IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Journal of immunology (Baltimore, Md. : 1950) 2008 imex curation Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). waiting for Birgit to make the complex Dark space = 35? livija.deban@humanitas.it Only protein-protein interactions imex curation in vitro In vitro protease assay protease assay western blot western blot Immuno blot Immuno blot Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). Solution Cofactor assay for C3b inactivation livija.deban@humanitas.it Accepted 2017-FEB-08 AT 11:19 GMT AT 11:19 GMT by ORCHARD Journal of immunology (Baltimore, Md. : 1950) 2008 Only protein-protein interactions imex curation imex curation EBI-11785636 is definitely Fig 1B as 1A is shown in EBI-11786163. Added the PTM as "required" in the short label. I have asked Birgit to create the complex. I have added the Y402H mutation as one of "no effect" I have added the new complex to fig 4B as well - EBI-11786487.; I think I have done what you ask here- (I cannot see any of the other interactions need C3B adding or replacing something else. -as not used in fig 1); Missing interaction- EBI-11786626 - moved- although I cannot imagine how it got into the other Expt. I have added the complex C3B to both interactions here. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Journal of immunology (Baltimore, Md. : 1950) 2008 imex curation Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). waiting for Birgit to make the complex Dark space = 35? livija.deban@humanitas.it Only protein-protein interactions imex curation in vitro In vitro solid phase assay solid phase assay antibody detection identification by antibody antibody detection Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). livija.deban@humanitas.it Accepted 2017-FEB-08 AT 11:19 GMT AT 11:19 GMT by ORCHARD Journal of immunology (Baltimore, Md. : 1950) 2008 Only protein-protein interactions imex curation imex curation EBI-11785636 is definitely Fig 1B as 1A is shown in EBI-11786163. Added the PTM as "required" in the short label. I have asked Birgit to create the complex. I have added the Y402H mutation as one of "no effect" I have added the new complex to fig 4B as well - EBI-11786487.; I think I have done what you ask here- (I cannot see any of the other interactions need C3B adding or replacing something else. -as not used in fig 1); Missing interaction- EBI-11786626 - moved- although I cannot imagine how it got into the other Expt. I have added the complex C3B to both interactions here. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Journal of immunology (Baltimore, Md. : 1950) 2008 imex curation Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). waiting for Birgit to make the complex Dark space = 35? livija.deban@humanitas.it Only protein-protein interactions imex curation in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). livija.deban@humanitas.it Accepted 2017-FEB-08 AT 11:19 GMT AT 11:19 GMT by ORCHARD Journal of immunology (Baltimore, Md. : 1950) 2008 Only protein-protein interactions imex curation imex curation EBI-11785636 is definitely Fig 1B as 1A is shown in EBI-11786163. Added the PTM as "required" in the short label. I have asked Birgit to create the complex. I have added the Y402H mutation as one of "no effect" I have added the new complex to fig 4B as well - EBI-11786487.; I think I have done what you ask here- (I cannot see any of the other interactions need C3B adding or replacing something else. -as not used in fig 1); Missing interaction- EBI-11786626 - moved- although I cannot imagine how it got into the other Expt. I have added the complex C3B to both interactions here. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. Journal of immunology (Baltimore, Md. : 1950) 2008 imex curation Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). waiting for Birgit to make the complex Dark space = 35? livija.deban@humanitas.it Only protein-protein interactions imex curation in vitro In vitro elisa enzyme linked immunosorbent assay ELISA ELISA elisa antibody detection identification by antibody antibody detection Deban L., Jarva H., Lehtinen MJ., Bottazzi B., Bastone A., Doni A., Jokiranta TS., Mantovani A., Meri S. This has now been returned for re-checking as the Complex has now been created. This process only took ~6 months! (Ac no available but complex not checked according to Birgit). livija.deban@humanitas.it Accepted 2017-FEB-08 AT 11:19 GMT AT 11:19 GMT by ORCHARD Journal of immunology (Baltimore, Md. : 1950) 2008 Only protein-protein interactions imex curation imex curation EBI-11785636 is definitely Fig 1B as 1A is shown in EBI-11786163. Added the PTM as "required" in the