{ "uniprot_canonical_ac": "P00734-1", "uniprot_ac": "P00734", "uniprot_id": "THRB_HUMAN", "mass": { "chemical_mass": 70037.0, "monoisotopic_mass": 70037.0 }, "refseq": { "ac": "NP_000497", "name": "prothrombin preproprotein", "summary": "This gene encodes the prothrombin protein (also known as coagulation factor II). This protein is proteolytically cleaved in multiple steps to form the activated serine protease thrombin. The activated thrombin enzyme plays an important role in thrombosis and hemostasis by converting fibrinogen to fibrin during blood clot formation, by stimulating platelet aggregation, and by activating additional coagulation factors. Thrombin also plays a role in cell proliferation, tissue repair, and angiogenesis as well as maintaining vascular integrity during development and postnatal life. Peptides derived from the C-terminus of this protein have antimicrobial activity against E. coli and P. aeruginosa. Mutations in this gene lead to various forms of thrombosis and dysprothrombinemia. Rapid increases in cytokine levels following coronavirus infections can dysregulate the coagulation cascade and produce thrombosis, compromised blood supply, and organ failure. [provided by RefSeq, May 2020].", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497" }, "gene_names": [ { "name": "F2", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/P00734", "id": "P00734" }, { "name": "F2", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497", "id": "NP_000497" }, { "name": "PT; RPRGL2; THPH1", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497", "id": "NP_000497" } ], "protein_names": [ { "name": "Prothrombin", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "P00734" }, { "name": "3.4.21.5", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P00734" }, { "name": "Coagulation factor II", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P00734" }, { "name": "prothrombin B-chain; prepro-coagulation factor II; thrombin factor II", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497", "id": "NP_000497" }, { "name": "prothrombin preproprotein", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497", "id": "NP_000497" } ], "function": [ { "annotation": "Activated protein C, protein S, and tissue factor pathway inhibitor cooperate to inhibit thrombin activation.", "evidence": [ { "database": "RefSeq", "id": "NP_000497", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497" }, { "database": "PubMed", "id": "37660436", "url": "https://glygen.org/publication/PubMed/37660436" } ] }, { "annotation": "C-terminal peptides of thrombin display antimicrobial activity against Gram-positive and Gram-negative bacteria. Publication Status: Online-Only", "evidence": [ { "database": "RefSeq", "id": "NP_000497", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497" }, { "database": "PubMed", "id": "20421939", "url": "https://glygen.org/publication/PubMed/20421939" } ] }, { "annotation": "Impact of Fibrinogen, Fibrin Thrombi, and Thrombin on Cancer Cell Extravasation Using In Vitro Microvascular Networks.", "evidence": [ { "database": "RefSeq", "id": "NP_000497", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497" }, { "database": "PubMed", "id": "37119127", "url": "https://glygen.org/publication/PubMed/37119127" } ] }, { "annotation": "Low alpha-thrombin/GPIb-alpha interaction may contribute to platelet hyperreactivity in COVID-19 patients", "evidence": [ { "database": "RefSeq", "id": "NP_000497", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497" }, { "database": "PubMed", "id": "37857294", "url": "https://glygen.org/publication/PubMed/37857294" } ] }, { "annotation": "This gene encodes the prothrombin protein (also known as coagulation factor II). This protein is proteolytically cleaved in multiple steps to form the activated serine protease thrombin. The activated thrombin enzyme plays an important role in thrombosis and hemostasis by converting fibrinogen to fibrin during blood clot formation, by stimulating platelet aggregation, and by activating additional coagulation factors. Thrombin also plays a role in cell proliferation, tissue repair, and angiogenesis as well as maintaining vascular integrity during development and postnatal life. Peptides derived from the C-terminus of this protein have antimicrobial activity against E. coli and P. aeruginosa. Mutations in this gene lead to various forms of thrombosis and dysprothrombinemia. Rapid increases in cytokine levels following coronavirus infections can dysregulate the coagulation cascade and produce thrombosis, compromised blood supply, and organ failure. [provided by RefSeq, May 2020].", "evidence": [ { "database": "RefSeq", "id": "NP_000497", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497" } ] }, { "annotation": "Thrombin, a Key Driver of Pathological Inflammation in the Brain. Review article Publication Status: Online-Only", "evidence": [ { "database": "RefSeq", "id": "NP_000497", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000497" }, { "database": "PubMed", "id": "37174621", "url": "https://glygen.org/publication/PubMed/37174621" } ] }, { "annotation": "Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.", "evidence": [ { "database": "UniProtKB", "id": "E9PIT3", "url": "https://www.uniprot.org/uniprot/E9PIT3#function" }, { "database": "UniProtKB", "id": "ARBA00025390", "url": "https://www.uniprot.org/uniprot/ARBA00025390#function" }, { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734#function" }, { "database": "PubMed", "id": "2856554", "url": "https://glygen.org/publication/PubMed/2856554" } ] } ], "disease": [ { "disease_id": "DOID:0080701", "recommended_name": { "id": "DOID:0080701", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:0080701", "name": "prothrombin thrombophilia", "description": "A thrombophilia that is characterized by increases the risk of blood clots including deep vein thrombosis and pulmonary embolism and that has_material_basis_in heterozygous mutation in the thrombin gene (F2 gene) on chromosome 11p11." }, "synonyms": [ { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia due to thrombin defect", "description": "The formation of a blood clot (thrombus) in the lumen of a vein." }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "Venous thromboembolism", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin-related thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia 1 due to thrombin defect", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia due to thrombin defect", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "venous thromboembolism, susceptibility to", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "venous thrombosis, protection against", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "THPH1", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "factor II-related thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "hyperprothrombinemia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin 20210G>A thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin G20210A thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thromboembolism, susceptibility to", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia due to factor 2 defect", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombosis, protection against", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "venous thrombosis", "description": "" }, { "id": "MIM:188050", "resource": "MIM", "url": "https://www.omim.org/entry/188050", "name": "Thrombophilia due to thrombin defect", "description": "Thrombophilia due to thrombin defect" } ], "evidence": [ { "id": "188050", "database": "MIM", "url": "https://www.omim.org/entry/188050" } ] }, { "disease_id": "DOID:2235", "recommended_name": { "id": "DOID:2235", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2235", "name": "prothrombin deficiency", "description": "A thrombophilia that is characterized by bleeding symptoms due to low levels of circulating prothrombin, and has_material_basis_in autosomal recessive inheritance of homozygous or compound heterozygous mutation in the gene encoding coagulation factor II, also known as prothrombin, on chromosome 11p11." }, "synonyms": [ { "id": "DOID:2235", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2235", "name": "Congenital factor II deficiency", "description": "" }, { "id": "DOID:2235", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2235", "name": "hypoprothrombinemia", "description": "" }, { "id": "DOID:2235", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2235", "name": "Hereditary factor II deficiency disease", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "congenital prothrombin deficiency", "description": "Congenital factor II deficiency is an inherited bleeding disorder due to reduced activity of factor II (FII, prothrombin) and characterized by mucocutaneous bleeding symptoms." }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "factor 2 deficiency", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "factor II deficiency", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "hypoprothrombinemia", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "prothrombin deficiency", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "Dysprothrombinemia", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "congenital prothrombin deficiency", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "hereditary prothrombin deficiency", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "congenital factor II deficiency", "description": "" }, { "id": "MONDO:0013361", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013361", "name": "prothrombin deficiency, congenital", "description": "" }, { "id": "MIM:613679", "resource": "MIM", "url": "https://www.omim.org/entry/613679", "name": "Factor II deficiency", "description": "Factor II deficiency" } ], "evidence": [ { "id": "613679", "database": "MIM", "url": "https://www.omim.org/entry/613679" } ] }, { "disease_id": "DOID:2452", "recommended_name": { "id": "DOID:2452", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2452", "name": "thrombophilia", "description": "A blood coagulation disease that is characterized by an increased tendency to form clots." }, "synonyms": [ { "id": "DOID:2452", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2452", "name": "hypercoagulability state", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia due to thrombin defect", "description": "The formation of a blood clot (thrombus) in the lumen of a vein." }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "Venous thromboembolism", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin-related thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia 1 due to thrombin defect", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia due to thrombin defect", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "venous thromboembolism, susceptibility to", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "venous thrombosis, protection against", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "THPH1", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "factor II-related thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "hyperprothrombinemia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin 20210G>A thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "prothrombin G20210A thrombophilia", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thromboembolism, susceptibility to", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombophilia due to factor 2 defect", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "thrombosis, protection against", "description": "" }, { "id": "MONDO:0008559", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008559", "name": "venous thrombosis", "description": "" }, { "id": "MIM:188050", "resource": "MIM", "url": "https://www.omim.org/entry/188050", "name": "Thrombophilia due to thrombin defect", "description": "Thrombophilia due to thrombin defect" } ], "evidence": [ { "id": "188050", "database": "MIM", "url": "https://www.omim.org/entry/188050" } ] }, { "disease_id": "DOID:3526", "recommended_name": { "id": "DOID:3526", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:3526", "name": "cerebral infarction", "description": "A cerebrovascular disease that is characterized by an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain." }, "synonyms": [ { "id": "DOID:3526", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:3526", "name": "CVA - Cerebral infarction", "description": "" }, { "id": "DOID:3526", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:3526", "name": "Cerebral infarct", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "obsolete susceptibility to ischemic stroke", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "cerebral infarction, susceptibility to", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "ischemic stroke, susceptibility to", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "stroke, ischemic, susceptibility to", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "stroke, susceptibility to", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "cerebral infarction", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "cerebrovascular