot-TrEMBL)
KLRB1 ProteinQ12918 (Uniprot-TrEMBL)
KLRB1 dimerComplexR-HSA-5685225 (Reactome)
KLRC1 ProteinP26715 (Uniprot-TrEMBL)
KLRC1ProteinP26715 (Uniprot-TrEMBL)
KLRD1 ProteinQ13241 (Uniprot-TrEMBL)
KLRD1ProteinQ13241 (Uniprot-TrEMBL)
KLRF1 ProteinQ9NZS2 (Uniprot-TrEMBL)
KLRF1 dimer:CLEC2B dimerComplexR-HSA-5685591 (Reactome)
KLRF1 dimerComplexR-HSA-5685224 (Reactome)
KLRG1 ProteinQ96E93 (Uniprot-TrEMBL)
KLRG1ProteinQ96E93 (Uniprot-TrEMBL)
KLRK1 ProteinP26718 (Uniprot-TrEMBL)
L-selectin

interacting with

known ligands		ComplexR-HSA-198924 (Reactome)
L-selectin ligandsR-HSA-198922 (Reactome)
LAIR1 ProteinQ6GTX8 (Uniprot-TrEMBL)
LAIR1:Collagen type XVIIComplexR-HSA-5686611 (Reactome)
LAIR1ProteinQ6GTX8 (Uniprot-TrEMBL)
LFA-1:ICAM 1-4ComplexR-HSA-198200 (Reactome)
LILR setR-HSA-198894 (Reactome)
LILR-interacting MHC Class I moleculesComplexR-HSA-199592 (Reactome)
Ligand interacting with NKG2DComplexR-HSA-198915 (Reactome)
Lymphoid-expressed Fc-gamma receptorsR-HSA-200284 (Reactome)
MADCAM1-1 ProteinQ13477-1 (Uniprot-TrEMBL)
MADCAM1-1ProteinQ13477-1 (Uniprot-TrEMBL)
MHC Class I

interacting with

CD160		ComplexR-HSA-198906 (Reactome)
MHC Class I

interacting with

LILRs		ComplexR-HSA-198896 (Reactome)
MHC Class I

molecules interacting with

CD160		R-HSA-199614 (Reactome)
MICB ProteinQ29980 (Uniprot-TrEMBL)
NCR1 ProteinO76036 (Uniprot-TrEMBL)
NCR1:FCRG1A:CD3Z dimer:HemagglutininComplexR-NUL-5685594 (Reactome)
NCR1:FCRG1A:CD3Z dimerComplexR-HSA-5685701 (Reactome)
NCR3 ProteinO14931 (Uniprot-TrEMBL)
NCR3:FCRG1A:CD3Z dimerComplexR-HSA-5685593 (Reactome)
NCR3LG1 ProteinQ68D85 (Uniprot-TrEMBL)
NKG2D complexed with DAP10ComplexR-HSA-198920 (Reactome)
NKG2D ligandR-HSA-198916 (Reactome)
PVR ProteinP15151 (Uniprot-TrEMBL)
PVRL2 ProteinQ92692 (Uniprot-TrEMBL)
PVRL2ProteinQ92692 (Uniprot-TrEMBL)
PVRProteinP15151 (Uniprot-TrEMBL)
RAET1E ProteinQ8TD07 (Uniprot-TrEMBL)
SAP,EAT2R-HSA-5685221 (Reactome)
SELL ProteinP14151 (Uniprot-TrEMBL)
SELLProteinP14151 (Uniprot-TrEMBL)
SH2D1A ProteinO60880 (Uniprot-TrEMBL)
SH2D1B ProteinO14796 (Uniprot-TrEMBL)
SIGLEC:sialic acidComplexR-HSA-5685595 (Reactome)
SIGLECR-HSA-5685222 (Reactome)
SLAMF6 ProteinQ96DU3 (Uniprot-TrEMBL)
SLAMF6:SLAMF6:SAP,EAT2ComplexR-HSA-5685227 (Reactome)
SLAMF6:SLAMF6ComplexR-HSA-5685229 (Reactome)
SLAMF6ProteinQ96DU3 (Uniprot-TrEMBL)
SLAMF7 ProteinQ9NQ25 (Uniprot-TrEMBL)
SLAMF7:SLAMF7ComplexR-HSA-5685228 (Reactome)
SLAMF7ProteinQ9NQ25 (Uniprot-TrEMBL)
Sialic acid MetaboliteCHEBI:28879 (ChEBI)
Sialic acidMetaboliteCHEBI:28879 (ChEBI)
T-cell receptor

alpha chain V region HPB-MLT

precursor 		ProteinP04436 (Uniprot-TrEMBL)
T-cell receptor

alpha chain V region PY14

precursor 		ProteinP01737 (Uniprot-TrEMBL)
T-cell receptor complex with CD8ComplexR-HSA-198898 (Reactome)
TCR interacting with

