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

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1, 4, 10, 50, 60...3032, 39, 46, 55, 59...8716, 3145, 6543, 89, 909, 35, 52, 66, 8225406817, 1814, 51, 5423, 27, 4926, 8111, 42, 6123, 27, 495, 8, 4138, 6745, 6537, 8423, 27, 491233, 5623, 27, 4958, 8322, 7515, 2129, 62, 6443, 89, 903, 6, 2820, 2423, 27, 4948, 70, 8823, 27, 499, 35, 44, 77745772, 7913, 34, 6923, 27, 4938, 7871cytosolcytosolcytosolcytosolcytosolvirion membraneAntigen-bound Ig GAntibodyCLEC2B GalNAc-GD1a HLA class I histocompatibility antigen, Cw-1 alpha chain HLA class I histocompatibility antigen, Cw-6 alpha chain precursor HLA class I histocompatibility antigen, Cw-17 alpha chain HLA-C group 1interacting withKIR2DL2/3ICAM3 LAIR2 OSCARclass I MHC B52 CD1:B2M:self-lipidclass I MHC B46 HLA class I histocompatibility antigen, A-66 alpha chain VCAM1Ig kappa chain V-III region POM MHC Class Iinteracting withCD160ICAM3 Ig kappa chain V-I region AG HLA class I histocompatibility antigen, A-29 alpha chain KLRF1 dimerCD1B KIR3DL2 HemagglutininHLA class I histocompatibility antigen, A-68 alpha chain IGLC7 class I MHC B46 HLA class I histocompatibility antigen, A-24 alpha chain HLA class I histocompatibility antigen, A-32 alpha chain HLA class I histocompatibility antigen, A-74 alpha chain B2M(21-119) CLEC2B Collagen types I,II,III Ig heavy chain V-III region TRO IgH heavy chain V-III region VH26 precursor HLA class I histocompatibility antigen, A-74 alpha chain CD22 B2M(21-119) CD160HLA class I histocompatibility antigen, E alpha chain precursor HLA class I histocompatibility antigen, E alpha chain precursor HLA class I histocompatibility antigen, A-26 alpha chain Ac2SGL CD1A ULBP3 KIR2DL3 Antigen C30 mannosyl MPM class I MHC B37 SIGLECSLAMF7 HLA class I histocompatibility antigen, E alpha chain precursor TRAC HLA class I histocompatibility antigen, A-43 alpha chain TRBV12-3 Ig lambda chain V-I region HA SIGLEC12 CD19 KIR3DL1CD3E class I MHC B73 HLA class I histocompatibility antigen, A-32 alpha chain GLYCAM1 HLA class I histocompatibility antigen, Cw-6 alpha chain precursor Ig kappa chain V region EV15 LAM PVRL2class I MHC B38 TCRB Ig heavy chain V-II region ARH-77 NCR1 cd21(1-?) LILRA5 CD40-1 DDM-838 Ig kappa chain V-III region VG COLEC12 class I MHC B51 AMICA1HLA class I histocompatibility antigen, A-1 alpha chain precursor CXADR HLA class I histocompatibility antigen, A-30 alpha chain class I MHC B7 TYROBP TRBC1 CD40LG(1-261) class I MHC B53 IGLV1-40(1-?) HLA class I histocompatibility antigen, A-3 alpha chain precursor TCRA class I MHC B73 MICB CD247-1 ICAM5 class I MHC B53 HLA-C Ig lambda chain V-I region NEWM CD33 IGLC1 HLA class I histocompatibility antigen, Cw-3 alpha chain precursor Ig lambda chain V region 4A IGLC6 HLA class I histocompatibility antigen, A-11 alpha chain IGKV3D-20 class I MHC B8 SIGLEC5 IGHV(1-?) PIANP class I MHC B15 CD247-1 CD34-1 KLRG1HCST SLAMF7class I MHC B49 ICAM4 class I MHC B53 ITGA4 Ig lambda chain V-IV region Kern Ig lambda chain V-IV region Kern HLA class I histocompatibility antigen, Cw-15 alpha chain NPDC1 HLA class I histocompatibility antigen, A-29 alpha chain Ig heavy chain V-III region DOB HA HLA class I histocompatibility antigen, A-33 alpha chain CLEC2D dimer:KLRB1dimerIGKC CD99 CERA,PE,PSSIGLEC5 KLRK1 Ig heavy chain V-I region HG3 CD247-1 MHC Class Imoleculesinteracting withCD160HLA class I histocompatibility antigen, A-1 alpha chain precursor HLA class I histocompatibility antigen, Cw-17 alpha chain ICAM4 Ig lambda chain V-I region NEWM MHC Class Iinteracting withLILRsHLA class I histocompatibility antigen, A-24 alpha chain CD1D B2M(21-119) class I MHC B40 Ig lambda chain V-I region HA IGLV(23-?) HLA class I histocompatibility antigen, A-32 alpha chain IGLV11-55(1-?) HLA class I histocompatibility antigen, A-43 alpha chain CD1C Collagen type III fibril IGLV5-45(1-?) NCR3LG1:NCR3:FCRG3A:CD3Z dimerHLA-C GMM class I MHC B59 CD1B HLA class I histocompatibility antigen, A-31 alpha chain class I MHC B27 HLA class I histocompatibility antigen, A-1 alpha chain precursor TYROBP HLA-H Ig lambda chain V-VI region AR ICAM5 CD22 LILRA3 Ig lambda chain V-VI region AR class I MHC B56 CD96 Antigen CD247-1 CD1D Collagen type XVIIfibrilSH2D1A HLA class I histocompatibility antigen, Cw-18 alpha chain Ig kappa chain V-II region Cum SH2D1A CERA class I MHC B44 CLEC2D ITGA4 HLA class I histocompatibility antigen, A-3 alpha chain precursor HLA-G interactingwith KIR2DL4HLA class I histocompatibility antigen, Cw-12 alpha chain LAIR1:Collagen typeXVIIHLA-H HN TCRB IGLV11-55(1-?) HLA class I histocompatibility antigen, A-36 alpha chain CD8B HLA-E interactingwith KLRC1:KLRD1TRAC HLA class I histocompatibility antigen, A-68 alpha chain IGLV4-3(1-?) CRTAM SIGLEC10 class I MHC B57 Ig kappa chain V-I region Daudi TRAV19 CD1A TRAV19 class I MHC B18 Ig heavy chain V-II region OU IGLV3-22(1-?) class I MHC B7 NCR3LG1Ig lambda chain V-IV region Bau Ig heavy chain V-III region BUT Antigen IGLV7-46(1-?) class I MHC B49 IGLV8-61(1-?) CD226:PVRPILRACMVPP65:NCR3:FCRG3A:CD3Z dimerclass I MHC B52 Ig kappa chain V-I region Daudi class I MHC B52 Ig heavy chain V-II region WAH class I MHC B56 B2M(21-119) CD160 class I MHC B45 CD3D PILRA B2M(21-119) HLA-C KLRD1 Ig kappa chain V-I region Gal IGLV2-11(1-?) HLA class I histocompatibility antigen, A-30 alpha chain class I MHC B37 B2M(21-119) class I MHC B78 HLA class I histocompatibility antigen, Cw-4 alpha chain precursor IGLV(23-?) B2M(21-119) class I MHC B58 class I MHC B13 Ig lambda chain V-II region NEI KIR2DS1 complexedwith DAP12FCGR3A CD3E KIR3DL1 TRAC B2M(21-119) IGLC2 HLA class I histocompatibility antigen, A-80 alpha chain IGLV5-37(1-?) HLA class I histocompatibility antigen, A-2 alpha chain IGLV3-12(1-?) CD200 bound toCD200RKLRB1 dimerIg lambda chain V-I region VOR IGLV3-16(1-?) Ig kappa chain V-I region BAN FCGR3A IGKVA18(21-?) KLRB1 Antigen LILRB1 class I MHC B51 LAIR1 class I MHC B15 NPDC1 LILRA2 HLA-GHLA-C group 2interacting withKIR2DL1HLA class I histocompatibility antigen, Cw-6 alpha chain precursor LILRB5 HLA class I histocompatibility antigen, A-31 alpha chain HLA class I histocompatibility antigen, Cw-2 alpha chain IGLV4-60(1-?) LAIR1KIR2DL1cd21(1-?) ULBP1 HLA class I histocompatibility antigen, A-23 alpha chain PVRL2 HLA class I histocompatibility antigen, A-31 alpha chain CD3D Ig lambda chain V-IV region Hil class I MHC B8 IGLC3 HLA class I histocompatibility antigen, E alpha chain precursor KLRK1 class I MHC B82 HLA-C Cw4 (group 2)HLA class I histocompatibility antigen, A-23 alpha chain Ig heavy chain V-III region BRO HLA class I histocompatibility antigen, alpha chain F precursor HLA-C Ig heavy chain V-II region NEWM HLA class I histocompatibility antigen, A-33 alpha chain alpha-mycolic acid Ig lambda chain V-III region LOI class I MHC B44 HLA class I histocompatibility antigen, Cw-16 alpha chain PE HLA class I histocompatibility antigen, Cw-3 alpha chain precursor HLA class I histocompatibility antigen, Cw-8 alpha chain GalNAc-GD1a class I MHC B39 class I MHC B41 ITGA4 IGKV1-12 class I MHC B18 Ig lambda chain V-II region TOG GM1 Antigen-boundantibody bound tolymphoid Fc gammareceptorsIg kappa chain V-II region RPMI 6410 HLA class I histocompatibility antigen, Cw-14 alpha chain HLA class I histocompatibility antigen, Cw-16 alpha chain CRTAMclass I MHC B59 TCRB CD226 HLA class I histocompatibility antigen, A-36 alpha chain KIR2DL4LILRA1 HLA class I histocompatibility antigen, Cw-4 alpha chain precursor HLA class I histocompatibility antigen, A-1 alpha chain precursor