short label. I have asked Birgit to create the complex. I have added the Y402H mutation as one of "no effect" I have added the new complex to fig 4B as well - EBI-11786487.; I think I have done what you ask here- (I cannot see any of the other interactions need C3B adding or replacing something else. -as not used in fig 1); Missing interaction- EBI-11786626 - moved- although I cannot imagine how it got into the other Expt. I have added the complex C3B to both interactions here. calcium(2+) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) c1qc_human Complement C1q subcomponent subunit C C1QC C1QG protein protein human Homo sapiens Human MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD FA17117EB7ABFC12 p05156-pro_0000027568 Complement factor I CFI IF C3B/C4B inactivator protein protein human Homo sapiens Human KVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV 19 583 7D5CFD93EBB4C26D p01024-pro_0000005908 Complement C3 beta chain C3 CPAMD1 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 protein protein human Homo sapiens Human SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAA 23 667 C4754001F1A97259 ptx3_human Pentraxin-related protein PTX3 Pentaxin-related protein PTX3 TNFAIP5 TSG14 Tumor necrosis factor alpha-induced protein 5 Tumor necrosis factor-inducible gene 14 protein PTX3 protein protein human Homo sapiens Human MHLLAILFCALWSAVLAENSDDYDLMYVNLDNEIDNGLHPTEDPTPCACGQEHSEWDKLFIMLENSQMRERMLLQATDDVLRGELQRLREELGRLAESLARPCAPGAPAEARLTSALDELLQATRDAGRRLARMEGAEAQRPEEAGRALAAVLEELRQTRADLHAVQGWAARSWLPAGCETAILFPMRSKKIFGSVHPVRPMRLESFSACIWVKATDVLNKTILFSYGTKRNPYEIQLYLSYQSIVFVVGGEENKLVAEAMVSLGRWTHLCGTWNSEEGLTSLWVNGELAATTVEMATGHIVPEGGILQIGQEKNGCCVGGGFDETLAFSGRLTGFNIWDSVLSNEEIRETGGAESCHIRGNIVGWGVTEIQPHGGAQYVS 09BCE02E2A62D62A p01024-pro_0000005915 Complement C3d fragment C3 CPAMD1 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 protein protein human Homo sapiens Human HLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSR 1002 1303 D37DE55A093D6DF6 p01024-pro_0000005911 Complement C3b alpha' chain C3 CPAMD1 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 protein protein human Homo sapiens Human SNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN 749 1663 1E32EA0CEA20EA81 heparin Heparin small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) c1qa_human Complement C1q subcomponent subunit A C1QA protein protein human Homo sapiens Human MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFLIFPSA DIP protein P02745 original sequence version: null 8FF6B6AE02D49C4C cfah_human Complement factor H CFH HF HF1 HF2 H factor 1 protein protein human Homo sapiens Human MRLLAKIICLMLWAICVAEDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRCTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRVKTCSKSSIDIENGFISESQYTYALKEKAKYQCKLGYVTADGETSGSITCGKDGWSAQPTCIKSCDIPVFMNARTKNDFTWFKLNDTLDYECHDGYESNTGSTTGSIVCGYNGWSDLPICYERECELPKIDVHLVPDRKKDQYKVGEVLKFSCKPGFTIVGPNSVQCYHFGLSPDLPICKEQVQSCGPPPELLNGNVKEKTKEEYGHSEVVEYYCNPRFLMKGPNKIQCVDGEWTTLPVCIVEESTCGDIPELEHGWAQLSSPPYYYGDSVEFNCSESFTMIGHRSITCIHGVWTQLPQCVAIDKLKKCKSSNLIILEEHLKNKKEFDHNSNIRYRCRGKEGWIHTVCINGRWDPEVNCSMAQIQLCPPPPQIPNSHNMTTTLNYRDGEKVSVLCQENYLIQEGEEITCKDGRWQSIPLCVEKIPCSQPPQIEHGTINSSRSSQESYAHGTKLSYTCEGGFRISEENETTCYMGKWSSPPQCEGLPCKSPPEISHGVVAHMSDSYQYGEEVTYKCFEGFGIDGPAIAKCLGEKWSHPPSCIKTDCLSLPSFENAIPMGEKKDVYKAGEQVTYTCATYYKMDGASNVTCINSRWTGRPTCRDTSCVNPPTVQNAYIVSRQMSKYPSGERVRYQCRSPYEMFGDEEVMCLNGNWTEPPQCKDSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR DIP protein P08603 original sequence version: 161 DIP protein P08603-1 original sequence version: 149 3C26D62A2BF9BFEE c1qb_human Complement C1q subcomponent subunit B C1QB protein protein human Homo sapiens Human MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA D80C753C0D430EDC ptx3-cfh-1 5 15 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 10 unspecified role unspecified role prey prey required_ptm glycores glycosylated residue GlycoRes undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined observed-ptm observed-ptm observed ptm observed-ptm crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 1B, 2F cfh-ptx3-2 3 15 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 10 unspecified role unspecified role prey prey region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 1C cfh-ptx3-3 4 15 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 10 unspecified role unspecified role prey prey crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 1D c1q_human-ptx3-1 4 30 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 10 unspecified role unspecified role prey prey crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. physical association physical association 1E c1q_human-ptx3-2 3 30 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 10 unspecified role unspecified role prey prey region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. physical association physical association 1F c1q_human-ptx3-3 3 15 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 10 unspecified role unspecified role prey prey region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 1Fi cfh-ptx3-4 3 15 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 10 unspecified role unspecified role prey prey region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. 