Cell surface interactions at the vascular wall (Homo sapiens)

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26, 34, 44, 88, 99...34, 5646, 6514, 4713, 9011, 19, 28, 10755, 643, 23, 4815, 7412, 7127, 30, 66, 10634, 8951, 9020, 45, 908417775930102, 10534, 1002, 33, 34, 4180, 1013210, 29, 50, 79863169, 108869796356, 8121, 221, 6861, 9053, 5816, 40, 54, 654, 705134710334, 39, 67, 10975369, 49, 7252, 92, 11034, 915724, 34, 938362, 8725876, 78, 94, 95, 104189861, 9020, 451760cytosolGolgi lumencytosolcytosolcytosolSyndecans1-4 Integrin alphaVbeta3ANGPT2opaH SLC7A8 TNFRSF10DFCAMRMIF opaC IGLV8-61(1-?) JAM3 GLG1 Ca2+ PPIA Ig lambda chain V-I region HA opaA CD99 SLC16A1 PSG1 Ig heavy chain V-III region JON Collagen type I fibril BSGJAM2 Ig kappa chain V-I region AG Ig kappa chain V-II region Cum Ig lambda chain V-II region NEI FCER1G p-5Y,S1119-TEK Ig heavy chain V-II region WAH Ig kappa chain V-II region FR Ig kappa chain V-III region B6 CD244Ig heavy chain V-III region DOB IGLV1-40(1-?) DOK2Immunoglobulin Muwith SurrogateLight ChainIg lambda chain V region 4A Ig heavy chain V-II region WAH p-5Y,S1119-TEK Ig kappa chain V-I region AU IntegrinalphaXbeta2:JAM3CEACAM1 TGFB1 PROCR Ig heavy chain V-II region NEWM thrombin heavy chain IGLC6 Ig heavy chain V-III region CAM SLC7A9 IgH heavy chain V-III region VH26 precursor S-Farn-Me KRAS4B Ig lambda chain V-I region NEWM SLC3A2 Grb2 bound to Tie2IGLV3-16(1-?) eba-175,ebl1,eba-140Ig heavy chain V-III region BUT PSGs2xIgA:JCHAINTNFRSF10B IGKVA18(21-?) Phosphorylated Tie2in Tie2/Akt dimerp-5Y,S1119-TEK SELPLG IGLV1-40(1-?) SELPLG SELP IGLV(23-?) CD74 Ig heavy chain V-II region MCE TREM-1 bound to itsligandIGLV7-46(1-?) eba-175 SIRPG GDP IGLC3 MonocarboxylateTransporter Set(MCT)11xCbxE-PROS1 ITGAX PROCR:Activatedprotein CITGB2 IGHV7-81(1-?) PTPN11 TEKIg heavy chain V-II region NEWM SELE ligandsSLC7A5 p-Y663,Y686-PECAM1(27-?)LYN CEACAM1,3,5,6:opaproteinsANGPT4ANGPT4:TEKTie2 and Dok-2complexIg lambda chain V-II region NEI IGLV2-18(1-?) IGHV(1-?) IGLV3-25(1-?) SIRPA Ig heavy chain V-II region OU CD2 SLC7A10 SLC16A3 PSG2 Ig kappa chain V-III region POM GPC1 YES1 PSG5 Neutrophil CEACAMsaffecting integrinbinding tofibronectinGYPA,GYPB,GYPC:eba-175,ebl1,eba-140PECAM-1:PLC gamma1complexANGPT1 Src family tyrosinekinases (SFKs)ANGPT1 BSG CD74 trimerGYPA,GYPB,GYPCIg lambda chain V-II region MGC PPIL2 BSG Ca2+ Ig lambda chain V-IV region Kern ITGB1 opaE IGLV8-61(1-?) IGLV4-3(1-?) VPREB1 PIK3R1 p85 bound to Tie2CD177 IGHV(1-?) IGKV4-1(21-?) TSPAN7:PICK1Ig heavy chain V-III region WEA ATPPECAM1 ATP1B3 ITGB1 ATP1B2 IGLV2-33(1-?) ITGAM L1CAM SLC7A11 Ig heavy chain V-III region BRO opa68 opaK Ig lambda chain V-I region NEWM pTie2 and SHP2complexIntegrinalpha5beta1:FN1dimerIGHV1-2 opaD Selectins:2xSELPGOLR1 bound tooxidized LDLGYPC p-Y663,Y686-PECAM1(27-?) TEK Ig heavy chain V-III region BUT MERTK:MERKT ligandsIg kappa chain V-III region VG PSG6 ITGB3 PIK3CB PECAM1 dimerCEACAM6 TNFRSF10A,TNFRSF10BIGKV2D-30 CD47Ig kappa chain V-I region DEE PSG4 SELP IgM Heavy ChainCEACAM8 Ig heavy chain V-III region DOB Ig lambda chain V-I region VOR Ig heavy chain V-III region JON eba-140 SLC7A11 SelectinsPLCG1ATP1B1 ANGPT1:TEKopaG TAGs ANGPT1 FYN OLR1 Ig heavy chain V-III region DOB BSG BSG LCK Ig heavy chain V-III region TRO JAM2 dimerGDPIgH heavy chain V-III region VH26 precursor CXADR CHOL opaA ITGB2 Ig lambda chain V-I region NEW GRB14CEACAM5 TNFRSF10B opaI Ig heavy chain V-III region CAM Basigin:CD98hccomplexSIRPG GRB2-1 Ig heavy chain V-II region OU Ig heavy chain V-III region JON THBD eba-140 TEK PPIATie2 and Grb14complexSELE IGLV2-33(1-?) Ig kappa chain V-II region FR ITGA3(33-1051) p-Y663,Y686-PECAM1(27-?) Ig kappa chain V-II region Cum opa65 Ig heavy chain V-II region MCE ANGPT1:p-5Y,S119-TEK:SHC1IGLV7-43(1-?) IGLV5-37(1-?) IGKV1-12 Platelet Factor 4LDLopaG IGLV2-23(1-?) Ig heavy chain V-III region TRO Ig heavy chain V-II region ARH-77 IGLV4-69(1-?) SOS1IGLV2-11(1-?) IGLV1-36(1-?) GYPC S-Farn-Me-2xPalmS HRAS BSG:MMP1(100-469)PSG4 Ig lambda chain V-II region MGC PECAM-1:SHIP1complexIg heavy chain V-III region KOL VPREB1 Mannose-carryingcell recognitionmoleculesGYPB BSGIGLV4-3(1-?) BSG MERTK CD98hc complexPSG7 CD47-binding SIRPsPSG3 CEACAM heterodimeropaB ANGPT1 Ig heavy chain V-II region WAH piiC IGHA1 JAM2 Ig lambda chain V-VI region AR PSG8 Ig kappa chain V-I region Gal CEACAM8 PIK3R2 PI3KIGKV2-28 opaF IGLC1 CAV1 Ig heavy chain V-I region EU Ig heavy chain V-III region BRO FN1 dimeropaE GRB7Ig lambda chain V-II region BOH ESAM CD58:CD2CD44 Ig heavy chain V-III region WEA GRB2-1 CD84 Integrin alpha5beta1ANGPT4 IntegrinalphaLbeta2:F11RIGLV3-27(1-?) PROCR:Protein CopaC Ig kappa chain V-I region Wes op28 CD244 2xSELE ligands:SELEF11R IGLV11-55(1-?) IGLV4-69(1-?) Ig heavy chain V-III region KOL ITGB3 opaH IGLV3-22(1-?) TNFRSF10A,B:TNFRSF10DITGB2 IGLL1 IGLC2 p-5Y,S1119-TEK Ig heavy chain V-I region HG3 IGHV1-2 IGHA1 TEK Ig heavy chain V-III region TRO CEACAM3 ANGPT1 PIK3CB IGHA2 Ig heavy chain V-III region WEA 8xCbxE-3D-PROC(43-197) IgH heavy chain V-III region VH26 precursor Ig heavy chain V-II region WAH Basigin:Mannose-carrying cell recognition moleculesactivatedthrombin:thrombomodulinIg lambda chain V-III region LOI CD2ITGAL Ig kappa chain V-I region DEE opaD Ig heavy chain V-II region MCE PTPN11PSG5 opaF INPP5D Ig heavy chain V-I region EU CXADRIGLV1-44(1-?) MAG FYN FYN ANGPT1 SELPLGopa67 ANGPT1 ITGB1 BSG JCHAIN SLC3A2 p-5Y,S1119-TEK opa proteinsITGAM opa65 BSG:SPNIg kappa chain V-I region HK101 GRB2-1CEACAM6 IGHM PL IGKV3D-20 CEACAM6 JCHAIN AMICA1 IGLC1 GYPA CD99:CD99L2SELL CD47-bindingSIRPs:CD47L1CAM ANGPT1Ig heavy chain V-III region BRO p21 RAS:GDPCXADR bound to JAMLPSG9 GTP ITGB2 Ig heavy chain V-III region TRO Caveolin-1 bound toBasiginANGPT2:TEKIg kappa chain V-III region POM JAM3 PROC(212-461) SLC16A1 SLC7A7 PLCG1 GYPA PIK3CA IGLC2 IntegrinalphaMbeta2:JAM3SLC16A8 IGLV10-54(1-?) CD44 PSG9 IGKV1-5(23-?) Ig kappa chain V-I region Daudi PSGs:Proteoglycan,TGFB1JAM2Ig heavy chain V-III region KOL SLC7A6 Ligand to TREM-1 on the platelet membrane ANGPT1 CEACAM3 ATP1B2 Ig heavy chain V-III region KOL IGLV2-11(1-?) DOK2 11xCbxE-GAS6(39-691) CD74 IGLV3-12(1-?) AMICA1PECAM-1:SHP-2complexIGLV7-46(1-?) IGLV5-45(1-?) MERTKIGLV2-18(1-?) Ig heavy chain V-I region HG3 opaJ TEK CD58 SLC7A6 IGKC p-Y663,Y686-PECAM1(27-?) Ig heavy chain V-II region NEWM IGHV7-81(1-?) Ig heavy chain V-III region DOB thrombin light chain IGKC Ig kappa chain V-II region RPMI 6410 Ig heavy chain V-I region EU CD58CHEST ITGA4 PSG11 piiC IGKV2-28 IGLV4-60(1-?) PECAM-1:SHP-1complexF11RCHOL PSG2 CEACAM1 PICK1 Ig kappa chain V-I region BAN ITGAX IGHA2 IGLV(23-?) GPC1 GRB14 opaJ S-Farn-Me-PalmS KRAS4A TREM1Ig lambda chain V region 4A GLG1 Integrin alphaLbeta2ITGB2 BSG ebl1 S-Farn-Me KRAS4B IGLV5-37(1-?) p-Y663,Y686-PECAM1(27-?) GPVI:FceRIgamma:FYN:LYNBSG EPCAMIGLV3-25(1-?) MIF trimer:CD74trimerIgH heavy chain V-III region VH26 precursor Ig kappa chain V-III region VG SOS1 ESAM Ig heavy chain V-I region EU TNFRSF10D CAV1CD99L2VPREB3 ITGAV(31-1048) PF4V1(31-104) Ig kappa chain V-III region B6 GP6 integrinalpha4beta1:JAM2:JAM3Ig lambda chain V-II region TOG CyP60 complexed withBasiginProteoglycans,TGFB1PROC(200-211)APOB(28-4563) Ig kappa chain V-I region AG SPN FN1(32-2386) SHC1ebl1 PECAM1 PSG3 SELE Ig kappa chain V-II region RPMI 6410 IGKV1-12 FCER1G IGLV1-36(1-?) PECAM1 ITGA3(33-1051) Ig kappa chain V region EV15 JAM2 TSPAN7opa67 GRB7 MMP1(100-469)ITGA6(24-1130) PICK1ITGA5(42-894) Ig lambda chain V-II region BOH IGHV(1-?) SLC16A8 ITGB1 CD48:CD244CD48 MAG IGLV3-22(1-?) Ig lambda chain V-VI region AR CD84IGLL1 CEACAM1 opaI p-5Y,S1119-TEK GP6 MIF trimerS-Farn-Me-2xPalmS HRAS PTPN6 p-5Y,S1119-TEK SLC7A7 GYPB ITGA4:ITGB1PL SLC7A9 PPIL2Tie2:Grb7 complexIg heavy chain V-II region OU OLR1HSATPSELE SLC7A8 FCAMR CD99Integrin alphaXbeta2IGHV1-2 GTPSIRPA TGFB1 Ig heavy chain V-II region ARH-77 IGLC6 BSG:PPIAS-Farn-Me PalmS NRAS IGLV3-27(1-?) ANGPT1 CD99L2 CHEST 8xCbxE-3D-PROC(43-197) PIK3R1 Collagen type IfibrilLYN SOS-1 bound toTie2:Grb2IGHV(1-?) Ig kappa chain V-I region HK101 FCAMR:2xIgA:JCHAINIg heavy chain V-II region MCE IntegrinalphaVbeta3:PECAM1CEACAM1,3,5,6Ig heavy chain V-II region OU EPCAM dimerBSG PIK3CA SELEIg lambda chain V-II region TOG IGLV1-44(1-?) F11R dimerp-5Y,S1119-TEK p-5Y,S1119-TEK JAM3 ANGPT1:p-5Y,S119-TEKSELL IGLV7-43(1-?) ATP1B1 IGLC3 IGLC7 BSG dimerCEACAM1 IGKV3D-20 ITGB1 PROCR CD84 dimerANGPT1 Ig kappa chain V-I region BAN Ligand to TREM-1 onthe plateletmembraneIntegrinalpha3beta1,alpha6beta1PSG8 11xCbxE-GAS6(39-691) PTPN11 JAM2:JAM3Ig heavy chain V-I region HG3 FN1(32-2386) SLC7A10 Ig lambda chain V-IV region Kern Ig lambda chain V-III region SH JAM3 ANGPT2 Ig lambda chain V-I region NEW Syndecans1-4 PTPN6CEACAM5 Ig kappa chain V-I region Daudi Integrin alphaMbeta2IGKV1-5(23-?) IGLV4-60(1-?) PSG1 IGLV11-55(1-?) TREM1 IGHM TNFRSF10A Mn2+IGLC7 Ig kappa chain V-I region Gal Ig lambda chain V-IV region Hil Ig lambda chain V-III region LOI Ig heavy chain V-II region NEWM eba-175 IGLV10-54(1-?) IGHV7-81(1-?) Ig heavy chain V-I region HG3 CEACAM6 IGLV2-23(1-?) TNFRSF10A IGLV3-16(1-?) opa66 SHC1 Ig lambda chain V-IV region Bau Ig lambda chain V-III region SH ADPIg heavy chain V-II region ARH-77 IGKVA18(21-?) BSG SLC7A5 IGLV3-12(1-?) p-5Y,S1119-TEK p-Y663,Y686-PECAM1(27-?) Ig lambda chain V-IV region Bau Ig lambda chain V-IV region Hil Ig kappa chain V region EV15 PROC(200-461) ITGAV(31-1048) Ig heavy chain V-III region BUT ITGB1 opa68 Ig heavy chain V-III region BRO PIK3R2 opaB Ig kappa chain V-I region Wes INPP5DSLC16A3 VPREB3 opa66 Ig lambda chain V-I region HA p-Y663,Y686-PECAM1dimerIg lambda chain V-I region VOR ITGA4 SPNJAM3 dimerIg heavy chain V-III region BUT ITGA6(24-1130) ITGB2 IGHV7-81(1-?) SPN APOB(28-4563) Ig heavy chain V-III region WEA Pre-B Cell SurrogateLight ChainPSG11 ITGAL S-Farn-Me PalmS NRAS SRC-1 TSPAN7 SPN PF4(32-101) 2xANGPT1:TEKCD47 PSG7 ADPANGPT1 JAM3ITGA5(42-894) opaK Ig heavy chain V-III region CAM MIF Ig kappa chain V-I region AU ATP1B3 PECAM1p21 RAS:GTPS-Farn-Me-PalmS KRAS4A IGKV2D-30 IGLV5-45(1-?) PSG6 11xCbxE-PROS1 LYN ANGPT1 IGHV1-2 SELPLG op28 BSG:MCTsCD48Mn2+ MMP1(100-469) Ig heavy chain V-II region ARH-77 GPVI:FceRIgamma:FYN:LYN:Collagen type IF11R JAM3 Ig heavy chain V-III region JON IGKV4-1(21-?) EPCAM PECAM1:CD177TAGs BSG:Integrinalpha3beta1,alpha6beta1CD177Ig heavy chain V-III region CAM MERTK ligands2566436824337, 8563667325386337, 42, 8537, 42, 857337, 81, 8537, 81, 85