KIR2DS2 class I MHC B8 LILRB2 HLA class I histocompatibility antigen, A-26 alpha chain L-selectininteracting withknown ligandsFCGR1A FCGR2B class I MHC B27 Ig kappa chain V-I region AU SLAMF6 dimerclass I MHC B13 C3d fragment ICAM1 LAIR2HLA class I histocompatibility antigen, A-80 alpha chain HLA class I histocompatibility antigen, Cw-1 alpha chain class I MHC B41 PS HLA class I histocompatibility antigen, alpha chain F precursor CD1:B2M:microbiallipidCD3G HLA class I histocompatibility antigen, Cw-4 alpha chain precursor class I MHC B47 NCR3LG1 CD247-1 Ig kappa chain V-III region VG HLA class I histocompatibility antigen, Cw-4 alpha chain precursor Ig kappa chain V region EV15 PILRA:PIANP,NPDC1,CLEC4G,COLEC12 trimerHLA class I histocompatibility antigen, E alpha chain precursor class I MHC B45 TRBC1 class I MHC B57 IGLV5-37(1-?) class I MHC B50 class I MHC B46 HLA class I histocompatibility antigen, alpha chain F precursor HLA-EHLA class I histocompatibility antigen, A-33 alpha chain TRBV12-3 C3d fragment Ig heavy chain V-III region BUT HLA class I histocompatibility antigen, A-3 alpha chain precursor class I MHC B67 SLAMF6:SLAMF6:SAP,EAT2TCRB HLA class I histocompatibility antigen, A-25 alpha chain class I MHC B41 HLA class I histocompatibility antigen, A-36 alpha chain HLA-C Cw3 (group 1)class I MHC B45 TRAV19 CD40-1 CD247-1 CXADRclass I MHC B82 Antigen peptidebound class I MHCC3d complexed withantigenFCGR1A HLA class I histocompatibility antigen, A-29 alpha chain class I MHC B50 squalene COLEC12 HLA class I histocompatibility antigen, B-48 alpha chain IGLV3-25(1-?) HLA class I histocompatibility antigen, Cw-18 alpha chain SIGLEC10 TRBV12-3 class I MHC B15 Ig heavy chain V-II region MCE class I MHC B59 C30 mannosyl MPM CD3G HLA class I histocompatibility antigen, Cw-12 alpha chain HLA class I histocompatibility antigen, B-48 alpha chain IGLV7-43(1-?) HLA-A3class I MHC B42 HLA class I histocompatibility antigen, alpha chain G precursor HLA class I histocompatibility antigen, A-2 alpha chain KLRC1class I MHC B39 HLA class I histocompatibility antigen, A-68 alpha chain HLA-C HLA-C group 1interacting withKIR2DS2TRAV19 T-cell receptor alpha chain V region PY14 precursor SIGLEC6 HLA class I histocompatibility antigen, A-36 alpha chain TRAC Ig heavy chain V-II region WAH CD3E IGLV1-44(1-?) SAP,EAT2LILRA5 Ig heavy chain V-III region TRO NCR1:FCRG1A:CD3ZdimerPG TRAC HLA class I histocompatibility antigen, alpha chain G precursor ICAM2 BbGL-2c CD1A CMVPP65class I MHC B46 HLA class I histocompatibility antigen, A-2 alpha chain KIR2DL4 LILR setRAET1E MADCAM1-1 class I MHC B13 class I MHC B45 HLA class I histocompatibility antigen, Cw-8 alpha chain IGKV1-12 class I MHC B38 HLA class I histocompatibility antigen, A-26 alpha chain Ligand interactingwith NKG2Dclass I MHC B27 squalene class I MHC B40 HLA class I histocompatibility antigen, alpha chain G precursor NCR3 CD226 SLAMF6 IGKV1-5(23-?) HLA class I histocompatibility antigen, alpha chain G precursor CD3E Ig heavy chain V-III region WEA IGLV2-23(1-?) HLA class I histocompatibility antigen, A-29 alpha chain HLA class I histocompatibility antigen, Cw-15 alpha chain HLA class I histocompatibility antigen, A-24 alpha chain Ig lambda chain V-I region VOR class I MHC B44 IGLV1-36(1-?) TRBV12-3 class I MHC B52 LILRB2 KIR2DL2 Ig lambda chain V-II region TOG IGLV4-69(1-?) Antigen B2M(21-119) B2M(21-119) HLA class I histocompatibility antigen, A-74 alpha chain NCR3 class I MHC B18 SELL TYROBP PVRL2 IGHV(1-?) CLEC4G Integrin alphaLbeta2HLA class I histocompatibility antigen, A-2 alpha chain MADCAM1-1HLA class I histocompatibility antigen, Cw-12 alpha chain OSCAR:CollagenI,II,III/SP-DHLA class I histocompatibility antigen, A-2 alpha chain KIR3DL2HLA class I histocompatibility antigen, A-26 alpha chain Ig heavy chain V-I region EU CD96:PVRCDH1(155-882) Ig lambda chain V-I region NEW SLAMF7 dimerT-cell receptor alpha chain V region PY14 precursor HLA class I histocompatibility antigen, Cw-3 alpha chain precursor OSCAR CD1B HLA-C group 2interacting withKIR2DS1class I MHC B40 Integrin alpha4beta7HLA class I histocompatibility antigen, Cw-3 alpha chain precursor Integrin alpha4beta1class I MHC B38 HLA class I histocompatibility antigen, alpha chain G precursor HLA class I histocompatibility antigen, A-69 alpha chain IGLV2-11(1-?) MICA Glc-DAG-s2 class I MHC B81 SIGLEC9 SIGLEC11 IGLC2 HLA class I histocompatibility antigen, Cw-14 alpha chain class I MHC B55 B2M(21-119) class I MHC B47 IGLV3-12(1-?) PVR class I MHC B55 HLA class I histocompatibility antigen, A-3 alpha chain precursor class I MHC B56 CD200R1B2M(21-119) HLA class I histocompatibility antigen, Cw-14 alpha chain CD3D Sialic acid HLA class I histocompatibility antigen, Cw-3 alpha chain precursor class I MHC B18 IGLV4-3(1-?) CD300 HLA class I histocompatibility antigen, E alpha chain precursor IGLC1 CD33 B2M(21-119) B2M(21-119) MADCAM1-1 IFITM1 HLA class I histocompatibility antigen, Cw-5 alpha chain precursor class I MHC B49 IGLV5-45(1-?) LILRB5 KLRG1 B2M(21-119) class I MHC B53 C16 sulfatide class I MHC B78 HLA class I histocompatibility antigen, A-25 alpha chain CD200TCRA Collagen types I,IIIHLA class I histocompatibility antigen, Cw-3 alpha chain precursor T-cell receptorcomplexULBP1 CD81 Lymphoid-expressedFc-gamma receptorsGalA-GSL class I MHC B41 Ig kappa chain V-I region Gal MHC Class I Sialic acidSIGLEC7 IGHV7-81(1-?) class I MHC B7 HLA class I histocompatibility antigen, Cw-1 alpha chain Ig lambda chain V-I region NEW TCRA IGLV10-54(1-?) class I MHC B82 Ig kappa chain V-I region AG class I MHC B35 B2M(21-119) CXADR bound to JAMLIg kappa chain V-II region Cum class I MHC B54 B2M(21-119) PI CLEC2B dimerIg kappa chain V-III region POM CLEC2D dimerIg heavy chain V-III region DOB HLA class I histocompatibility antigen, Cw-12 alpha chain class I MHC B14 IGKVA18(21-?) Ig kappa chain V-III region B6 ITGB2 class I MHC B35 CD3E FCGR1A Ig lambda chain V-IV region Bau alpha-mycolic acid IFITM1 HLA class I histocompatibility antigen, A-33 alpha chain IGLV10-54(1-?) Antigen PILRB IGLV8-61(1-?) class I MHC B13 class I MHC B27 NCR1 IGHV1-2 HLA class I histocompatibility antigen, alpha chain G precursor HLA class I histocompatibility antigen, Cw-3 alpha chain precursor class I MHC B44 class I MHC B56 B2M(21-119) KLRC1 IGKV4-1(21-?) CD40LG trimerB2M(21-119) class I MHC B49 LILRA4 IGLV2-18(1-?) class I MHC B15 CD1A IgH heavy chain V-III region VH26 precursor HLA class I histocompatibility antigen, A-34 alpha chain Ig heavy chain V-III region WEA class I MHC B8 HLA class I histocompatibility antigen, A-43 alpha chain PE TRBC1 CD1B CD247-1 T-cell receptorcomplex with CD8TYROBP class I MHC B78 HLA class I histocompatibility antigen, Cw-15 alpha chain HLA class I histocompatibility antigen, A-1 alpha chain precursor IGLV7-46(1-?) Ig heavy chain V-II region MCE SIGLEC8 ITGB1 HLA class I histocompatibility antigen, Cw-16 alpha chain Ig lambda chain V-II region MGC HLA class I histocompatibility antigen, Cw-6 alpha chain precursor CD8B T-cell receptor alpha chain V region PY14 precursor ITGB2 CRTAM bound to NECL2HLA class I histocompatibility antigen, Cw-4 alpha chain precursor class I MHC B82 HLA-H PILRB class I MHC B8 HLA class I histocompatibility antigen, E alpha chain precursor IGLV2-33(1-?) IGLV4-69(1-?) SIGLEC1 Ig lambda chain V region 4A IGLV3-22(1-?) class I MHC B59 IGLV2-33(1-?) class I MHC B14 class I MHC B7 IGKV4-1(21-?) KIR2DS1 class I MHC B7 Ig heavy chain V-III region JON NKG2D complexed withDAP10IGKV3D-20 CD247-1 Ig kappa chain V-II region FR HLA class I histocompatibility