antigen-bearing MHC

Class I		ComplexR-HSA-198897 (Reactome)
TCRA ProteinP04437 (Uniprot-TrEMBL)
TCRB ProteinP04435 (Uniprot-TrEMBL)
TRAC ProteinP01848 (Uniprot-TrEMBL)
TRBC1 ProteinP01850 (Uniprot-TrEMBL)
TRBV12-3 ProteinP01733 (Uniprot-TrEMBL)
TYROBP ProteinO43914 (Uniprot-TrEMBL)
ULBP1 ProteinQ9BZM6 (Uniprot-TrEMBL)
ULBP3 ProteinQ9BZM4 (Uniprot-TrEMBL)
VCAM1 ProteinP19320 (Uniprot-TrEMBL)
VCAM1ProteinP19320 (Uniprot-TrEMBL)
cd21(1-?) ProteinO15181 (Uniprot-TrEMBL)
class I MHC B13 ProteinP30461 (Uniprot-TrEMBL)
class I MHC B14 ProteinP30462 (Uniprot-TrEMBL)
class I MHC B15 ProteinP30464 (Uniprot-TrEMBL)
class I MHC B18 ProteinP30466 (Uniprot-TrEMBL)
class I MHC B27 ProteinP03989 (Uniprot-TrEMBL)
class I MHC B35 ProteinP30685 (Uniprot-TrEMBL)
class I MHC B37 ProteinP18463 (Uniprot-TrEMBL)
class I MHC B38 ProteinQ95365 (Uniprot-TrEMBL)
class I MHC B39 ProteinP30475 (Uniprot-TrEMBL)
class I MHC B40 ProteinQ04826 (Uniprot-TrEMBL)
class I MHC B41 ProteinP30479 (Uniprot-TrEMBL)
class I MHC B42 ProteinP30480 (Uniprot-TrEMBL)
class I MHC B44 ProteinP30481 (Uniprot-TrEMBL)
class I MHC B45 ProteinP30483 (Uniprot-TrEMBL)
class I MHC B46 ProteinP30484 (Uniprot-TrEMBL)
class I MHC B47 ProteinP30485 (Uniprot-TrEMBL)
class I MHC B49 ProteinP30487 (Uniprot-TrEMBL)
class I MHC B50 ProteinP30488 (Uniprot-TrEMBL)
class I MHC B51 ProteinP18464 (Uniprot-TrEMBL)
class I MHC B52 ProteinP30490 (Uniprot-TrEMBL)
class I MHC B53 ProteinP30491 (Uniprot-TrEMBL)
class I MHC B54 ProteinP30492 (Uniprot-TrEMBL)
class I MHC B55 ProteinP30493 (Uniprot-TrEMBL)
class I MHC B56 ProteinP30495 (Uniprot-TrEMBL)
class I MHC B57 ProteinP18465 (Uniprot-TrEMBL)
class I MHC B58 ProteinP10319 (Uniprot-TrEMBL)
class I MHC B59 ProteinQ29940 (Uniprot-TrEMBL)
class I MHC B67 ProteinQ29836 (Uniprot-TrEMBL)
class I MHC B7 ProteinP01889 (Uniprot-TrEMBL)
class I MHC B73 ProteinQ31612 (Uniprot-TrEMBL)
class I MHC B78 ProteinP30498 (Uniprot-TrEMBL)
class I MHC B8 ProteinP30460 (Uniprot-TrEMBL)
class I MHC B81 ProteinQ31610 (Uniprot-TrEMBL)
class I MHC B82 ProteinQ29718 (Uniprot-TrEMBL)
integrin alpha4beta1:VCAM1ComplexR-HSA-198199 (Reactome)
pp65 ProteinP06725 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
AMICA1R-HSA-199093 (Reactome)
Antigen peptide bound class I MHCR-HSA-198955 (Reactome)
Antigen-bound

