Complement cascade (Homo sapiens)

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1. Chen CB, Wallis R.; ''Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation.''; PubMed Europe PMC Scholia
2. Liu Y, Endo Y, Iwaki D, Nakata M, Matsushita M, Wada I, Inoue K, Munakata M, Fujita T.; ''Human M-ficolin is a secretory protein that activates the lectin complement pathway.''; PubMed Europe PMC Scholia
3. Law SK, Levine RP.; ''Interaction between the third complement protein and cell surface macromolecules.''; PubMed Europe PMC Scholia
4. Fujita T, Gigli I, Nussenzweig V.; ''Human C4-binding protein. II. Role in proteolysis of C4b by C3b-inactivator.''; PubMed Europe PMC Scholia
5. Kuraya M, Ming Z, Liu X, Matsushita M, Fujita T.; ''Specific binding of L-ficolin and H-ficolin to apoptotic cells leads to complement activation.''; PubMed Europe PMC Scholia
6. Tsujimura M, Miyazaki T, Kojima E, Sagara Y, Shiraki H, Okochi K, Maeda Y.; ''Serum concentration of Hakata antigen, a member of the ficolins, is linked with inhibition of Aerococcus viridans growth.''; PubMed Europe PMC Scholia
7. Hourcade DE, Mitchell L, Kuttner-Kondo LA, Atkinson JP, Medof ME.; ''Decay-accelerating factor (DAF), complement receptor 1 (CR1), and factor H dissociate the complement AP C3 convertase (C3bBb) via sites on the type A domain of Bb.''; PubMed Europe PMC Scholia
8. Aleshin AE, DiScipio RG, Stec B, Liddington RC.; ''Crystal structure of C5b-6 suggests structural basis for priming assembly of the membrane attack complex.''; PubMed Europe PMC Scholia
9. Campbell WD, Lazoura E, Okada N, Okada H.; ''Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.''; PubMed Europe PMC Scholia
10. Daha MR, Fearon DT, Austen KF.; ''C3 requirements for formation of alternative pathway C5 convertase.''; PubMed Europe PMC Scholia
11. Rawal N, Pangburn MK.; ''Formation of high affinity C5 convertase of the classical pathway of complement.''; PubMed Europe PMC Scholia
12. Alcorlo M, Tortajada A, Rodríguez de Córdoba S, Llorca O.; ''Structural basis for the stabilization of the complement alternative pathway C3 convertase by properdin.''; PubMed Europe PMC Scholia
13. Teillet F, Gaboriaud C, Lacroix M, Martin L, Arlaud GJ, Thielens NM.; ''Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins.''; PubMed Europe PMC Scholia
14. Scharfstein J, Ferreira A, Gigli I, Nussenzweig V.; ''Human C4-binding protein. I. Isolation and characterization.''; PubMed Europe PMC Scholia
15. Krisinger MJ, Goebeler V, Lu Z, Meixner SC, Myles T, Pryzdial EL, Conway EM.; ''Thrombin generates previously unidentified C5 products that support the terminal complement activation pathway.''; PubMed Europe PMC Scholia
16. DiScipio RG, Davie EW.; ''Characterization of protein S, a gamma-carboxyglutamic acid containing protein from bovine and human plasma.''; PubMed Europe PMC Scholia
17. Zacho RM, Jensen L, Terp R, Jensenius JC, Thiel S.; ''Studies of the pattern recognition molecule H-ficolin: specificity and purification.''; PubMed Europe PMC Scholia
18. Ziccardi RJ, Dahlback B, Müller-Eberhard HJ.; ''Characterization of the interaction of human C4b-binding protein with physiological ligands.''; PubMed Europe PMC Scholia
19. Aoyagi Y, Adderson EE, Rubens CE, Bohnsack JF, Min JG, Matsushita M, Fujita T, Okuwaki Y, Takahashi S.; ''L-Ficolin/mannose-binding lectin-associated serine protease complexes bind to group B streptococci primarily through N-acetylneuraminic acid of capsular polysaccharide and activate the complement pathway.''; PubMed Europe PMC Scholia
20. Weiler JM, Daha MR, Austen KF, Fearon DT.; ''Control of the amplification convertase of complement by the plasma protein beta1H.''; PubMed Europe PMC Scholia
21. Kjaer TR, Hansen AG, Sørensen UB, Nielsen O, Thiel S, Jensenius JC.; ''Investigations on the pattern recognition molecule M-ficolin: quantitative aspects of bacterial binding and leukocyte association.''; PubMed Europe PMC Scholia
22. Lynch NJ, Roscher S, Hartung T, Morath S, Matsushita M, Maennel DN, Kuraya M, Fujita T, Schwaeble WJ.; ''L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of Gram-positive bacteria, and activates the lectin pathway of complement.''; PubMed Europe PMC Scholia
23. Law SK, Lichtenberg NA, Holcombe FH, Levine RP.; ''Interaction between the labile binding sites of the fourth (C4) and fifth (C5) human complement proteins and erythrocyte cell membranes.''; PubMed Europe PMC Scholia
24. Gigli I, Fujita T, Nussenzweig V.; ''Modulation of the classical pathway C3 convertase by plasma proteins C4 binding protein and C3b inactivator.''; PubMed Europe PMC Scholia
25. Keshi H, Sakamoto T, Kawai T, Ohtani K, Katoh T, Jang SJ, Motomura W, Yoshizaki T, Fukuda M, Koyama S, Fukuzawa J, Fukuoh A, Yoshida I, Suzuki Y, Wakamiya N.; ''Identification and characterization of a novel human collectin CL-K1.''; PubMed Europe PMC Scholia
26. Masaki T, Matsumoto M, Nakanishi I, Yasuda R, Seya T.; ''Factor I-dependent inactivation of human complement C4b of the classical pathway by C3b/C4b receptor (CR1, CD35) and membrane cofactor protein (MCP, CD46).''; PubMed Europe PMC Scholia
27. Vorup-Jensen T, Petersen SV, Hansen AG, Poulsen K, Schwaeble W, Sim RB, Reid KB, Davis SJ, Thiel S, Jensenius JC.; ''Distinct pathways of mannan-binding lectin (MBL)- and C1-complex autoactivation revealed by reconstitution of MBL with recombinant MBL-associated serine protease-2.''; PubMed Europe PMC Scholia
28. Scibek JJ, Plumb ME, Sodetz JM.; ''Binding of human complement C8 to C9: role of the N-terminal modules in the C8 alpha subunit.''; PubMed Europe PMC Scholia
29. Alcorlo M, Martínez-Barricarte R, Fernández FJ, Rodríguez-Gallego C, Round A, Vega MC, Harris CL, de Cordoba SR, Llorca O.; ''Unique structure of iC3b resolved at a resolution of 24 Å by 3D-electron microscopy.''; PubMed Europe PMC Scholia
30. Dahlbäck B, Smith CA, Müller-Eberhard HJ.; ''Visualization of human C4b-binding protein and its complexes with vitamin K-dependent protein S and complement protein C4b.''; PubMed Europe PMC Scholia
31. Goldberger G, Bruns GA, Rits M, Edge MD, Kwiatkowski DJ.; ''Human complement factor I: analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4.''; PubMed Europe PMC Scholia
32. Honoré C, Rørvig S, Hummelshøj T, Skjoedt MO, Borregaard N, Garred P.; ''Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain.''; PubMed Europe PMC Scholia
33. Lehto T, Morgan BP, Meri S.; ''Binding of human and rat CD59 to the terminal complement complexes.''; PubMed Europe PMC Scholia
34. Sim RB, Reboul A, Arlaud GJ, Villiers CL, Colomb MG.; ''Interaction of 125I-labelled complement subcomponents C-1r and C-1s with protease inhibitors in plasma.''; PubMed Europe PMC Scholia
35. Kalant D, Cain SA, Maslowska M, Sniderman AD, Cianflone K, Monk PN.; ''The chemoattractant receptor-like protein C5L2 binds the C3a des-Arg77/acylation-stimulating protein.''; PubMed Europe PMC Scholia
36. Davis AE, Harrison RA, Lachmann PJ.; ''Physiologic inactivation of fluid phase C3b: isolation and structural analysis of C3c, C3d,g (alpha 2D), and C3g.''; PubMed Europe PMC Scholia
37. Kishore U, Ghai R, Greenhough TJ, Shrive AK, Bonifati DM, Gadjeva MG, Waters P, Kojouharova MS, Chakraborty T, Agrawal A.; ''Structural and functional anatomy of the globular domain of complement protein C1q.''; PubMed Europe PMC Scholia
38. Ziccardi RJ, Cooper NR.; ''Activation of C1r by proteolytic cleavage.''; PubMed Europe PMC Scholia
39. Teh C, Le Y, Lee SH, Lu J.; ''M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-D-glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli.''; PubMed Europe PMC Scholia
40. Jokiranta TS, Cheng ZZ, Seeberger H, Jòzsi M, Heinen S, Noris M, Remuzzi G, Ormsby R, Gordon DL, Meri S, Hellwage J, Zipfel PF.; ''Binding of complement factor H to endothelial cells is mediated by the carboxy-terminal glycosaminoglycan binding site.''; PubMed Europe PMC Scholia
41. Butkowski RJ, Elion J, Downing MR, Mann KG.; ''Primary structure of human prethrombin 2 and alpha-thrombin.''; PubMed Europe PMC Scholia
42. Fearon DT.; ''Regulation of the amplification C3 convertase of human complement by an inhibitory protein isolated from human erythrocyte membrane.''; PubMed Europe PMC Scholia
43. Bokisch VA, Müller-Eberhard HJ.; ''Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase.''; PubMed Europe PMC Scholia
44. Bhakdi S, Käflein R, Halstensen TS, Hugo F, Preissner KT, Mollnes TE.; ''Complement S-protein (vitronectin) is associated with cytolytic membrane-bound C5b-9 complexes.''; PubMed Europe PMC Scholia
45. Teillet F, Dublet B, Andrieu JP, Gaboriaud C, Arlaud GJ, Thielens NM.; ''The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases.''; PubMed Europe PMC Scholia
46. Dahlbäck B, Stenflo J.; ''High molecular weight complex in human plasma between vitamin K-dependent protein S and complement component C4b-binding protein.''; PubMed Europe PMC Scholia
47. Müller-Eberhard HJ.; ''Molecular organization and function of the complement system.''; PubMed Europe PMC Scholia
48. Gasque P.; ''Complement: a unique innate immune sensor for danger signals.''; PubMed Europe PMC Scholia
49. Sheehan M, Morris CA, Pussell BA, Charlesworth JA.; ''Complement inhibition by human vitronectin involves non-heparin binding domains.''; PubMed Europe PMC Scholia
50. Nagasawa S, Ichihara C, Stroud RM.; ''Cleavage of C4b by C3b inactivator: production of a nicked form of C4b, C4b', as an intermediate cleavage product of C4b by C3b inactivator.''; PubMed Europe PMC Scholia
51. Kishore U, Reid KB.; ''C1q: structure, function, and receptors.''; PubMed Europe PMC Scholia
52. Nonaka M, Yoshizaki F.; ''Evolution of the complement system.''; PubMed Europe PMC Scholia
53. Matsumoto AK, Martin DR, Carter RH, Klickstein LB, Ahearn JM, Fearon DT.; ''Functional dissection of the CD21/CD19/TAPA-1/Leu-13 complex of B lymphocytes.''; PubMed Europe PMC Scholia
54. Garlatti V, Martin L, Lacroix M, Gout E, Arlaud GJ, Thielens NM, Gaboriaud C.; ''Structural insights into the recognition properties of human ficolins.''; PubMed Europe PMC Scholia
55. Farries TC, Lachmann PJ, Harrison RA.; ''Analysis of the interactions between properdin, the third component of complement (C3), and its physiological activation products.''; PubMed Europe PMC Scholia
56. Tschopp J, Chonn A, Hertig S, French LE.; ''Clusterin, the human apolipoprotein and complement inhibitor, binds to complement C7, C8 beta, and the b domain of C9.''; PubMed Europe PMC Scholia
57. Wu J, Wu YQ, Ricklin D, Janssen BJ, Lambris JD, Gros P.; ''Structure of complement fragment C3b-factor H and implications for host protection by complement regulators.''; PubMed Europe PMC Scholia
58. Fearon DT, Austen KF.; ''Initiation of C3 cleavage in the alternative complement pathway.''; PubMed Europe PMC Scholia
59. Wittenborn T, Thiel S, Jensen L, Nielsen HJ, Jensenius JC.; ''Characteristics and biological variations of M-ficolin, a pattern recognition molecule, in plasma.''; PubMed Europe PMC Scholia
60. Budayova-Spano M, Lacroix M, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C.; ''The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex.''; PubMed Europe PMC Scholia
61. Ma YG, Cho MY, Zhao M, Park JW, Matsushita M, Fujita T, Lee BL.; ''Human mannose-binding lectin and L-ficolin function as specific pattern recognition proteins in the lectin activation pathway of complement.''; PubMed Europe PMC Scholia
62. Matsushita M, Kuraya M, Hamasaki N, Tsujimura M, Shiraki H, Fujita T.; ''Activation of the lectin complement pathway by H-ficolin (Hakata antigen).''; PubMed Europe PMC Scholia