antigen, Cw-5 alpha chain precursor IGKV1-5(23-?) CD34-1 SIGLEC11 class I MHC B40 LILRB4 Ig lambda chain V-II region BOH PILRA IGLV3-25(1-?) HLA class I histocompatibility antigen, Cw-2 alpha chain Ig lambda chain V-II region NEI HLA class I histocompatibility antigen, Cw-4 alpha chain precursor LFA-1:ICAM 1-5LILRA6 HLA class I histocompatibility antigen, A-3 alpha chain precursor SH2D1B CD226ICAM 1-5HLA class I histocompatibility antigen, alpha chain F precursor class I MHC B39 GalA-GSL HLA class I histocompatibility antigen, A-11 alpha chain LILRA6 SIGLEC1 TREMs HLA class I histocompatibility antigen, A-23 alpha chain HLA class I histocompatibility antigen, Cw-5 alpha chain precursor NCR1:FCRG1A:CD3Zdimer:HemagglutininIg heavy chain V-I region HG3 class I MHC B35 Ac2SGL HLA class I histocompatibility antigen, Cw-4 alpha chain precursor class I MHC B42 class I MHC B54 L-selectin ligandsIg heavy chain V-III region JON class I MHC B7 LILRA4 Ig heavy chain V-III region KOL class I MHC B37 LAIR2:Collagen typeI,IIIIGLV4-60(1-?) KLRF1 dimer:CLEC2BdimerHLA class I histocompatibility antigen, Cw-18 alpha chain CD3G CMVPP65 class I MHC B38 CD8A class I MHC B55 NKG2D ligandRAET1E B2M(21-119) Complex of CD19,CD81, CD225 andCD21NCR3 PS CERA class I MHC B50 HLA class I histocompatibility antigen, A-30 alpha chain ULBP3 HLA class I histocompatibility antigen, A-66 alpha chain Ig kappa chain V-I region Wes Ig heavy chain V-II region ARH-77 IGHV7-81(1-?) NCR3:FCRG1A:CD3ZdimerHLA class I histocompatibility antigen, alpha chain F precursor HLA class I histocompatibility antigen, Cw-17 alpha chain class I MHC B37 HLA class I histocompatibility antigen, B-48 alpha chain HLA class I histocompatibility antigen, A-31 alpha chain class I MHC B54 IGLV2-23(1-?) HA ITGB1 class I MHC B50 Ig lambda chain V-II region MGC HLA class I histocompatibility antigen, Cw-4 alpha chain precursor TCRA ITGB7 PILRA PIANP Ig heavy chain V-II region OU KLRB1 Ig heavy chain V-III region CAM class I MHC B67 TREM, CD300TRAV19 MHC Class I Ig kappa chain V-II region RPMI 6410 Ig kappa chain V-I region BAN Collagen types I,II,III PILRA,PILRB:CD99CD8A CLEC2D SIGLEC12 HLA class I histocompatibility antigen, Cw-5 alpha chain precursor Ig kappa chain V-I region AU HLA Bw4 interactingwith KIR3DL1TRIM, CD300:lipidsCDH1(155-882)CD1:B2M:microbiallipid:TCRITGAL HLA class I histocompatibility antigen, Cw-8 alpha chain CD1D C16 sulfatide KLRD1CLEC4G Complex of CD19,CD81, CD225 andCD21 with C3d-boundAntigenMICA HLA-Bw4PVR IGLV1-40(1-?) PIANP,NPDC1,CLEC4G,COLEC12 trimerBbGL-2c class I MHC B81 HLA class I histocompatibility antigen, Cw-6 alpha chain precursor CD96IGLC3 class I MHC B73 PG SIGLEC9 SIGLEC:sialic acidHLA class I histocompatibility antigen, A-43 alpha chain class I MHC B27 Ig lambda chain V-III region SH SFTPD oligomer TCRB TREMs GM1 IGLC6 MADCAM1-1 HLA class I histocompatibility antigen, Cw-17 alpha chain HLA class I histocompatibility antigen, A-69 alpha chain class I MHC B81 HLA class I histocompatibility antigen, A-34 alpha chain LILRA2 Ig heavy chain V-I region EU CD1:B2M:self-lipid:TCRSLAMF6class I MHC B42 ITGA4 Ig lambda chain V-III region SH B2M(21-119) HLA class I histocompatibility antigen, B-48 alpha chain TRBV12-3 KIR2DS2 complexedwith DAP12class I MHC B38 HLA class I histocompatibility antigen, Cw-3 alpha chain precursor Ig kappa chain V-I region DEE HLA class I histocompatibility antigen, Cw-15 alpha chain CD1D KIR2DS2 HLA class I histocompatibility antigen, A-74 alpha chain CD81 HLA class I histocompatibility antigen, A-30 alpha chain Collagen type I fibril HLA class I histocompatibility antigen, Cw-3 alpha chain precursor class I MHC B57 Collagen type I fibril AMICA1 class I MHC B47 ICAM2 TRBC1 Collagen type III fibril IGLV1-36(1-?) KIR2DS1 HLA class I histocompatibility antigen, A-1 alpha chain precursor class I MHC B15 KIR2DL3 Ig heavy chain V-III region KOL HLA class I histocompatibility antigen, A-23 alpha chain Ig kappa chain V-I region HK101 HLA class I histocompatibility antigen, A-32 alpha chain class I MHC B39 IGKV2-28 TCRA class I MHC B67 IGKV2D-30 class I MHC B58 FCGR1A CD226 bound toNectin 2Collagen typesI,II,III/SP-DIGLV1-44(1-?) HLA class I histocompatibility antigen, alpha chain G precursor class I MHC B58 KLRF1 IGKC ITGB7 class I MHC B47 IGLC7 class I MHC B38 class I MHC B78 IGKV2-28 HLA class I histocompatibility antigen, A-3 alpha chain precursor SIGLEC7 HLA class I histocompatibility antigen, E alpha chain precursor T-cell receptor alpha chain V region PY14 precursor T-cell receptor alpha chain V region PY14 precursor KIR2DL2 GMM CD3G IGLV2-18(1-?) TCR interacting withantigen-bearing MHCClass IGlc-DAG-s2 integrinalpha4beta1:VCAM1class I MHC B67 class I MHC B51 HLA class I histocompatibility antigen, Cw-2 alpha chain CD19 PVRclass I MHC B14 class I MHC B81 LILRB4 IGLV3-16(1-?) CD200R1 class I MHC B55 FCGR1A HLA class I histocompatibility antigen, A-34 alpha chain CD247-1 IGKV2D-30 LILRB3 CD3G HLA class I histocompatibility antigen, A-69 alpha chain CD99class I MHC B35 Ig lambda chain V-IV region Hil class I MHC B73 HLA class I histocompatibility antigen, Cw-2 alpha chain class I MHC B42 ITGAL KIR2DL1 Ig lambda chain V-II region BOH LILRA1 CD1C SELLIGLV7-43(1-?) B2M(21-119) E-cadherin bound toKLRG1HLA class I histocompatibility antigen, alpha chain F precursor HN HLA class I histocompatibility antigen, Cw-14 alpha chain MICB Ig kappa chain V-II region FR SIGLEC6 CD40:CD40L trimerHLA-Cgroup-I-interactingKIRsIg kappa chain V-I region Wes CD247-1 Ig heavy chain V-III region BRO B2M(21-119) HLA class I histocompatibility antigen, A-66 alpha chain KLRF1 class I MHC B54 IGLV3-27(1-?) VCAM1 HLA class I histocompatibility antigen, A-25 alpha chain HLA class I histocompatibility antigen, Cw-4 alpha chain precursor CD3D SFTPD oligomer HLA class I histocompatibility antigen, Cw-8 alpha chain SLAMF6 LAM Ig kappa chain V-I region DEE HLA class I histocompatibility antigen, alpha chain G precursor CD3D HLA class I histocompatibility antigen, A-34 alpha chain CD300 IGLV3-27(1-?) HLA class I histocompatibility antigen, A-2 alpha chain CD40LG(1-261) CD40 trimerclass I MHC B8 Ig kappa chain V-III region B6 Ig heavy chain V-III region CAM B2M(21-119) HLA class I histocompatibility antigen, Cw-18 alpha chain CD200 DDM-838 PI HLA class I histocompatibility antigen, Cw-16 alpha chain LILRB1 HLA class I histocompatibility antigen, Cw-6 alpha chain precursor HLA-C HLA class I histocompatibility antigen, A-80 alpha chain FCGR2B HLA class I histocompatibility antigen, A-11 alpha chain HLA class I histocompatibility antigen, Cw-1 alpha chain SIGLEC8 HLA class I histocompatibility antigen, A-3 alpha chain precursor Ig heavy chain V-II region NEWM HLA class I histocompatibility antigen, A-11 alpha chain Integrinalpha4beta7:MADCAM1Ig lambda chain V-III region LOI Collagen type XVII fibril class I MHC B15 class I MHC B27 HLA class I histocompatibility antigen, A-80 alpha chain class I MHC B51 HLA class I histocompatibility antigen, A-25 alpha chain SH2D1B GLYCAM1 Ig kappa chain V-I region HK101 HLA class I histocompatibility antigen, A-68 alpha chain ICAM1 LILRB3 class I MHC B14 HLA class I histocompatibility antigen, A-24 alpha chain TRBC1 LILRA3 HLA-A3 interactingwith KIR3DL2PILRA,PILRBclass I MHC B57 IGHV1-2 class I MHC B58 HCST HLA class I histocompatibility antigen, A-66 alpha chain HLA-H LILR-interacting MHCClass I moleculesHLA class I histocompatibility antigen, A-69 alpha chain HLA class I histocompatibility antigen, A-3 alpha chain precursor 2, 19, 36, 63, 8523, 5323, 5323, 5347723, 537