accident", "description": "" }, { "id": "MONDO:0020671", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0020671", "name": "stroke, ischemic", "description": "" }, { "id": "MIM:601367", "resource": "MIM", "url": "https://www.omim.org/entry/601367", "name": "Ischemic stroke", "description": "Ischemic stroke" } ], "evidence": [ { "id": "601367", "database": "MIM", "url": "https://www.omim.org/entry/601367" } ] }, { "disease_id": "MONDO:0013728", "recommended_name": { "id": "MONDO:0013728", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013728", "name": "pregnancy loss, recurrent, susceptibility to, 2", "description": "Any pregnancy loss, recurrent, susceptibility in which the cause of the disease is a mutation in the F2 gene." }, "synonyms": [ { "id": "MONDO:0013728", "resource": "MONDO", "url": 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"description": "Pregnancy loss, recurrent, 2" } ], "evidence": [ { "id": "614390", "database": "MIM", "url": "https://www.omim.org/entry/614390" } ] } ], "snv": [ { "evidence": [ { "id": "rs1419091834", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs1419091834" }, { "id": "rs1419091834", "database": "TOPMed", "url": "https://www.ncbi.nlm.nih.gov/snp/rs1419091834#frequency_tab" }, { "id": "rs1419091834", "database": "gnomAD", "url": "http://gnomad.broadinstitute.org/awesome?query=rs1419091834" } ], "glycoeffect": [ "n-glyco-sequon-gain" ], "start_pos": 109, "end_pos": 109, "sequence_org": "A", "sequence_mut": "T", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-gain (NCA->NCT).", "chr_id": "11", "chr_pos": "46723188", "ref_nt": "A", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "A109", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "rs1592410144", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs1592410144" }, { "id": "rs1592410144", "database": "ENSEMBL", "url": "https://www.ensembl.org/id/rs1592410144" } ], "glycoeffect": [ "n-glyco-sequon-loss", "o-glyco-site-loss" ], "start_pos": 123, "end_pos": 123, "sequence_org": "T", "sequence_mut": "P", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-loss (NIT->NIP).", "chr_id": "11", "chr_pos": "46723230", "ref_nt": "C", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "T123", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "P00734", "database": "BioMuta", "url": "https://hive.biochemistry.gwu.edu/biomuta/proteinview/P00734" } ], "glycoeffect": [ "n-glyco-sequon-loss", "o-glyco-site-loss" ], "start_pos": 144, "end_pos": 144, "subjects_tested": "0", "subjects_positive": "0", "frequency": "0.0", "sequence_org": "S", "sequence_mut": "P", "comment": "Somatic mutation passed 1 out of 6 filters: n-glyco-sequon-loss (NST->NPT).", 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"https://monarchinitiative.org/disease/MONDO:0012597", "name": "HPC9", "description": "" }, { "id": "MONDO:0012741", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012741", "name": "prostate cancer, hereditary, 12", "description": "Any familial prostate cancer in which the cause of the disease is a mutation in the EHBP1 gene." }, { "id": "MONDO:0012741", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012741", "name": "EHBP1 familial prostate cancer", "description": "" }, { "id": "MONDO:0012741", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012741", "name": "familial prostate cancer caused by mutation in EHBP1", "description": "" }, { "id": "MONDO:0012741", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012741", "name": "prostate cancer, hereditary, 12", "description": "" }, { "id": "MONDO:0012741", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012741", "name": "prostate cancer, hereditary, type 12", "description": "" }, { "id": "MONDO:0012741", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012741", "name": "HPC12", "description": "" }, { "id": "MONDO:0012244", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012244", "name": "prostate cancer, hereditary, 5", "description": "" }, { "id": "MONDO:0012244", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012244", "name": "prostate cancer, hereditary, 5", "description": "" }, { "id": "MONDO:0012244", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012244", "name": "prostate cancer, hereditary, type 5", "description": "" }, { "id": "MONDO:0012244", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012244", "name": "HPC5", "description": "" }, { "id": "MONDO:0012093", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012093", "name": "prostate cancer, hereditary, 3", "description": "" }, { "id": "MONDO:0012093", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012093", "name": "prostate cancer, hereditary, 3", "description": "" }, { "id": "MONDO:0012093", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012093", "name": "prostate cancer, hereditary, type 3", "description": "" }, { "id": "MONDO:0012093", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012093", "name": "prostate cancer, susceptibility to, 3", "description": "" }, { "id": "MONDO:0012093", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012093", "name": "HPC3", "description": "" }, { "id": "MONDO:0012094", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012094", "name": "prostate cancer, hereditary, 4", "description": "" }, { "id": "MONDO:0012094", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012094", "name": "prostate cancer, hereditary, 4", "description": "" }, { "id": "MONDO:0012094", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012094", "name": "prostate cancer, hereditary, type 4", "description": "" }, { "id": "MONDO:0012094", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012094", "name": "prostate cancer, susceptibility to, 4", "description": "" }, { "id": "MONDO:0012094", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012094", "name": "HPC4", "description": "" }, { "id": "MONDO:0012094", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012094", "name": "prostate cancer, hereditary, on chromosome 7", "description": "" }, { "id": "MONDO:0012758", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012758", "name": "prostate cancer, hereditary, 13", "description": "Any familial 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"https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, hereditary, 8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, hereditary, 8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, hereditary, type 8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "HPC8", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "predisposing for prostate cancer", "description": "" }, { "id": "MONDO:0011270", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011270", "name": "prostate cancer, susceptibility to", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, hereditary, 6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, hereditary, 6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, hereditary, type 6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "HPC6", "description": "" }, { "id": "MONDO:0012300", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012300", "name": "prostate cancer, susceptibility to", "description": "" }, { "id": "MONDO:0012620", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012620", "name": "prostate cancer, hereditary, 10", "description": "" }, { "id": "MONDO:0012620", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012620", "name": "HPC10", "description": "" }, { "id": "MONDO:0012620", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012620", "name": "prostate cancer, hereditary, 10", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "familial prostate carcinoma", "description": "Prostate carcinoma that has developed in relatives of patients with a history of prostate carcinoma." }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "familial prostate cancer", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "hereditary prostate cancer", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "hereditary prostate carcinoma", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, familial, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, somatic", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, familial", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, hereditary", "description": "" }, { "id": "MONDO:0012470", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012470", "name": "prostate cancer, hereditary, 7", "description": "" }, { "id": "MONDO:0012470", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012470", "name": "HPC7", "description": "" }, { "id": "MONDO:0012470", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012470", "name": "prostate cancer, hereditary, 7", "description": "" }, { "id": "MONDO:0012470", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012470", "name": "prostate cancer aggressiveness", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer, hereditary, 1", "description": "Any familial prostate cancer in which the cause of the disease is a mutation in the RNASEL gene." }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "RNASEL familial prostate cancer", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "familial prostate cancer caused by mutation in RNASEL", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer 1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer, hereditary, 1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "prostate cancer, hereditary, type 1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "HPC1", "description": "" }, { "id": "MONDO:0011098", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011098", "name": "Prca1", "description": "" }, { "id": "MONDO:0012768", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012768", "name": "prostate cancer, hereditary, 11", "description": "" }, { "id": "MONDO:0012768", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012768", "name": "HPC11", "description": "" }, { "id": "MONDO:0012768", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012768", "name": "prostate cancer, hereditary, 11", "description": "" }, { "id": "MONDO:0012769", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012769", "name": "prostate cancer, hereditary, 14", "description": "" }, { "id": "MONDO:0012769", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012769", "name": "HPC14", "description": "" }, { "id": "MONDO:0012769", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012769", "name": "prostate cancer, hereditary, 14", "description": "" }, { "id": "MONDO:0012770", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012770", "name": "prostate cancer, hereditary, 15", "description": "" }, { "id": "MONDO:0012770", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012770", "name": "HPC15", "description": "" }, { "id": "MONDO:0012770", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012770", "name": "prostate cancer, hereditary, 15", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "prostate cancer, hereditary, X-linked 1", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "HPCX1", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "prostate cancer, hereditary, X-linked 1", "description": "" }, { "id": "MONDO:0010257", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010257", "name": "prostate cancer susceptibility, X-linked", "description": "" }, { "id": "MONDO:0010405", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010405", "name": "prostate cancer, hereditary, X-linked 2", "description": "" }, { "id": "MONDO:0010405", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010405", "name": "HPCX2", "description": "" }, { "id": "MONDO:0010405", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0010405", "name": "prostate cancer, hereditary, X-linked 2", "description": "" }, { "id": "MIM:611868", "resource": "MIM", "url": "https://www.omim.org/entry/611868", "name": "Prostate cancer, hereditary, 12", "description": "Prostate cancer, hereditary, 12" }, { "id": "MIM:611928", "resource": "MIM", "url": "https://www.omim.org/entry/611928", "name": "Prostate cancer, hereditary, 13", "description": "Prostate cancer, hereditary, 13" }, { "id": "MIM:176807", "resource": "MIM", "url": "https://www.omim.org/entry/176807", "name": "Prostate cancer", "description": "Prostate cancer" }, { "id": "MIM:601518", "resource": "MIM", "url": "https://www.omim.org/entry/601518", "name": "Prostate cancer, hereditary, 1", "description": "Prostate cancer, hereditary, 1" }, { "id": "MIM:611955", "resource": "MIM", "url": "https://www.omim.org/entry/611955", "name": "Prostate cancer, hereditary, 11", "description": "Prostate cancer, hereditary, 11" } ] } ] }, { "significant": "Yes", "trend": "up", "name": "Stomach cancer [DO disease name]", "url": "http://disease-ontology.org/term/DOID:10534", "evidence": [ { "database": "BioXpress", "id": "P00734", "url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P00734" } ], "disease": [ { "disease_id": "DOID:10534", "recommended_name": { "id": "DOID:10534", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:10534", "name": "stomach cancer", "description": "A gastrointestinal system cancer that is located_in the stomach." }, "synonyms": [ { "id": "DOID:10534", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:10534", "name": "gastric cancer", "description": "" }, { "id": "DOID:10534", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:10534", "name": "gastric neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer", "description": "A primary or metastatic malignant neoplasm involving the stomach." }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "Ca lesser curvature - stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "cancer of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer risk after h. pylori infection", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer, somatic", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant gastric neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant gastric tumor", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant gastric tumour", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant neoplasm of lesser curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant neoplasm of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant neoplasm of the stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant stomach neoplasm", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of body of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of greater curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of lesser curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumor of the stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of body of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of greater curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of lesser curve of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant tumour of the stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "stomach cancer", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "Ca body - stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "ca greater curvature of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "malignant neoplasm of body of stomach", "description": "" }, { "id": "MONDO:0001056", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001056", "name": "gastric cancer, intestinal", "description": "" }, { "id": "MIM:613659", "resource": "MIM", "url": "https://www.omim.org/entry/613659", "name": "Gastric cancer", "description": "Gastric cancer" } ] } ] }, { "significant": "Yes", "trend": "up", "name": "Urinary bladder cancer [DO disease name]", "url": "http://disease-ontology.org/term/DOID:11054", "evidence": [ { "database": "BioXpress", "id": "P00734", "url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P00734" } ], "disease": [ { "disease_id": "DOID:11054", "recommended_name": { "id": "DOID:11054", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:11054", "name": "urinary bladder cancer", "description": "An urinary system cancer that results_in malignant growth located_in the urinary bladder." }, "synonyms": [ { "id": "DOID:11054", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:11054", "name": "bladder cancer", "description": "" }, { "id": "DOID:11054", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:11054", "name": "tumor of the bladder", "description": "" }, { "id": "MONDO:0001187", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001187", "name": "urinary bladder 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"https://monarchinitiative.org/disease/MONDO:0001187", "name": "malignant bladder tumor", "description": "" }, { "id": "MONDO:0001187", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001187", "name": "malignant bladder tumour", "description": "" }, { "id": "MONDO:0001187", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001187", "name": "malignant neoplasm of bladder", "description": "" }, { "id": "MONDO:0001187", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001187", "name": "malignant neoplasm of the bladder", "description": "" }, { "id": "MONDO:0001187", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001187", "name": "malignant neoplasm of the urinary bladder", "description": "" }, { "id": "MONDO:0001187", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0001187", "name": "malignant neoplasm of urinary bladder", "description": "" }, { "id": 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{ "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "malignant neoplasm of breast", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "malignant tumor of the breast", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "mammary cancer", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "mammary tumor", "description": "" }, { "id": "DOID:1612", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1612", "name": "primary breast cancer", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast carcinoma", "description": "Breast carcinoma that has developed in relatives of patients with history of breast carcinoma." }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer susceptibility, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, early-onset, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, invasive ductal, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, lobular, somatic", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast 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"description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial cancer of breast", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "familial cancer of the breast", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast cancer", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "hereditary breast carcinoma", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, familial", "description": "" }, { "id": "MONDO:0016419", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0016419", "name": "breast cancer, familial Male", "description": "" }, { "id": "MIM:114480", "resource": "MIM", "url": "https://www.omim.org/entry/114480", "name": "Breast cancer", "description": "Breast cancer" } ] } ] }, { "significant": "No", "trend": "up", "name": "Thyroid cancer [DO disease name]", "url": "http://disease-ontology.org/term/DOID:1781", "evidence": [ { "database": "BioXpress", "id": "P00734", "url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P00734" } ], "disease": [ { "disease_id": "DOID:1781", "recommended_name": { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "thyroid cancer", "description": "An endocrine gland cancer located in the thryoid gland located in the neck below the thyroid cartilage." }, "synonyms": [ { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "thyroid gland cancer", "description": "" }, { "id": "DOID:1781", "resource": "Disease Ontology", 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"MGWGLLAGQSTQSWPLMFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEA", "length": 324, "header": "tr|C9JV37-1|THRB_HUMAN Computationally mapped isoform of Prothrombin OS=Homo sapiens OX=9606 GN=F2 PE=1 SV=1 CANONICAL=P00734-1" }, "locus": { "chromosome": "11", "start_pos": 46726625, "end_pos": 46719367, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000442468.1", "url": "https://www.ensembl.org/id/ENST00000442468.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000387413.1", "url": "https://www.ensembl.org/id/ENSP00000387413.1" } ] } }, { "isoform_ac": "E9PIT3-1", "url": "", "sequence": { "sequence": "MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPSLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE", "length": 583, "header": "tr|E9PIT3-1|THRB_HUMAN Computationally mapped isoform of Prothrombin OS=Homo sapiens OX=9606 GN=F2 PE=1 SV=1 CANONICAL=P00734-1" }, "locus": { "chromosome": "11", "start_pos": 46739405, "end_pos": 46719236, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000530231.5", "url": "https://www.ensembl.org/id/ENST00000530231.5" }, { "database": "Ensembl Peptide", "id": "ENSP00000433907.1", "url": "https://www.ensembl.org/id/ENSP00000433907.1" } ] } }, { "isoform_ac": "P00734-1", "url": "", "sequence": { "sequence": "MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE", "length": 622, "header": "sp|P00734-1|THRB_HUMAN Isoform 1 of Prothrombin OS=Homo sapiens OX=9606 GN=F2 PE=1 SV=2 CANONICAL=P00734-1" }, "locus": { "chromosome": "11", "start_pos": 46739405, "end_pos": 46719236, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000311907.10", "url": "https://www.ensembl.org/id/ENST00000311907.10" }, { "database": "Ensembl Peptide", "id": "ENSP00000308541.5", "url": "https://www.ensembl.org/id/ENSP00000308541.5" } ] } } ], "glycosylation": [ { "glytoucan_ac": "G00912UN", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "P00734", "database": "UniCarbKB", "url": "" }, { "id": "29671580", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29671580" }, { "id": "22171320", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/22171320" }, { "id": "24841998", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/24841998" } ] }, { "glytoucan_ac": "G06356OH", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "30237853", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/30237853" }, { "id": "29671580", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29671580" } ] }, { "glytoucan_ac": "G10486CT", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "P00734", "database": "UniCarbKB", "url": "" }, { "id": "24841998", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/24841998" }, { "id": "22171320", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/22171320" } ] }, { "glytoucan_ac": "G12793SR", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "30237853", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/30237853" } ] }, { "glytoucan_ac": "G38663NM", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "29391424", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29391424" } ] }, { "glytoucan_ac": "G48414YA", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "24841998", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/24841998" }, { "id": "30237853", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/30237853" }, { "id": "29671580", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29671580" } ] }, { "glytoucan_ac": "G50045TK", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", 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"site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "30237853", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/30237853" } ] }, { "glytoucan_ac": "G56784JY", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "29391424", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29391424" } ] }, { "glytoucan_ac": "G59626AS", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "P00734", "database": "UniCarbKB", "url": "" }, { "id": "29671580", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29671580" }, { "id": "P00734@N121", "database": "GPTwiki", "url": "https://edwardslab.bmcb.georgetown.edu/gptwiki/P00734@N121" } ] }, { "glytoucan_ac": "G75850OP", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "GlycoSuiteDB curation notes. 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Reported structure can be attached to the following: N-121, N-143, N-416", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "P00734", "database": "UniCarbKB", "url": "" }, { "id": "7309709", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/7309709" } ] }, { "glytoucan_ac": "G91365ZQ", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "GlycoSuiteDB curation notes. Reported structure can be attached to the following: N-121, N-143, N-416", "start_pos": 121, "start_aa": "Asn", "end_pos": 121, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn121", "evidence": [ { "id": "P00734", "database": "UniCarbKB", "url": "" }, { "id": "7309709", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/7309709" } ] }, { "glytoucan_ac": "", "type": "N-linked", "subtype": "Complex", "site_category": "reported", "site_seq": "N", "relation": "attached", "comment": "N-linked (GlcNAc...) 