antibody bound to lymphoid Fc gamma

receptors		ArrowR-HSA-199161 (Reactome)
Antigen-bound Ig G AntibodyR-HSA-199161 (Reactome)
BAG6,NCR3LG1,pp65:NCR3:FCRG3A:CD3Z dimerArrowR-HSA-5685602 (Reactome)
BAG6,NCR3LG1,pp65R-HSA-5685602 (Reactome)
C3d complexed with antigenR-HSA-199518 (Reactome)
CD160R-HSA-199169 (Reactome)
CD200 bound to CD200RArrowR-HSA-199154 (Reactome)
CD200R-HSA-199154 (Reactome)
CD200R1R-HSA-199154 (Reactome)
CD226 bound to Nectin 2ArrowR-HSA-199144 (Reactome)
CD226:PVRArrowR-HSA-199131 (Reactome)
CD226R-HSA-199131 (Reactome)
CD226R-HSA-199144 (Reactome)
CD40 trimerR-HSA-199404 (Reactome)
CD40:CD40L trimerArrowR-HSA-199404 (Reactome)
CD40LG trimerR-HSA-199404 (Reactome)
CD96:PVRArrowR-HSA-199014 (Reactome)
CD96R-HSA-199014 (Reactome)
CDH1(155-882)R-HSA-199079 (Reactome)
CLEC2B dimerR-HSA-5685608 (Reactome)
CLEC2D dimer:KLRB1 dimerArrowR-HSA-5685606 (Reactome)
CLEC2D dimerR-HSA-5685606 (Reactome)
CRTAM bound to NECL2ArrowR-HSA-199112 (Reactome)
CRTAMR-HSA-199112 (Reactome)
CXADR bound to JAMLArrowR-HSA-199093 (Reactome)
CXADRR-HSA-199093 (Reactome)
Collagen type XVII fibrilR-HSA-5686625 (Reactome)
Complex of CD19,

CD81, CD225 and CD21 with C3d-bound

Antigen		ArrowR-HSA-199518 (Reactome)
Complex of CD19,

CD81, CD225 and

CD21		R-HSA-199518 (Reactome)
E-cadherin bound to KLRG1ArrowR-HSA-199079 (Reactome)
HLA Bw4 interacting with KIR3DL1ArrowR-HSA-199566 (Reactome)
HLA-A3 interacting with KIR3DL2ArrowR-HSA-199576 (Reactome)
HLA-A3R-HSA-199576 (Reactome)
HLA-Bw4R-HSA-199566 (Reactome)
HLA-C

group-I-interacting

KIRs		R-HSA-198958 (Reactome)
HLA-C Cw3 (group 1)R-HSA-199558 (Reactome)
HLA-C Cw3 (group 1)R-HSA-199583 (Reactome)
HLA-C Cw4 (group 2)R-HSA-198958 (Reactome)
HLA-C Cw4 (group 2)R-HSA-199587 (Reactome)
HLA-C group 1

interacting with

KIR2DL2/3		ArrowR-HSA-198958 (Reactome)
HLA-C group 1

interacting with

KIR2DS2		ArrowR-HSA-199583 (Reactome)
HLA-C group 2

interacting with

KIR2DL1		ArrowR-HSA-199558 (Reactome)
HLA-C group 2

interacting with

KIR2DS1		ArrowR-HSA-199587 (Reactome)
HLA-E interacting with KLRC1:KLRD1ArrowR-HSA-199062 (Reactome)
HLA-ER-HSA-199062 (Reactome)
HLA-G interacting with KIR2DL4ArrowR-HSA-199579 (Reactome)
HLA-GR-HSA-199579 (Reactome)
HemagglutininR-HSA-5685600 (Reactome)
ICAM 1-4R-HSA-199050 (Reactome)
Integrin alpha4beta7:MADCAM1ArrowR-HSA-199032 (Reactome)
Integrin alpha4beta1R-HSA-198941 (Reactome)
Integrin alpha4beta7R-HSA-199032 (Reactome)
Integrin alphaLbeta2R-HSA-199050 (Reactome)
KIR2DL1R-HSA-199558 (Reactome)
KIR2DL4R-HSA-199579 (Reactome)
KIR2DS1 complexed with DAP12R-HSA-199587 (Reactome)
KIR2DS2 complexed with DAP12R-HSA-199583 (Reactome)
KIR3DL1R-HSA-199566 (Reactome)
KIR3DL2R-HSA-199576 (Reactome)
KLRB1 dimerR-HSA-5685606 (Reactome)
KLRC1R-HSA-199062 (Reactome)
KLRD1R-HSA-199062 (Reactome)
KLRF1 dimer:CLEC2B dimerArrowR-HSA-5685608 (Reactome)
KLRF1 dimerR-HSA-5685608 (Reactome)
KLRG1R-HSA-199079 (Reactome)
L-selectin

interacting with

known ligands		ArrowR-HSA-199046 (Reactome)
L-selectin ligandsR-HSA-199046 (Reactome)
LAIR1:Collagen type XVIIArrowR-HSA-5686625 (Reactome)
LAIR1R-HSA-5686625 (Reactome)
LFA-1:ICAM 1-4ArrowR-HSA-199050 (Reactome)
LILR setR-HSA-199043 (Reactome)
LILR-interacting MHC Class I moleculesR-HSA-199043 (Reactome)
Ligand interacting with NKG2DArrowR-HSA-198983 (Reactome)
Lymphoid-expressed Fc-gamma receptorsR-HSA-199161 (Reactome)
MADCAM1-1R-HSA-199032 (Reactome)
MHC Class I