63. Petersen SV, Thiel S, Jensenius JC.; ''The mannan-binding lectin pathway of complement activation: biology and disease association.''; PubMed Europe PMC Scholia
64. Preissner KP, Podack ER, Müller-Eberhard HJ.; ''SC5b-7, SC5b-8 and SC5b-9 complexes of complement: ultrastructure and localization of the S-protein (vitronectin) within the macromolecules.''; PubMed Europe PMC Scholia
65. Ross GD, Lambris JD, Cain JA, Newman SL.; ''Generation of three different fragments of bound C3 with purified factor I or serum. I. Requirements for factor H vs CR1 cofactor activity.''; PubMed Europe PMC Scholia
66. Huang Y, Fedarovich A, Tomlinson S, Davies C.; ''Crystal structure of CD59: implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex.''; PubMed Europe PMC Scholia
67. Pangburn MK, Schreiber RD, Müller-Eberhard HJ.; ''Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein beta1H for cleavage of C3b and C4b in solution.''; PubMed Europe PMC Scholia
68. Lehto T, Meri S.; ''Interactions of soluble CD59 with the terminal complement complexes. CD59 and C9 compete for a nascent epitope on C8.''; PubMed Europe PMC Scholia
69. Hadders MA, Bubeck D, Roversi P, Hakobyan S, Forneris F, Morgan BP, Pangburn MK, Llorca O, Lea SM, Gros P.; ''Assembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9.''; PubMed Europe PMC Scholia
70. Krych-Goldberg M, Hauhart RE, Subramanian VB, Yurcisin BM, Crimmins DL, Hourcade DE, Atkinson JP.; ''Decay accelerating activity of complement receptor type 1 (CD35). Two active sites are required for dissociating C5 convertases.''; PubMed Europe PMC Scholia
71. Schmidt BZ, Colten HR.; ''Complement: a critical test of its biological importance.''; PubMed Europe PMC Scholia
72. Schreiber RD, Pangburn MK, Lesavre PH, Müller-Eberhard HJ.; ''Initiation of the alternative pathway of complement: recognition of activators by bound C3b and assembly of the entire pathway from six isolated proteins.''; PubMed Europe PMC Scholia
73. Kerr MA.; ''The human complement system: assembly of the classical pathway C3 convertase.''; PubMed Europe PMC Scholia
74. Lesavre PH, Müller-Eberhard HJ.; ''Mechanism of action of factor D of the alternative complement pathway.''; PubMed Europe PMC Scholia
75. Huang Y, Smith CA, Song H, Morgan BP, Abagyan R, Tomlinson S.; ''Insights into the human CD59 complement binding interface toward engineering new therapeutics.''; PubMed Europe PMC Scholia
76. Fujita T, Matsushita M, Endo Y.; ''The lectin-complement pathway--its role in innate immunity and evolution.''; PubMed Europe PMC Scholia
77. Ponnuraj K, Xu Y, Macon K, Moore D, Volanakis JE, Narayana SV.; ''Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase.''; PubMed Europe PMC Scholia
78. Neth O, Jack DL, Dodds AW, Holzel H, Klein NJ, Turner MW.; ''Mannose-binding lectin binds to a range of clinically relevant microorganisms and promotes complement deposition.''; PubMed Europe PMC Scholia
79. Mold C, Medof ME.; ''C3 nephritic factor protects bound C3bBb from cleavage by factor I and human erythrocytes.''; PubMed Europe PMC Scholia
80. Podack ER, Tschoop J, Müller-Eberhard HJ.; ''Molecular organization of C9 within the membrane attack complex of complement. Induction of circular C9 polymerization by the C5b-8 assembly.''; PubMed Europe PMC Scholia
81. Morgan HP, Schmidt CQ, Guariento M, Blaum BS, Gillespie D, Herbert AP, Kavanagh D, Mertens HD, Svergun DI, Johansson CM, Uhrín D, Barlow PN, Hannan JP.; ''Structural basis for engagement by complement factor H of C3b on a self surface.''; PubMed Europe PMC Scholia
82. Seya T, Atkinson JP.; ''Functional properties of membrane cofactor protein of complement.''; PubMed Europe PMC Scholia
83. Harris CL, Pettigrew DM, Lea SM, Morgan BP.; ''Decay-accelerating factor must bind both components of the complement alternative pathway C3 convertase to mediate efficient decay.''; PubMed Europe PMC Scholia
84. Brodbeck WG, Liu D, Sperry J, Mold C, Medof ME.; ''Localization of classical and alternative pathway regulatory activity within the decay-accelerating factor.''; PubMed Europe PMC Scholia
85. MUELLER-EBERHARD HJ, LEPOW IH.; ''C'1 ESTERASE EFFECT ON ACTIVITY AND PHYSICOCHEMICAL PROPERTIES OF THE FOURTH COMPONENT OF COMPLEMENT.''; PubMed Europe PMC Scholia
86. Nagasawa S, Stroud RM.; ''Cleavage of C2 by C1s into the antigenically distinct fragments C2a and C2b: demonstration of binding of C2b to C4b.''; PubMed Europe PMC Scholia
87. Troegeler A, Lugo-Villarino G, Hansen S, Rasolofo V, Henriksen ML, Mori K, Ohtani K, Duval C, Mercier I, Bénard A, Nigou J, Hudrisier D, Wakamiya N, Neyrolles O.; ''Collectin CL-LK Is a Novel Soluble Pattern Recognition Receptor for Mycobacterium tuberculosis.''; PubMed Europe PMC Scholia
88. Müller-Eberhard HJ, Polley MJ, Calcott MA.; ''Formation and functional significance of a molecular complex derived from the second and the fourth component of human complement.''; PubMed Europe PMC Scholia
89. Pangburn MK, Schreiber RD, Müller-Eberhard HJ.; ''Formation of the initial C3 convertase of the alternative complement pathway. Acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3.''; PubMed Europe PMC Scholia
90. Gerard NP, Gerard C.; ''The chemotactic receptor for human C5a anaphylatoxin.''; PubMed Europe PMC Scholia
91. Garlatti V, Martin L, Gout E, Reiser JB, Fujita T, Arlaud GJ, Thielens NM, Gaboriaud C.; ''Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch.''; PubMed Europe PMC Scholia
92. Weis JJ, Tedder TF, Fearon DT.; ''Identification of a 145,000 Mr membrane protein as the C3d receptor (CR2) of human B lymphocytes.''; PubMed Europe PMC Scholia
93. Medicus RG, Götze O, Müller-Eberhard HJ.; ''Alternative pathway of complement: recruitment of precursor properdin by the labile C3/C5 convertase and the potentiation of the pathway.''; PubMed Europe PMC Scholia
94. Barilla-LaBarca ML, Liszewski MK, Lambris JD, Hourcade D, Atkinson JP.; ''Role of membrane cofactor protein (CD46) in regulation of C4b and C3b deposited on cells.''; PubMed Europe PMC Scholia
95. Becherer JD, Lambris JD.; ''Identification of the C3b receptor-binding domain in third component of complement.''; PubMed Europe PMC Scholia
96. Matsushita M, Endo Y, Fujita T.; ''Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease.''; PubMed Europe PMC Scholia
97. Hajela K, Kojima M, Ambrus G, Wong KH, Moffatt BE, Ferluga J, Hajela S, Gál P, Sim RB.; ''The biological functions of MBL-associated serine proteases (MASPs).''; PubMed Europe PMC Scholia
98. Sepp A, Dodds AW, Anderson MJ, Campbell RD, Willis AC, Law SK.; ''Covalent binding properties of the human complement protein C4 and hydrolysis rate of the internal thioester upon activation.''; PubMed Europe PMC Scholia
99. Cain SA, Monk PN.; ''The orphan receptor C5L2 has high affinity binding sites for complement fragments C5a and C5a des-Arg(74).''; PubMed Europe PMC Scholia
100. Kinoshita T, Medof ME, Nussenzweig V.; ''Endogenous association of decay-accelerating factor (DAF) with C4b and C3b on cell membranes.''; PubMed Europe PMC Scholia
101. Garlatti V, Belloy N, Martin L, Lacroix M, Matsushita M, Endo Y, Fujita T, Fontecilla-Camps JC, Arlaud GJ, Thielens NM, Gaboriaud C.; ''Structural insights into the innate immune recognition specificities of L- and H-ficolins.''; PubMed Europe PMC Scholia
102. Ziccardi RJ, Cooper NR.; ''Physicochemical and functional characterization of the C1r subunit of the first complement component.''; PubMed Europe PMC Scholia
103. Pangburn MK, Müller-Eberhard HJ.; ''Kinetic and thermodynamic analysis of the control of C3b by the complement regulatory proteins factors H and I.''; PubMed Europe PMC Scholia
104. Medof ME, Kinoshita T, Nussenzweig V.; ''Inhibition of complement activation on the surface of cells after incorporation of decay-accelerating factor (DAF) into their membranes.''; PubMed Europe PMC Scholia
105. Goicoechea de Jorge E, Caesar JJ, Malik TH, Patel M, Colledge M, Johnson S, Hakobyan S, Morgan BP, Harris CL, Pickering MC, Lea SM.; ''Dimerization of complement factor H-related proteins modulates complement activation in vivo.''; PubMed Europe PMC Scholia
106. Degen SJ, Davie EW.; ''Nucleotide sequence of the gene for human prothrombin.''; PubMed Europe PMC Scholia
107. Forneris F, Ricklin D, Wu J, Tzekou A, Wallace RS, Lambris JD, Gros P.; ''Structures of C3b in complex with factors B and D give insight into complement convertase formation.''; PubMed Europe PMC Scholia
108. Smith CA, Pangburn MK, Vogel CW, Müller-Eberhard HJ.; ''Molecular architecture of human properdin, a positive regulator of the alternative pathway of complement.''; PubMed Europe PMC Scholia
109. Gout E, Garlatti V, Smith DF, Lacroix M, Dumestre-Pérard C, Lunardi T, Martin L, Cesbron JY, Arlaud GJ, Gaboriaud C, Thielens NM.; ''Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin.''; PubMed Europe PMC Scholia
110. Honoré C, Rørvig S, Munthe-Fog L, Hummelshøj T, Madsen HO, Borregaard N, Garred P.; ''The innate pattern recognition molecule Ficolin-1 is secreted by monocytes/macrophages and is circulating in human plasma.''; PubMed Europe PMC Scholia
111. Christmas SE, Christmas SE, de la Mata Espinosa CT, Halliday D, Buxton CA, Cummerson JA, Johnson PM.; ''Levels of expression of complement regulatory proteins CD46, CD55 and CD59 on resting and activated human peripheral blood leucocytes.''; PubMed Europe PMC Scholia
112. Sim RB, Laich A.; ''Serine proteases of the complement system.''; PubMed Europe PMC Scholia
113. Ames RS, Li Y, Sarau HM, Nuthulaganti P, Foley JJ, Ellis C, Zeng Z, Su K, Jurewicz AJ, Hertzberg RP, Bergsma DJ, Kumar C.; ''Molecular cloning and characterization of the human anaphylatoxin C3a receptor.''; PubMed Europe PMC Scholia
114. Dodds AW, Ren XD, Willis AC, Law SK.; ''The reaction mechanism of the internal thioester in the human complement component C4.''; PubMed Europe PMC Scholia
115. Arlaud GJ, Reboul A, Sim RB, Colomb MG.; ''Interaction of C1-inhibitor with the C1r and C1s subcomponents in human C1.''; PubMed Europe PMC Scholia

History

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Compare	Revision	Action	Time	User	Comment
	115062	view	17:00, 25 January 2021	ReactomeTeam	Reactome version 75
	113506	view	11:58, 2 November 2020	ReactomeTeam	Reactome version 74
	112706	view	16:10, 9 October 2020	ReactomeTeam	Reactome version 73
	101621	view	11:49, 1 November 2018	ReactomeTeam	reactome version 66
	101157	view	21:35, 31 October 2018	ReactomeTeam	reactome version 65
	100683	view	20:08, 31 October 2018	ReactomeTeam	reactome version 64
	100233	view	16:53, 31 October 2018	ReactomeTeam	reactome version 63
	99785	view	15:18, 31 October 2018	ReactomeTeam	reactome version 62 (2nd attempt)
	99338	view	12:47, 31 October 2018	ReactomeTeam	reactome version 62
	93740	view	13:33, 16 August 2017	ReactomeTeam	reactome version 61
	93254	view	11:18, 9 August 2017	ReactomeTeam	reactome version 61
	86332	view	09:15, 11 July 2016	ReactomeTeam	reactome version 56
	83391	view	11:06, 18 November 2015	ReactomeTeam	Version54
	81582	view	13:07, 21 August 2015	ReactomeTeam	Version53
	77042	view	08:34, 17 July 2014	ReactomeTeam	Fixed remaining interactions
	76747	view	12:11, 16 July 2014	ReactomeTeam	Fixed remaining interactions
	76072	view	10:13, 11 June 2014	ReactomeTeam	Re-fixing comment source
	75782	view	11:30, 10 June 2014	ReactomeTeam	Reactome 48 Update
	75419	view	10:07, 29 May 2014	Lifish	Modified description
	75132	view	14:08, 8 May 2014	Anwesha	Fixing comment source for displaying WikiPathways description
	74779	view	08:52, 30 April 2014	ReactomeTeam	Reactome46
	44996	view	14:41, 6 October 2011	MartijnVanIersel	Ontology Term : 'signaling pathway in the innate immune response' added !