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"end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn143", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "29671580", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29671580" } ] }, { "glytoucan_ac": "G22310AV", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 143, "start_aa": "Asn", "end_pos": 143, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn143", "evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "29391424", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29391424" }, { "id": "29671580", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29671580" } ] }, { "glytoucan_ac": "G24084IV", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", 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(complex) asparagine Complex", "start_pos": 143, "start_aa": "Asn", "end_pos": 143, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn143", "evidence": [ { "id": "P00734", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00734#ptm_processing" }, { "id": "14760718", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/14760718" }, { "id": "16335952", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/16335952" }, { "id": "22171320", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/22171320" }, { "id": "E9PIT3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9PIT3#ptm_processing" }, { "id": "PIRSR001149-3", "database": "PIR Site Rule", "url": "https://proteininformationresource.org/cgi-bin/pirrule?id=PIRSR001149-3" }, { "id": "4NZQ", "database": "RCSB PDB", "url": "https://www.rcsb.org/sequence/4NZQ" }, { "id": "4O03", "database": "RCSB PDB", "url": "https://www.rcsb.org/sequence/4O03" }, { "id": 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"evidence": [ { "id": "518", "database": "GlyConnect", "url": "https://glyconnect.expasy.org/browser/proteins/518" }, { "id": "29741879", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29741879" } ] }, { "glytoucan_ac": "G05933EN", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 416, "start_aa": "Asn", "end_pos": 416, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn416", "evidence": [ { "id": "P00734@N416", "database": "GPTwiki", "url": "https://edwardslab.bmcb.georgetown.edu/gptwiki/P00734@N416" } ] }, { "glytoucan_ac": "G06356OH", "type": "N-linked", "subtype": "", "site_category": "reported_with_glycan", "site_seq": "N", "relation": "attached", "comment": "", "start_pos": 416, "start_aa": "Asn", "end_pos": 416, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn416", "evidence": [ { "id": "518", "database": "GlyConnect", "url": 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"publication": [ { "title": "Proteomics Analysis of O-GalNAc Glycosylation in Human Serum by an Integrated Strategy", "journal": "Anal. 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Role in complex formation with insulin-like growth factor (IGF)-binding protein-3 and the IGFs.", "journal": "The Journal of biological chemistry", "date": "1999", "authors": "Janosi JB, Firth SM, Bond JJ, Baxter RC, Delhanty PJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10026136", "url": "https://glygen.org/publication/PubMed/10026136" } ] }, { "title": "Relocating the active site of activated protein C eliminates the need for its protein S cofactor. 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process", "id": "GO:2000379", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000379", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "regulation of cell shape", "id": "GO:0008360", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008360", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "negative regulation of cytokine production involved in inflammatory response", "id": "GO:1900016", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1900016", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "positive regulation of blood coagulation", "id": "GO:0030194", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030194", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "positive regulation of receptor signaling pathway via JAK-STAT", "id": "GO:0046427", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046427", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "negative regulation of proteolysis", "id": "GO:0045861", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045861", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "positive regulation of protein localization to nucleus", "id": "GO:1900182", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1900182", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "negative regulation of platelet activation", "id": "GO:0010544", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010544", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "regulation of blood coagulation", "id": "GO:0030193", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030193", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "cytolysis by host of symbiont cells", "id": "GO:0051838", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051838", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "negative regulation of astrocyte differentiation", "id": "GO:0048712", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048712", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway", "id": "GO:1900738", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1900738", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "positive regulation of lipid kinase activity", "id": "GO:0090218", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0090218", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "ligand-gated ion channel signaling pathway", "id": "GO:1990806", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1990806", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" } ] }, { "name": "Molecular Function", "total": 7, "go_terms": [ { "name": "serine-type endopeptidase activity", "id": "GO:0004252", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004252", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "signaling receptor binding", "id": "GO:0005102", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005102", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "heparin binding", "id": "GO:0008201", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008201", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "calcium ion binding", "id": "GO:0005509", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005509", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "growth factor activity", "id": "GO:0008083", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008083", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "lipopolysaccharide binding", "id": "GO:0001530", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001530", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "thrombospondin receptor activity", "id": "GO:0070053", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070053", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" } ] }, { "name": "Cellular Component", "total": 8, "go_terms": [ { "name": "extracellular region", "id": "GO:0005576", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005576", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "extracellular space", "id": "GO:0005615", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005615", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "endoplasmic reticulum lumen", "id": "GO:0005788", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005788", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "Golgi lumen", "id": "GO:0005796", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005796", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "plasma membrane", "id": "GO:0005886", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005886", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "extracellular exosome", "id": "GO:0070062", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070062", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "blood microparticle", "id": "GO:0072562", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0072562", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" }, { "name": "collagen-containing extracellular matrix", "id": "GO:0062023", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0062023", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" } ], "pmid": "" } ] } ] }, "pro_annotation": [ { "name": "prothrombin N-glycosylated 1 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-121 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G00912UN. Example: UniProtKB:P00734-1, Asn-121, MOD:00160~GNO:G00912UN. [PRO:DNx, PMID:22171320, PMID:24841998, PMID:29671580]", "evidence": [ { "id": "PR:000051038", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051038" } ] }, { "name": "prothrombin N-glycosylated 2 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-121 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G10486CT. Example: UniProtKB:P00734-1, Asn-121, MOD:00160~GNO:G10486CT. [PRO:DNx, PMID:22171320, PMID:24841998]", "evidence": [ { "id": "PR:000051039", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051039" } ] }, { "name": "prothrombin N-glycosylated 3 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-121 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G59626AS. Example: UniProtKB:P00734-1, Asn-121, MOD:00160~GNO:G59626AS. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051040", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051040" } ] }, { "name": "prothrombin N-glycosylated 4 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-121 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G75850OP. Example: UniProtKB:P00734-1, Asn-121, MOD:00160~GNO:G75850OP. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051041", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051041" } ] }, { "name": "prothrombin N-glycosylated 5 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-121 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G84467IZ. Example: UniProtKB:P00734-1, Asn-121, MOD:00160~GNO:G84467IZ. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051042", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051042" } ] }, { "name": "prothrombin N-glycosylated 6 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-121 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G91365ZQ. Example: UniProtKB:P00734-1, Asn-121, MOD:00160~GNO:G91365ZQ. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051043", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051043" } ] }, { "name": "prothrombin N-glycosylated 7 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G00912UN. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G00912UN. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051044", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051044" } ] }, { "name": "prothrombin N-glycosylated 8 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G06247RL. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G06247RL. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051045", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051045" } ] }, { "name": "prothrombin N-glycosylated 9 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G08293MJ. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G08293MJ. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051046", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051046" } ] }, { "name": "prothrombin N-glycosylated 10 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G10486CT. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G10486CT. [PRO:DNx, PMID:22171320, PMID:29671580]", "evidence": [ { "id": "PR:000051047", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051047" } ] }, { "name": "prothrombin N-glycosylated 11 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G27947YN. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G27947YN. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051048", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051048" } ] }, { "name": "prothrombin N-glycosylated 12 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G37399XV. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G37399XV. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051049", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051049" } ] }, { "name": "prothrombin N-glycosylated 13 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G42358LZ. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G42358LZ. [PRO:DNx, PMID:24279413]", "evidence": [ { "id": "PR:000051050", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051050" } ] }, { "name": "prothrombin N-glycosylated 14 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G59626AS. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G59626AS. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051051", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051051" } ] }, { "name": "prothrombin N-glycosylated 15 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G75850OP. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G75850OP. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051052", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051052" } ] }, { "name": "prothrombin N-glycosylated 16 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G84467IZ. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G84467IZ. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051053", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051053" } ] }, { "name": "prothrombin N-glycosylated 17 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G88374WZ. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G88374WZ. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051054", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051054" } ] }, { "name": "prothrombin N-glycosylated 18 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G91365ZQ. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G91365ZQ. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051055", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051055" } ] }, { "name": "prothrombin N-glycosylated 19 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G94917XT. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G94917XT. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051056", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051056" } ] }, { "name": "prothrombin N-glycosylated 20 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-143 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G95865ZB. Example: UniProtKB:P00734-1, Asn-143, MOD:00160~GNO:G95865ZB. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051057", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051057" } ] }, { "name": "prothrombin N-glycosylated 21 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-416 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G00912UN. Example: UniProtKB:P00734-1, Asn-416, MOD:00160~GNO:G00912UN. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051058", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051058" } ] }, { "name": "prothrombin N-glycosylated 22 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-416 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G22140GZ. Example: UniProtKB:P00734-1, Asn-416, MOD:00160~GNO:G22140GZ. [PRO:DNx, PMID:19838169]", "evidence": [ { "id": "PR:000051059", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051059" } ] }, { "name": "prothrombin N-glycosylated 23 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-416 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G42358LZ. Example: UniProtKB:P00734-1, Asn-416, MOD:00160~GNO:G42358LZ. [PRO:DNx, PMID:24279413]", "evidence": [ { "id": "PR:000051060", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051060" } ] }, { "name": "prothrombin N-glycosylated 24 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-416 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G59626AS. Example: UniProtKB:P00734-1, Asn-416, MOD:00160~GNO:G59626AS. [PRO:DNx, PMID:29671580]", "evidence": [ { "id": "PR:000051061", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051061" } ] }, { "name": "prothrombin N-glycosylated 25 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-416 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G75850OP. Example: UniProtKB:P00734-1, Asn-416, MOD:00160~GNO:G75850OP. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051062", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051062" } ] }, { "name": "prothrombin N-glycosylated 26 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-416 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G84467IZ. Example: UniProtKB:P00734-1, Asn-416, MOD:00160~GNO:G84467IZ. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051063", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051063" } ] }, { "name": "prothrombin N-glycosylated 27 (human)", "definition": "A prothrombin (human) that has been N-glycosylated at the residue equivalent to Asn-416 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan structure is represented by GlyTouCan:G91365ZQ. Example: UniProtKB:P00734-1, Asn-416, MOD:00160~GNO:G91365ZQ. [PRO:DNx, PMID:7309709]", "evidence": [ { "id": "PR:000051064", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051064" } ] }, { "name": "prothrombin O-glycosylated 1 (human)", "definition": "A prothrombin (human) that has been O-glycosylated at the residue equivalent to Ser-207 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G43417UB. Example: UniProtKB:P00734-1, Ser-207, MOD:00002~GNO:G43417UB. [PRO:DNx, PMID:30459171]", "evidence": [ { "id": "PR:000051065", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051065" } ] }, { "name": "prothrombin O-glycosylated 2 (human)", "definition": "A prothrombin (human) that has been O-glycosylated at the residue equivalent to Thr-145 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G43417UB. Example: UniProtKB:P00734-1, Thr-145, MOD:00005~GNO:G43417UB. [PRO:DNx, PMID:30459171]", "evidence": [ { "id": "PR:000051066", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051066" } ] }, { "name": "prothrombin O-glycosylated 3 (human)", "definition": "A prothrombin (human) that has been O-glycosylated at the residue equivalent to Thr-192 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G43417UB. Example: UniProtKB:P00734-1, Thr-192, MOD:00005~GNO:G43417UB. [PRO:DNx, PMID:30459171]", "evidence": [ { "id": "PR:000051067", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051067" } ] }, { "name": "prothrombin O-glycosylated 4 (human)", "definition": "A prothrombin (human) that has been O-glycosylated at the residue equivalent to Thr-315 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G43417UB. Example: UniProtKB:P00734-1, Thr-315, MOD:00005~GNO:G43417UB. [PRO:DNx, PMID:30459171]", "evidence": [ { "id": "PR:000051068", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051068" } ] }, { "name": "prothrombin O-glycosylated 5 (human)", "definition": "A prothrombin (human) that has been O-glycosylated at the residue equivalent to Thr-317 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G43417UB. Example: UniProtKB:P00734-1, Thr-317, MOD:00005~GNO:G43417UB. [PRO:DNx, PMID:30459171]", "evidence": [ { "id": "PR:000051069", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051069" } ] }, { "name": "prothrombin O-glycosylated 6 (human)", "definition": "A prothrombin (human) that has been O-glycosylated at the residue equivalent to Thr-78 of the amino acid sequence represented by UniProtKB:P00734-1, in which the glycan composition is represented by GlyTouCan:G43417UB. Example: UniProtKB:P00734-1, Thr-78, MOD:00005~GNO:G43417UB. [PRO:DNx, PMID:30459171]", "evidence": [ { "id": "PR:000051070", "database": "PRO", "url": "https://proconsortium.org/app/entry/PR:000051070" } ] } ], "site_annotation": [ { "start_pos": 121, "end_pos": 123, "annotation": "n_glycosylation_sequon" }, { "start_pos": 143, "end_pos": 145, "annotation": "n_glycosylation_sequon" }, { "start_pos": 205, "end_pos": 207, "annotation": "n_glycosylation_sequon" }, { "start_pos": 416, "end_pos": 418, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [ { "annotation": "In the penultimate step of the coagulation cascade, prothrombin is converted to thrombin by the prothrombinase complex composed of factor Xa (F10), cofactor Va (F5), and phospholipids. This activation requires factor Xa-catalyzed sequential cleavage at 2 sites, Arg-314 and Arg-363, along 2 possible pathways. In the first pathway, the first cleavage occurs at Arg-314, leading to the formation of the inactive intermediate prethrombin-2. This pathway preferentially occurs on platelets and in the absence of cofactor Va. In the second pathway, the first cleavage occurs at Arg-363, which separates protease domain into 2 chains that remain connected through a disulfide bond and generates the active intermediate meizothrombin. The presence of cofactor Va directs activation along the meizothrombin pathway and greatly accelerates the rate of cleavage at Arg-363, but has a smaller effect on the cleavage of meizothrombin at Arg-314. Meizothrombin accumulates as an intermediate when prothrombinase is assembled on the membrane of red blood cells.", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" }, { "database": "PubMed", "id": "34265300", "url": "https://glygen.org/publication/PubMed/34265300" } ] }, { "annotation": "N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" }, { "database": "PubMed", "id": "19838169", "url": "https://glygen.org/publication/PubMed/19838169" }, { "database": "PubMed", "id": "19159218", "url": "https://glygen.org/publication/PubMed/19159218" }, { "database": "PubMed", "id": "14760718", "url": "https://glygen.org/publication/PubMed/14760718" }, { "database": "PubMed", "id": "16335952", "url": "https://glygen.org/publication/PubMed/16335952" }, { "database": "PubMed", "id": "19139490", "url": "https://glygen.org/publication/PubMed/19139490" }, { "database": "PubMed", "id": "873923", "url": "https://glygen.org/publication/PubMed/873923" }, { "database": "PubMed", "id": "22171320", "url": "https://glygen.org/publication/PubMed/22171320" } ] }, { "annotation": "The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.", "evidence": [ { "database": "UniProtKB", "id": "P00734", "url": "https://www.uniprot.org/uniprot/P00734" }, { "database": "PubMed", "id": "6305407", "url": "https://glygen.org/publication/PubMed/6305407" }, { "database": "PubMed", "id": "3759958", "url": "https://glygen.org/publication/PubMed/3759958" } ] } ], "interactions": [], "reactions": [ { "id": "R-HSA-114697", "name": "Activated thrombin (factor IIa) cleaves PAR3,4, activating them", "equation": "", "summary": "Thrombin signaling is mediated at least in part by a small family of G protein-coupled Proteinase Activated Receptors (PARs). Human platelet activation by thrombin is mediated predominantly by PAR1; PAR4-induced platelet responses are less pronounced. PAR2 is not present in human platelets. PARs 1, 3 and 4 are activated when thrombin cleaves an N-terminal exodomain. This cleavage event unmasks a new N-terminus that serves as a tethered ligand that binds intramolecularly to the body of the receptor to effect transmembrane signaling. Intermolecular ligation of one PAR molecule by another can occur but, not surprisingly, appears to be less efficient than self-ligation. A synthetic peptide of sequence SFLLRN, the first six amino acids of the new N-terminus generated when thrombin cleaves PAR1, can activate PAR1 independent of protease and receptor cleavage. In addition to providing evidence for the tethered ligand mechanism, such tethered ligand-mimicking peptides have provided a convenient pharmacological tool for probing the effects of PAR activation in cells and tissues.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-114697", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-114697" } ] }, { "id": "R-HSA-140599", "name": "factor XIII -> factor XIII cleaved tetramer + 2 factor XIII A activation peptides", "equation": "", "summary": "Activated thrombin cleaves the A chains of factor XIII tetramers in a reaction stimulated by the presence of fibrin multimers (Lewis et al. 1985). The amino terminal portions of the A chains are released as activation peptides, which have no known function. The resulting factor XIII tetramer remains catalytically inactive.", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P04070-1", "P00734-1", "P00488-1" ], "evidence": [ { "id": "R-HSA-140599", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140599" } ] }, { "id": "R-HSA-140664", "name": "prothrombin -> activated thrombin (factor IIa) + thrombin activation peptide (prothrombinase catalyst)", "equation": "", "summary": "The membrane-bound Va:Xa (prothrombinase) complex rapidly activates large amounts of thrombin. Factor Xa (aka Factor X heavy chain), a cleavage product of coagulation factor X (F10), is a vitamin K-dependent glycoprotein able to convert prothrombin to thrombin during the blood clotting process (Mann et al. 1988, Orfeo et al. 2004). Factor Xa is a target for direct oral anticoagulant (DOAC) drugs that are direct factor Xa inhibitors (the so-called 'xabans') and used in the treatment and prevention of thromboembolic disorders (Galanis et al. 2014). Rivaroxaban (brand name Xarelto) binds to and inhibits both free factor Xa and factor Xa bound in the prothrombinase complex (Va:Xa) (Roehrig et al. 2005). Rivaroxaban was the first medically approved drug of this class (Abrams & Emerson 2009, Misselwitz et al. 2011). In patients with non-valvular atrial fibrillation, 'xabans' appears to be as effective as warfarin in preventing nonhemorrhagic strokes and embolic events (Patel et al. 2011, Gomez-Outes et al. 2013). The most serious side-effect of rivaroxaban is GI bleeding, and with there being no antidote for rivaroxaban, bleeding events can be difficult to manage (Siegal et al. 2014). Other 'xabans' such as apixaban (Bhanwra & Ahluwalia 2014), edoxaban (Minor et al. 2015), eribaxaban (Bondarenko et al. 2013) and betrixaban (Zhang et al. 2009) share a similar mechanism of action to rivaroxaban (Nutescu et al. 2016). Unlike warfarin, the 'xabans' exhibit a predictable dose response and do not require routine coagulation monitoring.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [ "R-HSA-140674" ], "output_participant_list": [ "R-HSA-156786", "R-HSA-140786" ], "enzyme_list": [ "P00742-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-140664", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140664" } ] }, { "id": "R-HSA-140696", "name": "factor V -> factor Va + factor V activation peptide", "equation": "", "summary": "Activated thrombin (factor IIa) catalyzes the conversion of factor V to factor Va (activated factor V). The activation peptide released in this reaction has no known function.", "cellular_location": "extracellular region", "input_participant_list": [ "R-HSA-140697" ], "output_participant_list": [ "R-HSA-140692", "R-HSA-140787" ], "enzyme_list": [ "P04070-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-140696", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140696" } ] }, { "id": "R-HSA-140700", "name": "prothrombin -> activated thrombin (factor IIa) + thrombin activation peptide (Xa catalyst)", "equation": "", "summary": "Membrane-bound factor Xa catalyzes the activation of small amounts of thrombin. The amino terminal portion of prothrombin is released as an activation peptide, which can be cleaved further by activated thrombin. Neither the full-length activation peptide nor its cleavage products have known functions.