Description

Leukocyte extravasation is a rigorously controlled process that guides white cell movement from the vascular lumen to sites of tissue inflammation. The powerful adhesive interactions that are required for leukocytes to withstand local flow at the vessel wall is a multistep process mediated by different adhesion molecules. Platelets adhered to injured vessel walls form strong adhesive substrates for leukocytes. For instance, the initial tethering and rolling of leukocytes over the site of injury are mediated by reversible binding of selectins to their cognate cell-surface glycoconjugates.

Endothelial cells are tightly connected through various proteins, which regulate the organization of the junctional complex and bind to cytoskeletal proteins or cytoplasmic interaction partners that allow the transfer of intracellular signals. An important role for these junctional proteins in governing the transendothelial migration of leukocytes under normal or inflammatory conditions has been established.<p>

This pathway describes some of the key interactions that assist in the process of platelet and leukocyte interaction with the endothelium, in response to injury.

View original pathway at Reactome.</div>

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 202733
Reactome-version 
Reactome version: 73
Reactome Author 
Reactome Author: Ouwehand, WH

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Bibliography

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  55. Wilkins AL, Yang W, Yang JJ.; ''Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design.''; PubMed Europe PMC Scholia
  56. Langer HF, Daub K, Braun G, Schönberger T, May AE, Schaller M, Stein GM, Stellos K, Bueltmann A, Siegel-Axel D, Wendel HP, Aebert H, Roecken M, Seizer P, Santoso S, Wesselborg S, Brossart P, Gawaz M.; ''Platelets recruit human dendritic cells via Mac-1/JAM-C interaction and modulate dendritic cell function in vitro.''; PubMed Europe PMC Scholia
  57. Tsuji M, Ezumi Y, Arai M, Takayama H.; ''A novel association of Fc receptor gamma-chain with glycoprotein VI and their co-expression as a collagen receptor in human platelets.''; PubMed Europe PMC Scholia
  58. Newton JP, Hunter AP, Simmons DL, Buckley CD, Harvey DJ.; ''CD31 (PECAM-1) exists as a dimer and is heavily N-glycosylated.''; PubMed Europe PMC Scholia
  59. Xu D, Hemler ME.; ''Metabolic activation-related CD147-CD98 complex.''; PubMed Europe PMC Scholia
  60. Khunkaewla P, Schiller HB, Paster W, Leksa V, Cermák L, Andera L, Horejsí V, Stockinger H.; ''LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147.''; PubMed Europe PMC Scholia
  61. Han DC, Shen TL, Guan JL.; ''The Grb7 family proteins: structure, interactions with other signaling molecules and potential cellular functions.''; PubMed Europe PMC Scholia
  62. Piali L, Hammel P, Uherek C, Bachmann F, Gisler RH, Dunon D, Imhof BA.; ''CD31/PECAM-1 is a ligand for alpha v beta 3 integrin involved in adhesion of leukocytes to endothelium.''; PubMed Europe PMC Scholia
  63. Schröder AK, Uciechowski P, Fleischer D, Rink L.; ''Crosslinking of CD66B on peripheral blood neutrophils mediates the release of interleukin-8 from intracellular storage.''; PubMed Europe PMC Scholia
  64. Bayas MV, Kearney A, Avramovic A, van der Merwe PA, Leckband DE.; ''Impact of salt bridges on the equilibrium binding and adhesion of human CD2 and CD58.''; PubMed Europe PMC Scholia
  65. Ward NL, Dumont DJ.; ''The angiopoietins and Tie2/Tek: adding to the complexity of cardiovascular development.''; PubMed Europe PMC Scholia
  66. Brakebusch C, Fässler R.; ''beta 1 integrin function in vivo: adhesion, migration and more.''; PubMed Europe PMC Scholia
  67. Ostermann G, Fraemohs L, Baltus T, Schober A, Lietz M, Zernecke A, Liehn EA, Weber C.; ''Involvement of JAM-A in mononuclear cell recruitment on inflamed or atherosclerotic endothelium: inhibition by soluble JAM-A.''; PubMed Europe PMC Scholia
  68. Master Z, Jones N, Tran J, Jones J, Kerbel RS, Dumont DJ.; ''Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak.''; PubMed Europe PMC Scholia
  69. Barton WA, Tzvetkova D, Nikolov DB.; ''Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition.''; PubMed Europe PMC Scholia
  70. Martin M, Romero X, de la Fuente MA, Tovar V, Zapater N, Esplugues E, Esplugues E, Pizcueta P, Bosch J, Engel P.; ''CD84 functions as a homophilic adhesion molecule and enhances IFN-gamma secretion: adhesion is mediated by Ig-like domain 1.''; PubMed Europe PMC Scholia
  71. Neumann S, Hasenauer J, Pollak N, Scheurich P.; ''Dominant negative effects of tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) receptor 4 on TRAIL receptor 1 signaling by formation of heteromeric complexes.''; PubMed Europe PMC Scholia
  72. Deora AA, Philp N, Hu J, Bok D, Rodriguez-Boulan E.; ''Mechanisms regulating tissue-specific polarity of monocarboxylate transporters and their chaperone CD147 in kidney and retinal epithelia.''; PubMed Europe PMC Scholia
  73. DiScipio RG, Davie EW.; ''Characterization of protein S, a gamma-carboxyglutamic acid containing protein from bovine and human plasma.''; PubMed Europe PMC Scholia
  74. Sachs UJ, Andrei-Selmer CL, Maniar A, Weiss T, Paddock C, Orlova VV, Choi EY, Newman PJ, Preissner KT, Chavakis T, Santoso S.; ''The neutrophil-specific antigen CD177 is a counter-receptor for platelet endothelial cell adhesion molecule-1 (CD31).''; PubMed Europe PMC Scholia
  75. Boriack-Sjodin PA, Margarit SM, Bar-Sagi D, Kuriyan J.; ''The structural basis of the activation of Ras by Sos.''; PubMed Europe PMC Scholia
  76. Moriwaki H, Kume N, Sawamura T, Aoyama T, Hoshikawa H, Ochi H, Nishi E, Masaki T, Kita T.; ''Ligand specificity of LOX-1, a novel endothelial receptor for oxidized low density lipoprotein.''; PubMed Europe PMC Scholia
  77. Pushkarsky T, Yurchenko V, Vanpouille C, Brichacek B, Vaisman I, Hatakeyama S, Nakayama KI, Sherry B, Bukrinsky MI.; ''Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60.''; PubMed Europe PMC Scholia
  78. Xie Q, Matsunaga S, Niimi S, Ogawa S, Tokuyasu K, Sakakibara Y, Machida S.; ''Human lectin-like oxidized low-density lipoprotein receptor-1 functions as a dimer in living cells.''; PubMed Europe PMC Scholia
  79. Cartron JP, Rahuel C.; ''Human erythrocyte glycophorins: protein and gene structure analyses.''; PubMed Europe PMC Scholia
  80. Merzaban JS, Burdick MM, Gadhoum SZ, Dagia NM, Chu JT, Fuhlbrigge RC, Sackstein R.; ''Analysis of glycoprotein E-selectin ligands on human and mouse marrow cells enriched for hematopoietic stem/progenitor cells.''; PubMed Europe PMC Scholia
  81. Kisiel W.; ''Human plasma protein C: isolation, characterization, and mechanism of activation by alpha-thrombin.''; PubMed Europe PMC Scholia
  82. Wen DZ, Dittman WA, Ye RD, Deaven LL, Majerus PW, Sadler JE.; ''Human thrombomodulin: complete cDNA sequence and chromosome localization of the gene.''; PubMed Europe PMC Scholia
  83. Barclay AN, Brown MH.; ''The SIRP family of receptors and immune regulation.''; PubMed Europe PMC Scholia
  84. Audero E, Cascone I, Maniero F, Napione L, Arese M, Lanfrancone L, Bussolino F.; ''Adaptor ShcA protein binds tyrosine kinase Tie2 receptor and regulates migration and sprouting but not survival of endothelial cells.''; PubMed Europe PMC Scholia
  85. Foster D, Davie EW.; ''Characterization of a cDNA coding for human protein C.''; PubMed Europe PMC Scholia
  86. Peters KG, Kontos CD, Lin PC, Wong AL, Rao P, Huang L, Dewhirst MW, Sankar S.; ''Functional significance of Tie2 signaling in the adult vasculature.''; PubMed Europe PMC Scholia
  87. Buckley CD, Doyonnas R, Newton JP, Blystone SD, Brown EJ, Watt SM, Simmons DL.; ''Identification of alpha v beta 3 as a heterotypic ligand for CD31/PECAM-1.''; PubMed Europe PMC Scholia
  88. Becker BF, Heindl B, Kupatt C, Zahler S.; ''Endothelial function and hemostasis.''; PubMed Europe PMC Scholia
  89. Ludwig RJ, Zollner TM, Santoso S, Hardt K, Gille J, Baatz H, Johann PS, Pfeffer J, Radeke HH, Schön MP, Kaufmann R, Boehncke WH, Podda M.; ''Junctional adhesion molecules (JAM)-B and -C contribute to leukocyte extravasation to the skin and mediate cutaneous inflammation.''; PubMed Europe PMC Scholia
  90. Jones N, Master Z, Jones J, Bouchard D, Gunji Y, Sasaki H, Daly R, Alitalo K, Dumont DJ.; ''Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration.''; PubMed Europe PMC Scholia
  91. Mandicourt G, Iden S, Ebnet K, Aurrand-Lions M, Imhof BA.; ''JAM-C regulates tight junctions and integrin-mediated cell adhesion and migration.''; PubMed Europe PMC Scholia
  92. Moore KL, Eaton SF, Lyons DE, Lichenstein HS, Cummings RD, McEver RP.; ''The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine.''; PubMed Europe PMC Scholia
  93. Santoso S, Sachs UJ, Kroll H, Linder M, Ruf A, Preissner KT, Chavakis T.; ''The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1.''; PubMed Europe PMC Scholia
  94. Yoshida H, Kondratenko N, Green S, Steinberg D, Quehenberger O.; ''Identification of the lectin-like receptor for oxidized low-density lipoprotein in human macrophages and its potential role as a scavenger receptor.''; PubMed Europe PMC Scholia
  95. Sawamura T, Kume N, Aoyama T, Moriwaki H, Hoshikawa H, Aiba Y, Tanaka T, Miwa S, Katsura Y, Kita T, Masaki T.; ''An endothelial receptor for oxidized low-density lipoprotein.''; PubMed Europe PMC Scholia
  96. Jackson DE, Ward CM, Wang R, Newman PJ.; ''The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling.''; PubMed Europe PMC Scholia
  97. Cicmil M, Thomas JM, Sage T, Barry FA, Leduc M, Bon C, Gibbins JM.; ''Collagen, convulxin, and thrombin stimulate aggregation-independent tyrosine phosphorylation of CD31 in platelets. Evidence for the involvement of Src family kinases.''; PubMed Europe PMC Scholia
  98. Heller M, von der Ohe M, Kleene R, Mohajeri MH, Schachner M.; ''The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach.''; PubMed Europe PMC Scholia
  99. Schober A, Weber C.; ''Mechanisms of monocyte recruitment in vascular repair after injury.''; PubMed Europe PMC Scholia