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. View original pathway at:Reactome.</div>

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 198933
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: de Bono, Bernard

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Bibliography

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  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)
Ac2SGL MetaboliteCHEBI:62113 (ChEBI) CD1B-presented diacylated sulfoglycolipid produced by Mycobacterium tuberculosis (Gilleron M et al. 2004).
Antigen R-ALL-173548 (Reactome)
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)
BbGL-2c MetaboliteCHEBI:60453 (ChEBI) a CD1D-presented glycolipids from Borrelia burgdorfer (Wang J et al. 2005)
C16 sulfatide MetaboliteCHEBI:60366 (ChEBI)
C30 mannosyl MPM MetaboliteCHEBI:77480 (ChEBI) Mycobacterium tuberculosis antigen
C3d complexed with antigenComplexR-HSA-199000 (Reactome)
C3d fragment ProteinP01024 (Uniprot-TrEMBL)
CD160 ProteinO95971 (Uniprot-TrEMBL)
CD160ProteinO95971 (Uniprot-TrEMBL)
CD19 ProteinP15391 (Uniprot-TrEMBL)
CD1:B2M:microbial lipid:TCRComplexR-HSA-8848850 (Reactome)
CD1:B2M:microbial lipidComplexR-HSA-8848835 (Reactome)
CD1:B2M:self-lipid:TCRComplexR-HSA-8850222 (Reactome)
CD1:B2M:self-lipidComplexR-HSA-8850280 (Reactome)
CD1A ProteinP06126 (Uniprot-TrEMBL)
CD1B ProteinP29016 (Uniprot-TrEMBL)
CD1C ProteinP29017 (Uniprot-TrEMBL)
CD1D ProteinP15813 (Uniprot-TrEMBL)
CD200 ProteinP41217 (Uniprot-TrEMBL)
CD200 bound to CD200RComplexR-HSA-198191 (Reactome)
CD200ProteinP41217 (Uniprot-TrEMBL)
CD200R1 ProteinQ8TD46 (Uniprot-TrEMBL)
CD200R1ProteinQ8TD46 (Uniprot-TrEMBL)
CD22 ProteinP20273 (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)
CD300 R-HSA-5696349 (Reactome)
CD33 ProteinP20138 (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)
CD99 ProteinP14209 (Uniprot-TrEMBL)
CD99ProteinP14209 (Uniprot-TrEMBL)
CDH1(155-882) ProteinP12830 (Uniprot-TrEMBL)
CDH1(155-882)ProteinP12830 (Uniprot-TrEMBL)
CERA MetaboliteCHEBI:17761 (ChEBI)
CERA,PE,PSComplexR-ALL-5696348 (Reactome)
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)
CLEC4G ProteinQ6UXB4 (Uniprot-TrEMBL)
CMVPP65 ProteinP06725 (Uniprot-TrEMBL)
CMVPP65:NCR3:FCRG3A:CD3Z dimerComplexR-HSA-6793270 (Reactome)
CMVPP65ProteinP06725 (Uniprot-TrEMBL)
COLEC12 ProteinQ5KU26 (Uniprot-TrEMBL)
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 I fibril R-HSA-1474201 (Reactome)
Collagen type III fibril R-HSA-1474212 (Reactome)
Collagen type XVII fibrilR-HSA-2172656 (Reactome)
Collagen type XVII fibril R-HSA-2172656 (Reactome)
Collagen types I,II,III/SP-DComplexR-HSA-5696350 (Reactome)
Collagen types I,II,III R-HSA-5696346 (Reactome)
Collagen types I,IIIComplexR-HSA-5696343 (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)
DDM-838 MetaboliteCHEBI:62384 (ChEBI)
E-cadherin bound to KLRG1ComplexR-HSA-198192 (Reactome)
FCGR1A ProteinP12314 (Uniprot-TrEMBL)
FCGR2B ProteinP31994 (Uniprot-TrEMBL)
FCGR3A ProteinP08637 (Uniprot-TrEMBL)
GLYCAM1 ProteinQ8IVK1 (Uniprot-TrEMBL)
GM1 MetaboliteCHEBI:61048 (ChEBI)
GMM MetaboliteCHEBI:42782 (ChEBI) CD1B-presented glycolipid antigen produced by mycobacteria.
GalA-GSL MetaboliteCHEBI:528825 (ChEBI) CD1D-presented glycolipids from Sphingomonas spp. bacteria (Kinjo Y et al. 2005).
GalNAc-GD1a MetaboliteCHEBI:59228 (ChEBI)
Glc-DAG-s2 MetaboliteCHEBI:68524 (ChEBI) A bacterial metabolite that can be presented to T cell receptors by CD1D. Found in Streptococcus pneumoniae.
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, B-48 alpha chain ProteinP30486 (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-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		ComplexR-HSA-199540 (Reactome)
HLA-C Cw3 (group 1)ComplexR-HSA-199562 (Reactome)
HLA-C Cw4 (group 2)ComplexR-HSA-198911 (Reactome)
HLA-C ProteinP10321 (Uniprot-TrEMBL)
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)
HLA-H ProteinP01893 (Uniprot-TrEMBL)
HN ProteinP04853 (Uniprot-TrEMBL)
HemagglutininComplexR-NUL-9038349 (Reactome)
ICAM 1-5ComplexR-HSA-198193 (Reactome)
ICAM1 ProteinP05362 (Uniprot-TrEMBL)
ICAM2 ProteinP13598 (Uniprot-TrEMBL)
ICAM3 ProteinP32942 (Uniprot-TrEMBL)
ICAM4 ProteinQ14773 (Uniprot-TrEMBL)
ICAM5 ProteinQ9UMF0 (Uniprot-TrEMBL)
IFITM1 ProteinP13164 (Uniprot-TrEMBL)
IGHV(1-?) ProteinA2KUC3 (Uniprot-TrEMBL)
IGHV1-2 ProteinP23083 (Uniprot-TrEMBL)
IGHV7-81(1-?) ProteinQ6PIL0 (Uniprot-TrEMBL)
IGKC ProteinP01834 (Uniprot-TrEMBL)
IGKV1-12 ProteinA0A0C4DH73 (Uniprot-TrEMBL)
IGKV1-5(23-?) ProteinP01602 (Uniprot-TrEMBL)
IGKV2-28 ProteinA0A075B6P5 (Uniprot-TrEMBL)
IGKV2D-30 ProteinA0A075B6S6 (Uniprot-TrEMBL)
IGKV3D-20 ProteinA0A0C4DH25 (Uniprot-TrEMBL)
IGKV4-1(21-?) ProteinP06312 (Uniprot-TrEMBL)
IGKVA18(21-?) ProteinA2NJV5 (Uniprot-TrEMBL)
IGLC1 ProteinP0CG04 (Uniprot-TrEMBL)
IGLC2 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-II region ARH-77 ProteinP06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region MCE ProteinP01817 (Uniprot-TrEMBL)
Ig heavy chain V-II region NEWM ProteinP01825 (Uniprot-TrEMBL)
Ig heavy chain V-II region OU ProteinP01814 (Uniprot-TrEMBL)
Ig heavy chain V-II region WAH ProteinP01824 (Uniprot-TrEMBL)
Ig heavy chain V-III region BRO ProteinP01766 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUT ProteinP01767 (Uniprot-TrEMBL)
Ig heavy chain V-III region CAM ProteinP01768 (Uniprot-TrEMBL)
Ig heavy chain V-III region DOB ProteinP01782 (Uniprot-TrEMBL)
Ig heavy chain V-III region JON ProteinP01780 (Uniprot-TrEMBL)
Ig heavy chain V-III region KOL ProteinP01772 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO ProteinP01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA ProteinP01763 (Uniprot-TrEMBL)
Ig kappa chain V region EV15 ProteinP06315 (Uniprot-TrEMBL)
Ig kappa chain V-I region AG ProteinP01593 (Uniprot-TrEMBL)