Factor Xa (aka Factor X heavy chain), a cleavage product of coagulation factor X (F10), is a vitamin K-dependent glycoprotein able to convert prothrombin to thrombin during the blood clotting process. Factor Xa is a target for direct oral anticoagulant (DOAC) drugs that are direct factor Xa inhibitors (the so-called 'xabans') and used in the treatment and prevention of thromboembolic disorders (Galanis et al. 2014). Rivaroxaban (brand name Xarelto) binds to and inhibits both free factor Xa and factor Xa bound in the prothrombinase complex (Va:Xa) (Roehrig et al. 2005). Rivaroxaban was the first medically approved drug of this class (Abrams & Emerson 2009, Misselwitz et al. 2011). In patients with non-valvular atrial fibrillation, 'xabans' appears to be as effective as warfarin in preventing nonhemorrhagic strokes and embolic events (Patel et al. 2011, Gomez-Outes et al. 2013). The most serious side-effect of rivaroxaban is GI bleeding, and with there being no antidote for rivaroxaban, bleeding events can be difficult to manage (Siegal et al. 2014). Other 'xabans' such as apixaban (Bhanwra & Ahluwalia 2014), edoxaban (Minor et al. 2015), eribaxaban (Bondarenko et al. 2013) and betrixaban (Zhang et al. 2009) share a similar mechanism of action to rivaroxaban (Nutescu et al. 2016). Unlike warfarin, the 'xabans' exhibit a predictable dose response and do not require routine coagulation monitoring.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00742-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-140700", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140700" } ] }, { "id": "R-HSA-140791", "name": "activated thrombin (factor IIa) + antithrombin III:heparin -> thrombin:antithrombin III:heparin", "equation": "", "summary": "Activated thrombin binds to the antithrombin III:heparin complex on the cell surface.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-140791", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140791" } ] }, { "id": "R-HSA-140840", "name": "fibrinogen -> fibrin monomer + 2 fibrinopeptide A + 2 fibrinopeptide B", "equation": "", "summary": "The alpha and beta chains of fibrinogen hexamer are cleaved by thrombin to generate fibrin monomer (Ni et al. 1989). The amino terminal regions of the cleaved alpha and beta chains are released (fibrinopeptides A and B respectively).", "cellular_location": "extracellular region", "input_participant_list": [ "R-HSA-114618" ], "output_participant_list": [ "R-HSA-140586", "R-HSA-140867", "R-HSA-140876" ], "enzyme_list": [ "P04070-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-140840", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140840" } ] }, { "id": "R-HSA-140870", "name": "thrombin:antithrombin III:heparin -> thrombin:cleaved antithrombin III:heparin", "equation": "", "summary": "Antithrombin III in the complex is cleaved by thrombin, thereupon undergoing a conformational change that stabilizes the thrombin:antithrombin III complex, trapping and inactivating the thrombin moiety.", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-140870", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140870" } ] }, { "id": "R-HSA-140872", "name": "thrombin:cleaved SERPINC1:SERPINC1 activators -> thrombin:cleaved SERPINC1 + SERPINC1 activators", "equation": "", "summary": "The same conformational change that traps thrombin in its complex with cleaved antithrombin III also decreases the affinity of the latter for heparin, and the complex of cleaved antithrombin III and thrombin dissociates from the cell-bound heparin molecule.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-140872", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-140872" } ] }, { "id": "R-HSA-141040", "name": "Activated thrombin:thrombomodulin cleaves PROCR:Protein C to PROCR:Activated protein C", "equation": "", "summary": "Thrombin complexed with thrombomodulin at the endothelial cell surface cleaves the heavy chain of protein C, generating activated protein C and an activation peptide. The activation peptide has no known function.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P04070-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-141040", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-141040" } ] }, { "id": "R-HSA-141046", "name": "activated thrombin (factor IIa) + thrombomodulin -> activated thrombin:thrombomodulin", "equation": "", "summary": "Activated thrombin (factor IIa) binds to thrombomodulin at the external face of the plasma membrane, forming a thrombin:thrombomodulin complex. In this complexed form, the activity of thrombin towards protein C is greatly increased, and as thrombomodulin is particularly abundant on the surfaces of endothelial cells, this association plays a major role in restricting clot formation.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [ "R-HSA-141030" ], "output_participant_list": [ "R-HSA-141038" ], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-141046", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-141046" } ] }, { "id": "R-HSA-158137", "name": "factor VIII:von Willibrand factor multimer -> factor VIIIa + factor VIIIa B A3 acidic polypeptide + von Willibrand factor multimer", "equation": "", "summary": "Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989).", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P04070-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-158137", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-158137" } ] }, { "id": "R-HSA-158419", "name": "factor XI:platelet glycoprotein (GP) Ib:IX:V complex -> factor XIa:platelet glycoprotein (GP) Ib:IX:V complex (thrombin catalyst)", "equation": "", "summary": "Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). In the body, this reaction occurs on the surfaces of activated platelets (Baglia et al. 2002). Small quantities of factor XI can be activated in a reaction catalyzed by factor XIIa, to initiate formation of a fibrin clot. However, the efficient activation of larger quantities of factor XI, needed to propagate the blood clotting process, appears to be mediated by thrombin (Baglia and Walsh 2000; Gailani and Broze 1993; Naito and Fujikawa 1991; Oliver et al. 1999; Monroe et al. 2002).", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P04070-1", "P00734-1", "P03951-1" ], "evidence": [ { "id": "R-HSA-158419", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-158419" } ] }, { "id": "R-HSA-159728", "name": "Furin cleaves pro-prothrombin to prothrombin", "equation": "", "summary": "Furin, associated with the Golgi membrane, cleaves pro-prothrombin to form mature, gamma-carboxylated prothrombin (Wasley et al. 1993).", "cellular_location": "Golgi lumen, Golgi membrane", "input_participant_list": [ "R-HSA-159841" ], "output_participant_list": [ "R-HSA-159759", "R-HSA-159845" ], "enzyme_list": [ "P09958-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-159728", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-159728" } ] }, { "id": "R-HSA-159826", "name": "GGCX gamma-carboxylates F2(25-622) (pro-prothrombin)", "equation": "", "summary": "GGCX (gamma glutamyl carboxylase) in the endoplasmic reticulum gamma-carboxylates ten glutamate residues on F2(25-622) (pro-prothrombin). MK4 (vitamin K hydroquinone) is oxidized to MK4 epoxide in the process (Berkner 2000; Furie et al. 1999; Stenina et al. 2001; Morris et al. 1995).", "cellular_location": "endoplasmic reticulum lumen, endoplasmic reticulum membrane", "input_participant_list": [ "R-HSA-159739" ], "output_participant_list": [ "R-HSA-159800" ], "enzyme_list": [ "P00734-1", "P38435-1" ], "evidence": [ { "id": "R-HSA-159826", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-159826" } ] }, { "id": "R-HSA-159843", "name": "Gamma-carboxy pro-prothrombin transport from the endoplasmic reticulum to the Golgi apparatus", "equation": "", "summary": "Gamma-carboxylated pro-prothrombin (factor II) is transported from the endoplasmic reticulum to the Golgi apparatus (Kirchhausen 2000).", "cellular_location": "COPII-coated ER to Golgi transport vesicle, Golgi lumen, endoplasmic reticulum lumen", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-159843", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-159843" } ] }, { "id": "R-HSA-379048", "name": "Liganded Gq/11-activating GPCRs act as GEFs for Gq/11", "equation": "", "summary": "G alpha q protein (or Gq/11) consists of four family members (G-alpha 11, -alpha 14, -alpha 15 and -alpha q). It activates phospholipase C (PLC) (Dowal L et al, 2006). PLC hydrolyzes phosphatidylinositol (PIP2) to diacyl glycerol (DAG) and inositol triphosphate (IP3). DAG acts as a second messenger that activates protein kinase C (PKC) and IP3 can bind to IP3 receptors, particular calcium channels in the endoplasmic reticulum (ER). Calcium flow causes the cytosolic concentration of calcium to increase, causing a cascade of intracellular changes and activity.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-379048", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-379048" } ] }, { "id": "R-HSA-381446", "name": "Thrombin proteolyzes IGF:IGFBP3:ALS", "equation": "", "summary": "Thrombin cleaves IGFBP-3 in the IGF:IGFBP-3:ALS Complex between amino acids 124 and 125 and between amino acids 233 and 234, releasing IGF.", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-381446", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381446" } ] }, { "id": "R-HSA-389463", "name": "Proteinase-activated receptors can bind thrombin", "equation": "", "summary": "Thrombin (Butkowski RJ et al, 1977) plays a vital role in blood homeostasis, inflammation and wound healing. Thrombin (which cleaves bonds after arginine and lysine) converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII. Complexed with thrombomodulin it can also activate protein C. It performs these functions by binding to four proteinase-activated receptors (PAR1-4) (Kahn ML, et al, 1999; Bohm SK et al, 1996). These complexes couple to G proteins which stimulate phosphoinositide hydrolysis.