interacting with

CD160		ArrowR-HSA-199169 (Reactome)
MHC Class I

interacting with

LILRs		ArrowR-HSA-199043 (Reactome)
MHC Class I

molecules interacting with

CD160		R-HSA-199169 (Reactome)
NCR1:FCRG1A:CD3Z dimer:HemagglutininArrowR-HSA-5685600 (Reactome)
NCR1:FCRG1A:CD3Z dimerR-HSA-5685600 (Reactome)
NCR3:FCRG1A:CD3Z dimerR-HSA-5685602 (Reactome)
NKG2D complexed with DAP10R-HSA-198983 (Reactome)
NKG2D ligandR-HSA-198983 (Reactome)
PVRL2R-HSA-199112 (Reactome)
PVRL2R-HSA-199144 (Reactome)
PVRR-HSA-199014 (Reactome)
PVRR-HSA-199131 (Reactome)
R-HSA-198941 (Reactome) Integrins play a central role in mediating lymphocyte

adhesion to a number of surfaces. LFA-1 interacts with ICAMs 1-3 that are typically expressed on other immune system cells. ICAM-4 also interacts with LFA-1, and is known to be

expressed on telencepahlic neurons.

VCAM-1 regulates lymphocyte adhesion to activated endothelial cells via Very Late Antigen-4 (VLA-4).

To function in a circulating mode, leukocytes express LFA-1 and VLA-4 in a low ligand binding capacity. When leukocytes reach sites of imflammation, these integrins are switched to a higher binding state to guide the complex process of transmigration, tethering, rolling, arrest, adhesion and shape change.

Signal cascades between LFA-1 and VLA-4 may cross-talk affecting binding affinities in a reciprocal fashion.

R-HSA-198955 (Reactome) T cells distinguish foreign material from self through presentation of fragments of the antigen by the MHC cell surface receptors. Only if an MHC molecule presents an appropriate antigenic peptide will a cellular immune response be triggered. The orchestration of recognition and signaling events, from the initial recognition of antigenic peptides to the lysis of the target cell, is performed in a localized environment on the T cell, called the immunological synapse, and requires the coordinated activities of several T-Cell Receptor (TCR)-associated molecules. This particular reaction depicts the interaction of the TCR with MHC Class I molecules on somatic cell, requiring the support of CD3 and CD8 proteins.
R-HSA-198958 (Reactome) A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

R-HSA-198983 (Reactome) NKG2D is an activating immunoreceptor. By engaging NKG2D, HlA Class I-like molecules such as MICA, MICB, ULBP1-4 and RAE-1 provide powerful costimulation for NK cells and T-cells and can determine the magnitude and outcome of certain effector functions. NKG2D ligands are upregulated on the surfaces of cells under conditions of stress, for example infection or tumorigenesis, and therefore act as molecular flags to the immune system that something is wrong.
R-HSA-199014 (Reactome) NK cells express adhesion molecules that allow interaction with their tumour targets, promoting their lysis.

For instance, the activating receptor CD226 is known to be involved in cytotoxic lymphocyte formation, as well as platelet adhesion to the endothelium. The cytoplasmic domain of CD226 contains binding motifs for members of the band 4.1 family of proteins, and for members of the membrane-associated guanylate kinase homolog (MAGUK) family. These proteins connect the CD226 receptor to the cytoskeleton and may promote clustering with LFA-1 integrin (also discussed in this pathway), which is known to participate in CD226's signaling cascade. CD226 plays a role in transendothelial migration, where it facilitates adherence to endothelial cells and migration between cell junctions.

Nectin-2 binds CD226. It is ubiquitously expressed in cells of various tissues, especially in epithelial cells, neurons and fibroblasts. Like many other nectin and Necl proteins, nectin-2 serves as a viral entry receptor for alpha-herpesviruses including herpes simplex virus (HSV-1 and HSV-2). The other CD226 ligand, Necl-5, was initially identified as a receptor for poliovirus.

CD96, another ligand for Necl-5, is strongly upregulated in activated NK cells.

CRTAM is similarly up-regulated, and has been shown to to bind Necl-2, promoting NK cell cytotoxicity towards otherwise poorly immunogenic targets.

R-HSA-199032 (Reactome) Mucosal addressin cell adhesion molecule (MADCAM1) is present in the endothelium of mucosa, and binds alpha-4 beta-7 integrin and L-selectin, regulating both the passage and retention of leukocytes in mucosal tissues. MADCAM1 has been shown to be present as a homodimer.
R-HSA-199043 (Reactome) Leukocyte immunoglobulin (Ig)-like receptors [LILRs, also known as Ig-like transcripts (ILTs)] are a family of inhibitory and stimulatory receptors encoded within the leukocyte receptor complex and are expressed by immune cell types of both myeloid and lymphoid lineage. Several members of the LILR family recognize major histocompatibility complex class I. The immunomodulatory role of LILR receptors indicates that they may exert an influence on signaling pathways of both innate and adaptive immune systems.