	42021	view	21:50, 4 March 2011	MaintBot	Automatic update
	39824	view	05:51, 21 January 2011	MaintBot	New pathway

External references

DataNodes

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Name	Type	Database reference	Comment
1,3-beta-D-glucan [plasma membrane]	Metabolite	CHEBI:37671 (ChEBI)
11xCbxE-PROS1 [extracellular region]	Protein	P07225 (Uniprot-TrEMBL)
11xCbxE-PROS1	Protein	P07225 (Uniprot-TrEMBL)
Antigen: antibody: C1 (activated C1R and C1S) complex	Complex	REACT_8066 (Reactome)
Antigen: antibody: C1 (activated C1R) complex	Complex	REACT_8973 (Reactome)
Antigen: antibody: C1 complex	Complex	REACT_8034 (Reactome)
Bacterial mannose-based carbohydrate surface pattern		REACT_8923 (Reactome)
C-reactive protein pentamer:phosphocholine:C1Q	Complex	REACT_25403 (Reactome)
C1QA [extracellular region]	Protein	P02745 (Uniprot-TrEMBL)
C1QB(26-251) [extracellular region]	Protein	P02746 (Uniprot-TrEMBL)
C1QC [extracellular region]	Protein	P02747 (Uniprot-TrEMBL)
C1R C-terminal fragment [extracellular region]	Protein	P00736 (Uniprot-TrEMBL)
C1R N-terminal fragment [extracellular region]	Protein	P00736 (Uniprot-TrEMBL)
C1R(18-705) [extracellular region]	Protein	P00736 (Uniprot-TrEMBL)
C1S C-terminal fragment [extracellular region]	Protein	P09871 (Uniprot-TrEMBL)
C1S N-terminal fragment [extracellular region]	Protein	P09871 (Uniprot-TrEMBL)
C1S(16-688) [extracellular region]	Protein	P09871 (Uniprot-TrEMBL)
C2	Protein	P06681 (Uniprot-TrEMBL)
C2a [extracellular region]	Protein	P06681 (Uniprot-TrEMBL)
C2a	Protein	P06681 (Uniprot-TrEMBL)
C2b	Protein	P06681 (Uniprot-TrEMBL)
C3 alpha chain [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
C3 beta chain [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
C3 beta chain [plasma membrane]	Protein	P01024 (Uniprot-TrEMBL)
C3 convertases		REACT_8751 (Reactome)
C3(H2O):Factor B	Complex	REACT_8649 (Reactome)
C3(H2O):Factor Bb	Complex	REACT_8857 (Reactome)
C3(H2O)	Complex	REACT_8268 (Reactome)
C3a	Protein	P01024 (Uniprot-TrEMBL)
C3b alpha' [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
C3b:Factor Bb:C3b:Properdin complex	Complex	REACT_8784 (Reactome)
C3b	Complex	REACT_8621 (Reactome)	Linked by disulphide bond between positions 559 and 816.
C3c alpha' chain fragment 1 [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
C3c alpha' chain fragment 1 precursor [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
C3c alpha' chain fragment 1 precursor [plasma membrane]	Protein	P01024 (Uniprot-TrEMBL)
C3c alpha' chain fragment 2 [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
C3c alpha' chain fragment 2 [plasma membrane]	Protein	P01024 (Uniprot-TrEMBL)
C3c	Complex	REACT_164188 (Reactome)
C3dg	Protein	P01024 (Uniprot-TrEMBL)
C3f [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
C3f	Protein	P01024 (Uniprot-TrEMBL)
C4 activator		REACT_8154 (Reactome)
C4 alpha [extracellular region]	Protein	P0C0L4 (Uniprot-TrEMBL)	C4 alpha chain has a thioester bond between Cys 1010 and Gln 1013
C4 binding protein:C4bC2a	Complex	REACT_120190 (Reactome)
C4 binding protein:protein S	Complex	REACT_119894 (Reactome)
C4-binding protein:C4b	Complex	REACT_118966 (Reactome)
C4A alpha b [extracellular region]	Protein	P0C0L4 (Uniprot-TrEMBL)	C4 alpha chain has a thioester bond between Cys 1010 and Gln 1013
C4A alpha3 [extracellular region]	Protein	P0C0L4 (Uniprot-TrEMBL)
C4A alpha4 fragment [extracellular region]	Protein	P0C0L4 (Uniprot-TrEMBL)
C4A beta [extracellular region]	Protein	P0C0L4 (Uniprot-TrEMBL)
C4A gamma [extracellular region]	Protein	P0C0L4 (Uniprot-TrEMBL)
C4B alpha [extracellular region]	Protein	P0C0L5 (Uniprot-TrEMBL)
C4B alpha chain fragment b [extracellular region]	Protein	P0C0L5 (Uniprot-TrEMBL)
C4B alpha3 [extracellular region]	Protein	P0C0L5 (Uniprot-TrEMBL)
C4B alpha4 fragment [extracellular region]	Protein	P0C0L5 (Uniprot-TrEMBL)
C4B beta [extracellular region]	Protein	P0C0L5 (Uniprot-TrEMBL)
C4B gamma [extracellular region]	Protein	P0C0L5 (Uniprot-TrEMBL)
C4BPA [plasma membrane]	Protein	P04003 (Uniprot-TrEMBL)
C4BPB [plasma membrane]	Protein	P20851 (Uniprot-TrEMBL)
C4a	Protein	REACT_25991 (Reactome)
C4b with hydrolysed thioester	Complex	REACT_164040 (Reactome)
C4b, C3b	Complex	REACT_119260 (Reactome)
C4b-binding protein:Factor I	Complex	REACT_119445 (Reactome)
C4b-binding protein	Complex	REACT_120080 (Reactome)
C4b:C2a:C3b	Complex	REACT_8556 (Reactome)
C4bC2a, C3bBb	Complex	REACT_119171 (Reactome)
C4c, C3f	Complex	REACT_119917 (Reactome)
C4c	Complex	REACT_119729 (Reactome)
C4d, iC3b	Protein	REACT_119732 (Reactome)
C4d	Protein	REACT_119059 (Reactome)
C5 alpha [extracellular region]	Protein	P01031 (Uniprot-TrEMBL)
C5 beta [extracellular region]	Protein	P01031 (Uniprot-TrEMBL)
C5 convertases		REACT_8864 (Reactome)
C5a	Protein	P01031 (Uniprot-TrEMBL)
C5b alpha' [extracellular region]	Protein	P01031 (Uniprot-TrEMBL)
C5b:C6 complex	Complex	REACT_8500 (Reactome)
C5b:C6:C7 complex	Complex	REACT_8333 (Reactome)
C5b:C6:C7 complex	Complex	REACT_8454 (Reactome)
C5b:C6:C7:C8 complex	Complex	REACT_8352 (Reactome)
C5b	Complex	REACT_8814 (Reactome)	Linked by disulphide bond between positions 559 and 816.
C6 [extracellular region]	Protein	P13671 (Uniprot-TrEMBL)
C6	Protein	P13671 (Uniprot-TrEMBL)
C7(22-843) [extracellular region]	Protein	P10643 (Uniprot-TrEMBL)
C7(22-843)	Protein	P10643 (Uniprot-TrEMBL)
C8A [extracellular region]	Protein	P07357 (Uniprot-TrEMBL)
C8B [extracellular region]	Protein	P07358 (Uniprot-TrEMBL)
C8G [extracellular region]	Protein	P07360 (Uniprot-TrEMBL)
C8	Complex	REACT_8563 (Reactome)
C9(22-559) [extracellular region]	Protein	P02748 (Uniprot-TrEMBL)
C9(22-559)	Protein	P02748 (Uniprot-TrEMBL)
CD46 [plasma membrane]	Protein	P15529 (Uniprot-TrEMBL)
CD46	Protein	P15529 (Uniprot-TrEMBL)
CD55 [plasma membrane]	Protein	P08174 (Uniprot-TrEMBL)
CD55	Protein	P08174 (Uniprot-TrEMBL)
CD59 [plasma membrane]	Protein	P13987 (Uniprot-TrEMBL)
CD59:C5b-C9	Complex	REACT_164087 (Reactome)
CD59	Protein	P13987 (Uniprot-TrEMBL)
CFB(26-259)	Protein	P00751 (Uniprot-TrEMBL)
CFB(26-764) [extracellular region]	Protein	P00751 (Uniprot-TrEMBL)
CFB(26-764)	Protein	P00751 (Uniprot-TrEMBL)
CFB(260-764) [extracellular region]	Protein	P00751 (Uniprot-TrEMBL)
CFB(260-764) [plasma membrane]	Protein	P00751 (Uniprot-TrEMBL)
CFB(260-764)	Protein	P00751 (Uniprot-TrEMBL)
CFD	Protein	P00746 (Uniprot-TrEMBL)
CFH [extracellular region]	Protein	P08603 (Uniprot-TrEMBL)
CFH	Protein	P08603 (Uniprot-TrEMBL)
CFI(19-335) [extracellular region]	Protein	P05156 (Uniprot-TrEMBL)
CFI(19-335)	Protein	P05156 (Uniprot-TrEMBL)
CFI(340-583) [extracellular region]	Protein	P05156 (Uniprot-TrEMBL)
CFI(340-583)	Protein	P05156 (Uniprot-TrEMBL)
CR1 [plasma membrane]	Protein	P17927 (Uniprot-TrEMBL)
CR1:C3bBb, C4bC2a complexes	Complex	REACT_120030 (Reactome)
CR1:C3b	Complex	REACT_119014 (Reactome)
CR1:C4b	Complex	REACT_119535 (Reactome)
CR1:iC3b	Complex	REACT_164751 (Reactome)
CR1	Protein	P17927 (Uniprot-TrEMBL)
CRP(19-224) [extracellular region]	Protein	P02741 (Uniprot-TrEMBL)
Ca2+ [extracellular region]	Metabolite	CHEBI:29108 (ChEBI)
Ca2+	Metabolite	CHEBI:29108 (ChEBI)
Cell surface:C3b:Factor Bb:Properdin	Complex	REACT_8531 (Reactome)
Cell surface:C3b:Factor Bb	Complex	REACT_8668 (Reactome)
Cell surface:C3b:Factor B complex	Complex	REACT_8205 (Reactome)
Cell surface:FH,FHR3:C3bBb	Complex	REACT_118983 (Reactome)
Cell surface:FH,FHR3:C3b	Complex	REACT_119386 (Reactome)
Cell surface:C3b	Complex	REACT_26114 (Reactome)
Cell surface:C4b:C2a	Complex	REACT_8917 (Reactome)
Cell surface:C4b	Complex	REACT_25739 (Reactome)
Cell surface		REACT_26575 (Reactome)	This entity is intended to represent any molecule that might be at the outer cell surface of any cell, host or microbial.