  100. Cunningham SA, Rodriguez JM, Arrate MP, Tran TM, Brock TA.; ''JAM2 interacts with alpha4beta1. Facilitation by JAM3.''; PubMed Europe PMC Scholia
  101. Graves BJ, Crowther RL, Chandran C, Rumberger JM, Li S, Huang KS, Presky DH, Familletti PC, Wolitzky BA, Burns DK.; ''Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains.''; PubMed Europe PMC Scholia
  102. Bos MP, Grunert F, Belland RJ.; ''Differential recognition of members of the carcinoembryonic antigen family by Opa variants of Neisseria gonorrhoeae.''; PubMed Europe PMC Scholia
  103. 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
  104. Shi X, Niimi S, Ohtani T, Machida S.; ''Characterization of residues and sequences of the carbohydrate recognition domain required for cell surface localization and ligand binding of human lectin-like oxidized LDL receptor.''; PubMed Europe PMC Scholia
  105. Popp A, Dehio C, Grunert F, Meyer TF, Gray-Owen SD.; ''Molecular analysis of neisserial Opa protein interactions with the CEA family of receptors: identification of determinants contributing to the differential specificities of binding.''; PubMed Europe PMC Scholia
  106. Zhang Z, Morla AO, Vuori K, Bauer JS, Juliano RL, Ruoslahti E.; ''The alpha v beta 1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin.''; PubMed Europe PMC Scholia
  107. Balzar M, Winter MJ, de Boer CJ, Litvinov SV.; ''The biology of the 17-1A antigen (Ep-CAM).''; PubMed Europe PMC Scholia
  108. Bogdanovic E, Nguyen VP, Dumont DJ.; ''Activation of Tie2 by angiopoietin-1 and angiopoietin-2 results in their release and receptor internalization.''; PubMed Europe PMC Scholia
  109. Fraemohs L, Koenen RR, Ostermann G, Heinemann B, Weber C.; ''The functional interaction of the beta 2 integrin lymphocyte function-associated antigen-1 with junctional adhesion molecule-A is mediated by the I domain.''; PubMed Europe PMC Scholia
  110. da Costa Martins P, van den Berk N, Ulfman LH, Koenderman L, Hordijk PL, Zwaginga JJ.; ''Platelet-monocyte complexes support monocyte adhesion to endothelium by enhancing secondary tethering and cluster formation.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
112591view15:56, 9 October 2020ReactomeTeamReactome version 73
101507view11:37, 1 November 2018ReactomeTeamreactome version 66
101043view21:18, 31 October 2018ReactomeTeamreactome version 65
100574view19:51, 31 October 2018ReactomeTeamreactome version 64
100123view16:37, 31 October 2018ReactomeTeamreactome version 63
99673view15:07, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99268view12:45, 31 October 2018ReactomeTeamreactome version 62
94057view13:54, 16 August 2017ReactomeTeamreactome version 61
93737view13:25, 16 August 2017ReactomeTeamreactome version 61
93686view11:31, 9 August 2017ReactomeTeamreactome version 61
87157view19:14, 18 July 2016MkutmonOntology Term : 'hemostasis pathway' added !
86809view09:27, 11 July 2016ReactomeTeamreactome version 56
83824view13:10, 13 December 2015EgonwMarked heparan sulfate (HS) as a metabolite.
83200view10:21, 18 November 2015ReactomeTeamVersion54
81579view13:07, 21 August 2015ReactomeTeamVersion53
77039view08:33, 17 July 2014ReactomeTeamFixed remaining interactions
76744view12:10, 16 July 2014ReactomeTeamFixed remaining interactions
76069view10:13, 11 June 2014ReactomeTeamRe-fixing comment source
75779view11:29, 10 June 2014ReactomeTeamReactome 48 Update
75129view14:07, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74859view15:22, 2 May 2014EgonwMarked a metabolite as a DataNode type="Metabolite"...
74776view08:51, 30 April 2014ReactomeTeamReactome46
42017view21:50, 4 March 2011MaintBotAutomatic update
39820view05:51, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
11xCbxE-GAS6(39-691) ProteinQ14393 (Uniprot-TrEMBL)
11xCbxE-PROS1 ProteinP07225 (Uniprot-TrEMBL)
2xANGPT1:TEKComplexR-HSA-210862 (Reactome)
2xIgA:JCHAINComplexR-HSA-8858031 (Reactome)
2xSELE ligands:SELEComplexR-HSA-2870225 (Reactome)
8xCbxE-3D-PROC(43-197) ProteinP04070 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:456216 (ChEBI)
AMICA1 ProteinQ86YT9 (Uniprot-TrEMBL)
AMICA1ProteinQ86YT9 (Uniprot-TrEMBL)
ANGPT1 ProteinQ15389 (Uniprot-TrEMBL)
ANGPT1:TEKComplexR-HSA-204807 (Reactome)
ANGPT1:p-5Y,S119-TEK:SHC1ComplexR-HSA-204857 (Reactome)
ANGPT1:p-5Y,S119-TEKComplexR-HSA-204783 (Reactome)
ANGPT1ProteinQ15389 (Uniprot-TrEMBL)
ANGPT2 ProteinO15123 (Uniprot-TrEMBL)
ANGPT2:TEKComplexR-HSA-204810 (Reactome)
ANGPT2ProteinO15123 (Uniprot-TrEMBL)
ANGPT4 ProteinQ9Y264 (Uniprot-TrEMBL)
ANGPT4:TEKComplexR-HSA-204789 (Reactome)
ANGPT4ProteinQ9Y264 (Uniprot-TrEMBL)
APOB(28-4563) ProteinP04114 (Uniprot-TrEMBL)
ATP1B1 ProteinP05026 (Uniprot-TrEMBL)
ATP1B2 ProteinP14415 (Uniprot-TrEMBL)
ATP1B3 ProteinP54709 (Uniprot-TrEMBL)
ATPMetaboliteCHEBI:30616 (ChEBI)
BSG ProteinP35613 (Uniprot-TrEMBL)
BSG dimerComplexR-HSA-204594 (Reactome)
BSG:Integrin

alpha3beta1,

alpha6beta1		ComplexR-HSA-204472 (Reactome)
BSG:MCTsComplexR-HSA-204396 (Reactome)
BSG:MMP1(100-469)ComplexR-HSA-375089 (Reactome)
BSG:PPIAComplexR-HSA-204480 (Reactome)
BSG:SPNComplexR-HSA-204467 (Reactome)
BSGProteinP35613 (Uniprot-TrEMBL)
Basigin:CD98hc complexComplexR-HSA-375086 (Reactome)
Basigin:Mannose-carrying cell recognition moleculesComplexR-HSA-375090 (Reactome)
CAV1 ProteinQ03135 (Uniprot-TrEMBL)
CAV1ProteinQ03135 (Uniprot-TrEMBL)
CD177 ProteinQ8N6Q3 (Uniprot-TrEMBL)
CD177ProteinQ8N6Q3 (Uniprot-TrEMBL)
CD2 ProteinP06729 (Uniprot-TrEMBL)
CD244 ProteinQ9BZW8 (Uniprot-TrEMBL)
CD244ProteinQ9BZW8 (Uniprot-TrEMBL)
CD2ProteinP06729 (Uniprot-TrEMBL)
CD44 ProteinP16070 (Uniprot-TrEMBL)
CD47 ProteinQ08722 (Uniprot-TrEMBL)
CD47-binding SIRPs:CD47ComplexR-HSA-202787 (Reactome)
CD47-binding SIRPsComplexR-HSA-202788 (Reactome)
CD47ProteinQ08722 (Uniprot-TrEMBL)
CD48 ProteinP09326 (Uniprot-TrEMBL)
CD48:CD244ComplexR-HSA-202790 (Reactome)
CD48ProteinP09326 (Uniprot-TrEMBL)
CD58 ProteinP19256 (Uniprot-TrEMBL)
CD58:CD2ComplexR-HSA-202794 (Reactome)
CD58ProteinP19256 (Uniprot-TrEMBL)
CD74 ProteinP04233 (Uniprot-TrEMBL)
CD74 trimerComplexR-HSA-2130505 (Reactome)
CD84 ProteinQ9UIB8 (Uniprot-TrEMBL)
CD84 dimerComplexR-HSA-202774 (Reactome)
CD84ProteinQ9UIB8 (Uniprot-TrEMBL)
CD98hc complexComplexR-HSA-375088 (Reactome)
CD99 ProteinP14209 (Uniprot-TrEMBL)
CD99:CD99L2ComplexR-HSA-8867105 (Reactome)
CD99L2 ProteinQ8TCZ2 (Uniprot-TrEMBL)
CD99L2ProteinQ8TCZ2 (Uniprot-TrEMBL)
CD99ProteinP14209 (Uniprot-TrEMBL)
CEACAM heterodimerComplexR-HSA-202716 (Reactome)
CEACAM1 ProteinP13688 (Uniprot-TrEMBL)
CEACAM1,3,5,6:opa proteinsComplexR-HSA-8867145 (Reactome)
CEACAM1,3,5,6ComplexR-HSA-8867228 (Reactome)
CEACAM3 ProteinP40198 (Uniprot-TrEMBL)
CEACAM5 ProteinP06731 (Uniprot-TrEMBL)
CEACAM6 ProteinP40199 (Uniprot-TrEMBL)
CEACAM8 ProteinP31997 (Uniprot-TrEMBL)
CHEST MetaboliteCHEBI:17002 (ChEBI)
CHOL MetaboliteCHEBI:16113 (ChEBI)
CXADR ProteinP78310 (Uniprot-TrEMBL)
CXADR bound to JAMLComplexR-HSA-198198 (Reactome)
CXADRProteinP78310 (Uniprot-TrEMBL)
Ca2+ MetaboliteCHEBI:29108 (ChEBI)
Caveolin-1 bound to BasiginComplexR-HSA-204550 (Reactome)
Collagen type I fibrilR-HSA-1474201 (Reactome)
Collagen type I fibril R-HSA-1474201 (Reactome)
CyP60 complexed with BasiginComplexR-HSA-204498 (Reactome)
DOK2 ProteinO60496 (Uniprot-TrEMBL)
DOK2ProteinO60496 (Uniprot-TrEMBL)
EPCAM ProteinP16422 (Uniprot-TrEMBL)
EPCAM dimerComplexR-HSA-8867172 (Reactome)
EPCAMProteinP16422 (Uniprot-TrEMBL)
ESAM ProteinQ96AP7 (Uniprot-TrEMBL)
F11R ProteinQ9Y624 (Uniprot-TrEMBL)
F11R dimerComplexR-HSA-202763 (Reactome)
F11RProteinQ9Y624 (Uniprot-TrEMBL)
FCAMR ProteinQ8WWV6 (Uniprot-TrEMBL)
FCAMR:2xIgA:JCHAINComplexR-HSA-8858512 (Reactome)
FCAMRProteinQ8WWV6 (Uniprot-TrEMBL)
FCER1G ProteinP30273 (Uniprot-TrEMBL)
FN1 dimerComplexR-HSA-266103 (Reactome)
FN1(32-2386) ProteinP02751 (Uniprot-TrEMBL)
FYN ProteinP06241 (Uniprot-TrEMBL)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GLG1 ProteinQ92896 (Uniprot-TrEMBL)
GP6 ProteinQ9HCN6 (Uniprot-TrEMBL)
GPC1 ProteinP35052 (Uniprot-TrEMBL)
GPVI:FceRI gamma:FYN:LYN:Collagen type IComplexR-HSA-434812 (Reactome)
GPVI:FceRI gamma:FYN:LYNComplexR-HSA-432297 (Reactome)
GRB14 ProteinQ14449 (Uniprot-TrEMBL)
GRB14ProteinQ14449 (Uniprot-TrEMBL)
GRB2-1 ProteinP62993-1 (Uniprot-TrEMBL)
GRB2-1ProteinP62993-1 (Uniprot-TrEMBL)
GRB7 ProteinQ14451 (Uniprot-TrEMBL)
GRB7ProteinQ14451 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
GYPA ProteinP02724 (Uniprot-TrEMBL)
GYPA,GYPB,GYPC:eba-175,ebl1,eba-140ComplexR-HSA-8867180 (Reactome)
GYPA,GYPB,GYPCComplexR-HSA-8867165 (Reactome)
GYPB ProteinP06028 (Uniprot-TrEMBL)
GYPC ProteinP04921 (Uniprot-TrEMBL)
Grb2 bound to Tie2ComplexR-HSA-204865 (Reactome)
HSMetaboliteCHEBI:28815 (ChEBI)
IGHA1 ProteinP01876 (Uniprot-TrEMBL)
IGHA2 ProteinP01877 (Uniprot-TrEMBL)
IGHM ProteinP01871 (Uniprot-TrEMBL)
IGHV(1-?) ProteinA2KUC3 (Uniprot-TrEMBL)
IGHV1-2 ProteinP23083 (Uniprot-TrEMBL)
IGHV7-81(1-?) ProteinQ6PIL0 (Uniprot-TrEMBL)
IGKC ProteinP01834 (Uniprot-TrEMBL)
IGKV1-12 ProteinA0A0C4DH73 (Uniprot-TrEMBL)
IGKV1-5(23-?) ProteinP01602 (Uniprot-TrEMBL)
IGKV2-28 ProteinA0A075B6P5 (Uniprot-TrEMBL)
IGKV2D-30 ProteinA0A075B6S6 (Uniprot-TrEMBL)
IGKV3D-20 ProteinA0A0C4DH25 (Uniprot-TrEMBL)
IGKV4-1(21-?) ProteinP06312 (Uniprot-TrEMBL)
IGKVA18(21-?) ProteinA2NJV5 (Uniprot-TrEMBL)
IGLC1 ProteinP0CG04 (Uniprot-TrEMBL)
IGLC2 ProteinP0DOY2 (Uniprot-TrEMBL)
IGLC3 ProteinP0DOY3 (Uniprot-TrEMBL)
IGLC6 ProteinP0CF74 (Uniprot-TrEMBL)
IGLC7 ProteinA0M8Q6 (Uniprot-TrEMBL)
IGLL1 ProteinP15814 (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)
INPP5D ProteinQ92835 (Uniprot-TrEMBL)
INPP5DProteinQ92835 (Uniprot-TrEMBL)
ITGA3(33-1051) ProteinP26006 (Uniprot-TrEMBL)
ITGA4 ProteinP13612 (Uniprot-TrEMBL)
ITGA4:ITGB1ComplexR-HSA-198201 (Reactome)
ITGA5(42-894) ProteinP08648 (Uniprot-TrEMBL)
ITGA6(24-1130) ProteinP23229 (Uniprot-TrEMBL)
ITGAL ProteinP20701 (Uniprot-TrEMBL)
ITGAM ProteinP11215 (Uniprot-TrEMBL)
ITGAV(31-1048) ProteinP06756 (Uniprot-TrEMBL)
ITGAX ProteinP20702 (Uniprot-TrEMBL)
ITGB1 ProteinP05556 (Uniprot-TrEMBL)
ITGB2 ProteinP05107 (Uniprot-TrEMBL)
ITGB3 ProteinP05106 (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)
IgM Heavy ChainComplexR-HSA-983669 (Reactome)
Immunoglobulin Mu