Signaling mechanisms are employed that are similar to the ones adopted by the closely related killer cell inhibitory receptors (KIRs). ITIMs recruit inhibitory phosphatases that dephosphorylate ITIM and ITAM domains in order to influence intracellular signaling cascades. In contrast, activating LILRs, which lack any signaling domains of their own, rely on association with an adaptor protein such as FceRI-gamma to transmit their signal through its intracellular ITAMs.

R-HSA-199046 (Reactome) L-selectin plays a major role in leukocyte traffic through lymph node high endothelial venules.

Both MAdCAM and GlyCAM-1 are major L-selectin ligands produced by these venules and mediate leukocyte rolling, particularly in lymphocytes. They are also expressed in mammary tissue and play an important role in the transfer of immune cells into milk secretions.

The adhesive properties of CD34 and its potential role in homing lymphocytes to lymphoid tissues mimics the mechanims leukocytes adopt to travel to inflammatory sites.

R-HSA-199050 (Reactome) Integrins play a central role in mediating lymphocyte

adhesion to a number of surfaces. LFA-1 interacts with ICAMs 1-3 that are typically expressed on other immune system cells. ICAM-4 also interacts with LFA-1, and is known to be

expressed on telencepahlic neurons.

VCAM-1 regulates lymphocyte adhesion to activated endothelial cells via Very Late Antigen-4 (VLA-4).

To function in a circulating mode, leukocytes express LFA-1 and VLA-4 in a low ligand binding capacity. When leukocytes reach sites of imflammation, these integrins are switched to a higher binding state to guide the complex process of transmigration, tethering, rolling, arrest, adhesion and shape change.

Signal cascades between LFA-1 and VLA-4 may cross-talk affecting binding affinities in a reciprocal fashion.

R-HSA-199062 (Reactome) After interaction with its ligand HLA-E, which is expressed on normal cells, the C-type lectin inhibitory receptor CD94/NKG2A suppresses activation signaling processes. CD94/NKG2A receptors continuously recycle from the cell surface through endosomal compartments and back again in a process that requires energy and the cytoskeleton. This steady state process appears to be largely unaffected by exposure to ligand.
R-HSA-199079 (Reactome) The lectin-like NK cell receptor KLRG1 binds to cadherins on epithelial cells and transmits inhibitory signals to the leukocyte.
R-HSA-199093 (Reactome) JAM members, such as JAML, bind coxsackie and adenovirus receptor (CXADR) on epithelial and endothelial cells.
R-HSA-199112 (Reactome) NK cells express adhesion molecules that allow interaction with their tumour targets, promoting their lysis.

For instance, the activating receptor CD226 is known to be involved in cytotoxic lymphocyte formation, as well as platelet adhesion to the endothelium. The cytoplasmic domain of CD226 contains binding motifs for members of the band 4.1 family of proteins, and for members of the membrane-associated guanylate kinase homolog (MAGUK) family. These proteins connect the CD226 receptor to the cytoskeleton and may promote clustering with LFA-1 integrin (also discussed in this pathway), which is known to participate in CD226's signaling cascade. CD226 plays a role in transendothelial migration, where it facilitates adherence to endothelial cells and migration between cell junctions.

Nectin-2 binds CD226. It is ubiquitously expressed in cells of various tissues, especially in epithelial cells, neurons and fibroblasts. Like many other nectin and Necl proteins, nectin-2 serves as a viral entry receptor for alpha-herpesviruses including herpes simplex virus (HSV-1 and HSV-2). The other CD226 ligand, Necl-5, was initially identified as a receptor for poliovirus.

CD96, another ligand for Necl-5, is strongly upregulated in activated NK cells.

CRTAM is similarly up-regulated, and has been shown to to bind Necl-2, promoting NK cell cytotoxicity towards otherwise poorly immunogenic targets.

R-HSA-199131 (Reactome) NK cells express adhesion molecules that allow interaction with their tumour targets, promoting their lysis.

For instance, the activating receptor CD226 is known to be involved in cytotoxic lymphocyte formation, as well as platelet adhesion to the endothelium. The cytoplasmic domain of CD226 contains binding motifs for members of the band 4.1 family of proteins, and for members of the membrane-associated guanylate kinase homolog (MAGUK) family. These proteins connect the CD226 receptor to the cytoskeleton and may promote clustering with LFA-1 integrin (also discussed in this pathway), which is known to participate in CD226's signaling cascade. CD226 plays a role in transendothelial migration, where it facilitates adherence to endothelial cells and migration between cell junctions.

Nectin-2 binds CD226. It is ubiquitously expressed in cells of various tissues, especially in epithelial cells, neurons and fibroblasts. Like many other nectin and Necl proteins, nectin-2 serves as a viral entry receptor for alpha-herpesviruses including herpes simplex virus (HSV-1 and HSV-2). The other CD226 ligand, Necl-5, was initially identified as a receptor for poliovirus.

CD96, another ligand for Necl-5, is strongly upregulated in activated NK cells.