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-389463", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389463" } ] }, { "id": "R-HSA-429529", "name": "Thrombin binding to GP1b:IX:V", "equation": "", "summary": "Thrombin binds to the GP1b-IX-V receptor during platelet aggregation. This leads to increased PAR activation, possibly due to favourable orientation of thrombin towards the PAR extracellular domain.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-429529", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-429529" } ] }, { "id": "R-HSA-5578883", "name": "Heparin cofactor 2 (SERPIND1) binds activated thrombin (factor IIa)", "equation": "", "summary": "SERPIND1 (Heparin cofactor 2) is a serine endopeptidase inhibitor (SERPIN) that acts as a pseudosubstrate for activated thrombin, forming a stable complex which has the effect of inactivating thrombin protease activity (Church et al. 1985), although with slower kinetics than SERPINC1 (antithrombin-III). The presence of the glycosaminoglycans heparin or dermatan sulphate increases thrombin inactivation 1000-fold (Van Deerlin & Tollefsen 199) by facilitating the interaction between the active site of thrombin and the reactive site of SERPIND1. Thrombin specificity is conferred by a 90-residue N-terminal extension that contains two acidic motifs containing sulphated Tyr residues, resembling the C-terminus of hirudin (Tollefsen et al. 1997). SERPIND1 also inhibits chymotrypsin and neutrophil cathepsin G, but in a glycosaminoglycan independent manner (Church et al. 1985). In contrast to SERPINC1 deficiency, SERPIND1 deficiency is not associated with venous thrombosis (Corral et al. 2004).", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-5578883", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5578883" } ] }, { "id": "R-HSA-5602080", "name": "Protease nexin-1 (PN1) is a specific and extremely efficient inhibitor of thrombin.", "equation": "", "summary": "SERPINE2 (Protease nexin-1, PN1) is a specific and extremely efficient inhibitor of thrombin. Unlike other thrombin inhibitors belonging to the serpin family, SERPINE2 does not circulate in the blood (Bouton et al. 2012). Rather, it is bound to glycosaminoglycans on the surface of cell types including macrophages, smooth muscle cells and platelets, where it inhibits the signaling functions of thrombin. SERPINE2 sets the threshold for thrombin-induced platelet activation (Gronke et al. 1987, Boulaftali et al. 2010) and has been implicated in atherosclerosis (Bouton et al. 2012). Recent studies have demonstrated an important antithrombotic effect of platelet SERPINE2 in vitro and in vivo (Boulaftali et al. 2010).", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-5602080", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5602080" } ] }, { "id": "R-HSA-749448", "name": "Liganded Gq-activating GPCRs bind inactive heterotrimeric Gq", "equation": "", "summary": "Numerous functionally unrelated GPCRs couple with the Gq G-protein subtype.", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-749448", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-749448" } ] }, { "id": "R-HSA-749452", "name": "The Ligand:GPCR:Gq complex dissociates", "equation": "", "summary": "The classical view of G-protein signalling is that the G-protein alpha subunit dissociates from the beta:gamma dimer. Activated G alpha (q) and the beta:gamma dimer then participate in separate signaling cascades. Although G protein dissociation has been contested (e.g. Bassi et al. 1996), recent in vivo experiments have demonstrated that dissociation does occur, though possibly not to completion (Lambert 2008).", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-749452", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-749452" } ] }, { "id": "R-HSA-8852716", "name": "Thrombin, ELANE cleave C5", "equation": "", "summary": "Thrombin, coagulation factors XIa, Xa, IXa and plasmin (Amara et al. 2010) can cleave C3 and C5 to generate C3a and C5a. Neutrophil elastase (ELANE) can cleave C5 generating an active C5a-like fragment (Vogt 2000).

Under normal conditions, thrombin cleavage of C5 may not be a physiologically significant reaction (Bagic et al. 2015) but the combined action of thrombin and convertases appears to enhance the efficiency of the lytic pathway (Krisinger et al. 2012). Clotting-induced production of thrombin leads to cleavage of C5 at the atypical site R947 in the CUB domain. C5a can be released from the atypical C5a fragment (termed C5aT) by conventional C5 convertases; the truncated C5b fragment, termed C5bT, can form a C5bT-9 membrane attack complex that has significantly increased lytic activity (Krisinger et al. 2012).", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P08246-1", "P00734-1" ], "evidence": [ { "id": "R-HSA-8852716", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8852716" } ] }, { "id": "R-HSA-9015379", "name": "Factor IIa inhibitors (compounds) binds IIa", "equation": "", "summary": "In the blood coagulation process, prothrombin is proteolytically cleaved to form thrombin (factor IIa) which in turn, acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin. Specifically, thrombin converts factor XI to XIa, factor VIII to VIIIa, factor V to Va, fibrinogen to fibrin, and factor XIII to XIIIa. The direct oral anticoagulant (DOAC) synthetic organic drugs dabigatran (brand name Pradaxa), argatroban (brand name Acova, Novastan; Exembol in the UK) and melagatran are potent, competitive direct thrombin inhibitors (DTIs). They reversibly and specifically bind both clot-bound and free thrombin (unlike warfarin or heparin), as well as inhibiting thrombin-induced platelet aggregation (Wienen et al. 2007, Stangier et al. 2007).

Commercially, dabigatran is formulated as a lipophilic prodrug, dabigatran etexilate, to promote gastrointestinal absorption before it is metabolised to the active drug. The kidneys excrete the majority (80%) of unchanged drug (Stangier et al. 2007). Argatroban is a synthetic inhibitor of thrombin derived from L-arginine, which has a relatively short period of binding only to thrombin\u2019s active site (Hursting et al. 1997). It is given intravenously and is metabolised in the liver. Because of its hepatic metabolism, it may be used in patients with renal dysfunction. Melagatran is the active drug formed from the prodrug ximelagatran and is a competitive and rapid inhibitor of thrombin (Gustafsson et al. 1998). DuP 714 is a potent and specific thrombin inhibitor (Chiu et al. 1991).

A major downside of DOACs is that they don't have reversing antidotes if internal bleeding arises from their use. However, in the case of severe bleeding of patients on dabigatran, the antibody fragment idarucizumab reversed the anticoagulation effects of dabigatran within minutes (Pollack et al. 2015). This represents a novel anticoagulation reversing mechanism for a DOAC.", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-9015379", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9015379" } ] }, { "id": "R-HSA-9603302", "name": "Factor IIa inhibitors (peptide) binds IIa", "equation": "", "summary": "In the blood coagulation process, prothrombin is proteolytically cleaved to form thrombin (factor IIa) which in turn, acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin. Specifically, thrombin converts factor XI to XIa, factor VIII to VIIIa, factor V to Va, fibrinogen to fibrin, and factor XIII to XIIIa. Direct thrombin inhibitors (DTIs) represent a new class; of promising anticoagulation agents. DTIs are increasingly; being used instead of heparin to provide initial,; rapid anticoagulation. Unlike heparin, which requires a mediator (antithrombin) to potentiate anticoagulation, Peptide DTIs can inhibit free and bound thrombin directly. Lepirudin (brand name Refludan) is a recombinant hirudin derived from yeast cells (Weitz et al. 1990). Hirudin is a naturally occurring anticoagulant produced by the salivary glands of medicinal leeches. Bivalirudin (brand name Angiomax, Angiox) is a synthetic analog of hirudin, with a shorter period of binding to thrombin (Gladwell 2002). Desirudin (brand name Iprivask) is another recombinant hirudin derivative that directly inhibits free and fibrin-bound thrombin (Graetz et al. 2011).", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-9603302", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9603302" } ] }, { "id": "R-HSA-9653249", "name": "Cleavage of factor XII variant by activated thrombin", "equation": "", "summary": "The plasma protein factor XII (FXII, F12 or Hageman factor) is a serine protease that is mainly produced in the liver and circulates in plasma (40\u202f\u03bcg/mL) as a single chain zymogen. Following contact with anionic surfaces such as extracellular RNA, endotoxin, neutrophil extracellular traps (NETs), polyphosphates released from activated platelets, collagen exposed on injured endothelium, heparin secreted from mast cells, and phosphatidylserine on apoptotic cells, FXII undergoes autoactivation to FXIIa (F12a) via proteolysis of the peptide bond R372-V373 in FXII zymogen (Renn\u00e9 T et al. 2012; M\u00fcller F et al. 2009; Oschatz C et al. 2011; Ivanov I et al. 2017; Mailer RKW et al. 2019). Active protease FXIIa is composed of a heavy (20-372) chain and a light (373-615) chain. The light chain harbors the enzymatic protease domain and is linked to the heavy chain by a single disulfide bridge. FXIIa then cleaves plasma prekallikrein to kallikrein, which in turn reciprocally activates additional molecules of FXII and amplifies FXIIa generation (Renn\u00e9 T et al. 2012). Kallikrein also cleaves high-molecular-weight kininogen (HK), releasing the vasoactive peptide bradykinin (BK) (Renn\u00e9 T et al. 2012). BK binds to kinin receptors (B2 and B1 receptors) and triggers inflammation (Leeb-Lundberg LM et al. 2005). The contact system is controlled mainly by C1 inhibitor (C1-Inh or SERPING1) that inhibits both FXIIa and kallikrein.