Complement Factor 4	Complex	REACT_26761 (Reactome)
Complement factor I:Cell surface:FH,FHR3:C3b	Complex	REACT_119579 (Reactome)
Complement factor I:Factor H:C3b	Complex	REACT_119450 (Reactome)
Complement factor 3	Complex	REACT_8213 (Reactome)	Linked by disulphide bond between positions 559 and 816.
Complement factor 5	Complex	REACT_8215 (Reactome)
Complement factor D	Protein	REACT_161511 (Reactome)	This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis.
Complement factor I	Complex	REACT_119465 (Reactome)
D-fucose [plasma membrane]	Metabolite	CHEBI:28847 (ChEBI)
DAF:C3 convertase complexes	Complex	REACT_119393 (Reactome)
DAF:C3b	Complex	REACT_119929 (Reactome)
DAF:C4b	Complex	REACT_119228 (Reactome)
FCN1 [extracellular region]	Protein	O00602 (Uniprot-TrEMBL)
FCN1 ligand	Metabolite	REACT_165133 (Reactome)
FCN1:MASP2 dimer:MASP1 dimer	Complex	REACT_164741 (Reactome)
FCN1:MASPs:Ca2+:FCN1 ligand	Complex	REACT_165421 (Reactome)
FCN2 [extracellular region]	Protein	Q15485 (Uniprot-TrEMBL)
FCN2 ligand	Metabolite	REACT_164334 (Reactome)
FCN2:MASP2 dimer:MASP1 dimer	Complex	REACT_165253 (Reactome)
FCN2:MASPs:Ca2+:FCN2 ligand	Complex	REACT_164948 (Reactome)
FCN3 [extracellular region]	Protein	O75636 (Uniprot-TrEMBL)
FCN3 ligand	Metabolite	REACT_165296 (Reactome)
FCN3:MASP2 dimer:MASP1 dimer	Complex	REACT_165152 (Reactome)
FCN3:MASPs:Ca2+:FCN3 ligand	Complex	REACT_164302 (Reactome)
FH, FHR-3	Protein	REACT_119141 (Reactome)
Factor H:C3b	Complex	REACT_120113 (Reactome)
Factor H:Host cell surface	Complex	REACT_119254 (Reactome)
Factor I:MCP, CR1:C4b, C3b complexes	Complex	REACT_120091 (Reactome)
H2O	Metabolite	CHEBI:15377 (ChEBI)
Heparins [plasma membrane]	Metabolite	CHEBI:24505 (ChEBI)
Host cell surface	Complex	REACT_119096 (Reactome)
IGHG1(1-330) [extracellular region]	Protein	P01857 (Uniprot-TrEMBL)
IGHG2(1-326) [extracellular region]	Protein	P01859 (Uniprot-TrEMBL)
IGHG3 [extracellular region]	Protein	P01860 (Uniprot-TrEMBL)
IGHG4(1-327) [extracellular region]	Protein	P01861 (Uniprot-TrEMBL)
IGHV(1-?) [extracellular region]	Protein	A2KUC3 (Uniprot-TrEMBL)
IGHV7-81(1-?) [extracellular region]	Protein	Q6PIL0 (Uniprot-TrEMBL)
IGKC(1-106) [extracellular region]	Protein	P01834 (Uniprot-TrEMBL)
IGKV1-5(23-?) [extracellular region]	Protein	P01602 (Uniprot-TrEMBL)
IGKV4-1(21-?) [extracellular region]	Protein	P06312 (Uniprot-TrEMBL)
IGKVA18(21-?) [extracellular region]	Protein	A2NJV5 (Uniprot-TrEMBL)
IGLC1(1-105) [extracellular region]	Protein	P0CG04 (Uniprot-TrEMBL)
IGLC2(?-106) [extracellular region]	Protein	P0CG05 (Uniprot-TrEMBL)
IGLC3(?-106) [extracellular region]	Protein	P0CG06 (Uniprot-TrEMBL)
IGLC6(?-106) [extracellular region]	Protein	P0CF74 (Uniprot-TrEMBL)
IGLC7(?-106) [extracellular region]	Protein	A0M8Q6 (Uniprot-TrEMBL)
IGLV(23-?) [extracellular region]	Protein	A2NXD2 (Uniprot-TrEMBL)
IGLV1-36(1-?) [extracellular region]	Protein	Q5NV67 (Uniprot-TrEMBL)
IGLV1-40(1-?) [extracellular region]	Protein	Q5NV69 (Uniprot-TrEMBL)
IGLV1-44(1-?) [extracellular region]	Protein	Q5NV81 (Uniprot-TrEMBL)
IGLV10-54(1-?) [extracellular region]	Protein	Q5NV86 (Uniprot-TrEMBL)
IGLV11-55(1-?) [extracellular region]	Protein	Q5NV87 (Uniprot-TrEMBL)
IGLV2-11(1-?) [extracellular region]	Protein	Q5NV84 (Uniprot-TrEMBL)
IGLV2-18(1-?) [extracellular region]	Protein	Q5NV65 (Uniprot-TrEMBL)
IGLV2-23(1-?) [extracellular region]	Protein	Q5NV89 (Uniprot-TrEMBL)
IGLV2-33(1-?) [extracellular region]	Protein	Q5NV66 (Uniprot-TrEMBL)
IGLV3-12(1-?) [extracellular region]	Protein	Q5NV85 (Uniprot-TrEMBL)
IGLV3-16(1-?) [extracellular region]	Protein	Q5NV64 (Uniprot-TrEMBL)
IGLV3-22(1-?) [extracellular region]	Protein	Q5NV75 (Uniprot-TrEMBL)
IGLV3-25(1-?) [extracellular region]	Protein	Q5NV90 (Uniprot-TrEMBL)
IGLV3-27(1-?) [extracellular region]	Protein	Q5NV91 (Uniprot-TrEMBL)
IGLV4-3(1-?) [extracellular region]	Protein	Q5NV61 (Uniprot-TrEMBL)
IGLV4-60(1-?) [extracellular region]	Protein	Q5NV79 (Uniprot-TrEMBL)
IGLV4-69(1-?) [extracellular region]	Protein	Q5NV92 (Uniprot-TrEMBL)
IGLV5-37(1-?) [extracellular region]	Protein	Q5NV68 (Uniprot-TrEMBL)
IGLV5-45(1-?) [extracellular region]	Protein	Q5NV82 (Uniprot-TrEMBL)
IGLV7-43(1-?) [extracellular region]	Protein	Q5NV80 (Uniprot-TrEMBL)
IGLV7-46(1-?) [extracellular region]	Protein	Q5NV83 (Uniprot-TrEMBL)
IGLV8-61(1-?) [extracellular region]	Protein	Q5NV62 (Uniprot-TrEMBL)
Ig heavy chain V-I region EU [extracellular region]	Protein	P01742 (Uniprot-TrEMBL)
Ig heavy chain V-I region HG3 [extracellular region]	Protein	P01743 (Uniprot-TrEMBL)
Ig heavy chain V-I region Mot [extracellular region]	Protein	P06326 (Uniprot-TrEMBL)
Ig heavy chain V-I region ND [extracellular region]	Protein	P01744 (Uniprot-TrEMBL)
Ig heavy chain V-I region SIE [extracellular region]	Protein	P01761 (Uniprot-TrEMBL)
Ig heavy chain V-I region WOL [extracellular region]	Protein	P01760 (Uniprot-TrEMBL)
Ig heavy chain V-II region ARH-77 [extracellular region]	Protein	P06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region COR [extracellular region]	Protein	P01815 (Uniprot-TrEMBL)
Ig heavy chain V-II region DAW [extracellular region]	Protein	P01816 (Uniprot-TrEMBL)
Ig heavy chain V-II region HE [extracellular region]	Protein	P01818 (Uniprot-TrEMBL)
Ig heavy chain V-II region MCE [extracellular region]	Protein	P01817 (Uniprot-TrEMBL)
Ig heavy chain V-II region NEWM [extracellular region]	Protein	P01825 (Uniprot-TrEMBL)
Ig heavy chain V-II region OU [extracellular region]	Protein	P01814 (Uniprot-TrEMBL)
Ig heavy chain V-II region SESS [extracellular region]	Protein	P04438 (Uniprot-TrEMBL)
Ig heavy chain V-II region WAH [extracellular region]	Protein	P01824 (Uniprot-TrEMBL)
Ig heavy chain V-III region BRO [extracellular region]	Protein	P01766 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUR [extracellular region]	Protein	P01773 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUT [extracellular region]	Protein	P01767 (Uniprot-TrEMBL)
Ig heavy chain V-III region CAM [extracellular region]	Protein	P01768 (Uniprot-TrEMBL)
Ig heavy chain V-III region DOB [extracellular region]	Protein	P01782 (Uniprot-TrEMBL)
Ig heavy chain V-III region GA [extracellular region]	Protein	P01769 (Uniprot-TrEMBL)
Ig heavy chain V-III region GAL [extracellular region]	Protein	P01781 (Uniprot-TrEMBL)
Ig heavy chain V-III region HIL [extracellular region]	Protein	P01771 (Uniprot-TrEMBL)
Ig heavy chain V-III region JON [extracellular region]	Protein	P01780 (Uniprot-TrEMBL)
Ig heavy chain V-III region KOL [extracellular region]	Protein	P01772 (Uniprot-TrEMBL)
Ig heavy chain V-III region LAY [extracellular region]	Protein	P01775 (Uniprot-TrEMBL)
Ig heavy chain V-III region NIE [extracellular region]	Protein	P01770 (Uniprot-TrEMBL)
Ig heavy chain V-III region POM [extracellular region]	Protein	P01774 (Uniprot-TrEMBL)
Ig heavy chain V-III region TEI [extracellular region]	Protein	P01777 (Uniprot-TrEMBL)
Ig heavy chain V-III region TIL [extracellular region]	Protein	P01765 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO [extracellular region]	Protein	P01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region TUR [extracellular region]	Protein	P01779 (Uniprot-TrEMBL)
Ig heavy chain V-III region WAS [extracellular region]	Protein	P01776 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA [extracellular region]	Protein	P01763 (Uniprot-TrEMBL)
Ig heavy chain V-III region ZAP [extracellular region]	Protein	P01778 (Uniprot-TrEMBL)
Ig kappa chain V region EV15 [extracellular region]	Protein	P06315 (Uniprot-TrEMBL)
Ig kappa chain V-I region AG [extracellular region]	Protein	P01593 (Uniprot-TrEMBL)
Ig kappa chain V-I region AU [extracellular region]	Protein	P01594 (Uniprot-TrEMBL)
Ig kappa chain V-I region BAN [extracellular region]	Protein	P04430 (Uniprot-TrEMBL)
Ig kappa chain V-I region Bi [extracellular region]	Protein	P01595 (Uniprot-TrEMBL)
Ig kappa chain V-I region CAR [extracellular region]	Protein	P01596 (Uniprot-TrEMBL)
Ig kappa chain V-I region DEE [extracellular region]	Protein	P01597 (Uniprot-TrEMBL)
Ig kappa chain V-I region Daudi [extracellular region]	Protein	P04432 (Uniprot-TrEMBL)
Ig kappa chain V-I region EU [extracellular region]	Protein	P01598 (Uniprot-TrEMBL)
Ig kappa chain V-I region Gal [extracellular region]	Protein	P01599 (Uniprot-TrEMBL)
Ig kappa chain V-I region HK101 [extracellular region]	Protein	P01601 (Uniprot-TrEMBL)
Ig kappa chain V-I region Hau [extracellular region]	Protein	P01600 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ka [extracellular region]	Protein	P01603 (Uniprot-TrEMBL)