with Surrogate

Light Chain		ComplexR-HSA-983671 (Reactome)
Integrin

alpha3beta1,

alpha6beta1		ComplexR-HSA-204466 (Reactome)
Integrin

alpha5beta1:FN1

dimer		ComplexR-HSA-202708 (Reactome)
Integrin alphaLbeta2:F11RComplexR-HSA-202749 (Reactome)
Integrin alphaMbeta2:JAM3ComplexR-HSA-202754 (Reactome)
Integrin alphaVbeta3:PECAM1ComplexR-HSA-210229 (Reactome)
Integrin alphaXbeta2:JAM3ComplexR-HSA-202765 (Reactome)
Integrin alpha5beta1ComplexR-HSA-202730 (Reactome)
Integrin alphaLbeta2ComplexR-HSA-198196 (Reactome)
Integrin alphaMbeta2ComplexR-HSA-202755 (Reactome)
Integrin alphaVbeta3ComplexR-HSA-210216 (Reactome)
Integrin alphaXbeta2ComplexR-HSA-202766 (Reactome)
JAM2 ProteinP57087 (Uniprot-TrEMBL)
JAM2 dimerComplexR-HSA-202780 (Reactome)
JAM2:JAM3ComplexR-HSA-202761 (Reactome)
JAM2ProteinP57087 (Uniprot-TrEMBL)
JAM3 ProteinQ9BX67 (Uniprot-TrEMBL)
JAM3 dimerComplexR-HSA-202782 (Reactome)
JAM3ProteinQ9BX67 (Uniprot-TrEMBL)
JCHAIN ProteinP01591 (Uniprot-TrEMBL)
L1CAM ProteinP32004 (Uniprot-TrEMBL)
LCK ProteinP06239 (Uniprot-TrEMBL)
LDLComplexR-HSA-171131 (Reactome) LDL (low density lipoproteins) are complexes of a single molecule of apoprotein B-100 (apoB-100) non-covalently associated with triacylglycerol, free cholesterol, cholesterol esters, and phospholipids. LDL complexes contain single molecules of apoB-100, but their content of lipids is variable (Chapman et al. 1988; Mateu et al. 1972; Tardieu et al. 1976). High levels of LDL in the blood are strongly correlated with increased risk of atherosclerosis, and recent studies have raised the possibility that this risk is further increased in individuals whose blood LDL population is enriched in high-density (low lipid content) LDL complexes (Rizzo and Berneis 2006). The LDL complex annotated here contains an average lipid composition.
LYN ProteinP07948 (Uniprot-TrEMBL)
Ligand to TREM-1 on

the platelet

membrane		R-ALL-203159 (Reactome)
Ligand to TREM-1 on the platelet membrane R-ALL-203159 (Reactome)
MAG ProteinP20916 (Uniprot-TrEMBL)
MERTK ProteinQ12866 (Uniprot-TrEMBL)
MERTK ligandsComplexR-HSA-202771 (Reactome)
MERTK:MERKT ligandsComplexR-HSA-202770 (Reactome)
MERTKProteinQ12866 (Uniprot-TrEMBL)
MIF ProteinP14174 (Uniprot-TrEMBL)
MIF trimer:CD74 trimerComplexR-HSA-5676093 (Reactome)
MIF trimerComplexR-HSA-5676088 (Reactome)
MMP1(100-469) ProteinP03956 (Uniprot-TrEMBL)
MMP1(100-469)ProteinP03956 (Uniprot-TrEMBL)
Mannose-carrying

cell recognition

molecules		ComplexR-HSA-375083 (Reactome)
Mn2+ MetaboliteCHEBI:29035 (ChEBI)
Mn2+MetaboliteCHEBI:29035 (ChEBI)
Monocarboxylate

