MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities. Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities. The Journal of biological chemistry 2017 imex curation Águila S., Izaguirre G., Martínez-Martínez I., Vicente V., Olson ST., Corral J. Rare diseases - Interactions investigated in the context of Rare genetic disease FXa (8 μm) or FIIa (19 μm) (Enzyme Research Laboratories, Swansea, UK) -> human origin, data-processing comment added. Protease assay (Table 1) not captured as no info on substrates. According to data-sheet information, FXa and FIIa are of human origin. stolson@uic.edu Only protein-protein interactions imex curation human-293 ebna Homo sapiens 293 ebna 293 ebna comigration in gel comigration in gel electrophoresis comigration in gel weight identificat confirmation by molecular weight weight identificat Águila S., Izaguirre G., Martínez-Martínez I., Vicente V., Olson ST., Corral J. Rare diseases - Interactions investigated in the context of Rare genetic disease FXa (8 μm) or FIIa (19 μm) (Enzyme Research Laboratories, Swansea, UK) -> human origin, data-processing comment added. Protease assay (Table 1) not captured as no info on substrates. According to data-sheet information, FXa and FIIa are of human origin. stolson@uic.edu Accepted 2021-JUL-04 AT 15:13 BST AT 15:13 BST by KALPANAP The Journal of biological chemistry 2017 Only protein-protein interactions imex curation imex curation Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities. Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities. The Journal of biological chemistry 2017 imex curation Águila S., Izaguirre G., Martínez-Martínez I., Vicente V., Olson ST., Corral J. Rare diseases - Interactions investigated in the context of Rare genetic disease FXa (8 μm) or FIIa (19 μm) (Enzyme Research Laboratories, Swansea, UK) -> human origin, data-processing comment added. Protease assay (Table 1) not captured as no info on substrates. According to data-sheet information, FXa and FIIa are of human origin. stolson@uic.edu Only protein-protein interactions imex curation human-plasma homo sapiens blood plasma plasma blood plasma comigration in gel comigration in gel electrophoresis comigration in gel weight identificat confirmation by molecular weight weight identificat Águila S., Izaguirre G., Martínez-Martínez I., Vicente V., Olson ST., Corral J. Rare diseases - Interactions investigated in the context of Rare genetic disease FXa (8 μm) or FIIa (19 μm) (Enzyme Research Laboratories, Swansea, UK) -> human origin, data-processing comment added. Protease assay (Table 1) not captured as no info on substrates. According to data-sheet information, FXa and FIIa are of human origin. stolson@uic.edu Accepted 2021-JUL-04 AT 15:13 BST AT 15:13 BST by KALPANAP The Journal of biological chemistry 2017 Only protein-protein interactions imex curation imex curation p00742-pro_0000027787 Coagulation factor X Stuart factor Stuart-Prower factor F10 protein protein human Homo sapiens Human ANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK 41 488 8B7187997CC1D910 p00734-pro_0000028160 Prothrombin F2 Coagulation factor II protein protein human Homo sapiens Human ANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE 44 622 66DD4325E7CB9F07 p01008-pro_0000032489 Antithrombin-III Serpin C1 PRO0309 SERPINC1 AT3 protein protein human Homo sapiens Human HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK 33 464 2DD065FEBA9738B5 antithrombin-dimer-1 2 5 unspecified role unspecified role neutral component neutral component purified purified P01008-PRO_0000032489:p.Ser365Leu mutation causing mutation causing an interaction mutation enabling interaction mutation causing mutation causing an interaction certain certain sequence position certain certain certain sequence position certain S L Thu Apr 22 12:09:55 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'PRO_0000032489:p.Ser365Leu' disulfide bond disulfide bond disulfide bridge SS-bond Fig. 2A serpinc1-3 1 5 unspecified role unspecified role unspecified role unspecified role purified purified P01008-PRO_0000032489:p.Ser365Leu mutation causing mutation causing an interaction mutation enabling interaction mutation causing mutation causing an interaction certain certain sequence position certain certain certain sequence position certain S L Thu Apr 22 12:52:26 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'PRO_0000032489:p.Ser365Leu' disulfide bond disulfide bond disulfide bridge SS-bond Fig. 2B f2-serpinc1-1 1 4 unspecified role unspecified role neutral component neutral component purified purified 5 unspecified role unspecified role neutral component neutral component purified purified P01008-PRO_0000032489:p.Ser365Leu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain S L Thu Apr 22 13:31:56 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'PRO_0000032489:p.Ser365Leu' direct interaction direct interaction Fig. 3A CHEBI:28304 - heparin f10-serpinc1-1 1 3 unspecified role unspecified role neutral component neutral component purified purified 5 unspecified role unspecified role neutral component neutral component purified purified P01008-PRO_0000032489:p.Ser365Leu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain S L Thu Apr 22 11:32:28 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'PRO_0000032489:p.Ser365Leu' direct interaction direct interaction Fig. 3B CHEBI:35369 - pentasaccharide