Ig kappa chain V-I region Kue [extracellular region]	Protein	P01604 (Uniprot-TrEMBL)
Ig kappa chain V-I region Lay [extracellular region]	Protein	P01605 (Uniprot-TrEMBL)
Ig kappa chain V-I region Mev [extracellular region]	Protein	P01612 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ni [extracellular region]	Protein	P01613 (Uniprot-TrEMBL)
Ig kappa chain V-I region OU [extracellular region]	Protein	P01606 (Uniprot-TrEMBL)
Ig kappa chain V-I region Rei [extracellular region]	Protein	P01607 (Uniprot-TrEMBL)
Ig kappa chain V-I region Roy [extracellular region]	Protein	P01608 (Uniprot-TrEMBL)
Ig kappa chain V-I region Scw [extracellular region]	Protein	P01609 (Uniprot-TrEMBL)
Ig kappa chain V-I region WAT [extracellular region]	Protein	P80362 (Uniprot-TrEMBL)
Ig kappa chain V-I region WEA [extracellular region]	Protein	P01610 (Uniprot-TrEMBL)
Ig kappa chain V-I region Walker [extracellular region]	Protein	P04431 (Uniprot-TrEMBL)
Ig kappa chain V-I region Wes [extracellular region]	Protein	P01611 (Uniprot-TrEMBL)
Ig kappa chain V-II region Cum [extracellular region]	Protein	P01614 (Uniprot-TrEMBL)
Ig kappa chain V-II region FR [extracellular region]	Protein	P01615 (Uniprot-TrEMBL)
Ig kappa chain V-II region GM607 [extracellular region]	Protein	P06309 (Uniprot-TrEMBL)
Ig kappa chain V-II region MIL [extracellular region]	Protein	P01616 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 [extracellular region]	Protein	P06310 (Uniprot-TrEMBL)
Ig kappa chain V-II region TEW [extracellular region]	Protein	P01617 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 [extracellular region]	Protein	P01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region CLL [extracellular region]	Protein	P04207 (Uniprot-TrEMBL)
Ig kappa chain V-III region GOL [extracellular region]	Protein	P04206 (Uniprot-TrEMBL)
Ig kappa chain V-III region HAH [extracellular region]	Protein	P18135 (Uniprot-TrEMBL)
Ig kappa chain V-III region HIC [extracellular region]	Protein	P18136 (Uniprot-TrEMBL)
Ig kappa chain V-III region IARC/BL41 [extracellular region]	Protein	P06311 (Uniprot-TrEMBL)
Ig kappa chain V-III region NG9 [extracellular region]	Protein	P01621 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM [extracellular region]	Protein	P01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region SIE [extracellular region]	Protein	P01620 (Uniprot-TrEMBL)
Ig kappa chain V-III region Ti [extracellular region]	Protein	P01622 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG [extracellular region]	Protein	P04433 (Uniprot-TrEMBL)
Ig kappa chain V-III region VH [extracellular region]	Protein	P04434 (Uniprot-TrEMBL)
Ig kappa chain V-III region WOL [extracellular region]	Protein	P01623 (Uniprot-TrEMBL)
Ig kappa chain V-IV region B17 [extracellular region]	Protein	P06314 (Uniprot-TrEMBL)
Ig kappa chain V-IV region JI [extracellular region]	Protein	P06313 (Uniprot-TrEMBL)
Ig kappa chain V-IV region Len [extracellular region]	Protein	P01625 (Uniprot-TrEMBL)
Ig kappa chain V-IV region STH [extracellular region]	Protein	P83593 (Uniprot-TrEMBL)
Ig lambda chain V-III region LOI [extracellular region]	Protein	P80748 (Uniprot-TrEMBL)
Ig lambda chain V-III region SH [extracellular region]	Protein	P01714 (Uniprot-TrEMBL)
Ig lambda chain V-VII region MOT [extracellular region]	Protein	P01720 (Uniprot-TrEMBL)
Ig lambda chain V region 4A [extracellular region]	Protein	P04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region BL2 [extracellular region]	Protein	P06316 (Uniprot-TrEMBL)
Ig lambda chain V-I region EPS [extracellular region]	Protein	P06888 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA [extracellular region]	Protein	P01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region MEM [extracellular region]	Protein	P06887 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEW [extracellular region]	Protein	P01701 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEWM [extracellular region]	Protein	P01703 (Uniprot-TrEMBL)
Ig lambda chain V-I region NIG-64 [extracellular region]	Protein	P01702 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR [extracellular region]	Protein	P01699 (Uniprot-TrEMBL)
Ig lambda chain V-I region WAH [extracellular region]	Protein	P04208 (Uniprot-TrEMBL)
Ig lambda chain V-II region BO [extracellular region]	Protein	P01710 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH [extracellular region]	Protein	P01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region BUR [extracellular region]	Protein	P01708 (Uniprot-TrEMBL)
Ig lambda chain V-II region MGC [extracellular region]	Protein	P01709 (Uniprot-TrEMBL)
Ig lambda chain V-II region NEI [extracellular region]	Protein	P01705 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-58 [extracellular region]	Protein	P01713 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-84 [extracellular region]	Protein	P04209 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG [extracellular region]	Protein	P01704 (Uniprot-TrEMBL)
Ig lambda chain V-II region TRO [extracellular region]	Protein	P01707 (Uniprot-TrEMBL)
Ig lambda chain V-II region VIL [extracellular region]	Protein	P01711 (Uniprot-TrEMBL)
Ig lambda chain V-II region WIN [extracellular region]	Protein	P01712 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Bau [extracellular region]	Protein	P01715 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Hil [extracellular region]	Protein	P01717 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Kern [extracellular region]	Protein	P01718 (Uniprot-TrEMBL)
Ig lambda chain V-IV region MOL [extracellular region]	Protein	P06889 (Uniprot-TrEMBL)
Ig lambda chain V-IV region X [extracellular region]	Protein	P01716 (Uniprot-TrEMBL)
Ig lambda chain V-V region DEL [extracellular region]	Protein	P01719 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR [extracellular region]	Protein	P01721 (Uniprot-TrEMBL)
Ig lambda chain V-VI region EB4 [extracellular region]	Protein	P06319 (Uniprot-TrEMBL)
Ig lambda chain V-VI region NIG-48 [extracellular region]	Protein	P01722 (Uniprot-TrEMBL)
Ig lambda chain V-VI region SUT [extracellular region]	Protein	P06317 (Uniprot-TrEMBL)
Ig lambda chain V-VI region WLT [extracellular region]	Protein	P06318 (Uniprot-TrEMBL)
IgH heavy chain V-III region VH26 precursor [extracellular region]	Protein	P01764 (Uniprot-TrEMBL)
Lipoteichoic acid [plasma membrane]	Metabolite	CHEBI:28640 (ChEBI)
MASP1(20-448) [extracellular region]	Protein	P48740 (Uniprot-TrEMBL)
MASP1(20-699) [extracellular region]	Protein	P48740 (Uniprot-TrEMBL)
MASP1(449-699) [extracellular region]	Protein	P48740 (Uniprot-TrEMBL)
MASP2-1 [extracellular region]	Protein	O00187-1 (Uniprot-TrEMBL)
MASP2-1(16-444) [extracellular region]	Protein	O00187-1 (Uniprot-TrEMBL)
MASP2-1(445-686) [extracellular region]	Protein	O00187-1 (Uniprot-TrEMBL)
MBL bound to mannose-based carbohydrates on bacterial surfaces	Complex	REACT_8711 (Reactome)
MBL-II:MASP-2 dimer:MASP-1 dimer complex	Complex	REACT_8380 (Reactome)
MBL/FCN:activated MASP:carbohydrate patterns	Complex	REACT_165602 (Reactome)
MBL/Ficolin:MASPs bound to carbohydrate patterns	Complex	REACT_165125 (Reactome)
MBL2 [extracellular region]	Protein	P11226 (Uniprot-TrEMBL)
MBL:activated MASPs:mannose-based carbohydrates	Complex	REACT_8515 (Reactome)
MCP, CR1:C4b:C3b complexes	Complex	REACT_120251 (Reactome)
MCP, CR1	Protein	REACT_119720 (Reactome)	CR1 and MCP are widely distributed cell surface molecules that bind C4b and C3b, and act as cofactors for Complement factor I, thereby regulating the classical and alternative C3 convertases.
MCP:C3b	Complex	REACT_119903 (Reactome)
MCP:C4b	Complex	REACT_119237 (Reactome)
Membrane Attack Complex	Complex	REACT_8325 (Reactome)
N-acetyl-D-glucosamine [plasma membrane]	Metabolite	CHEBI:28009 (ChEBI)
N-acetylgalactosamine [plasma membrane]	Metabolite	CHEBI:40356 (ChEBI)
PCho [plasma membrane]	Metabolite	CHEBI:36700 (ChEBI)
Properdin oligomer		REACT_8730 (Reactome)
Sialic acid [plasma membrane]	Metabolite	CHEBI:28879 (ChEBI)
VTN(20-?) [extracellular region]	Protein	P04004 (Uniprot-TrEMBL)
VTN(20-?)	Protein	P04004 (Uniprot-TrEMBL)
VTN:C5b:C6:C7:C8:C9	Complex	REACT_164606 (Reactome)
VTN:C5b:C6:C7	Complex	REACT_165289 (Reactome)
dNQ-C3(672-1663) [extracellular region]	Protein	P01024 (Uniprot-TrEMBL)
dNQ-C4A(757-1446) [extracellular region]	Protein	P0C0L4 (Uniprot-TrEMBL)
dNQ-C4B(757-1446) [extracellular region]	Protein	P0C0L5 (Uniprot-TrEMBL)
iC3b	Complex	REACT_119218 (Reactome)
iC3b	Complex	REACT_120169 (Reactome)
thioester-C1010-Q1013-C4b	Complex	REACT_26471 (Reactome)

Annotated Interactions

View all...