Transporter Set

(MCT)		ComplexR-HSA-374008 (Reactome)
Neutrophil CEACAMs

affecting integrin binding to

fibronectin		ComplexR-HSA-202719 (Reactome)
OLR1 ProteinP78380 (Uniprot-TrEMBL)
OLR1 bound to oxidized LDLComplexR-HSA-203127 (Reactome)
OLR1ProteinP78380 (Uniprot-TrEMBL)
PECAM-1:PLC gamma1 complexComplexR-HSA-210240 (Reactome)
PECAM-1:SHIP1 complexComplexR-HSA-210218 (Reactome)
PECAM-1:SHP-1 complexComplexR-HSA-210221 (Reactome)
PECAM-1:SHP-2 complexComplexR-HSA-210219 (Reactome)
PECAM1 ProteinP16284 (Uniprot-TrEMBL)
PECAM1 dimerComplexR-HSA-210238 (Reactome)
PECAM1:CD177ComplexR-HSA-202785 (Reactome)
PECAM1ProteinP16284 (Uniprot-TrEMBL)
PF4(32-101) ProteinP02776 (Uniprot-TrEMBL)
PF4V1(31-104) ProteinP10720 (Uniprot-TrEMBL)
PI3KComplexR-HSA-74693 (Reactome)
PICK1 ProteinQ9NRD5 (Uniprot-TrEMBL)
PICK1ProteinQ9NRD5 (Uniprot-TrEMBL)
PIK3CA ProteinP42336 (Uniprot-TrEMBL)
PIK3CB ProteinP42338 (Uniprot-TrEMBL)
PIK3R1 ProteinP27986 (Uniprot-TrEMBL)
PIK3R2 ProteinO00459 (Uniprot-TrEMBL)
PL MetaboliteCHEBI:16247 (ChEBI)
PLCG1 ProteinP19174 (Uniprot-TrEMBL)
PLCG1ProteinP19174 (Uniprot-TrEMBL)
PPIA ProteinP62937 (Uniprot-TrEMBL)
PPIAProteinP62937 (Uniprot-TrEMBL)
PPIL2 ProteinQ13356 (Uniprot-TrEMBL)
PPIL2ProteinQ13356 (Uniprot-TrEMBL)
PROC(200-211)ProteinP04070 (Uniprot-TrEMBL)
PROC(200-461) ProteinP04070 (Uniprot-TrEMBL)
PROC(212-461) ProteinP04070 (Uniprot-TrEMBL)
PROCR ProteinQ9UNN8 (Uniprot-TrEMBL)
PROCR:Activated protein CComplexR-HSA-5603469 (Reactome)
PROCR:Protein CComplexR-HSA-5603321 (Reactome)
PSG1 ProteinP11464 (Uniprot-TrEMBL)
PSG11 ProteinQ9UQ72 (Uniprot-TrEMBL)
PSG2 ProteinP11465 (Uniprot-TrEMBL)
PSG3 ProteinQ16557 (Uniprot-TrEMBL)
PSG4 ProteinQ00888 (Uniprot-TrEMBL)
PSG5 ProteinQ15238 (Uniprot-TrEMBL)
PSG6 ProteinQ00889 (Uniprot-TrEMBL)
PSG7 ProteinQ13046 (Uniprot-TrEMBL)
PSG8 ProteinQ9UQ74 (Uniprot-TrEMBL)
PSG9 ProteinQ00887 (Uniprot-TrEMBL)
PSGs:Proteoglycan,TGFB1ComplexR-HSA-8870733 (Reactome)
PSGsComplexR-HSA-8870760 (Reactome)
PTPN11 ProteinQ06124 (Uniprot-TrEMBL)
PTPN11ProteinQ06124 (Uniprot-TrEMBL)
PTPN6 ProteinP29350 (Uniprot-TrEMBL)
PTPN6ProteinP29350 (Uniprot-TrEMBL)
Phosphorylated Tie2 in Tie2/Akt dimerComplexR-HSA-210859 (Reactome)
Platelet Factor 4ComplexR-HSA-203105 (Reactome)
Pre-B Cell Surrogate Light ChainComplexR-HSA-983678 (Reactome)
Proteoglycans,TGFB1ComplexR-HSA-8870734 (Reactome)
S-Farn-Me KRAS4B ProteinP01116-2 (Uniprot-TrEMBL)
S-Farn-Me PalmS NRAS ProteinP01111 (Uniprot-TrEMBL)
S-Farn-Me-2xPalmS HRAS ProteinP01112 (Uniprot-TrEMBL)
S-Farn-Me-PalmS KRAS4A ProteinP01116-1 (Uniprot-TrEMBL)
SELE ProteinP16581 (Uniprot-TrEMBL)
SELE ligandsComplexR-HSA-3274516 (Reactome)
SELEProteinP16581 (Uniprot-TrEMBL)
SELL ProteinP14151 (Uniprot-TrEMBL)
SELP ProteinP16109 (Uniprot-TrEMBL)
SELPLG ProteinQ14242 (Uniprot-TrEMBL)
SELPLGProteinQ14242 (Uniprot-TrEMBL)
SHC1 ProteinP29353 (Uniprot-TrEMBL)
SHC1ProteinP29353 (Uniprot-TrEMBL)
SIRPA ProteinP78324 (Uniprot-TrEMBL)
SIRPG ProteinQ9P1W8 (Uniprot-TrEMBL)
SLC16A1 ProteinP53985 (Uniprot-TrEMBL)
SLC16A3 ProteinO15427 (Uniprot-TrEMBL)
SLC16A8 ProteinO95907 (Uniprot-TrEMBL)
SLC3A2 ProteinP08195 (Uniprot-TrEMBL)
SLC7A10 ProteinQ9NS82 (Uniprot-TrEMBL)
SLC7A11 ProteinQ9UPY5 (Uniprot-TrEMBL)
SLC7A5 ProteinQ01650 (Uniprot-TrEMBL)
SLC7A6 ProteinQ92536 (Uniprot-TrEMBL)
SLC7A7 ProteinQ9UM01 (Uniprot-TrEMBL)
SLC7A8 ProteinQ9UHI5 (Uniprot-TrEMBL)
SLC7A9 ProteinP82251 (Uniprot-TrEMBL)
SOS-1 bound to Tie2:Grb2ComplexR-HSA-210970 (Reactome)
SOS1 ProteinQ07889 (Uniprot-TrEMBL)
SOS1ProteinQ07889 (Uniprot-TrEMBL)
SPN ProteinP16150 (Uniprot-TrEMBL)
SPNProteinP16150 (Uniprot-TrEMBL)
SRC-1 ProteinP12931-1 (Uniprot-TrEMBL)
Selectins:2xSELPGComplexR-HSA-202776 (Reactome)
SelectinsComplexR-HSA-203453 (Reactome)
Src family tyrosine kinases (SFKs)ComplexR-HSA-211064 (Reactome)
Syndecans1-4 R-HSA-8870754 (Reactome)
TAGs MetaboliteCHEBI:17855 (ChEBI)
TEK ProteinQ02763 (Uniprot-TrEMBL)
TEKProteinQ02763 (Uniprot-TrEMBL)
TGFB1 ProteinP01137 (Uniprot-TrEMBL)
THBD ProteinP07204 (Uniprot-TrEMBL)
TNFRSF10A ProteinO00220 (Uniprot-TrEMBL)
TNFRSF10A,B:TNFRSF10DComplexR-HSA-5635735 (Reactome)
TNFRSF10A,TNFRSF10BComplexR-HSA-5634815 (Reactome)
TNFRSF10B ProteinO14763 (Uniprot-TrEMBL)
TNFRSF10D ProteinQ9UBN6 (Uniprot-TrEMBL)
TNFRSF10DProteinQ9UBN6 (Uniprot-TrEMBL)
TREM-1 bound to its ligandComplexR-HSA-203154 (Reactome)
TREM1 ProteinQ9NP99 (Uniprot-TrEMBL)
TREM1ProteinQ9NP99 (Uniprot-TrEMBL)
TSPAN7 ProteinP41732 (Uniprot-TrEMBL)
TSPAN7:PICK1ComplexR-HSA-8858433 (Reactome)
TSPAN7ProteinP41732 (Uniprot-TrEMBL)
Tie2 and Dok-2 complexComplexR-HSA-204788 (Reactome)
Tie2 and Grb14 complexComplexR-HSA-204809 (Reactome)
Tie2:Grb7 complexComplexR-HSA-204799 (Reactome)
VPREB1 ProteinP12018 (Uniprot-TrEMBL)
VPREB3 ProteinQ9UKI3 (Uniprot-TrEMBL)
YES1 ProteinP07947 (Uniprot-TrEMBL)
activated thrombin:thrombomodulinComplexR-HSA-141038 (Reactome)
eba-140 ProteinQ76NM5 (Uniprot-TrEMBL)
eba-175 ProteinP19214 (Uniprot-TrEMBL)
eba-175,ebl1,eba-140ComplexR-PFA-8867216 (Reactome)
ebl1 ProteinQ9U4X0 (Uniprot-TrEMBL)
integrin alpha4beta1:JAM2:JAM3ComplexR-HSA-202759 (Reactome)
op28 ProteinP11297 (Uniprot-TrEMBL)
opa proteinsComplexR-NGO-8867104 (Reactome)
opa65 ProteinQ04885 (Uniprot-TrEMBL)
opa66 ProteinQ05033 (Uniprot-TrEMBL)
opa67 ProteinQ05034 (Uniprot-TrEMBL)
opa68 ProteinQ04881 (Uniprot-TrEMBL)
opaA ProteinQ04876 (Uniprot-TrEMBL)
opaB ProteinQ04874 (Uniprot-TrEMBL)
opaC ProteinP11296 (Uniprot-TrEMBL)
opaD ProteinQ04883 (Uniprot-TrEMBL)
opaE ProteinQ04878 (Uniprot-TrEMBL)
opaF ProteinQ04879 (Uniprot-TrEMBL)
opaG ProteinQ04875 (Uniprot-TrEMBL)
opaH ProteinQ04884 (Uniprot-TrEMBL)
opaI ProteinQ04877 (Uniprot-TrEMBL)
opaJ ProteinQ04882 (Uniprot-TrEMBL)
opaK ProteinQ04880 (Uniprot-TrEMBL)
p-5Y,S1119-TEK ProteinQ02763 (Uniprot-TrEMBL)
p-Y663,Y686-PECAM1 dimerComplexR-HSA-211539 (Reactome)
p-Y663,Y686-PECAM1(27-?) ProteinP16284 (Uniprot-TrEMBL)
p-Y663,Y686-PECAM1(27-?)ProteinP16284 (Uniprot-TrEMBL)
p21 RAS:GDPComplexR-HSA-109796 (Reactome)
p21 RAS:GTPComplexR-HSA-109783 (Reactome)
p85 bound to Tie2ComplexR-HSA-204834 (Reactome)
pTie2 and SHP2 complexComplexR-HSA-204767 (Reactome)
piiC ProteinP09888 (Uniprot-TrEMBL)
thrombin heavy chain ProteinP00734 (Uniprot-TrEMBL)
thrombin light chain ProteinP00734 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
2xANGPT1:TEKArrowR-HSA-210881 (Reactome)
2xANGPT1:TEKR-HSA-210872 (Reactome)
2xIgA:JCHAINR-HSA-8858428 (Reactome)
2xSELE ligands:SELEArrowR-HSA-2870221 (Reactome)
ADPArrowR-HSA-210291 (Reactome)
ADPArrowR-HSA-210872 (Reactome)
AMICA1R-HSA-199093 (Reactome)
ANGPT1:TEKArrowR-HSA-204779 (Reactome)
ANGPT1:TEKR-HSA-210881 (Reactome)
ANGPT1:TEKmim-catalysisR-HSA-210872 (Reactome)
ANGPT1:p-5Y,S119-TEK:SHC1ArrowR-HSA-204861 (Reactome)
ANGPT1:p-5Y,S119-TEKR-HSA-204773 (Reactome)
ANGPT1:p-5Y,S119-TEKR-HSA-204798 (Reactome)
ANGPT1:p-5Y,S119-TEKR-HSA-204813 (Reactome)
ANGPT1:p-5Y,S119-TEKR-HSA-204850 (Reactome)
ANGPT1:p-5Y,S119-TEKR-HSA-204861 (Reactome)
ANGPT1:p-5Y,S119-TEKR-HSA-204871 (Reactome)
ANGPT1:p-5Y,S119-TEKR-HSA-204873 (Reactome)
ANGPT1R-HSA-204779 (Reactome)
ANGPT2:TEKArrowR-HSA-204863 (Reactome)
ANGPT2R-HSA-204863 (Reactome)
ANGPT4:TEKArrowR-HSA-204824 (Reactome)
ANGPT4R-HSA-204824 (Reactome)
ATPR-HSA-210291 (Reactome)
ATPR-HSA-210872 (Reactome)
BSG dimerArrowR-HSA-204600 (Reactome)
BSG:Integrin

alpha3beta1,

alpha6beta1		ArrowR-HSA-204434 (Reactome)
BSG:MCTsArrowR-HSA-204392 (Reactome)
BSG:MMP1(100-469)ArrowR-HSA-375135 (Reactome)
BSG:PPIAArrowR-HSA-204485 (Reactome)
BSG:SPNArrowR-HSA-204465 (Reactome)
BSGR-HSA-204392 (Reactome)
BSGR-HSA-204434 (Reactome)
BSGR-HSA-204465 (Reactome)
BSGR-HSA-204485 (Reactome)
BSGR-HSA-204500 (Reactome)
BSGR-HSA-204549 (Reactome)
BSGR-HSA-204600 (Reactome)
BSGR-HSA-375131 (Reactome)
BSGR-HSA-375133 (Reactome)
BSGR-HSA-375135 (Reactome)
Basigin:CD98hc complexArrowR-HSA-375131 (Reactome)
Basigin:Mannose-carrying cell recognition moleculesArrowR-HSA-375133 (Reactome)
CAV1R-HSA-204549 (Reactome)
CD177R-HSA-202702 (Reactome)
CD244R-HSA-202722 (Reactome)
CD2R-HSA-202714 (Reactome)
CD47-binding SIRPs:CD47ArrowR-HSA-202703 (Reactome)
CD47-binding SIRPsR-HSA-202703 (Reactome)
CD47R-HSA-202703 (Reactome)
CD48:CD244ArrowR-HSA-202722 (Reactome)
CD48R-HSA-202722 (Reactome)
CD58:CD2ArrowR-HSA-202714 (Reactome)
CD58R-HSA-202714 (Reactome)
CD74 trimerR-HSA-5676133 (Reactome)
CD84 dimerArrowR-HSA-202713 (Reactome)
CD84R-HSA-202713 (Reactome)
CD98hc complexR-HSA-375131 (Reactome)
CD99:CD99L2ArrowR-HSA-8867097 (Reactome)
CD99L2R-HSA-8867097 (Reactome)
CD99R-HSA-8867097 (Reactome)
CEACAM heterodimerArrowR-HSA-202717 (Reactome)
CEACAM heterodimerArrowR-HSA-202723 (Reactome)
CEACAM1,3,5,6:opa proteinsArrowR-HSA-8867135 (Reactome)
CEACAM1,3,5,6R-HSA-8867135 (Reactome)
CXADR bound to JAMLArrowR-HSA-199093 (Reactome)
CXADRR-HSA-199093 (Reactome)
Caveolin-1 bound to BasiginArrowR-HSA-204549 (Reactome)
Collagen type I fibrilR-HSA-114577 (Reactome)
CyP60 complexed with BasiginArrowR-HSA-204500 (Reactome)
DOK2R-HSA-204850 (Reactome)
EPCAM dimerArrowR-HSA-8867240 (Reactome)
EPCAMR-HSA-8867240 (Reactome)
F11R dimerArrowR-HSA-202726 (Reactome)
F11RR-HSA-202718 (Reactome)
F11RR-HSA-202726 (Reactome)
FCAMR:2xIgA:JCHAINArrowR-HSA-8858428 (Reactome)
FCAMRR-HSA-8858428 (Reactome)
FN1 dimerR-HSA-202723 (Reactome)
GDPArrowR-HSA-210977 (Reactome)
GPVI:FceRI gamma:FYN:LYN:Collagen type IArrowR-HSA-114577 (Reactome)
GPVI:FceRI gamma:FYN:LYNR-HSA-114577 (Reactome)
GRB14R-HSA-204813 (Reactome)
GRB2-1R-HSA-204871 (Reactome)
GRB7R-HSA-204773 (Reactome)
GTPR-HSA-210977 (Reactome)
GYPA,GYPB,GYPC:eba-175,ebl1,eba-140ArrowR-HSA-8867098 (Reactome)
GYPA,GYPB,GYPCR-HSA-8867098 (Reactome)
Grb2 bound to Tie2ArrowR-HSA-204871 (Reactome)
Grb2 bound to Tie2R-HSA-210974 (Reactome)
HSArrowR-HSA-204485 (Reactome)
INPP5DR-HSA-210290 (Reactome)
ITGA4:ITGB1R-HSA-202706 (Reactome)
IgM Heavy ChainR-HSA-8858498 (Reactome)
Immunoglobulin Mu