Ig kappa chain V-I region AU ProteinP01594 (Uniprot-TrEMBL)
Ig kappa chain V-I region BAN ProteinP04430 (Uniprot-TrEMBL)
Ig kappa chain V-I region DEE ProteinP01597 (Uniprot-TrEMBL)
Ig kappa chain V-I region Daudi ProteinP04432 (Uniprot-TrEMBL)
Ig kappa chain V-I region Gal ProteinP01599 (Uniprot-TrEMBL)
Ig kappa chain V-I region HK101 ProteinP01601 (Uniprot-TrEMBL)
Ig kappa chain V-I region Wes ProteinP01611 (Uniprot-TrEMBL)
Ig kappa chain V-II region Cum ProteinP01614 (Uniprot-TrEMBL)
Ig kappa chain V-II region FR ProteinP01615 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 ProteinP06310 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 ProteinP01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM ProteinP01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG ProteinP04433 (Uniprot-TrEMBL)
Ig lambda chain V region 4A ProteinP04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA ProteinP01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEW ProteinP01701 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEWM ProteinP01703 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR ProteinP01699 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH ProteinP01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region MGC ProteinP01709 (Uniprot-TrEMBL)
Ig lambda chain V-II region NEI ProteinP01705 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG ProteinP01704 (Uniprot-TrEMBL)
Ig lambda chain V-III region LOI ProteinP80748 (Uniprot-TrEMBL)
Ig lambda chain V-III region SH ProteinP01714 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Bau ProteinP01715 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Hil ProteinP01717 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Kern ProteinP01718 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR ProteinP01721 (Uniprot-TrEMBL)
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 ligandsComplexR-HSA-198922 (Reactome)
LAIR1 ProteinQ6GTX8 (Uniprot-TrEMBL)
LAIR1:Collagen type XVIIComplexR-HSA-5686611 (Reactome)
LAIR1ProteinQ6GTX8 (Uniprot-TrEMBL)
LAIR2 ProteinQ6ISS4 (Uniprot-TrEMBL)
LAIR2:Collagen type I,IIIComplexR-HSA-5696354 (Reactome)
LAIR2ProteinQ6ISS4 (Uniprot-TrEMBL)
LAM MetaboliteCHEBI:59524 (ChEBI) CD1B-presented lipoglycan lipoarabinomannan (LAM) is synthesized by the genera Mycobacterium, Corynebacterium,and Rhodococcus.
LFA-1:ICAM 1-5ComplexR-HSA-198200 (Reactome)
LILR setComplexR-HSA-198894 (Reactome)
LILR-interacting MHC Class I moleculesComplexR-HSA-199592 (Reactome)
LILRA1 ProteinO75019 (Uniprot-TrEMBL)
LILRA2 ProteinQ8N149 (Uniprot-TrEMBL)
LILRA3 ProteinQ8N6C8 (Uniprot-TrEMBL)
LILRA4 ProteinP59901 (Uniprot-TrEMBL)
LILRA5 ProteinA6NI73 (Uniprot-TrEMBL)
LILRA6 ProteinQ6PI73 (Uniprot-TrEMBL)
LILRB1 ProteinQ8NHL6 (Uniprot-TrEMBL)
LILRB2 ProteinQ8N423 (Uniprot-TrEMBL)
LILRB3 ProteinO75022 (Uniprot-TrEMBL)
LILRB4 ProteinQ8NHJ6 (Uniprot-TrEMBL)
LILRB5 ProteinO75023 (Uniprot-TrEMBL)
Ligand interacting with NKG2DComplexR-HSA-198915 (Reactome)
Lymphoid-expressed Fc-gamma receptorsComplexR-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		ComplexR-HSA-199614 (Reactome)
MHC Class I R-HSA-198889 (Reactome)
MICA ProteinQ29983 (Uniprot-TrEMBL)
MICB ProteinQ29980 (Uniprot-TrEMBL)
NCR1 ProteinO76036 (Uniprot-TrEMBL)
NCR1:FCRG1A:CD3Z dimer:HemagglutininComplexR-HSA-5685594 (Reactome)
NCR1:FCRG1A:CD3Z dimerComplexR-HSA-5685701 (Reactome)
NCR3 ProteinO14931 (Uniprot-TrEMBL)
NCR3:FCRG1A:CD3Z dimerComplexR-HSA-5685593 (Reactome)
NCR3LG1 ProteinQ68D85 (Uniprot-TrEMBL)
NCR3LG1:NCR3:FCRG3A:CD3Z dimerComplexR-HSA-6793269 (Reactome)
NCR3LG1ProteinQ68D85 (Uniprot-TrEMBL)
NKG2D complexed with DAP10ComplexR-HSA-198920 (Reactome)
NKG2D ligandComplexR-HSA-198916 (Reactome)
NPDC1 ProteinQ9NQX5 (Uniprot-TrEMBL)
OSCAR ProteinQ8IYS5 (Uniprot-TrEMBL)
OSCAR:Collagen I,II,III/SP-DComplexR-HSA-5696351 (Reactome)
OSCARProteinQ8IYS5 (Uniprot-TrEMBL)
PE MetaboliteCHEBI:16038 (ChEBI)
PG MetaboliteCHEBI:17517 (ChEBI)
PI MetaboliteCHEBI:28874 (ChEBI)
PIANP ProteinQ8IYJ0 (Uniprot-TrEMBL)
PIANP,NPDC1,CLEC4G,COLEC12 trimerComplexR-HSA-8959654 (Reactome)
PILRA ProteinQ9UKJ1 (Uniprot-TrEMBL)
PILRA,PILRB:CD99ComplexR-HSA-8862083 (Reactome)
PILRA,PILRBComplexR-HSA-8862072 (Reactome)
PILRA:PIANP,NPDC1,CLEC4G,COLEC12 trimerComplexR-HSA-8862077 (Reactome)
PILRAProteinQ9UKJ1 (Uniprot-TrEMBL)
PILRB ProteinQ9UKJ0 (Uniprot-TrEMBL)
PS MetaboliteCHEBI:18303 (ChEBI)
PVR ProteinP15151 (Uniprot-TrEMBL)
PVRL2 ProteinQ92692 (Uniprot-TrEMBL)
PVRL2ProteinQ92692 (Uniprot-TrEMBL)
PVRProteinP15151 (Uniprot-TrEMBL)
RAET1E ProteinQ8TD07 (Uniprot-TrEMBL)
SAP,EAT2ComplexR-HSA-5685221 (Reactome)
SELL ProteinP14151 (Uniprot-TrEMBL)
SELLProteinP14151 (Uniprot-TrEMBL)
SFTPD oligomer R-HSA-391097 (Reactome)
SH2D1A ProteinO60880 (Uniprot-TrEMBL)
SH2D1B ProteinO14796 (Uniprot-TrEMBL)
SIGLEC1 ProteinQ9BZZ2 (Uniprot-TrEMBL)
SIGLEC10 ProteinQ96LC7 (Uniprot-TrEMBL)
SIGLEC11 ProteinQ96RL6 (Uniprot-TrEMBL)
SIGLEC12 ProteinQ96PQ1 (Uniprot-TrEMBL)
SIGLEC5 ProteinO15389 (Uniprot-TrEMBL)
SIGLEC6 ProteinO43699 (Uniprot-TrEMBL)
SIGLEC7 ProteinQ9Y286 (Uniprot-TrEMBL)
SIGLEC8 ProteinQ9NYZ4 (Uniprot-TrEMBL)
SIGLEC9 ProteinQ9Y336 (Uniprot-TrEMBL)
SIGLEC:sialic acidComplexR-HSA-5685595 (Reactome)
SIGLECComplexR-HSA-5685222 (Reactome)
SLAMF6 ProteinQ96DU3 (Uniprot-TrEMBL)
SLAMF6 dimerComplexR-HSA-5685229 (Reactome)
SLAMF6:SLAMF6:SAP,EAT2ComplexR-HSA-5685227 (Reactome)
SLAMF6ProteinQ96DU3 (Uniprot-TrEMBL)
SLAMF7 ProteinQ9NQ25 (Uniprot-TrEMBL)
SLAMF7 dimerComplexR-HSA-5685228 (Reactome)
SLAMF7ProteinQ9NQ25 (Uniprot-TrEMBL)
Sialic acid MetaboliteCHEBI:28879 (ChEBI)
Sialic acidMetaboliteCHEBI:28879 (ChEBI)
T-cell receptor complex with CD8ComplexR-HSA-198898 (Reactome)
T-cell receptor complexComplexR-HSA-198901 (Reactome)
T-cell receptor alpha chain V region PY14 precursor ProteinP01737 (Uniprot-TrEMBL)
TCR interacting with