CRTAM is similarly up-regulated, and has been shown to to bind Necl-2, promoting NK cell cytotoxicity towards otherwise poorly immunogenic targets.

R-HSA-199144 (Reactome) NK cells express adhesion molecules that allow interaction with their tumour targets, promoting their lysis.

For instance, the activating receptor CD226 is known to be involved in cytotoxic lymphocyte formation, as well as platelet adhesion to the endothelium. The cytoplasmic domain of CD226 contains binding motifs for members of the band 4.1 family of proteins, and for members of the membrane-associated guanylate kinase homolog (MAGUK) family. These proteins connect the CD226 receptor to the cytoskeleton and may promote clustering with LFA-1 integrin (also discussed in this pathway), which is known to participate in CD226's signaling cascade. CD226 plays a role in transendothelial migration, where it facilitates adherence to endothelial cells and migration between cell junctions.

Nectin-2 binds CD226. It is ubiquitously expressed in cells of various tissues, especially in epithelial cells, neurons and fibroblasts. Like many other nectin and Necl proteins, nectin-2 serves as a viral entry receptor for alpha-herpesviruses including herpes simplex virus (HSV-1 and HSV-2). The other CD226 ligand, Necl-5, was initially identified as a receptor for poliovirus.

CD96, another ligand for Necl-5, is strongly upregulated in activated NK cells.

CRTAM is similarly up-regulated, and has been shown to to bind Necl-2, promoting NK cell cytotoxicity towards otherwise poorly immunogenic targets.

R-HSA-199154 (Reactome) While not ubiquitously distributed, CD200 is expressed on a wide range of cell types including thymocytes, B-cells, activated T-cells, follicular dendritic cells,

endothelium, CNS neurons in the central nervous system, cells in reproductive organs, keratinocytes and renal glomeruli.

CD200R is a myeloid-inhibitory receptor, despite the absence of classical ITIMs in the cytoplasmic portion of the protein.

Interestingly, CD200 is also expressed on neurons within the CNS and would be predicted to modulate activation of microglia through CD200R.
R-HSA-199161 (Reactome) Most cells of the immune system express receptors for the Fc region of IgG. This heterogeneous family of molecules plays a critical role in immunity, by linking the humoral to the cellular responses. NK cells and B cells have been shown to express exclusively Fc-gamma RIIIa and RIIb respectively.
R-HSA-199169 (Reactome) CD160 is a GPI-anchored lymphocyte surface receptor in which expression is mostly restricted to the highly cytotoxic NK cells. MHC class I molecules bind to CD160 receptors on circulating NK lymphocytes and this triggers their cytotoxic activity and cytokine production. NK cells stimulated by IL-15 secrete soluble CD160 protein that binds to MHC-I molecules, resulting in the inhibition of the cytotoxic CD8+ T lymphocyte activity and of the CD160-mediated NK cell cytotoxicity.
R-HSA-199404 (Reactome) CD40 is a member of the Tumour Necrosis Factor receptor family and its ligand CD40L is a type II transmembrane protein of the TNF superfamily. The latter is expressed preferentially on T-cells and platelets. In the immune system, CD40-CD40L interaction affects some key processes such as immune cell activation, differentiation, proliferation, and apoptosis. CD40-CD40L interaction also upregulates costimulatory molecules (ICAM-1, VCAM-1, E-selectin, LFA-3, B7.1, B7.2, class II MHC, and CD40 itself).
R-HSA-199518 (Reactome) CD19 is a lymphocyte cell surface molecule that functions as a general response regulator or rheostat, which defnes signalling thresholds. These responses are infuenced by signals transduced through a CD19-CD21 cell surface receptor complex, where the binding of complement C3d to CD21 links humoral immune responses with the innate immune system. The CD19-CD21 complex is composed of at least four non-covalently associated proteins: CD19, CD21(complement receptor 2),CD81 and CD225.
R-HSA-199558 (Reactome) A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

R-HSA-199566 (Reactome) A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

R-HSA-199576 (Reactome) A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

R-HSA-199579 (Reactome) A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

R-HSA-199583 (Reactome) A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

R-HSA-199587 (Reactome) A hallmark of human NK cells is the expression of HLA class I-specific killer-cell immunoglobulin-like receptors (KIR). KIRs are not only variably expressed on the level of single NK cells but they are also highly polymorphic and polygenic (i.e. the gene content of the KIR cluster varies from individual to individual).

There are 15 functional KIR genes known to date, 11 encoding receptors with two immunoglobulin domains (KIR2D genes) and 4 with three domains (KIR3D genes). Inhibitory KIR genes are characterized by long cytoplasmic tails featuring immunoreceptor tyrosine-based inhibitory motifs (ITIM), which upon engagement transmit inhibitory signals leading to the general shutdown of NK cell effector functions. There are six inhibitory KIRs with clearly defined specificities, all of the inhibitory kind and all for HLA class I allotypes: KIR2DL2 and KIR2DL3 for HLA-C group 1, KIR2DL1 for HLA-C group 2, KIR3DL1 for HLA-B (Bw4 epitope), KIR3DL2 with HLA-A3 and KIR2DL4 with HLA-G.