with Surrogate

Light Chain		ArrowR-HSA-8858498 (Reactome)
Integrin

alpha3beta1,

alpha6beta1		R-HSA-204434 (Reactome)
Integrin

alpha5beta1:FN1

dimer		ArrowR-HSA-202723 (Reactome)
Integrin alphaLbeta2:F11RArrowR-HSA-202718 (Reactome)
Integrin alphaMbeta2:JAM3ArrowR-HSA-202727 (Reactome)
Integrin alphaVbeta3:PECAM1ArrowR-HSA-210304 (Reactome)
Integrin alphaXbeta2:JAM3ArrowR-HSA-202704 (Reactome)
Integrin alpha5beta1R-HSA-202723 (Reactome)
Integrin alphaLbeta2R-HSA-202718 (Reactome)
Integrin alphaMbeta2R-HSA-202727 (Reactome)
Integrin alphaVbeta3R-HSA-210304 (Reactome)
Integrin alphaXbeta2R-HSA-202704 (Reactome)
JAM2 dimerArrowR-HSA-202709 (Reactome)
JAM2:JAM3ArrowR-HSA-202721 (Reactome)
JAM2:JAM3R-HSA-202706 (Reactome)
JAM2R-HSA-202709 (Reactome)
JAM2R-HSA-202721 (Reactome)
JAM3 dimerArrowR-HSA-202731 (Reactome)
JAM3R-HSA-202704 (Reactome)
JAM3R-HSA-202721 (Reactome)
JAM3R-HSA-202727 (Reactome)
JAM3R-HSA-202731 (Reactome)
LDLR-HSA-203130 (Reactome)
Ligand to TREM-1 on

the platelet

membrane		R-HSA-203156 (Reactome)
MERTK ligandsR-HSA-202710 (Reactome)
MERTK:MERKT ligandsArrowR-HSA-202710 (Reactome)
MERTKR-HSA-202710 (Reactome)
MIF trimer:CD74 trimerArrowR-HSA-5676133 (Reactome)
MIF trimerR-HSA-5676133 (Reactome)
MMP1(100-469)R-HSA-375135 (Reactome)
Mannose-carrying

cell recognition

molecules		R-HSA-375133 (Reactome)
Mn2+R-HSA-202723 (Reactome)
Monocarboxylate

Transporter Set

(MCT)		R-HSA-204392 (Reactome)
Neutrophil CEACAMs

affecting integrin binding to

fibronectin		R-HSA-202717 (Reactome)
OLR1 bound to oxidized LDLArrowR-HSA-203130 (Reactome)
OLR1R-HSA-203130 (Reactome)
PECAM-1:PLC gamma1 complexArrowR-HSA-210283 (Reactome)
PECAM-1:SHIP1 complexArrowR-HSA-210290 (Reactome)
PECAM-1:SHP-1 complexArrowR-HSA-210277 (Reactome)
PECAM-1:SHP-2 complexArrowR-HSA-210294 (Reactome)
PECAM1 dimerArrowR-HSA-210285 (Reactome)
PECAM1 dimerR-HSA-210291 (Reactome)
PECAM1:CD177ArrowR-HSA-202702 (Reactome)
PECAM1R-HSA-202702 (Reactome)
PECAM1R-HSA-210285 (Reactome)
PECAM1R-HSA-210304 (Reactome)
PI3KR-HSA-204798 (Reactome)
PICK1R-HSA-8858435 (Reactome)
PLCG1R-HSA-210283 (Reactome)
PPIAR-HSA-204485 (Reactome)
PPIL2R-HSA-204500 (Reactome)
PROC(200-211)ArrowR-HSA-141040 (Reactome)
PROCR:Activated protein CArrowR-HSA-141040 (Reactome)
PROCR:Protein CR-HSA-141040 (Reactome)
PSGs:Proteoglycan,TGFB1ArrowR-HSA-8870732 (Reactome)
PSGsR-HSA-8870732 (Reactome)
PTPN11R-HSA-204873 (Reactome)
PTPN11R-HSA-210294 (Reactome)
PTPN6R-HSA-210277 (Reactome)
Phosphorylated Tie2 in Tie2/Akt dimerArrowR-HSA-210872 (Reactome)
Platelet Factor 4ArrowR-HSA-141040 (Reactome)
Pre-B Cell Surrogate Light ChainR-HSA-8858498 (Reactome)
Proteoglycans,TGFB1R-HSA-8870732 (Reactome)
R-HSA-114577 (Reactome) GPVI receptor has little affinity for soluble forms of collagen but binds collagen fibrils. Recent structural models indicate that each GPVI receptor complex could bind up to 3 collagen fibrils (Jung & Moroi 2008). The Src family kinases Fyn and Lyn constitutively associate with the GPVI-FceRIgamma complex in platelets and initiate platelet activation through phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) in the FceRIgamma chain, leading to binding and activation of the tyrosine kinase Syk. Downstream of Syk, a series of adapter molecules and effectors lead to platelet activation.
R-HSA-141040 (Reactome) Thrombin complexed with thrombomodulin at the endothelial cell surface cleaves the heavy chain of protein C, generating activated protein C and an activation peptide. The activation peptide has no known function.
R-HSA-199093 (Reactome) JAM members, such as JAML, bind coxsackie and adenovirus receptor (CXADR) on epithelial and endothelial cells.
R-HSA-202702 (Reactome) CD177 is a 58- to 64-kDa glycosylphosphatidylinositol-anchored glycoprotein expressed exclusively by neutrophils, neutrophilic metamyelocytes, and myelocytes, but not by any other blood cells. It has been shown that neutrophil-specific CD177 is a heterophilic binding partner of PECAM-1, constituting a novel pathway that promotes neutrophil transmigration.
R-HSA-202703 (Reactome) Integrin-associated protein (IAP or CD47) is a receptor for thrombospondin family members, a ligand for the transmembrane signaling protein SIRP-alpha and -gamma, and a component of a supramolecular complex containing specific integrins, heterotrimeric G proteins and cholesterol.
R-HSA-202704 (Reactome) Although JAM-C is better known for its interaction with MAC-1, an interaction with CD11c/CD18 (known as alpha X beta 2), has also been described.
R-HSA-202706 (Reactome) Several key IgSF cell adhesion molecules engage integrin and in so doing impact on the multi-step paradigm of leukocyte emigration. The interaction between JAM2 (JAM-B) and Integrin alpha4beta1 (VLA-4) requires prior inding of JAM2 to JAM3 (JAM-C).
R-HSA-202709 (Reactome) Apart from its well-established interaction with Integrin alpha4beta1 (VLA-4), JAM2 (JAM-B) is also known to homodimerize.
R-HSA-202710 (Reactome) MerTK appears to be required for ingestion of apoptotic cells by professional phagocytes such as monocytes/macrophages, retinal pigment epithelial cells and dendritic cells. Mer appears to be able to induce the cytoskeletal remodelling that is required for engulfment during phagocytosis. For instance, a deletion in the MERTK gene was identified as the underlying cause for retinal dystrophy which involves an impairment in the ingestion of shed photoreceptor cell fragments by retinal pigment epithelial cells.

The biological ligands for MerTK are two highly similar vitamin K-dependent proteins, Gas6 and protein S (PS), a negative regulator of blood coagulation. Both proteins are composed an N-terminal region containing multiple post-translationally modified gamma-carboxyglutamic acid residues (Gla). The Gla region possesses the ability to interact in a conformationally specific manner with negatively charged membrane phospholipids, which is thought to mediate the binding of both Gas6 and PS to apoptotic cells. In this way, they are thought to act as recognition bridges between apoptotic cells and the phagocyte cell that ingest them.

R-HSA-202713 (Reactome) CD84 is a homophilic receptor expressed on T cells, B cells, dendritic cells, monocytes, macrophages, eosinophils, mast cells, granulocytes, and platelets. CD84 expression increases following activation of T cells, B cells, and dendritic cells. CD84 homophilic engagement is known to induce platelet stimulation.
R-HSA-202714 (Reactome) The crystal structure of the human CD2-CD58 complex also shows that most of the residues at the interface between these two proteins are charged and form several inter-protein salt bridges.
R-HSA-202717 (Reactome) The presence of CEACAM dimers was shown to lead to an increase in the binding of the integrin alph5 beta1 receptor to its ligand fibronectin, without changing its cell surface levels, resulting in increased adhesion of these cells to fibronectin.
R-HSA-202718 (Reactome) JAM-A plays a key role in leukocyte transmigration and inflammatory extravasation. Transmigration of human leukocytes has been shown to involve heterophilic interactions of JAM-A with its integrin receptor LFA-1.
R-HSA-202721 (Reactome) JAM2 and JAM3 bind each other and are strongly expressed by endothelial cells of high endothelial venules, the predominant site of leukocyte extravasation. JAM2 and JAM3 also bind to the leukocyte integrins VLA-4 and Mac-1 respectively.
R-HSA-202722 (Reactome) CD2, CD48, CD84, CD244 and CD58 have a similar extracellular domain arichitecture consisting of two IgSF domains. CD244 is closely related to CD84 in having a long cytoplasmic tail with tyrosine-based motifs (TxYxxI/V) resembling immunoreceptor tyrosine-based inhibitory motifs (ITIMs). CD2 has a cytoplasmic domain with proline-rich regions which recruit an Src homology 3 (SH3)- containing protein called CD2-associated protein (CD2AP). CD48 is glycosyl-phosphatidyl-inositol (GPI)-anchored to the membrane.

CD244 is known to be activated by binding to CD48 in humans.

R-HSA-202723 (Reactome) Alpha5beta1 integrin was the first integrin shown to bind fibronectin (FN1). Unlike other FN1-binding integrins it is a specialist at this task. In solution FN1 occurs as a dimer. Binding to alpha5beta1 integrin stimulates FN1 self-association; blocking the RGD-cell binding domain of FN1 blocks fibril formation (Fogerty et al. 1990). FN1 binding is believed to induce integrin clustering, which promotes FN1-FN1 interactions. Integrin clustering is mediated by association between integrins and intracellular actin stress fibers (Calderwood et al. 2000). Binding of integrins to each of the monomers in the FN1 dimer pair is thought to trigger a conformational change in FN1 that exposes 'cryptic' FN1 binding sites that allow additional fibronectin dimers to bind without the requirement for pre-association with integrins (Singh et al. 2010). This non-covalent interaction may involve interactions with fibrillin (Ohashi & Erickson 2009). I1-5 functions as a unit that is the primary FN matrix assembly domain (Sottile et al. 1991) but other units are likely to be involved (Singh et al. 2010). Other integrins able to bind FN1 include alphaIIbBeta3, which is highly expressed on platelets where it predominantly binds fibrinogen leading to thrombus formation but also binds FN1 (Savage et al. 1996). Alpha4beta1 mediates cell-cell contacts and cell-matrix contacts through the ligands VCAM-1 and FN1, respectively (Humphries et al. 1995). Integrins alpha3beta1, alpha4beta7, alphaVbeta1, 3 (Johansson et al. 1997), 6 (Busk et al. 1992) and alpha8beta1 (Muller et al. 1995, Farias et al. 2005) are all able to bind FN1.