antigen-bearing MHC

Class I		ComplexR-HSA-198897 (Reactome)
TCRA ProteinP04437 (Uniprot-TrEMBL)
TCRB ProteinP04435 (Uniprot-TrEMBL)
TRAC ProteinP01848 (Uniprot-TrEMBL)
TRAV19 ProteinA0A0A6YYK7 (Uniprot-TrEMBL)
TRBC1 ProteinP01850 (Uniprot-TrEMBL)
TRBV12-3 ProteinP01733 (Uniprot-TrEMBL)
TREM, CD300ComplexR-HSA-5696347 (Reactome)
TREMs R-HSA-5696345 (Reactome) Note: This family members include both membrane bound and soluble forms. TRML4 is soluble
TRIM, CD300:lipidsComplexR-HSA-5696352 (Reactome)
TYROBP ProteinO43914 (Uniprot-TrEMBL)
ULBP1 ProteinQ9BZM6 (Uniprot-TrEMBL)
ULBP3 ProteinQ9BZM4 (Uniprot-TrEMBL)
VCAM1 ProteinP19320 (Uniprot-TrEMBL)
VCAM1ProteinP19320 (Uniprot-TrEMBL)
alpha-mycolic acid MetaboliteCHEBI:59235 (ChEBI) CD1B-presented fatty acid produced by Mycobacterium tuberculosis
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)
squalene MetaboliteCHEBI:15440 (ChEBI)