Source	Target	Type	Database reference	Comment
11xCbxE-PROS1			REACT_118836 (Reactome)
	Antigen: antibody: C1 (activated C1R and C1S) complex	Arrow	REACT_7977 (Reactome)
	Antigen: antibody: C1 (activated C1R) complex	Arrow	REACT_7978 (Reactome)
Antigen: antibody: C1 (activated C1R) complex			REACT_7977 (Reactome)
Antigen: antibody: C1 (activated C1R) complex		mim-catalysis	REACT_7977 (Reactome)
Antigen: antibody: C1 complex			REACT_7978 (Reactome)
Antigen: antibody: C1 complex		mim-catalysis	REACT_7978 (Reactome)
Bacterial mannose-based carbohydrate surface pattern			REACT_7983 (Reactome)
C-reactive protein pentamer:phosphocholine:C1Q		Arrow	REACT_7978 (Reactome)
C2			REACT_7959 (Reactome)
	C2a	Arrow	REACT_118584 (Reactome)
	C2a	Arrow	REACT_118641 (Reactome)
	C2a	Arrow	REACT_118692 (Reactome)
	C2a	Arrow	REACT_118738 (Reactome)
	C2a	Arrow	REACT_7959 (Reactome)
C2a			REACT_8014 (Reactome)
	C2b	Arrow	REACT_7959 (Reactome)
C3 convertases			REACT_118641 (Reactome)
C3 convertases		mim-catalysis	REACT_7990 (Reactome)
	C3(H2O):Factor B	Arrow	REACT_8013 (Reactome)
C3(H2O):Factor B			REACT_7981 (Reactome)
	C3(H2O):Factor Bb	Arrow	REACT_7981 (Reactome)
C3(H2O):Factor Bb		mim-catalysis	REACT_7948 (Reactome)
	C3(H2O)	Arrow	REACT_118641 (Reactome)
	C3(H2O)	Arrow	REACT_8007 (Reactome)
C3(H2O)			REACT_8013 (Reactome)
	C3a	Arrow	REACT_7948 (Reactome)
	C3a	Arrow	REACT_7986 (Reactome)
	C3a	Arrow	REACT_7990 (Reactome)
	C3b:Factor Bb:C3b:Properdin complex	Arrow	REACT_7986 (Reactome)
	C3b	Arrow	REACT_118641 (Reactome)
	C3b	Arrow	REACT_7948 (Reactome)
	C3b	Arrow	REACT_7990 (Reactome)
C3b			REACT_118712 (Reactome)
C3b			REACT_25075 (Reactome)
	C3c	Arrow	REACT_163860 (Reactome)
	C3dg	Arrow	REACT_163860 (Reactome)
	C3f	Arrow	REACT_118650 (Reactome)
	C3f	Arrow	REACT_118841 (Reactome)
C4 activator		mim-catalysis	REACT_7959 (Reactome)
C4 activator		mim-catalysis	REACT_8002 (Reactome)
	C4 binding protein:C4bC2a	Arrow	REACT_118752 (Reactome)
C4 binding protein:C4bC2a			REACT_118738 (Reactome)
	C4 binding protein:protein S	Arrow	REACT_118836 (Reactome)
	C4-binding protein:C4b	Arrow	REACT_118738 (Reactome)
	C4-binding protein:C4b	Arrow	REACT_118763 (Reactome)
C4-binding protein:C4b			REACT_118647 (Reactome)
	C4a	Arrow	REACT_8002 (Reactome)
	C4b with hydrolysed thioester	Arrow	REACT_163768 (Reactome)
C4b, C3b			REACT_118575 (Reactome)
	C4b-binding protein:Factor I	Arrow	REACT_118647 (Reactome)
C4b-binding protein:Factor I			REACT_118719 (Reactome)
	C4b-binding protein	Arrow	REACT_118719 (Reactome)
C4b-binding protein			REACT_118752 (Reactome)
C4b-binding protein			REACT_118763 (Reactome)
C4b-binding protein			REACT_118836 (Reactome)
	C4b:C2a:C3b	Arrow	REACT_8022 (Reactome)
C4bC2a, C3bBb			REACT_118580 (Reactome)
C4bC2a, C3bBb			REACT_118782 (Reactome)
	C4c, C3f	Arrow	REACT_118673 (Reactome)
	C4c	Arrow	REACT_118719 (Reactome)
	C4d, iC3b	Arrow	REACT_118673 (Reactome)
	C4d	Arrow	REACT_118719 (Reactome)
C5 convertases		mim-catalysis	REACT_7989 (Reactome)
	C5a	Arrow	REACT_7989 (Reactome)
	C5b:C6 complex	Arrow	REACT_7976 (Reactome)
C5b:C6 complex			REACT_7950 (Reactome)
	C5b:C6:C7 complex	Arrow	REACT_7950 (Reactome)
	C5b:C6:C7 complex	Arrow	REACT_7982 (Reactome)
C5b:C6:C7 complex			REACT_163759 (Reactome)
C5b:C6:C7 complex			REACT_7946 (Reactome)
C5b:C6:C7 complex			REACT_7982 (Reactome)
	C5b:C6:C7:C8 complex	Arrow	REACT_7946 (Reactome)
C5b:C6:C7:C8 complex			REACT_163829 (Reactome)
C5b:C6:C7:C8 complex			REACT_7988 (Reactome)
	C5b	Arrow	REACT_7989 (Reactome)
C5b			REACT_7976 (Reactome)
C6			REACT_7976 (Reactome)
C7(22-843)			REACT_7950 (Reactome)
C8			REACT_163870 (Reactome)
C8			REACT_7946 (Reactome)
C9(22-559)			REACT_163829 (Reactome)
C9(22-559)			REACT_163870 (Reactome)
C9(22-559)			REACT_7988 (Reactome)
CD46			REACT_118575 (Reactome)
CD55			REACT_118782 (Reactome)
	CD59:C5b-C9	Arrow	REACT_163829 (Reactome)
CD59			REACT_163829 (Reactome)
	CFB(26-259)	Arrow	REACT_7981 (Reactome)
	CFB(26-259)	Arrow	REACT_8026 (Reactome)
CFB(26-764)			REACT_7966 (Reactome)
CFB(26-764)			REACT_8013 (Reactome)
	CFB(260-764)	Arrow	REACT_118584 (Reactome)
	CFB(260-764)	Arrow	REACT_118641 (Reactome)
	CFB(260-764)	Arrow	REACT_118692 (Reactome)
	CFB(260-764)	Arrow	REACT_118727 (Reactome)
	CFH	Arrow	REACT_118650 (Reactome)
CFH			REACT_118604 (Reactome)
CFH			REACT_118712 (Reactome)
CFI(19-335)			REACT_118674 (Reactome)
CFI(340-583)			REACT_118674 (Reactome)
	CR1:C3b	Arrow	REACT_118692 (Reactome)
	CR1:C3bBb, C4bC2a complexes	Arrow	REACT_118580 (Reactome)
CR1:C3bBb, C4bC2a complexes			REACT_118692 (Reactome)
	CR1:C4b	Arrow	REACT_118692 (Reactome)
CR1:iC3b			REACT_163860 (Reactome)
	CR1	Arrow	REACT_163860 (Reactome)
CR1			REACT_118580 (Reactome)
Ca2+			REACT_163715 (Reactome)
Ca2+			REACT_163747 (Reactome)
Ca2+			REACT_163758 (Reactome)
Ca2+			REACT_7983 (Reactome)
	Cell surface:C3b:Factor Bb:Properdin	Arrow	REACT_8018 (Reactome)
Cell surface:C3b:Factor Bb:Properdin			REACT_7986 (Reactome)
Cell surface:C3b:Factor Bb:Properdin		mim-catalysis	REACT_7986 (Reactome)
	Cell surface:C3b:Factor Bb	Arrow	REACT_8026 (Reactome)
Cell surface:C3b:Factor Bb			REACT_118710 (Reactome)
Cell surface:C3b:Factor Bb			REACT_8018 (Reactome)
	Cell surface:C3b:Factor B complex	Arrow	REACT_7966 (Reactome)
Cell surface:C3b:Factor B complex			REACT_8026 (Reactome)
	Cell surface:FH,FHR3:C3b	Arrow	REACT_118727 (Reactome)
	Cell surface:FH,FHR3:C3b	Arrow	REACT_118815 (Reactome)
	Cell surface:FH,FHR3:C3bBb	Arrow	REACT_118710 (Reactome)
Cell surface:FH,FHR3:C3bBb			REACT_118727 (Reactome)
Cell surface:FH,FHR3:C3b			REACT_118844 (Reactome)
	Cell surface:C3b	Arrow	REACT_25075 (Reactome)
Cell surface:C3b			REACT_118815 (Reactome)
Cell surface:C3b			REACT_7966 (Reactome)
Cell surface:C3b			REACT_8022 (Reactome)
	Cell surface:C4b:C2a	Arrow	REACT_118641 (Reactome)
	Cell surface:C4b:C2a	Arrow	REACT_8014 (Reactome)
Cell surface:C4b:C2a			REACT_118752 (Reactome)
Cell surface:C4b:C2a			REACT_8022 (Reactome)
	Cell surface:C4b	Arrow	REACT_118641 (Reactome)
	Cell surface:C4b	Arrow	REACT_25166 (Reactome)
Cell surface:C4b			REACT_8014 (Reactome)
Cell surface			REACT_25075 (Reactome)
Cell surface			REACT_25166 (Reactome)
Complement Factor 4			REACT_8002 (Reactome)
	Complement factor I:Cell surface:FH,FHR3:C3b	Arrow	REACT_118844 (Reactome)
Complement factor I:Cell surface:FH,FHR3:C3b			REACT_118841 (Reactome)
Complement factor I:Cell surface:FH,FHR3:C3b		mim-catalysis	REACT_118841 (Reactome)
	Complement factor I:Factor H:C3b	Arrow	REACT_118583 (Reactome)
Complement factor I:Factor H:C3b			REACT_118650 (Reactome)
Complement factor I:Factor H:C3b		mim-catalysis	REACT_118650 (Reactome)
Complement factor 3			REACT_7948 (Reactome)
Complement factor 3			REACT_7986 (Reactome)
Complement factor 3			REACT_7990 (Reactome)
Complement factor 3			REACT_8007 (Reactome)
Complement factor 5			REACT_7989 (Reactome)
Complement factor D		mim-catalysis	REACT_7981 (Reactome)
Complement factor D		mim-catalysis	REACT_8026 (Reactome)
	Complement factor I	Arrow	REACT_118650 (Reactome)
	Complement factor I	Arrow	REACT_118673 (Reactome)
	Complement factor I	Arrow	REACT_118674 (Reactome)
	Complement factor I	Arrow	REACT_118719 (Reactome)
	Complement factor I	Arrow	REACT_118841 (Reactome)
Complement factor I			REACT_118583 (Reactome)
Complement factor I			REACT_118631 (Reactome)
Complement factor I			REACT_118647 (Reactome)
Complement factor I			REACT_118844 (Reactome)
	DAF:C3 convertase complexes	Arrow	REACT_118782 (Reactome)
DAF:C3 convertase complexes			REACT_118584 (Reactome)
	DAF:C3b	Arrow	REACT_118584 (Reactome)
	DAF:C4b	Arrow	REACT_118584 (Reactome)
FCN1 ligand			REACT_163715 (Reactome)
FCN1:MASP2 dimer:MASP1 dimer			REACT_163715 (Reactome)
	FCN1:MASPs:Ca2+:FCN1 ligand	Arrow	REACT_163715 (Reactome)
FCN2 ligand			REACT_163747 (Reactome)
FCN2:MASP2 dimer:MASP1 dimer			REACT_163747 (Reactome)
	FCN2:MASPs:Ca2+:FCN2 ligand	Arrow	REACT_163747 (Reactome)
FCN3 ligand			REACT_163758 (Reactome)
FCN3:MASP2 dimer:MASP1 dimer			REACT_163758 (Reactome)
	FCN3:MASPs:Ca2+:FCN3 ligand	Arrow	REACT_163758 (Reactome)
	FH, FHR-3	Arrow	REACT_118841 (Reactome)
FH, FHR-3			REACT_118710 (Reactome)
FH, FHR-3			REACT_118815 (Reactome)
	Factor H:C3b	Arrow	REACT_118712 (Reactome)
Factor H:C3b			REACT_118583 (Reactome)
	Factor H:Host cell surface	Arrow	REACT_118604 (Reactome)
Factor H:Host cell surface		Arrow	REACT_118710 (Reactome)
Factor H:Host cell surface		Arrow	REACT_118815 (Reactome)
	Factor I:MCP, CR1:C4b, C3b complexes	Arrow	REACT_118631 (Reactome)
Factor I:MCP, CR1:C4b, C3b complexes			REACT_118673 (Reactome)
Factor I:MCP, CR1:C4b, C3b complexes		mim-catalysis	REACT_118673 (Reactome)
H2O			REACT_163768 (Reactome)
H2O			REACT_8007 (Reactome)
Host cell surface			REACT_118604 (Reactome)
	MBL bound to mannose-based carbohydrates on bacterial surfaces	Arrow	REACT_7983 (Reactome)
MBL-II:MASP-2 dimer:MASP-1 dimer complex			REACT_7983 (Reactome)
	MBL/FCN:activated MASP:carbohydrate patterns	Arrow	REACT_7965 (Reactome)
MBL/Ficolin:MASPs bound to carbohydrate patterns			REACT_7965 (Reactome)
MCP, CR1:C4b:C3b complexes			REACT_118631 (Reactome)
	MCP, CR1	Arrow	REACT_118673 (Reactome)
	MCP:C3b	Arrow	REACT_118575 (Reactome)
	MCP:C4b	Arrow	REACT_118575 (Reactome)
	Membrane Attack Complex	Arrow	REACT_7988 (Reactome)
	Properdin oligomer	Arrow	REACT_118641 (Reactome)
Properdin oligomer			REACT_8018 (Reactome)
			REACT_118575 (Reactome)	Membrane cofactor protein (MCP; CD46) is a widely distributed C3b/C4b-binding cell surface glycoprotein which is a cofactor for Complement factor I.