Tenacious binding of free fibronectin to cells leads to enhanced fibronectin matrix assembly and the formation of a polymerized fibronectin "cocoon" around the cells. This process is enhanced in the presence of CEACAM molecules.
R-HSA-202724 (Reactome) PSGL-1 is expressed as a homodimer of two 120-kDa subunits that binds all four selectins, with the highest affinity for P-selectin, and is known to be constitutively expressed on the surface of platelets and most types of leukocytes. Besides playing a critical role in the inflammatory response by mediating leukocyte-leukocyte and leukocyte-endothelium interactions, PSGL-1 also participates in the hemostatic process by mediating leukocyte-platelet interactions.
R-HSA-202726 (Reactome) F11R (JAM-A) is the most widely expressed member of the family, and has been shown to be expressed on endothelial and epithelial cells, on platelets, and on a number of leukocyte subsets. In endothelial cells, F11R locates to the tight junctions, where it appears to engage in homophilic binding to F11R on adjacent cells, an interaction that is considered to play a critical role in angiogenesis.
R-HSA-202727 (Reactome) Recruitment of monocytic cells to the vessel wall by platelets is mediated via CD11b/CD18 (Mac-1) and platelet JAM-C. In the case of dendritic cells, this interaction leads to their activation and platelet phagocytosis. This process may be of importance for progression of atherosclerotic lesions.
R-HSA-202731 (Reactome) JAM-C has been detected in epithelial-cell desmosomes. JAM-C homodimers are prominently located in endothelial-cell tight junctions.
R-HSA-203130 (Reactome) The lectin-like oxidized low density lipoprotein receptor- 1 (Lox-1) mediates the recognition and internalization of oxidatively modified low density lipoprotein. This interaction results in a number of pro-atherogenic cellular responses that probably play a significant role in the pathology of atherosclerosis.
R-HSA-203156 (Reactome) The triggering receptor expressed on myeloid cells 1 (TREM-1) plays an important role in the innate immune response related to severe infections and sepsis. Although the identity and occurrence of the natural TREM-1 ligands are so far unknown, the presence of a ligand for TREM-1 on human platelets has been established. It has been suggested that TREM1 recognizes soluble proteins or cell-surface proteins which are upregulated as a result of inflammation and/or tissue damage and also bacterial LPS (Tessarz & Cerwenka 2008).
R-HSA-204392 (Reactome) Proton-coupled monocarboxylate transporters (MCT) MCT1, MCT3, and MCT4 form heterodimeric complexes with the cell surface glycoprotein CD147 and exhibit tissue-specific polarized distributions that are essential for maintaining lactate and pH homeostasis.
R-HSA-204434 (Reactome) Basigin is a widely distributed cell-surface protein with two immunoglobulin domains and has shown to associate with both the integrins alpha3beta1 and alpha6beta1.
R-HSA-204465 (Reactome) CD43, a major leukocyte cell surface sialoglycoprotein, interacts directly with Basigin.
R-HSA-204485 (Reactome) Cyclophilin A (CyPA)1 is an intracellular protein belonging to the immunophilin family and is recognized as the major target for the potent immunosuppressive drug cyclosporin A. CD147 is the natural cell surface receptor for CyPA. It is demonstrated that CD147 is an essential component in the CyPA-initiated signaling cascade that culminates in ERK activation.
R-HSA-204500 (Reactome) Basigin serves as a signaling receptor for extracellular cyclophilins. Its been reported that cyclophilin 60 (Cyp60), a distinct member of the cyclophilin family is involved in the regulation of intracellular transport of basigin. The mechanism of this activity involves interaction of Cyp60 with the proline-containing region within or adjacent to the predicted transmembrane domain basigin. Cyp60 is co-localized with basigin at the plasma membrane suggesting that Cyp60 may function as a chaperone escorting basigin through the secretory pathway.
R-HSA-204549 (Reactome) Stromal fibroblasts secrete multiple matrix metalloproteinases (MMP)1 that can promote tumor cell growth, survival, invasion, angiogenesis, and metastasis. Basigin on the surface of carcinoma cells, stimulates production of MMP-1 (interstitial collagenase), MMP-2 (gelatinase A), and MMP-3 (stromelysin). Basigin has been shown to co-immunoprecipitate with caveolin-1. The second Ig domain of Basigin is required for this association, which leads to decreased Besigin self-association on the cell surface. Therefore, caveolin-1 is a negative regulator of CD147 self-association, and its MMP-inducing activity.
R-HSA-204600 (Reactome) Basigin (Bsg) is a highly glycosylated transmembrane protein belonging to the Ig superfamily with two Ig domains. Bsg forms homo-oligomers on the plasma membrane in a cis-dependent manner. The N-terminal Ig-like domain is functionally important in oligomer formation.

R-HSA-204773 (Reactome) Grb7 was initially identified as an EGF receptor binding protein and thereafter many binding partners have been reported. Grb7 interacts with Tie2/Tek in a phosphotyrosine-dependent manner through its SH2 domain.
R-HSA-204779 (Reactome) Tie receptors and their angiopoietin ligands play a critical role in angiogenesis or blood vessel formation. They are considered to control numerous signaling pathways that are involved in diverse cellular processes, such as cell migration, proliferation, survival and reorganization of the actin cytoskeleton.

Tie (tyrosine kinase with immunoglobulin and epidermal growth factor homology domains) represents a class of receptor tyrosine kinases (RTKs) that are predominately expressed by vascular endothelial cells. The angiopoietins are a family of growth factors that are largely specific for endothelium and they bind to Tie2/Tek RTKs.

Tie2 signaling initially involves the activation of Tie2 by the interaction of angiopoietin 1. Angiopoietin interacts with the Tie2 receptor with its fibrinogen like domain (FLD). This interaction leads to the dimerization of both the receptor and the ligand, and later initiate the trans-phosphorylation of Tie2.
R-HSA-204798 (Reactome) The p85 subunit of phosphatidylinositol 3-kinase (PI3-kinase) associates with Tie2, most likely at phosphotyrosine 1102. This association leads on to the activation of Akt/PKB, a process linked to cell survival and antiapoptosis, and that may in part account for Tie2's role in vascular growth and maintenance.
R-HSA-204813 (Reactome) Grb14 is also one of the signaling partners of Tie2. The SH2 domain of Grb2 mediates binding to Tie2. It binds residues Y816, Y1108 and Y1113 respectively, in the C-terminal tail region of Tie2/Tek.
R-HSA-204824 (Reactome) Ang4 represents a third protein of the Ang family that binds to the Tie2 receptor. The mouse Ang3 and human Ang4 are interspecies orthologs. Ang4 acts as an activating ligand and induces phosphorylation in Tie2.
R-HSA-204850 (Reactome) Dok-2 is a member of a docking proteins class, termed the DOK family. The DOK family members are characterized by an N-terminal pleckstrin homology (PH) domain followed by a central PTB domain and a proline- and tyrosine-rich C-terminal tail. Dok-2 is recruited to activated Tie2 via its PTB domain, which results in its subsequent tyrosine phosphorylation, thereby establishing binding sites for the small GTPase-activating protein for Ras, p120RasGAP (RasGAP) and the adapter protein Nck. The binding of DOK to the receptor leads to Nck recruitment and subsequent phosphorylation. Binding of Pak to Nck follows. this brings about the Ang-1-dependent phosphorylation of Pak in endothelial cells.
R-HSA-204861 (Reactome) ShcA, an SH2-containing adapter protein, acts as a scaffold for the assembly of signaling proteins involved in the activation of the Ras-MAPK pathway, and potentially other signaling pathways.
ShcA is one of the binding partners of endogenous Tie2 receptor on vascular endothelial cells. After Tie2 stimulation by Ang-1 interaction, ShcA associates with Tie2 and becomes tyrosine-phosphorylated. ShcA interacts with the cytoplasmic domain of Tie2 and Y1102 of Tie2 was identified as the primary binding site for the SH2 domain of ShcA. ShcA leads to a reduction of tyrosine phosphorylation of p85 subunit of PI3-kinase and is involved in the inhibition of endothelial cell migration and survival.
R-HSA-204863 (Reactome) The major ligands for Tie2 are Ang1 and Ang2. Ang1 has been considered as the primary activating ligand of Tie2 whereas role of Ang2 remains controversial. Ang2 acts as stimulating in some studies and inhibiting in others. The activity of Ang2 is concentration dependent. Ang2 possesses similar receptor affinity to Ang1 and they both share the same binding site on Tie2. The Ang2 fibrinogen domain is solely responsible for receptor recognition and binding, the coiled-coil motif mediates its oligomerization.
R-HSA-204871 (Reactome) Tie2/Tek provide mitogenic signals to endothelial cells by promoting the association of Grb2 to one of their phosphotyrosines. Grb2 is an adaptor protein that has been linked to activation of Ras and mitogen activated protein kinase (MAPK) cell growth signaling pathways. Grb2 also binds to the Y1102 of the kinase domain of Tie2 with one of its SH2 doamins.
R-HSA-204873 (Reactome) Shp2 interact with Tyr816 in the juxtamembrane region and Tyr1108 and Tyr1113, respectively, in the C-terminal tail region of Tie2/Tek.
R-HSA-210277 (Reactome) The phosphorylation of two tandem tyrosine residues (Y663 and Y686) within the cytoplasmic domain of PECAM-1 is required for the downstream signalling events observed following PECAM-1 ligation. Both SH2 domains of SHP-1 are required in tandem to bind PECAM-1.
R-HSA-210283 (Reactome) Like SHP-1 and SHP-2, PLC-gamma 1 also interacts with PECAM-1. PLC-gamma 1 binds with both the tyrosine residues (Y663 and Y686). Unlike the N-SH2 domain, the C-SH2 domain on PLC-gamma 1 can only bind phosphotyrosine 663. The engagement of PECAM-1 with PLC-gamma 1 may lead to PLC-gamma 1 activation and subsequent calcium influx.
R-HSA-210285 (Reactome) PECAM-mediated adhesion is complex, because it is capable of binding both to itself (homophilic adhesion) and to non-PECAM ligands (heterophilic adhesion). The trans-homophilic interaction between the two PECAM-1 molecules is mediated by their NH2-terminal membrane distal Ig homology domains 1 and 2 plus the proper spacing formed by the six Ig-homology domains.
R-HSA-210290 (Reactome) PECAM/CD31 is a member of the immunoglobulin superfamily (IgSF) and has been implicated to mediate the adhesion and trans-endothelial migration of T-lymphocytes into the vascular wall, T cell activation and angiogenesis. It has six Ig homology domains within its extracellularly and an ITIM motif within its cytoplasmic region.
PECAM-mediated adhesion is complex, because it is capable of binding both to itself (homophilic adhesion) and to non-PECAM ligands (heterophilic adhesion). The trans-homophilic interaction between the two PECAM-1 molecules is mediated by their NH2-terminal membrane distal Ig homology domains 1 and 2 plus the proper spacing formed by the six Ig-homology domains.
R-HSA-210291 (Reactome) PECAM-1 is capable of transmitting information into the cell following its engagement and becomes tyrosine-phosphorylated during the platelet aggregation process. The Src family of tyrosine kinases (more specifically, Src, Lyn, and c-src) has been widely implicated in the phosphorylation of PECAM-1. Conserved tyrosine residues (Tyr663 and Tyr686) within the PECAM-1 cytoplasmic ITIM motif have been shown to become phosphorylated. Tyrosine phosphorylation of PECAM-1 prompts its association with intracellular signal transduction molecules.
R-HSA-210294 (Reactome) PECAM-1 becomes tyrosine-phosphorylated during the platelet aggregation process; the phosphorylation of two tandem tyrosine residues (Y663 and Y686) within the cytoplasmic domain is required for downstream signalling events. Phosphorylation creates docking sites for the protein-tyrosine phosphatase SHP-2. The interaction between SHP-2 and PECAM-1 is dependent upon integrin-mediated platelet/platelet interactions and occurs via the Src homology 2 (SH2) domains of the phosphatase and highly conserved phosphatase-binding motifs encompassing phosphotyrosines 663 and 686 within the cytoplasmic domain of PECAM-1.
R-HSA-210304 (Reactome) Alpha v beta 3 integrin is one of the potential heterophilic ligands of PECAM-1 that is involved in down-regulation of T-cell responses. The heterophilic interaction of alpha v beta 3 integrin on endothelial cells with PEACAM-1 on leukocytes increases the adhesive function of beta integrins on T cells, monocytes, neutrophils and NK cells suggesting that leukocyte PEACAM-1 act as a signaling molecule.
R-HSA-210872 (Reactome) The dimerization of Tie2 leads to autophosphorylation and activation of its kinase domain. There are multiple tyrosine phosphorylation sites in the Tie2 kinase domain. The phosphorylated tyrosine residues provide the interaction site for the SH2 domains of other downstream signaling molecules like PI3K, Grb2, SHP2 etc.
R-HSA-210881 (Reactome) Receptor tyrosine kinase activation and signaling are typically initiated via dimerization of the receptors through homo-oligomeric ligand binding.