6 stimulator stimulator unspecified role unspecified role direct interaction direct interaction 1Fii The presence of 10 mM EGTA (calcium chelation) reduced significantly the PTX3-FH interaction. ptx3-cfh-2 5 15 unspecified role unspecified role prey prey scr/sushi_domain_7 required to bind necessary binding region required to bind range range range range scr/sushi_domains_19+20 sufficient to bind sufficient binding region sufficient to bind range range range range P08603:p.Tyr402His mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain Y H Wed May 02 18:21:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr402his' Tue Jun 30 16:39:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr402His' picpg Komagataella pastoris (strain GS115 / ATCC 20864) Yeast Pichia pastoris 10 unspecified role unspecified role bait bait crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 2A ptx3-cfh-3 5 15 unspecified role unspecified role prey prey c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range scr/sushi_domains_15+20 sufficient to bind sufficient binding region sufficient to bind range range range range spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection 10 unspecified role unspecified role bait bait n_terminal_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. 54 56 direct interaction direct interaction 2Ai, 2D ptx3-cfh-4 5 15 unspecified role unspecified role prey prey human-serum Homo sapiens serum Serum 10 unspecified role unspecified role bait bait n_terminal_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 1A, 2B, 3A The C-terminal region of PTX3 also bound to FH, but weakly. ptx3-cfh-5 5 15 unspecified role unspecified role prey prey c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range scr/sushi_domains_1-7 sufficient to bind sufficient binding region sufficient to bind range range range range spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection 10 unspecified role unspecified role bait bait c_terminal_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. 64 66 direct interaction direct interaction 2C ptx3-cfh-6 5 15 unspecified role unspecified role prey prey scr/sushi_domains_19+20 sufficient to bind sufficient binding region sufficient to bind range range range range picpg Komagataella pastoris (strain GS115 / ATCC 20864) Yeast Pichia pastoris 10 unspecified role unspecified role bait bait n_terminal_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. 71 69 direct interaction direct interaction 2E, 3B, 3C C3d exhibited no inhibitory effect on the FH–PTX3 interaction. ptx3-cfh-7 5 13 competitor competitor competitor unspecified role unspecified role 15 unspecified role unspecified role prey prey human-serum Homo sapiens serum Serum 10 unspecified role unspecified role bait bait n_terminal_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 3A The C-terminal region of PTX3 also bound to FH, but weakly. ptx3-cfh-8 5 13 competitor competitor competitor unspecified role unspecified role 15 unspecified role unspecified role prey prey scr/sushi_domains_19+20 sufficient to bind sufficient binding region sufficient to bind range range range range picpg Komagataella pastoris (strain GS115 / ATCC 20864) Yeast Pichia pastoris 10 unspecified role unspecified role bait bait n_terminal_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. 80 82 direct interaction direct interaction 3B ptx3-cfh-9 5 11 stimulator stimulator unspecified role unspecified role human-serum Homo sapiens serum Serum 15 unspecified role unspecified role prey prey picpg Komagataella pastoris (strain GS115 / ATCC 20864) Yeast Pichia pastoris 10 unspecified role unspecified role bait bait crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. direct interaction direct interaction 3C C3d exhibited no inhibitory effect on the FH–PTX3 interaction. ptx3-cfh-10 5 89 unspecified role unspecified role prey prey human-serum Homo sapiens serum Serum 15 unspecified role unspecified role prey prey picpg Komagataella pastoris (strain GS115 / ATCC 20864) Yeast Pichia pastoris 10 unspecified role unspecified role bait bait crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. physical association physical association 4A ptx3-cfh-11 5 89 unspecified role unspecified role bait bait human-serum Homo sapiens serum Serum 15 unspecified role unspecified role prey prey picpg Komagataella pastoris (strain GS115 / ATCC 20864) Yeast Pichia pastoris physical association physical association 4B The presence of PTX3 did not interfere with the binding of FH to C3b. 545w-1 2 8 enzyme enzyme neutral component neutral component human-serum Homo sapiens serum Serum 89 enzyme target enzyme target substrate substrate neutral component neutral component human-serum Homo sapiens serum Serum 15 ancillary ancillary neutral component neutral component human-serum Homo sapiens serum Serum protein cleavage protein cleavage 5A PTX3 had no inhibitory effect on the cofactor activity of FH in the fluid phase. c3-cfh-3 2 8 enzyme enzyme neutral component neutral component human-serum Homo sapiens serum Serum 89 enzyme target enzyme target substrate substrate neutral component neutral component human-serum Homo sapiens serum Serum 15 ancillary ancillary neutral component neutral component human-serum Homo sapiens serum Serum 10 ancillary ancillary neutral component neutral component crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. protein cleavage protein cleavage 5B When bound to a surface (PTX3-coated wells), PTX3 bound and retained FH and allowed it to perform its cofactor function. c1q_human Complement component C1q complex C1q Complement 1q C1QA-C1QB-C1QC complex 6xC1QA:6xC1QB:6xC1QC 16 unspecified role unspecified role cys-31 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qac binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role c1ab binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cys-32 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 14 unspecified role unspecified role cys-26 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qbc binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role c1ab binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cys-32 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 16 unspecified role unspecified role cys-31 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qac binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 14 unspecified role unspecified role cys-26 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qbc binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role c1ab binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cys-32 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 16 unspecified role unspecified role cys-31 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qac binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role c1ab binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cys-32 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 16 unspecified role unspecified role c1qac binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cys-31 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain 14 unspecified role unspecified role cys-26 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qbc binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 14 unspecified role unspecified role cys-26 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qbc binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 16 unspecified role unspecified role cys-31 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qac binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 14 unspecified role unspecified role cys-26 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qbc binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role c1ab binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cys-32 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role c1ab binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain cys-32 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 14 unspecified role unspecified role cys-26 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qbc binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 16 unspecified role unspecified role cys-31 direct binding direct binding region direct binding certain certain sequence position certain certain certain sequence position certain c1qac binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 111 105 106 112 108 115 109 109 130 124 115 151 130 118 114 121 148 124 117 120 139 123 127 151 148 126 138 132 136 129 133 135 141 144 145 147 142 154 150 157 153 156 physical association physical association human Homo sapiens Human stable complex stable complex physical interaction evidence used in manual assertion physical interaction evidence used in manual assertion IPI inferred from physical