			REACT_118580 (Reactome)	Complement Receptor 1 (CR1) is a widely distributed cell surface protein that is a decay accelerating factor for the conventional (C4bC2a) and alternative (C3bBb) C3 convertases (Coico & Sunshine 2009).
			REACT_118583 (Reactome)	Complement factor I binds the factor H:C3b complex.
			REACT_118584 (Reactome)	Decay accelerating factor (DAF, CD55) is a widely distributed membrane protein. It accelerates the dissociation of C3bBb and C4C2a, thereby inhibiting the amplification of complement. DAF can bind C3b and Bb but must bind both for efficient decay acceleration. The regulatory function of DAF is believed to be inhibition of activated C3 convertase enzymes rather than binding of inactive proenzymes (Harris et al. 2007).
			REACT_118604 (Reactome)	Factor H preferentially binds to host cells and surfaces that have negatively charged cell surface polyanions such as heparin and sialic acid commonly found on host cells (Kazatchkine et al. 1979, Meri & Pangburn 1990). This mediates protection of plasma-exposed host structures.
			REACT_118631 (Reactome)	Membrane cofactor protein (MCP) and Complement Receptor 1 (CR1) act as cofactors for the protease activity of complement factor I which binds MCP or CR1 complexes with C3b or C4b, inactivating C3b/C4b.
			REACT_118641 (Reactome)	C3b:Bb is naturally labile with a half-life of ~90 s. unless bound to properdin on the cell surface (Medicus et al. 1976). C4bC2a is also unstable, lasting at best a few minutes (Kerr et al. 1980). Decay is associated with the release of the Bb or C2a fragments respectively into the fluid phase. The liberated C3b/C4b is able to re-bind Bb/C2a if Factor B/C2 are present.
			REACT_118647 (Reactome)	C4b-binding protein is a cofactor for Complement Factor I, allowing it to bind and thereby mediating C4b proteolysis.
			REACT_118650 (Reactome)	Complement factor I cleaves the alpha chain of C3b at two positions, generating inactivated C3b (iC3b) and a small fragment C3f which is released. The majority of the alpha chain is retained as two fragments which are tethered by disulphide bonds. iC3b is proteolytically inactive.
			REACT_118673 (Reactome)	Factor I cleaves the truncated alpha (a') chain of C4b between Arg-1336 and Asn-1337 and then again between Arg-956 and Thr-957, producing a 16 kDa fragment known as alpha4, derived from the C terminus of the a' chain, followed by a 27 kDa alpha3 fragment. The remaining alpha 2 (C4d) fragment stays covalently bound to the cell membrane while the complex of disulfide-linked alpha3, alpha4, beta chain and gamma chain are released (C4c) into the fluid phase (Fujita et al. 1978).
			REACT_118674 (Reactome)	Complement factor I (CFI) is a complex of one heavy and one light chain, both cleaved from the same precursor peptide. It inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage of the alpha chains of C4b and C3b in the presence of cofactors such as Factor H, C4b binding protein, Complement receptor 1 (CR1) or MCP (CD46).
			REACT_118692 (Reactome)	Complement Receptor 1 (CR1) displaces the activated enzyme components Bb and C2a from the conventional and alternative C3 convertases C4bC2a and C3bBb, respectivley.
			REACT_118710 (Reactome)	Factor H (FH) binds to C3bBb, leading to displacement of Bb. Complement factor H-related protein 3 (FHR-3) has also been reported to bind C3Bb leading to inhibition of C3Bb C3 convertase activity (Fritsche et al. 2010). FH also acts as a cofactor for the factor I-mediated proteolytic inactivation of C3b to iC3b.
			REACT_118712 (Reactome)	Factor H (FH) regulates the alternative pathway C3 convertase C3bBb and its C3b component both in plasma and at host cell surfaces. FH binds to plasma C3b, making it unavailable, and acts as a cofactor for the factor I-mediated proteolytic inactivation of C3b to iC3b.
			REACT_118719 (Reactome)	C4b-binding protein is a cofactor in Factor I mediated C4b proteolysis. C4b is cleaved, releasing C4c, leaving C4d bound to the cell surface.
			REACT_118727 (Reactome)	Factor H greatly accelerates the displacement (decay) of Complement factor Bb from C3b.
			REACT_118738 (Reactome)	C4 binding protein accelerates the decay of C4bC2a in a dose-dependent fashion. The mechanism of this is poorly understood, but is distinct from Factor I mediated degradation of C4b and believed to represent the displacement of C2a from specific binding sites on C4b (Gigli et al. 1979).
			REACT_118752 (Reactome)	C4 binding protein accelerates the decay of C4bC2a in a dose-dependent fashion, without causing degradation of C4b, and is presumed to bind to the convertase to mediate this effect.
			REACT_118763 (Reactome)	The most abundant form of C4b-binding protein (C4BP) consists of seven alpha-chains (70kDa) and one beta-chain (45kDa) all linked by disulphide bonds to form a native protein with a molecular weight of 570kDa (Hilarp et al. 1989). Each alpha chain can bind C4b; it is not known whether full occupancy is necessary for subsequent events. The beta chain binds and inactivates Protein S, a component of the coagulation system. C4BP down-regulates complement activity in several ways: It binds to C4b thus inhibiting the formation of the classical pathway C3 convertase C4bC2a; it acts as a decay accelerating factor for existing convertases, probably by promoting dissociation of C2a; it is a cofactor in Factor I mediated C4b proteolysis.
			REACT_118782 (Reactome)	Decay-accelerating-factor (DAF, CD55) is a membrane- bound complement regulatory protein that inhibits autologous complement cascade activation. It is expressed on all cells that are in close contact with serum complement proteins, but also on cells outside the vascular space and on tumour cells. DAF binds to C3bBb and C4bC2a on cell surfaces, accelerating their dissociation and thereby inhibiting the amplification of complement. DAF can bind C3b and Bb, and must bind both for efficient decay acceleration. Although it can bind the inactive proenzymes C3b and C4b, the regulatory function of DAF is believed to be inhibition of activated C3 convertase enzymes (Harris et al. 2007).
			REACT_118815 (Reactome)	Factor H (FH) regulates the alternative pathway C3 convertase C3bBb and its C3b component both in plasma and at host cell surfaces. FH binds to membrane-associated C3b, competing with Factor B and thereby preventing formation of the active C3 convertase C3bBb. In addition, it acts as a cofactor for the Factor I-mediated proteolytic inactivation of C3b to iC3b.
			REACT_118836 (Reactome)	The beta subunit of C4b binding protein binds and inactivates Protein S, a vitamin K dependent anticoagulation factor. This may represent part of a mechanism for fine-tuning the process of phagocytosis (Kask et al. 2004).
			REACT_118841 (Reactome)	Following the displacement of Bb from C3bBb, Factor I cleaves Factor H-bound C3b producing iC3b, which remains bound to the membrane. The majority of the C3b alpha chain is retained as two fragments which are tethered to the beta chain by disulphide bonds. iC3b is proteolytically inactive and cannot contribute to the complement cascade process, though it still contributes to opsonization.
			REACT_118844 (Reactome)	Complement factor I binds to the Factor H:C3b complex.
			REACT_163715 (Reactome)	Ficolin-1 (M-ficolin or FCN1) was shown to localize at the cell surface of circulating monocytes and granulocytes, despite lacking an obvious transmembrane domain, (Teh C et al. 2000; Honore C et al. 2010). Ficolin-1 has also been found in human plasma (Honore C et al. 2008; Wittenborn T et al. 2010; Kjaer TR et al. 2011). Monocytes and macrophages, but not immature dendritic cells were reported to secrete Ficolin-1 into the serum (Honore C et al. 2010). Moreover, early studies revealed its presence in secretory granules of peripheral blood monocytes and granulocytes (Liu Y et al. 2005). Soluble Ficolin-1 was found to form a complex with MASP2, while cell surface-bound Ficolin-1 did not associate with MASP (Honore C et al. 2010; Kjaer TR et al. 2011). Ficolin-1 specifically recognizes sialic acid and can bind to acetylated compounds such as N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) (Garlatti V et al. 2007; Gout E et al. 2010; Kjaer TR et al. 2011).
			REACT_163747 (Reactome)	Human ficolin-2 (L-ficolin, P35 or FCN2) is synthesised in the liver and secreted into the bloodstream where it recognizes various capsulated bacteria and exhibits binding specificity for diverse ligands, such as lipoteichoic acid, 1,3-beta-d-glucan, and acetylated compounds [Lynch NJ et al. 2004; Aoyagi Y et al. 2008; Ma YG et al. 2004; Garlatti V et al. 2007; Gout E et al 2010]. Ficolin-2 also binds to apoptotic HL60, U937, and Jurkat cells [Kuraya M, et al. 2005].
			REACT_163758 (Reactome)	Ficolin-3 (H-ficolin, FCN3 or Hakata antigen) activates the lectin pathway of complement similar to mannose-binding lectin. Ficolin-3 is composed by a collagen-like strand and three C-terminal recognition domains which bind to carbohydrates on the target surface. Ficolin-3 circulates in plasma associated with mannan-binding lectin-associated serine proteases (MASPs). Upon ligand binding ficolin-3:MASPs complex triggers activation of the lectin pathway [Matsushita M et al. 2002; Teillet F et al. 2008; Zacho RM et al. 2012]. Ficolin-3 (FCN3 or H-ficolin) can specifically recognize Aerococcus viridans [Tsujimura M et al. 2002; Zacho RM et al. 2012]. Ficolin-3 has been shown to bind to patterns of bacterial polysaccharides such as d-fucose and galactose [Garlatti V et al. 2007]. In adition to pathogenic ligands ficolin-3 was reported to bind to apoptotic Jurkat cells [Kuraya M et al. 2005].
			REACT_163759 (Reactome)	Vitronectin interacts with C5b:C6:C7 complex preventing it from the binding with the cell membrane
			REACT_163768 (Reactome)	Cleavage of C4 exposes a highly reactive thioester bond on the C4b molecule. The thioester bond is rapidly inactivated by hydrolysis if C4b does not bind to the target cell surface [Sepp A et al 1993].
			REACT_163829 (Reactome)	CD59, the major inhibitor of the complement membrane attack complex, is an 18–20 kDa glycoprotein, linked to the membrane via a glycosylphosphatidylinositol (GPI)-anchor. It interacts with complement components C8 and C9 during assembly of the membrane attack complex (MAC) and inhibits C9 polymerization, thus preventing the formation of MAC [Lehto T and Meri S. 1993;Rollins SA et al 1991]
			REACT_163860 (Reactome)	Factor I (FI) inactivates C3 convertase activity by cleavage C3b producing iC3b, which remains bound to the membrane. A final proteolytic cleavage converts iC3b into two molecules, C3c, which is released into solution, and C3dg, which remains attached to the membrane. This cleavage requires CR1, which serves as a cofactor for cleavage of iC3b by factor I (Medof ME et al. 1982). iC3b and C3dg are active molecules, that can bind CR2 (CD21) to enhance B-cell immunity (Tuveson DA et al.1991; Sarrias MR et al. 2001).
			REACT_163870 (Reactome)	Complement proteins C8 and C9 can bind to VTN:C5b:C6:C7 to form soluble C5b-C9 complex in plasma. The vitronectin binding to C5b-C9 complex prevents C9 polymerization by rendering it water-soluble and lytic inactive.