Angiopoietin1 may form homotrimers, but in most cases it assembles into higher-order multimers. This oligomerization is mediated by the N-ter coiled coil domain (CCD).
The binding of Ang1 oligomers to Tie2 promotes the dimerization of Tie2, which is further assisted by the interaction between the kinase domains of the receptors.
R-HSA-210974 (Reactome) Grb2 binds directly to autophosphorylated Tie2 receptor. GRB2 also contains two SH3 domains, which bring various ligands to the sites of active signaling. One of the SH3 domains on Tie2-bound Grb2 recruits SOS1, an activating nucleotide exchange factor for Ras. This interaction of Sos1 to Grb2 brings Sos1 towards Ras molecules leading to Ras activation. Ras is implicated in the MAP kinase cascade, a pathway in cell growth stimulation, migration and differentiation.
R-HSA-210977 (Reactome) Sos-1 bound to Grb2:Tie2 complex promotes the exchange of inactive Ras-GDP to active Ras-GTP (Boriack-Sjodin et al.1998, Khan et al. 2004).
R-HSA-2870221 (Reactome) E-selectin is an adhesion molecule on the cell surface of endothelial cells. It participates in the binding of leukocytes to activated blood vascular endothelium during inflammation or metastasis (Haraldsen G et al. 1996). Leucocytes express E-selectin ligand 1 (ESL-1) and P-selectin glycoprotein ligand-1 (PCGL-1) which were identified as the ligands for E-selectin (Graves BJ et al 1994; Asa D et al 1995). E-selectin has been also implicated in mediating tissue-specific homing primitive hematopoietic progenitor cells (HPCs) into bone marrow (BM). PCGL-1, CD43, CD44 were shown to function as E-selectin ligands on human BM cells (Dimitroff CJ et al. 2001; Katayama Y et al. 2003; Merzaban JS et al. 2011).
R-HSA-375131 (Reactome) CD97hc is a multifunctional glycoprotein with a single transmembrane domain, is highly expressed on proliferating cells, and functions as a chaperone for transporters. CD98hc forms disulfide-bonded heterodimers with at least seven different light chains (SLC7A5-11) that serve as amino acid transporters. Covalent cross-linking, mass spectrometric protein identification, and co-immunoprecipitation shows selective CD147 association with CD98hc complex.
R-HSA-375133 (Reactome) Based on in vitro affinity chromatography study, basigin was found to bind to high mannose-carrying cell recognition molecules, such as myelin-associated glycoprotein, L1 and the beta2-subunit of Na+/K+-ATPase.
R-HSA-375135 (Reactome) Basigin (BSG, CD147, EMPRIN) is a glycoprotein expressed on the surface of most tumor cells. It stimulates stromal cells to produce elevated levels of several matrix metalloproteinases (MMP), including interstitial collagenase (MMP1). MMPs have been implicated in several aspects of tumor progression, including invasion through basement membranes and interstitial matrices, angiogenesis, and tumor cell growth. Basigin not only stimulates the production of MMP1 but also forms a complex with MMP1 at the tumor cell surface. This interaction may be important in modifying the tumor cell pericellular matrix to promote invasion.
R-HSA-5635741 (Reactome) TNFRSF10D (also known as DcR2 or TRAILR4) inhibits pro-apoptotic signaling by TRAIL (TNFSF10) receptors TNFRSF10A (TRAILR1, DR4) and TNFRSF10B (TRAILR2, DR5). TNFRSF10D has a truncated death domain (DD) but has the motifs involved in oligomerization of TRAIL receptors. While it was initially thought that TNFRSF10D functions as a decoy receptor that competes with TNFRSF10A and TNFRSF10B for ligand binding (Pan et al. 1997), latest studies indicate that it prevents TRAIL signaling by forming heterodimers with TNFRSF10A and TNFRSF10B and thus preventing formation of functional homotrimeric TRAIL ligand:receptor complexes (Neumann et al. 2014).
R-HSA-5676133 (Reactome) Macrophage migration inhibitory factor (MIF), one of the first cytokines to be described (George & Vaughan 1962), is an important regulator of innate and adaptive immunity. MIF is an upstream activator of monocytes/macrophages, centrally involved in the pathogenesis of septic shock, arthritis, and other inflammatory conditions (Nishihira 2000, Sanchez-Niño et al. 2013). High-expression Mif alleles are linked to severe rheumatoid arthritis (Morand & Leech 2005). MIF promotes monocyte/macrophage activation and it is required for the optimal expression of TNF-alpha, IL-1, and PGE2 (Calandra & Bucala 1997). MIF-treated macrophages are more phagocytic and better able to destroy intracellular pathogens, such as Leishmania (Rosado & Rodriguez-Sosa 2011). Active MIF is a 37.5 kDa homotrimer.

MIF can bind to CD74 (Leng et al. 2003) and the chemokine receptors CXCR2 and CXCR4 (Bernhagen et al. 2007). Leukocyte recruitment by MIF is mediated by interaction with CXCR2 and CXCR4 (Bernhagen et al. 2007). MIF interaction with CD74 mediates its proproliferative and antiproliferative effects, regulation of B-cell and tumor cell survival, fibrosis and angiogenesis (Starlets et al. 2006). MIF can suppress the immunosuppressive effects of glucocorticoids, inducing a sustained pattern of ERK-1/2 MAP kinase activation (Bach et al. 2009).

MIF is endocytosed to bind the cytosolic protein JAB1 (Schwartz et al. 2012), negatively regulating JAB1-controlled pathways (Kleemann et al. 2000). MIF inhibits JAB1-induced JNK activity, AP-1 activity and JAB1-dependent cell-cycle regulation by stabilizing p27Kip1 protein (Nguyen et al. 2003). Consequently, MIF blocks JAB1-mediated rescue of fibroblasts from growth arrest (Kleemann et al. 2000).
R-HSA-8858428 (Reactome) IgA nephropathy (IgAN), the most common glomerulonephritis, is characterized by the deposition of IgA immune complexes in the glomerular mesangium. This is the result of High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor (FCAMR, CD351) binding to IgA (McDonald et al. 2002).
R-HSA-8858435 (Reactome) Tetraspanin 7 (TSPAN7) a member of the tetraspanin superfamily associates dynamically with numerous partner proteins in tetraspanin-enriched microdomains (TEMs) of the plasma membrane (Boucheix and Rubinstein, 2001). TSPAN7 promotes filopodia and dendritic spine formation in cultured hippocampal neurons, and is required for spine stability and normal synaptic transmission. Via its C-terminus, TSPAN7 interacts with the PDZ domain of protein interacting with C kinase 1 (PICK1), to regulate PICK1 and GluR2/3 association and AMPA receptor trafficking (Bassani et al. 2012). PICK1 is involved in the internalization and recycling of AMPA receptors (AMPARs) (Perez et al. 2001). In hippocampal neurons, TSPAN7 may regulate AMPA receptor trafficking by limiting PICK1 accessibility to AMPA receptors and suggest an additional mechanism for the functional maturation of glutamatergic synapses, whose impairment is implicated in intellectual disability (Bassani et al. 2012).
R-HSA-8858498 (Reactome) The pre-BCR is a heterodimer composed of an immunoglobulin (Ig) heavy chain molecule (IgH) covalently associated with an immunoglobulin light chain-like molecule called the surrogate light chain (SL). The SL consists of two non-covalently associated proteins called lamda-5 (CD179a) and VPREB (CD179b) (Melchers 1993). Pre-BCR signalling promotes the generation of a large pool of precursor cells that can undergo light-chain gene rearrangement (Rickert 2013).
R-HSA-8867097 (Reactome) CD99 is a glycoprotein found on the leukocytes surface. It has been variously described as a human thymus leukemia Ag (Levy et al. 1979), a Ewing's sarcoma-specific membrane marker molecule (Hamilton et al. 1988) and a putative adhesion molecule (termed E2) involved in spontaneous rosette formation of T cells with erythrocytes (Aubrit et al. 1989, Bernard et al. 1988). CD99L2 is a paralog of CD99 that directly interacts with CD99 to form a heterodimer via its cytoplasmic domain. This interaction positively regulates CD99L2 trafficking to cell surfaces (Nam et al. 2013).
R-HSA-8867098 (Reactome) Red blood cell (RBC) glycophorins are integral membrane proteins that are rich in sialic acids. They carry blood group antigenic determinants and serve as ligands for viruses, bacteria, and parasites. They are used as markers to study normal and pathological differentiation of erythroid tissue. RBC glycophorins include glycophorins A (GPYA) to E and are divided into two groups. GPYA and GPYB carry MN and Ss blood group antigens and may act as receptors for Plasmodium falciparum (Cartron & Rahuel 1992). GPYA and GPYB are recognized by P. falciparum erythrocyte-binding antigen 175 (EBA-175) (Wanaguru et al. 2013) and erythrocyte-binding ligand 1 (EBL-1) (Mayer et al. 2009), respectively. GLYC codes for the Gerbich (Ge) blood group antigens and is a receptor for P. falciparum invasion, recognizing EBA-140 on the surface of merozoites (Maier et al. 2003).
R-HSA-8867135 (Reactome) The carcinoembryonic antigen (CEA) gene family, part of the immunoglobulin (Ig) gene superfamily, is a diverse set of highly glycosylated glycoproteins. Two types of membrane anchorage are found in the CEA subgroup of CEACAM proteins. CEACAM1 and CEACAM3 contain a hydrophobic transmembrane domain followed by a cytoplasmic domain, while CEA (also known as CEACAM5) and CEACAM6 are attached to the cell surface via a glycosylphosphatidylinositol (GPI) moiety (Hammarstrom et al. 1999). CEA, CEACAM1, CEACAM3, and CEACAM6 have been shown to serve as receptors for the neisserial phase-variable opacity-associated (Opa) adhesin proteins (Chen & Gotschlich, 1996, Bos et al. 1997, Popp et al. 1999). These adhesin proteins are a major surface component of Neisseria meningitidis and Neisseria gonorrhoeae, and are responsible for bacterial adherence and entry into host cells and interactions with the host immune system. These receptors also bind to DraE adhesin of Escherichia coli (Berger et al. 2004).
R-HSA-8867240 (Reactome) Epithelial cell adhesion molecule (EPCAM) is a type I membrane protein expressed in a variety of human epithelial tissues, cancers, and progenitor and stem cells. It consists of an extracellular domain with epidermal growth factor (EGF)-like and thyroglobulin repeat-like domains, a single transmembrane domain, and a short 26-amino acid intracellular domain called EpICD (Balzar et al. 1999). In normal cells EPCAM is predominantly present at the surfaces of intercellular spaces where epithelial cells form very tight junctions. The extracellular domain of EPCAM interacts with a second EPCAM molecule resulting in homotypic cell-cell adhesion (Litvinov et al. 1994, 1997). Formation of EPCAM-mediated adhesions has a negative regulatory effect on adhesions mediated by classic cadherins, which may have strong effects on the differentiation and growth of epithelial cells (Balzar et al. 1999).
R-HSA-8870732 (Reactome) The pregnancy-specific glycoproteins (PSGs) are the most abundant trophoblastic proteins in maternal blood during human pregnancy. They are secreted by the syncytiotrophoblast and are detected around day 14 post fertilization. The PSG family belongs to the carcinoembryonic antigen family. There are ten human protein-coding PSG genes (PSG1- PSG9, PSG11) (Thompson et al. 1990). Several studies indicate that PSGs have immunoregulatory, proangiogenic, and anti-platelet functions. PSGs (PSG1) binds to cell surface proteoglycans that have covalently attached glycosaminoglycans (GAGs), specifically to syndecans 1-4 and glypican-1, to induce endothelial tube formation (Lisboa et al. 2011). PSG1 interacts with and activates Transforming growth factor beta 1 (TGFB1) (Blois et al. 2014, Moore & Dveksler 2014). During pregnancy, TGFB1 regulates many processes essential for pregnancy success including trophoblast invasion and proliferation, angiogenesis, extracellular matrix formation and tolerance to the foetal semi-allograft (Jones et al. 2006). TGFB1 also regulates the production of vascular endothelial growth factor (VEGF) and this may contribute to PSG1-induced VEGF-A secretion (Ha et al. 2010). Therefore the pro-angiogenic properties of some PSGs are mediated by two different mechanisms, TGF-beta mediated induction of VEGF-A, and direct interaction of PSGs with GAGs on the surface of endothelial cells.
SELE ligandsR-HSA-2870221 (Reactome)
SELER-HSA-2870221 (Reactome)
SELPLGR-HSA-202724 (Reactome)
SHC1R-HSA-204861 (Reactome)
SOS-1 bound to Tie2:Grb2ArrowR-HSA-210974 (Reactome)
SOS-1 bound to Tie2:Grb2mim-catalysisR-HSA-210977 (Reactome)
SOS1R-HSA-210974 (Reactome)
SPNR-HSA-204465 (Reactome)
Selectins:2xSELPGArrowR-HSA-202724 (Reactome)
SelectinsR-HSA-202724 (Reactome)
Src family tyrosine kinases (SFKs)mim-catalysisR-HSA-210291 (Reactome)
TEKR-HSA-204779 (Reactome)
TEKR-HSA-204824 (Reactome)
TEKR-HSA-204863 (Reactome)
TNFRSF10A,B:TNFRSF10DArrowR-HSA-5635741 (Reactome)
TNFRSF10A,TNFRSF10BR-HSA-5635741 (Reactome)
TNFRSF10DR-HSA-5635741 (Reactome)
TREM-1 bound to its ligandArrowR-HSA-203156 (Reactome)
TREM1R-HSA-203156 (Reactome)
TSPAN7:PICK1ArrowR-HSA-8858435 (Reactome)
TSPAN7R-HSA-8858435 (Reactome)
Tie2 and Dok-2 complexArrowR-HSA-204850 (Reactome)
Tie2 and Grb14 complexArrowR-HSA-204813 (Reactome)
Tie2:Grb7 complexArrowR-HSA-204773 (Reactome)
activated thrombin:thrombomodulinmim-catalysisR-HSA-141040 (Reactome)
eba-175,ebl1,eba-140R-HSA-8867098 (Reactome)
integrin alpha4beta1:JAM2:JAM3ArrowR-HSA-202706 (Reactome)
opa proteinsR-HSA-8867135 (Reactome)
p-Y663,Y686-PECAM1 dimerArrowR-HSA-210291 (Reactome)
p-Y663,Y686-PECAM1(27-?)R-HSA-210277 (Reactome)
p-Y663,Y686-PECAM1(27-?)R-HSA-210283 (Reactome)
p-Y663,Y686-PECAM1(27-?)R-HSA-210290 (Reactome)
p-Y663,Y686-PECAM1(27-?)R-HSA-210294 (Reactome)
p21 RAS:GDPR-HSA-210977 (Reactome)
p21 RAS:GTPArrowR-HSA-210977 (Reactome)
p85 bound to Tie2ArrowR-HSA-204798 (Reactome)
pTie2 and SHP2 complexArrowR-HSA-204873 (Reactome)

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