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)
C3d complexed with antigenR-HSA-199518 (Reactome)
CD160R-HSA-199169 (Reactome)
CD1:B2M:microbial lipid:TCRArrowR-HSA-8850356 (Reactome)
CD1:B2M:microbial lipidR-HSA-8850356 (Reactome)
CD1:B2M:self-lipid:TCRArrowR-HSA-8850326 (Reactome)
CD1:B2M:self-lipidR-HSA-8850326 (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)
CD99R-HSA-8862084 (Reactome)
CDH1(155-882)R-HSA-199079 (Reactome)
CERA,PE,PSR-HSA-5696358 (Reactome)
CLEC2B dimerR-HSA-5685608 (Reactome)
CLEC2D dimer:KLRB1 dimerArrowR-HSA-5685606 (Reactome)
CLEC2D dimerR-HSA-5685606 (Reactome)
CMVPP65:NCR3:FCRG3A:CD3Z dimerArrowR-HSA-6793275 (Reactome)
CMVPP65R-HSA-6793275 (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)
Collagen types I,II,III/SP-DR-HSA-5696356 (Reactome)
Collagen types I,IIIR-HSA-5696357 (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 1-5R-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)
LAIR2:Collagen type I,IIIArrowR-HSA-5696357 (Reactome)
LAIR2R-HSA-5696357 (Reactome)
LFA-1:ICAM 1-5ArrowR-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)
NCR3:FCRG1A:CD3Z dimerR-HSA-6793275 (Reactome)
NCR3LG1:NCR3:FCRG3A:CD3Z dimerArrowR-HSA-5685602 (Reactome)
NCR3LG1R-HSA-5685602 (Reactome)
NKG2D complexed with DAP10R-HSA-198983 (Reactome)
NKG2D ligandR-HSA-198983 (Reactome)
OSCAR:Collagen I,II,III/SP-DArrowR-HSA-5696356 (Reactome)
OSCARR-HSA-5696356 (Reactome)
PIANP,NPDC1,CLEC4G,COLEC12 trimerR-HSA-8862090 (Reactome)
PILRA,PILRB:CD99ArrowR-HSA-8862084 (Reactome)
PILRA,PILRBR-HSA-8862084 (Reactome)
PILRA:PIANP,NPDC1,CLEC4G,COLEC12 trimerArrowR-HSA-8862090 (Reactome)
PILRAR-HSA-8862090 (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. Integrin alphaLbeta2 (LFA-1) interacts with Intercellular adhesion molecule (ICAM)1-5, which are typically expressed on other immune system cells. ICAM4 and 5 are 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. Integrin alphaLbeta2 (LFA-1) interacts with Intercellular adhesion molecule (ICAM)1-5, which are typically expressed on other immune system cells. ICAM4 and 5 are 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.
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).
R-HSA-5696356 (Reactome) Osteoclast-associated receptor (OSCAR) is specifically expressed by preosteoclasts and it signals through the ITAM-harboring adaptor protein Fc receptor gamma (FCRG) (Merck et al. 2004). Collagen types (Col)I, II, and III have been described as OSCAR ligands, and this interaction induce costimulatory signaling in receptor activator for NF-kB-dependent osteoclastogenesis (Barrow et al. 2011, Schultz et al. 2015).
Surfactant protein D (SP-D) is a member of the collagenous lectins (collectins), which provide a first line of humoral innate immune defense to pathogens at mucosal surfaces. SP-D is mainly produced by alveolar type II epithelial cells, but is also produced outside of the lung, in the gastrointestinal and genital mucosae, salivary glands, prostate, kidney, pancreas, skin, and endothelial cells (Madsen et al. 2000). Polymorphisms in the SP-D-encoding gene SFTPD have been associated with chronic obstructive pulmonary disease and ulcerative colitis. OSCAR binds with SP-D and is localized in an intracellular compartment of alveolar macrophages.This interaction may trigger TNF-alpha productiion by inflammatory monocytes (Barrow et al. 2015).
R-HSA-5696357 (Reactome) Leukocyte-associated immunoglobulin-like receptor 2 (LAIR2 or CD306) a soluble homolog of LAIR1 protein, also has high affinity for various collagen molecules and this can interfere with collagen-dependent platelet aggregation and adhesion. LAIR-2 may function as a natural competitor for LAIR-1, thereby regulating its inhibitory potential (Lebbink et al. 2008, Lenting et al. 2010).
R-HSA-5696358 (Reactome) The CD300 glycoproteins are a family of related leucocyte surface molecules that modulate a broad and diverse array of immune cell processes via their paired activating and inhibitory receptor functions (Clark et al. 2000, 2001, 2009a,b). Human CD300 family include 7 members and they have a single Ig-V like domain. Only CD300a and CD300f have long cytoplasmic tails with ITIMs (immunoreceptor tyrosine-based inhibitory motif), whereas the rest of the members have a short cytoplasmic tail and a short transmembrane residue and associate with adaptor proteins such as DDNAX associated protein (DAP)12, DAP10, and the Fc receptor gamma (FCRG) (Clark et al 2009a, Borrego 2013). CD300 receptors bind to polar lipids including extracellular ceramide, phosphatidylserine, and phosphatidylethanolamine, that are exposed on the outer leaflet of the plasma membrane of dead and activated cells. The CD300 gene complex has been linked to PSOR2, a susceptibility locus for psoriasis (Speckman et al. 2003, Tomfohrde et al. 1994).
R-HSA-6793275 (Reactome) Other potential NCR3 ligands include human cytomegalovirus (HCMV) tegument protein pp65 (CMVPP65). Interaction between NCR3 and pp65 resulted in NK cell inhibition (Arnon et al.2005).
R-HSA-8850326 (Reactome) T lymphocytes have developed the capacity to recognize as antigens a large variety of molecules including peptides, lipids, and vitamin metabolites (Moody DB et al. 2005; Rossjohn J et al. 2015; de Jong A 2015). Specific recognition of lipids by T-cell receptors (TCR) occurs when these molecules form antigenic complexes using functionally nonpolymorphic CD1 molecules (Beckman EM et al. 1994; De Libero G1 & Mori L 2005; Tatituri RV et al. 2013; Van Rhijn I et al. 2015).

Humans express five functional CD1 isotypes (CD1a-e), with CD1e being the only member that does not directly present antigens to T cells (Calabi F et al. 1989; Balk SP et al. 1989; de la Salle H et al. 2005). CD1a, CD1b, CD1c and CD1d are surface expressed proteins that can be found on the plasma membranes of antigen-presenting cells (APC) (Dougan SK et al. 2007). CD1 ectodomains consist of a heavy chain, which folds into three extracellular domains (alpha1, alpha2 and alpha3) noncovalently associated with beta2-microglobulin (B2M) (Moody DB et al. 2005). Antigen-binding grooves nestle between the alpha1 and alpha2 helices and are mostly lined by hydrophobic residues (Zeng Z et al. 1997). This allows the antigenic lipids to be anchored via their hydrophobic chains, so that polar motifs protrude toward the aqueous milieu (Gadola SD et al. 2002; Zajonc DM et al. 2003, 2005; Batuwangala T et al. 2004; Koch M et al. 2005; Zajonc DM et al. 2005; Scharf L et al. 2010; Garcia-Alles LF et al. 2011). Consequently, polar heads establish stimulatory contacts with TCRs, while variation in the number, length and saturation of alkyl chains may contribute to the binding to varying degrees (Borg NA et al. 2007; Garcia-Alles LF et al. 2011; Li Y et al. 2010; Pierce BG et al. 2014). Each of the four CD1 isoforms that directly present antigens to T cells differ in size of the antigen-binding grooves (Zajonc DM et al. 2005; Gadola SD et al. 2002; Zajonc DM et al. 2003, 2005; Batuwangala T et al. 2004; Koch M et al. 2005; Cheng TY et al. 2006; Borg NA et al. 2007; Scharf L et al. 2010; Garcia-Alles LF et al. 2011), intracellular trafficking patterns (Sugita M et al. 1999; Moody DB & Porcelli SA 2003), lipid ligand repertoire (Im JS et al. 2004; Huang S et al. 2011; Ly D & Moody DB 2014), and tissue distribution of expression (Dougan SK et al. 2007). Together with the observation that multiple CD1 isoforms have been maintained throughout mammalian evolution, this argues that each CD1 isoform plays a non-redundant role in the immune system (Dascher CC 2007; de Jong A 2015).

A large spectrum of self- and foreign lipids associates with members of CD1 family (Mattner J et al. 2005; Kinjo Y et al. 2005; Chang DH et al. 2008; Cohen NR et al. 2009; De Libero G et al. 2009; Zajonc DM & Girardi E 2015; Birkinshaw RW et al. 2015; de Jong A 2015). CD1-bound self-derived lipid antigens, including gangliosides, sulfatide, phosphoglycerolipids and sphingomyelin, can stimulate specialized subsets of T cells though the importance of self-lipid interactions with TCRs can vary (Birkinshaw RW et al. 2015; Borg NA et al. 2007; Luoma AM et al. 2013, 2014; Lepore M et al. 2014; Roy S et al. 2016). The ability of of both alphabeta and gammadelta T cells to recognize self lipid loaded CD1 molecules enables these lymphocytes to sense changes in the lipid composition of cells and tissues as a result of infections, inflammation, or malignancies (Brennan PJ et al. 2011; Chang DH et al. 2008; Cohen NR et al. 2009; Luoma et al. 2014; Lepore M et al. 2014; de Jong A 2014, 2015).

The Reactome event shows self lipid-based molecules that have been reported to function as antigens for CD1-restricted T cells (Shamshiev A et al. 2002; Birkinshaw RW et al. 2015; de Jong A 2015).

R-HSA-8850356 (Reactome) The hallmark of T cell activation is the direct binding of T-cell receptor (TCR) to an antigen that is presented by an antigen-presenting molecule. TCRs are able to recognize as antigens a large variety of molecules including peptides, lipids, and vitamin metabolites (Moody DB et al. 2005; Rossjohn J et al. 2015; de Jong A 2015). While TCR responds to peptides when they are presented by classical major histocompatibility complex (MHC)-encoded class I or II molecules, specific recognition of lipids by TCR occurs when lipid-based antigens form antigenic complexes with CD1 antigen-presenting molecules (Garboczi DN et al. 1996; Beckman EM et al. 1994; De Libero G1 & Mori L 2005; Tatituri RV et al. 2013; Van Rhijn I et al. 2015).