In contrast, stimulatory KIR have short cytoplasmic tails lacking ITIM, but have a charged amino acid in the transmembrane region that provides a docking site for the activating adapter molecule DAP12. KIR2DS1 is known to bind HLA-C group 2 and KIR2DS2 binds HLA-C group 1.

R-HSA-5685600 (Reactome) Natural killer (NK) cells express a multitude of activating and inactivating cell surface receptors through which they recognise tumors and infected cells. Among the activating receptors, the family of Ig-like molecules is termed natural cytotoxicity receptors (NCRs). These NCRs include Natural cytotoxicity triggering receptor 1 (NCR1 also referred as NKp46 or LY94), Natural cytotoxicity triggering receptor 2 (NCR2 also referred as NKp44) and Natural cytotoxicity triggering receptor 3 (NCR3 also referred as NKp30 ) (Hecht et al. 2009). All three NCRs are involved in the elimination of both tumor and virus infected cells. NCRs are coupled to different signal transducing adaptor proteins, including CD3zeta, FCER1G, and KARAP/DAP12.
NCR1 (NKp46) is selectively expressed by all resting and activated human NK cells (Sivori et al. 1997). NCRI recognises and targets the direct killing of virus-infected cells. The antiviral activity is initiated by the interaction of NCR1 with hemagglutinin of influenza virus or Sendai virus (Mandelboim et al. 2001). Biochemical analysis revealed that NCR1 molecules are coupled with associated adaptor proteins CD3z and FCERIG that contain immune tyrosine-based activating motifs (ITAM) (Moretta et al. 2001).
R-HSA-5685602 (Reactome) NCR3 (NKp30) is one of the natural cytotoxicity receptors (NCRs) expressed mainly on the surface of the natural killer (NK) cells. NKp30 is a major receptor targeting virus-infected cells, malignantly transformed cells, and immature dendritic cells. NCR3 (NKp30) recognizes tumor antigens B7H6, a member of the B7 family (Kaifu et al. 2011, Brandt et al. 2009). B7H6 is not expressed normally, and is found on tumor cells, and sensitizes targets to NCR3-dependent cytotoxicity by NK cells. Other potential NCR3 ligands include human cytomegalovirus (HCMV) tegument protein pp65 (Arnon et al.2005) and BCL2-associated athanogene 6 (BAG-6 also referred as BAT3) (Pogge et al. 2007, Simhadri et al. 2008, Binici et al. 2013). Interaction between NCR3 and pp65 resulted in NK cell inhibition (Arnon et al.2005).
R-HSA-5685603 (Reactome) The cytoplasmic tails of the SLAM-family receptors contain immunoreceptor tyrosine-based switch motifs (ITSMs). These ITSMs act as docking sites for the SH2 domain of SLAM-associated protein (SAP) and the related Ewing's sarcoma-associated transcript (EAT) 2 (Latour & Veillette 2004, Kageyama et al. 2012). Both SAP and EAT2 are expressed in natural killer (NK) cells, and their combined expression is essential for NK cells to kill abnormal hematopoietic cells. SAP mediates this effect by combining SLAM family receptors to the protein kinase FYN and exchange factor VAV, thereby promoting conjugate formation between NK cells and target cells. While EAT2 mediates its effects in NK cells by linking SLAM family receptors to phospholipase C-gamma, calcium fluxes amd ERK kinase (Perez-Quintero et al. 2014).
R-HSA-5685604 (Reactome) Members of the signaling lymphocytic-activation molecule (SLAM) family, are all encoded in the SLAM locus, and are mostly homotypic self-associating receptors expressed by cells of hemopoietic origin (Veillette et al. 2006). SLAMF6 (also called as NTB-A) is a homophilic receptor that stimulates cytotoxicity in natural killer (NK) cells, regulates bactericidal activities in neutrophils, and potentiates T helper 2 (Th2) responses (Cao et al. 2006).
R-HSA-5685605 (Reactome) Signaling Lymphocyte Activation Molecule family member F7 (SLAMF7 also called as CS1 or CRACC) is a member of the CD2 family. It is expressed on CD8+ cytotoxic T lymphocytes, activated B cells, NK cells and mature dendritic cells (Boles & Mathew 2001, Bouchon et al. 2001). It has been suggested that CS1 has both activating and inhibitory functions in NK cells. It may activate NK mediated cytotoxicity through an ERK-mediated pathway in a SAP-independent manner (Bouchon et al. 2001). Most of the CD2 members interact homophilically and CS1 is shown to be a self-ligand and that homophilic interaction regulate NK cell cytolytic activity (Kumaresan et al. 2002).