interaction Complement component C1q deficiency (C1QD) [MONDO:0013343]: a disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis. coronavirus The complex comprises of six heterotrimeric collagen-like triple helices, formed from triplets of the A, B, and C chains, that associate in their N-terminal half to form a stalk, then diverge to form individual stems, each terminating in a C-terminal globular domain. Each of the six heterotrimeric globular heads or domains is made up of the globular domains from one A, one B, and one C chain, each of which in turn has its own ligand specificity. The six collagen-like stalks appear to be fibril-like and exist in the central region. The collagen-like region and the globular heads can independently interact with a multiplicity of biological structures including pathogen-associated and cell associated molecules, also each of the individual globular head domains is capable of independently interacting with specific ligands. Chains A and B are disulfide-linked whilst the C chain forms a disulfide bond with the C chain of the next strand. Molecular weight 460 kDa. Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-1920), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning. Heterooctadecamer created with intact-jami-dbscripts c3b_human Complement C3b complex C3b dimer 12 unspecified role unspecified role C3 beta chain binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 unspecified role unspecified role C3b alpha(prime) chain binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 159 161 physical association physical association human Homo sapiens Human stable complex stable complex physical interaction evidence used in manual assertion physical interaction evidence used in manual assertion IPI inferred from physical interaction A protein complex of the alternative pathway of complement activation of the innate immune system. Complement C3 precurser is activated by cleavage into C3a and C3b by C3 convertases, either C4bC2a in the classical and lectin pathways or C3(H2O)Bb, C3bBb, C3bBbC3b, C3bBbP or C3bBbC3bP in the alternative pathway. C3b acts as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex (CPX-6159) assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response. Activation of C3b leads to an amplification cascade that generates more C3 convertase, deposits more C3b at the local site and switches C3 convertases to C5 convertases. To protect host cells from inadvertent complement activation the activation of C3b is tightly regulated by either disrupting the C3 convertases or aiding in the proteolytic degradation of C3b. Bacteria and viruses possess C3b proteases to evade the complement response. Lack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue. The alternative pathway is continuously activated at a low level. C3 precursor is first processed by the removal of 4 Arg residues and spontaneous hydrolysis due to the breakdown of the internal thioester bond forms C3(H2O) (disulfide bonded P01024-PRO_0000005909 & P01024-PRO_0000005908). C3(H2O) subsequently binds factor B that is cleaved by Factor D (P00746) into 2 fragments: CFBa and CFBb. CFBb, a serine protease, then combines with complement factor C3(H2O) or C3b to generate the C3 or C5 convertases. Proteolytic cleavage of C3 to C3b is accompanied by large conformational changes that result in the exposure of cryptic binding sites required for convertase assembly and regulation. This includes a significant movement of the thioester-bond-containing domain through which C3b attaches to target surfaces. Heterodimer Complement component 3 (C3) deficiency [Orphanet:280133]: a rare, autosomal recessive defect of the complement classical pathway. Patients develop recurrent, severe, pyogenic infections because of ineffective opsonization of pathogens. Some patients may also develop autoimmune disorders, such as arthralgia and vasculitic rashes, lupus-like syndrome and membranoproliferative glomerulonephritis. Atypical hemolytic-uremic syndrome with C3 anomaly [Orphanet:2134 & Orphanet:93575]: an autosomal dominant, atypical form of hemolytic-uremic syndrome (aHUS, a thrombotic microangiopathy) characterized by mechanical hemolytic anemia, thrombocytopenia, and renal dysfunction. Age-related macular degeneration [EFO:0001365]: age-related macular degeneration usually in older adults which results in a loss of vision in the center of the visual field (the macula lutea) because of damage to the retina. Manifests as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Occurs in dry and wet forms. Most common cause of irreversible vision loss in the developed world. Accepted 2017-JAN-19 by ORCHARD coronavirus