Humans express five functional CD1 isotypes (CD1a-e), with CD1e being the only member that does not directly present antigens to T cells (Calabi F et al. 1989; Balk SP et al. 1989; de la Salle H et al. 2005). CD1a, CD1b, CD1c and CD1d are surface expressed proteins that can be found on the plasma membranes of antigen-presenting cells (APC) (Dougan SK et al. 2007). CD1 ectodomains consist of a heavy chain, which folds into three extracellular domains (alpha1, alpha2 and alpha3) noncovalently associated with beta2-microglobulin (B2M) (Moody DB et al. 2005). Antigen-binding grooves nestle between the alpha1 and alpha2 helices and are mostly lined by hydrophobic residues (Zeng Z et al. 1997). This allows the antigenic lipids to be anchored via their hydrophobic chains, so that polar motifs protrude toward the aqueous milieu (Gadola SD et al. 2002; Zajonc DM et al. 2003, 2005; Batuwangala T et al. 2004; Koch M et al. 2005; Zajonc DM et al. 2005; Scharf L et al. 2010; Garcia-Alles LF et al. 2011). Consequently, polar heads establish stimulatory contacts with TCRs, while variation in the number, length and saturation of alkyl chains may contribute to the binding to varying degrees (Borg NA et al. 2007; Garcia-Alles LF et al. 2011; Li Y et al. 2010; Pei B et al 2012; Pierce BG et al. 2014). Each of the four CD1 isoforms that directly present antigens to T cells differ in size of the antigen-binding grooves (Zajonc DM et al. 2005; Gadola SD et al. 2002; Zajonc DM et al. 2003, 2005; Batuwangala T et al. 2004; Koch M et al. 2005; Cheng TY et al. 2006; Borg NA et al. 2007; Scharf L et al. 2010; Garcia-Alles LF et al. 2011), intracellular trafficking patterns (Sugita M et al. 1999; Moody DB & Porcelli SA 2003), lipid ligand repertoire (Im JS et al. 2004; Huang S et al. 2011; Ly D & Moody DB 2014), and tissue distribution of expression (Dougan SK et al. 2007). Together with the observation that multiple CD1 isoforms have been maintained throughout mammalian evolution, this argues that each CD1 isoform plays a non-redundant role in the immune system (Dascher CC 2007; de Jong A 2015).

T cells recognize both endogenous and exogenous (derived from intracellular microbial pathogens) lipid antigens bound to CD1 molecules (Mattner J et al. 2005; Kinjo Y et al. 2005; Chang DH et al. 2008; Cohen NR et al. 2009; De Libero G et al. 2009; Zajonc DM & Girardi E 2015; Birkinshaw RW et al. 2015; de Jong A 2015). Foreign lipid antigens are extremely diverse chemically and include naturally occurring lipopeptide, glycolipids and phospholipid structures that are distinct from mammalian lipids (Moran A 2009). The best studied lipid antigens of microbial origin are glycolipids derived from the cell envelope of Mycobacteria species (De Libero G et al. 2009). They include CD1b-restricted foreign lipid antigens such as lipoarabinomannan (LAM), lipomannan (LM), phosphatidylinositol mannosides (PIM), mycolic acid, glucose monomycolate (GMM), glycerol monomycolate and diacylated sulpholipids (Sieling PA et al. 1995; Moody DB et al. 2000; Layre E et al. 2009; Gilleron M et al. 2004; Kasmar AG et al. 2011). While most mammalian glycolipids have beta-linked carbohydrates attached to the lipid backbone, bacterial glycolipids typically have alpha-linkage. The structural difference in the linkage may contribute to the highly specific interaction of the TCR with the CD1:lipid antigen complex thus dictating the outcome of the immune response (Scott-Browne JP et al. 2007; Zajonc DM et al. 2005, 2007). In addition, lipopeptides, such as didehydroxymycobactin (DDM), an intermediate in the biosynthesis of the mycobacterial iron scavenger mycobactin siderophores, can be recognized by CD1a-restricted T cells (Moody DB et al. 2004; Zajonc DM et al. 2005). Diacylglycerols, such as the alpha-galactosyldiacylglycerol from the spirochete Borrelia burgdorferi or an alpha-linkage glycosphingolipid (alpha-glucuronosylceramide) found in alpha-proteobacteria can be presented by CD1d to stimulate invariant natural killer T (iNKT) cells (Sriram V et al. 2005; Kinjo Y et al. 2006). The ability of T cells to see lipid antigens bound to CD1 proteins enables these lymphocytes to sense changes in the lipid composition of cells and tissues as a result of infections or inflammation (Mattner J et al. 2005; Kinjo Y et al. 2005; Chang DH et al. 2008; Cohen NR et al. 2009; de Jong A 2015).

The Reactome event shows foreign lipid-based molecules that have been reported to function as antigens for CD1-restricted T cells (Batuwangala T et al. 2004; Roy S et al. 2014; Garcia-Alles LF et al. 2011; Wang J et al. 2010; Sieling PA et al. 1995; Guiard J et al. 2009; Kasmar AG et al. 2011).

R-HSA-8862084 (Reactome) The paired immunoglobulin-like type 2 receptors (PILR) comprise the inhibitory receptor PILRA and the activating receptor PILRB (Shiratori et al. 2004). The inhibitory PILRA is mainly expressed on macrophages, dendritic cells and granulocytes, whereas the activating PILRB is mainly on activated NK cells. Both recognize mouse CD99 as a ligand, but the binding affinity of PILRB is much lower (Tabata et al. 2008). Mouse NK cells expressing PILRB mediate cytotoxicity against CD99-positive target cells, suggesting that this receptor may be involved in NK cell recognition (Shiratori et al. 2004).
R-HSA-8862090 (Reactome) Paired immunoglobulin-like type 2 receptor alpha (PILRA) binds to multiple ligands including CD99 (Shiratori et al. 2004), PILR-associating neural protein (PIANP, PANP) (Kogure et al. 2011), Herpes simplex virus-1 glycoprotein B (Satoh et al. 2008), Collectin-12 (COLEC12), Neural proliferation differentiation and control protein 1 (NPDC1) and C-type lectin domain family 4 member G (CLEC4G) (Sun et al. 2012). Binding studies suggest that PILR recognizes a complex ligand domain involving both silica acid and protein motif(s). Thus, PILR is evolved to engage multiple ligands with common molecular determinants to modulate myeloid cell functions in anatomical settings where PILR ligands are expressed. The precise function of PILRa-Ligand interaction is not well understood (Sun et al. 2012).

PILRa negatively regulates inflammation and keeps myeloid system in check. Pilra KO mice produce more pathogenic cytokines during inflammation and are prone to enhanced autoimmune arthritis. Correspondingly, anti-PILRa mAb ameliorated inflammation in mouse arthritis models and suppressed the production of proinflammatory cytokines (Sun et al. 2014).


SAP,EAT2R-HSA-5685603 (Reactome)
SELLR-HSA-199046 (Reactome)
SIGLEC:sialic acidArrowR-HSA-5685607 (Reactome)
SIGLECR-HSA-5685607 (Reactome)
SLAMF6 dimerArrowR-HSA-5685604 (Reactome)
SLAMF6 dimerR-HSA-5685603 (Reactome)
SLAMF6:SLAMF6:SAP,EAT2ArrowR-HSA-5685603 (Reactome)
SLAMF6R-HSA-5685604 (Reactome)
SLAMF7 dimerArrowR-HSA-5685605 (Reactome)
SLAMF7R-HSA-5685605 (Reactome)
Sialic acidR-HSA-5685607 (Reactome)
T-cell receptor complex with CD8R-HSA-198955 (Reactome)
T-cell receptor complexR-HSA-8850326 (Reactome)
T-cell receptor complexR-HSA-8850356 (Reactome)
TCR interacting with

antigen-bearing MHC

Class I		ArrowR-HSA-198955 (Reactome)
TREM, CD300R-HSA-5696358 (Reactome)
TRIM, CD300:lipidsArrowR-HSA-5696358 (Reactome)
VCAM1R-HSA-198941 (Reactome)
integrin alpha4beta1:VCAM1ArrowR-HSA-198941 (Reactome)

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