R-HSA-5685606 (Reactome) Natural killer cell surface protein P1A (NKRP1A or KLRB1 or CD161) receptor is a lectin like surface molecule expressed as a type II disulphide-linked homodimer on natural killer (NK) cells and subsets of T cells (Lknair et al. 1994, Mesci et al. 2006). Its expression is upregulated on mature NK cells by interleukin-12 (Poggi et al. 2007). It is thought to be involved in the regulation of NK and NKT cell function. Lectin-like transcript-1 molecule (LLT1) (also referred to as CLEC2D) a member of the KLR (killer cell lectin-like receptor) family has been identified as a ligand for the human NKRP1A (Aldemir et al. 2005, Rosen et al. 2005).
R-HSA-5685607 (Reactome) Sialic acid binding immunoglobulins (Ig)-like lectins (SIGLECs) belong to I-type lectin with a selective expression on the haematopoetic cell lineages. These have amazing structural diversity each recognizing differently linked terminal sialic acid on glycoproteins and glycolipids expressed on host cells as well as pathogen (Powell & Varki 1995, Crocker 2002). Fifteen human SIGLECs have been identified so far. Interaction with various sialylated glycoconjugates, SIGLECs undertake various functions such as internalization of sialylated pathogens, attenuation of inflammation, restraining cellular activation, attenuation of damage-associated molecular pattern-mediated in?ammation along with inhibition of NK cell activation (von Gunten & Bochner 2008, Pillai et al. 2012, Matthew et al. 2014). The sialic acid-binding Ig-like lectins CD33 (SIGLEC3), SIGLEC7 and -9 are inhibitory receptors expressed on human NK cells and subsets of peripheral T cells that recognise sialic acid-containing carbohydrates (Hernández-Caselles et al. 2006, Falco et al. 1999).
R-HSA-5685608 (Reactome) Killer cell lectin-like receptor subfamily F member 1 (KLRF1 also referred as NKp80 or CLEC5C) is a homodimeric C-type lectin receptor (CTLR) expressed virtually on all human NK cells, and a minor subsets of effector memory CD8 alpha/beta T cells and gamma/delta T cells (Vitale et al. 2001). NKp80 binds to the genetically linked receptor C-type lectin domain family 2 member B (CLEC2B also referred as AICL) (Welte et al. 2006). CLEC2B is expressed as a myeloid-specific activating receptor that is upregulated by Toll-like receptor stimulation (Hamann et al. 1997). NKp80-CLEC2B interaction triggers NK cell-mediated cytolysis of malignant myeloid cells. Crosslinking of both NKp80 and CLEC2B was shown to promote an activating cross-talk between NK cells and monocytes in the presence of inflammatory cytokines (Welte et al. 2006, Klimosch et al. 2013).
R-HSA-5686625 (Reactome) Leukocyte-associated Ig-like receptor-1 (LAIR1 or CD305) is a member of the Ig superfamily (IgSF), which is expressed on almost all immune cells, mostly on PBMCs and thymocytes (Meyaard et al. 1997). Collagens are functional ligands for LAIR1 and upon their interaction mediate an inhibitory signal to immune cell activation (Lebbink et al. 2006, Meyaard 2008). An interesting implication of the discovery of LAIR1 as an inhibitory collagen receptor is that tumor cells, known to upregulate collagen expression, may use this interaction to downregulate responses directed against the tumor by various effector cells (Meyaard 2010). Upon cross-linking of the receptor with mAbs, LAIR1 gets phosphorylated on the tyrosine residues in the cytoplasmic ITIMs and recruits SHP1 and SHP2 and C-terminal Src Kinase (Csk) (Verbrugge et al. 2006).
SAP,EAT2R-HSA-5685603 (Reactome)
SELLR-HSA-199046 (Reactome)
SIGLEC:sialic acidArrowR-HSA-5685607 (Reactome)
SIGLECR-HSA-5685607 (Reactome)
SLAMF6:SLAMF6:SAP,EAT2ArrowR-HSA-5685603 (Reactome)
SLAMF6:SLAMF6ArrowR-HSA-5685604 (Reactome)
SLAMF6:SLAMF6R-HSA-5685603 (Reactome)
SLAMF6R-HSA-5685604 (Reactome)
SLAMF7:SLAMF7ArrowR-HSA-5685605 (Reactome)
SLAMF7R-HSA-5685605 (Reactome)
Sialic acidR-HSA-5685607 (Reactome)
T-cell receptor complex with CD8R-HSA-198955 (Reactome)
TCR interacting with

antigen-bearing MHC

Class I		ArrowR-HSA-198955 (Reactome)
VCAM1R-HSA-198941 (Reactome)
integrin alpha4beta1:VCAM1ArrowR-HSA-198941 (Reactome)

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