			REACT_25075 (Reactome)	Metastable C3b can bind a wide variety of proteins and carbohydrates expressed on biological surfaces (Coico & Sunshine, 2009; Kimball 2010). This is an essentially random event (Dodds & Law, 1998); binding may be to host or microorganism. However, certain surface sugars have greater C3b binding rates, perhaps explaining variations in microorganism suceptibility (Pangburn, M. in The Complement System, Ed. Rother et al. 1998).
			REACT_25166 (Reactome)	The cleavage of C4 into C4a and C4b releases an acyl group from the intrachain thioester bond, allowing C4b to bond covalently to any adjacent biological substrates (Dodds & Law 1998). C4 is encoded at two loci, C4A and C4B. The C4b proteins derived from these genes are not identical and have different binding preferences (Law et al 1984, Sepp et al. 1993); C4A-derived C4b binds more efficiently than C4B-derived C4b to amino groups, while C4B-derived C4b is more effective than C4A in binding to hydroxyl groups. The site of C4b deposition is not clearly established (Møller-Kristensen et al. 2003) but generally accepted to be the activating cell membrane surface, though it may be the activating complex itself.
			REACT_7946 (Reactome)
			REACT_7948 (Reactome)	C3(H2O):Factor Bb is a C3 convertase, sometimes referred to as the initial C3 convertase (iC3). The Factor Bb component catalyzes the hydrolysis of C3 to produce C3b and C3a. This reaction is not known to be directly coupled to the association of C3b complexes with a cell surface. It is believed that a small proportion of C3b spontaneously associates with the cell surface, otherwise it is rapidly inactivated (Muller-Eberhard 1988).
			REACT_7950 (Reactome)
			REACT_7959 (Reactome)	C2 is cleaved into the large C2a and the small C2b fragment. This irreversible, extracellular reaction can be catalyzed by activated MBL, generated through the lectin pathway of complement activation (Vorup-Jensen et al. 2000), and by activated C1, generated through the classical pathway (Nasagawa and Stroud 1977). N.B. Early literature refers to the larger fragment of C2 as C2a. However, complement scientists decided that the smaller of all C fragments should be designated with an 'a', the larger with a 'b', changing the nomenclature for C2. For this reason recent literature may refer to the larger C2 fragment as C2b, and the classical C3 convertase as C4bC2b. Throughout this pathway, Reactome uses the current (Feb 2012) Uniprot names which adhere to the original naming practice.
			REACT_7965 (Reactome)	MBL or ficolins binding to carbohydrates on the target surface results in conformational changes in the lectin:MASPs complex. It in turn promotes a cleavage of proenzyme form of MASP between the CCP2 and the serine protease domains, which results in the generation of the active form. The active form of MASP-2 is able to cleave C4 and C2 to generate the C3 convertase (Vorup-Jensen T et al. 2000; Chen CB and Wallis R 2004). The active form of MASP-1 was shown to facilitate the complement activation by either direct cleavage of complex-bound MASP-2 or cleavage of C2 bound to C4 (Matsushita M et al. 2000; Heja D et al. 2012).
			REACT_7966 (Reactome)	C3b on a surface binds Factor B from solution to form a complex (Schreiber et al. 1978; Muller-Eberhard 1988).
			REACT_7976 (Reactome)
			REACT_7977 (Reactome)	In this irreversible reaction, the activated C1r subunit of the C1:antibody:antigen complex cleaves the C1s subunit of the complex, activating it in turn (Ziccardi and Cooper 1976). The resulting complex is a C4 activator.
			REACT_7978 (Reactome)	C1 activation requires interaction with two separate Fc domains, so pentavalent IgM antibody is far more efficient at complement activation than IgG antibody (Muller-Eberhard and Kunkel 1961). Antibody binding results in a conformational change in the C1r component of the C1 complex and a proteolytic cleavage of C1r, activating it (Ziccardi and Cooper 1976). This reaction is irreversible under physiological conditions.
			REACT_7981 (Reactome)	Factor D, a constitutively active serine protease found in trace amounts in the blood, cleaves a specific Arg-Lys bond in the Factor B component of the soluble C3(H2O):Factor B complex, yielding C3(H2O):Factor Bb and an inactive polypeptide, Factor Ba (Fearon and Austin 1975; Lesavre and Muller-Eberhard 1978; Lesavre et al. 1979; Schreiber et al. 1978).
			REACT_7982 (Reactome)
			REACT_7983 (Reactome)	The MBL polypeptide chain consists of a short N-terminal cysteine-rich region, a collagen-like region comprising 19 Gly-X-Y triplets, a 34-residue hydrophobic stretch, and a C-terminal C-type lectin domain. MBL monomers associate via their cysteine-rich and collagen-like regions to form homotrimers, and these in turn associate into oligomers. The predominant oligomers found in human serum contain three (MBL-I) or four (MBL-II) homotrimers (Fujita et al. 2004; Teillet et al. 2005). Extracellular MBL oligomers circulate in plasma in complexes with MASP1/2. The carbohydrate recognition domain (CRD) of MBL binds carbohydrates with 3- and 4- OH groups in the pyranose ring, such as mannose and N-acetyl-D-glucosamine, in the presence of Ca2+. Such motifs occur on the surfaces of viruses, bacteria, fungi and protozoa. The affinity of any one MBL binding site for a carbohydrate ligand is low, but interaction between multiple binding sites on an MBL oligomer and a repetitive carbohydrate motif on a target surface allow high-avidity binding. The specificity of the MBL binding site (it does not bind glucose or sialic acid) and the requirement for a repeated target motif may account for the failure of MBL to bind human glycoproteins under normal conditions (Petersen et al. 2001). This reaction in particular represents the interaction of MBL with bacterial mannose repeats.
			REACT_7986 (Reactome)	The complex of C3b:Factor Bb, stabilized on the cell surface by properdin, catalyzes the cleavage of C3 to yield C3b and C3a. The C3b is recruited to the C3b:Factor B complex through its interaction with properdin (Daha et al. 1976; Medicus et al. 1976; Hourcade 2006), yielding the alternate C5 convertase.
			REACT_7988 (Reactome)	The membrane attack complex is composed of one C5:C6:C7:C8 complex and between 12-15 C9 molecules (Podack et al. 1982 - 12 represented in this reaction).
			REACT_7989 (Reactome)	The same complexes as for C3 activation are employed for the cleavage of C5. C3 convertases with an additional C3b molecule covalently deposited in the immediate vicinity form the C5 convertases C3bBbC3b and C4b2aC3b, respectively. The second C3b acts like an anvil for C5: it interacts with C5 and presents C5 in the correct conformation for cleavage by the C2a or Bb enzyme.
			REACT_7990 (Reactome)	C4b and C2a bind to form the classical pathway C3-convertase (C4b2a complex), C3b and the Bb fragment of Factor B form the alternative pathway C3 convertase. The C3(H2O):Bb C3 convertase is sometimes called the initiating convertase, and the C5 convertases also have C3 convertase activity (Rawal & Pangburn 2001).
			REACT_8002 (Reactome)	The alpha chain of C4 is cleaved, releasing an N-terminal portion of this chain as C4a. The beta and gamma chains are not cleaved and remain linked to the alpha chain by disulfide bonds (Nagasawa et al. 1976, 1980). The resulting C4b heterotrimer undergoes a gross conformational change; the internal thioester in C4b becomes exposed and able to form covalent bonds with surrounding molecules (Law and Dodds 1997). A large proportion of the bonds formed are with water, but some will attach C4b to biological surfaces (Rother et al. 1998). This irreversible reaction can be catalyzed by activated MBL, generated through the lectin pathway of complement activation (Fujita et al. 2004; Hajela et al. 2002), and by activated C1, generated through the classical pathway (Muller-Eberhard and Lepow 1965). N.B. Humans have two highly polymorphic loci for Complement factor 4, C4A and C4B. C4A alleles carry the Rodgers (Rg) blood group antigens while the C4B alleles carry the Chido (Ch) blood group antigens. The two loci encode non identical C4 peptides; C4 derived from C4A reacts more rapidly with the amino groups of peptide antigens while C4B allotypes react more rapidly with the hydroxyl group of carbohydrate antigens. The names of the two loci are always represented in uppercase. C4a and C4b refer to the peptide products of Complement Factor 4 cleavage.
			REACT_8007 (Reactome)	The thioester linkage between cysteine residue 1010 and glutamine residue 1013 in the alpha chain of Complement factor 3 (C3) can spontaneously hydrolyze, yielding so-called C3(H2O) (Tack et al. 1980; Pangburn & Muller-Eberhard 1980; Pangburn et al. 1981). Thioester bond hydrolysis causes conformational rearrangements that give C3(H2O) the ability to bind Factor B. The spontaneous hydrolysis rate of C3 under physiological conditions and temperature is about l% per hour, thus the C3b-like properties of C3(H2O) provide a continuous low level initiation of the alternative pathway of complement activation (Pangburn & Muller-Eberhard 1983). If not bound by Factor B, C3(H2O) binds Factor H and is inactivated by Factor I
			REACT_8013 (Reactome)	Thioester bond hydrolysis causes conformational rearrangements that give C3(H2O) the ability to bind Factor B (Schreiber et al. 1978). The spontaneous hydrolysis rate of C3 under physiological conditions and temperature is about l% per hour, thus the C3b-like properties of C3(H2O) provide a continuous low level initiation of the alternative pathway of complement activation (Pangburn & Muller-Eberhard 1983).
			REACT_8014 (Reactome)	C4b and C2a form a complex termed the classical pathway C3 convertase (Muller-Eberhard et al. 1967). C2a that fails to bind C4b is rapidly inactivated.
			REACT_8018 (Reactome)	C3b:Bb is naturally labile with a half-life of ~90 s; association of the complex with properdin extends the half-life to ~30 min. (Medicus et al. 1976). Properdin is found in the blood as a mixture of multivalent oligomers: 30% dimers, 45% trimers, 10% tetramers, and 15% higher oligomers. Monomers associate with one another in a head-to-tail arrangement, producing closed circular structures (Smith et al. 1984). These features suggest that the properdin oligomer associated with a C3b:Bb complex on a surface such as a cell membrane can facilitate recruitment of additional C3b:Bb complexes to the site (Farries et al. 1988; Hourcade 2006).
			REACT_8022 (Reactome)	C5 convertases are serine proteases that cleave C5 with high efficiency; the C3 convertases can cleave C5 but have a poor affinity for C5, with a Km of 6-9 microM. The high affinity C5 convertases are generated when the low affinity C3/C5 convertases such as C4b:C2a deposit C3b by cleaving native C3. These C3b-containing C3/C5 convertases have Km values of 0.005 microM, well below the normal concentration of C5 in blood (0.37 microM). They have very low Vmax rates, just one C5 cleaved per 1–4 min per enzyme (Rawal & Pangburn 1998).
			REACT_8026 (Reactome)	Factor D, a constitutively active serine protease found in trace amounts in the blood, cleaves a specific Arg-Lys bond in the Factor B component of the cell surface-associated C3b:Factor B complex, yielding the alternate C3 convertase C3bBb on the surface and releasing an inactive polypeptide, Factor Ba (Lesavre and Muller-Eberhard 1978; Lesavre et al. 1979; Schreiber et al. 1978).
VTN(20-?)			REACT_163759 (Reactome)
	VTN:C5b:C6:C7:C8:C9	Arrow	REACT_163870 (Reactome)
	VTN:C5b:C6:C7	Arrow	REACT_163759 (Reactome)
VTN:C5b:C6:C7			REACT_163870 (Reactome)
	iC3b	Arrow	REACT_118650 (Reactome)
	iC3b	Arrow	REACT_118841 (Reactome)
	thioester-C1010-Q1013-C4b	Arrow	REACT_8002 (Reactome)
thioester-C1010-Q1013-C4b			REACT_118763 (Reactome)
thioester-C1010-Q1013-C4b			REACT_163768 (Reactome)
thioester-C1010-Q1013-C4b			REACT_25166 (Reactome)