Hereditary angioedema (HAE) is a rare life-threatening inherited edema disorder that is characterized by recurrent episodes of acute swelling involving the skin or the oropharyngeal, laryngeal, or gastrointestinal mucosa (Zuraw BL & Christiansen SC 2016; de Maat S et al. 2018; Magerl M et al. 2017). Increased vascular permeability in HAE is due to excessive formation of the proinflammatory peptide hormone bradykinin (BK) (Joseph K et al. 2008). Elevated plasma levels of BK are consistently found during acute swelling attacks in HAE patients (Schapira M et al. 1983; Cugno M et al. 2003). Angioedema initiated by bradykinin is usually associated with SERPING1 (\u04211-Inh) deficiency (HAE type I and HAE type II) (Kaplan AP & Joseph K 2014, 2016; Levi M et al. 2018). More rarely, HAE occurs in individuals with normal SERPING1 activity, and has been linked to mutations in other proteins, including FXII, plasminogen, and angiopoietin (Magerl M et al. 2017; Zuraw BL 2018; Ivanov I et al. 2019). Using genome-wide linkage analyses, HAE type III was shown to be associated with single missense mutations (c.1032C>A or c.1032C>G) in the F12 gene (Dewald G & Bork K 2006; Cichon S et al. 2006). Both point mutations translate into amino acid substitution of threonine 328 by either a lysine or an arginine residue (T328K or T328R). FXII-linked HAE is an autosomal dominant inherited disorder, and a mixture of wild type and T328-mutated FXII circulates in plasma of patients with HAE type III (Cichon S et al. 2006). An FXII-neutralizing antibody attenuated pathological BK formation in the plasma of patients with HAE type III and blunted edema in a genetically altered, humanized mouse model of HAE type III (Bj\u00f6rkqvist J et al. 2015). Moreover, FXII T328K or T328R variants change protein O-linked glycosylation and introduce a new site that is sensitive to enzymatic cleavage by fibrinolytic and coagulation proteases such as plasmin, thrombin or FXIa (Bj\u00f6rkqvist J et al. 2015; de Maat S et al. 2016; Ivanov I et al. 2019). FXII T328K or T328R variants are cleaved after residue 328 by proteases, removing the protein\u2019s noncatalytic heavy chain (HC) region. Further, truncation of the pathological FXII T328K by plasmin was found to expose R372 for subsequent cleavage by plasma kallikrein in solution (de Maat S et al. 2016, 2019). The intrinsic capacity of the truncated form of FXII (329-615) variant to convert PK to kallikrein is greater than that of activated FXIIa leading to more kallikrein generated early during reciprocal activation (Ivanov I et al. 2019). Second, the truncated form of FXII (329-615) is a better kallikrein substrate than is FXII (Ivanov I et al. 2019). SERPING1 (C1-Inh), the major inhibitor of FXIIa, binds similarly to wild type (WT) and mutated FXIIa (Bj\u00f6rkqvist J et al. 2015). However, the accelerated kallikrein/FXII activation in HAE patients carrying FXII variants appears to overwhelm the regulatory function of SERPING1 at normal plasma levels leading to uncontrolled bradykinin formation in a surface-independent manner (de Maat S et al. 2016; Ivanov I et al. 2019).

The Reactome event describes a truncation of FXII variants after the residue 328 catalyzed by activated thrombin.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1", "P00748-1" ], "evidence": [ { "id": "R-HSA-9653249", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9653249" } ] }, { "id": "R-HSA-9666383", "name": "F8 variant is not cleaved by thrombin", "equation": "", "summary": "In normal human plasma factor VIII (FVIII) complexed to von Willibrand factor (vWF) is cleaved into several smaller polypeptides that remain associated. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on FVIII:vWF complexes under physiological conditions (Eaton D et al. 1986; Hill-Eubanks DC et al. 1989; Lollar P et al. 1988; Pieters et al. 1989). Thrombin cleaves FVIII after arginine residues 391 (A1-A2 domain junction) and 759 (A2-B domain junction) to yield heavy chain fragments and at R1708 (a3-A3 junction) to yield the light chain fragment (Eaton D et al. 1986; Hill-Eubanks DC et al. 1989; Kaufman et al 1997). Cleavage at R759 is rapid relative to the other two sites and results in the liberation of the B domain or its fragments from the factor VIII heavy chain (Hill-Eubanks DC & Lollar P 1990). The cleavage at R759 is thought to facilitate cleavages at R391 and R1701, which lead to FVIII activation (Newell JL & Fay PJ 2007). Cleavage at R391 exposes a cryptic functional factor IXa-interactive site in the A2 domain (Fay PJ et al. 2001). Proteolysis at R1708 results in the release of the acidic polypeptide (a3 subdomain) on the aminoterminal side of the A3 domain of the light chain. However, as this polypeptide mediates the association of FVIII with vWF, the active factor VIII dissociates from vWF. Thus, cleavage after R1708 is required to release the active FVIIIa from vWF (Lollar P et al. 1988; O'Brien DP & Tuddenham EG 1989; Aly AM & Hoyer LW 1992). The active FVIIIa acts as a cofactor for factor IXa that converts factor X to the activated form Xa and eventually leads to the formation of a blood clot.

Mutations affecting arginine residues located at the thrombin cleavage sites result in mild/moderate hemophilia A (HA) (Pattinson JK et al. 1990; Arai M et al. 1990; Schwaab R et al. 1991). Substitution of Arg391 was reported to impair thrombin cleavage of the heavy chain (Shima M et al. 1989; Arai M et al. 1989; O'Brien DP et al. 1990; Nogami K et al. 2005). Similarly, substitution of R1708 prevents cleavage of the FVIII light chain by thrombin (O'Brien DP & Tuddenham EG 1989; Arai M et al. 1990; Newell JL1 & Fay PJ 2009). The substitution of arginine for cysteine at position 1708 (FVIII R1708C, also known as East Hartford, FVIII-EH) has been identified in 5% of all patients with HA (Lazarchick and Hoyer 1978). Uncleaved FVIII R1708C variant was not released from vWF and thereby blocked procoagulant function of FVIII (O'Brien DP & Tuddenham EG 1989; Aly AM & Hoyer LW 1992). The incubation of plasma of FVIII R1708C hemophilic patients with cysteamine, a small aminothiol endogenously derived from coenzyme A degradation, caused dose- and time-dependent increases in FVIII activity and restored light chain cleavage by thrombin (Aly AM et al 1992). It has been suggested that C1708 is present in a disulfide bond which is converted by cysteamine treatment to a positively charged lysine analogue recovering the thrombin cleavage site (Aly AM et al 1992; Gallego-Villar L et al. 2017). In addition, mutations close to thrombin cleavage sites may also disrupt the activation of FVIII (Johnson DJ et al. 1994; Mumford AD et al. 2002). For example, FVIII Y365C variant plasma showed delayed thrombin activation and a greater subsequent rate of decay than wild-type FVIII (Mumford AD et al. 2002). This hypothesis is supported by the observations that the mutation Y365F, generated by site directed mutagenesis, results in a delayed thrombin-mediated activation of FVIII, because sulfation of this residue is crucial for thrombin cleavage at position 391 (Michnick DA et al. 1994). The Reactome event describes failed thrombin-mediated activation of HA-associated FVIII variants (such as R391C, R391H, S392L) due to defects at or close to thrombin cleavage sites.", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-9666383", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9666383" } ] }, { "id": "R-HSA-9708859", "name": "Activated thrombin (factor IIa) cleaves F2R (PAR1), activating it", "equation": "", "summary": "Thrombin activates proteinase activated receptors (PARs) that signal through heterotrimeric G proteins of the G12/13 and Gq families. In human platelets, PAR1 (F2R) is the predominant thrombin receptor (Vu et al. 1991). Gq is necessary for platelet secretion and aggregation in response to thrombin but is not necessary for thrombin-triggered shape change. G13 appears to contribute to platelet aggregation as well as shape change in response to low concentrations of thrombin but to be unnecessary at higher agonist concentrations; G12 appears to be dispensable for thrombin signaling in platelets.

The proprotein form of F2R is activated when thrombin cleaves the N-terminal exodomain. This cleavage event unmasks a new N-terminus that serves as a tethered ligand that binds intramolecularly to the body of the receptor to effect transmembrane signaling (Vu et al. 1991). Intermolecular ligation of one PAR molecule by another can occur but, not surprisingly, appears to be less efficient than self-ligation. A synthetic peptide of sequence SFLLRN, the first six amino acids of the new N-terminus generated when thrombin cleaves PAR1, can activate PAR1 independent of protease and receptor cleavage. In addition to providing evidence for the tethered ligand mechanism, such tethered ligand-mimicking peptides have provided a convenient pharmacological tool for probing the effects of PAR activation in cells and tissues.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [ "R-HSA-9708861" ], "output_participant_list": [ "R-HSA-114586", "R-HSA-114531" ], "enzyme_list": [ "P00734-1" ], "evidence": [ { "id": "R-HSA-9708859", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9708859" } ] } ], "reaction_participants": [ { "participant_id": "R-HSA-114531", "participant_name": "Activated F2R [plasma membrane]", "crossref": [ { "id": "3BEF", "database": "PDB", "url": "" }, { "id": "NP_001298242.1", "database": "RefSeq", "url": "" }, { "id": "1NRO", "database": "PDB", "url": "" }, { "id": "P25116", "database": "UniProt", "url": "" }, { "id": "PAR1_HUMAN", "database": "ZINC - World Drugs", "url": "" }, { "id": "1NRR", "database": "PDB", "url": "" }, { "id": "3HKI", "database": "PDB", "url": "" }, { "id": "1NRP", "database": "PDB", "url": "" }, { "id": "NP_001983.2", "database": "RefSeq", "url": "" }, { "id": "3HKJ", "database": "PDB", "url": "" }, { "id": "PAR1_HUMAN", "database": "ZINC - Investigational", "url": "" }, { "id": "347", "database": "Guide to Pharmacology - Targets", "url": "" }, { "id": "1NRN", "database": "PDB", "url": "" }, { "id": "3VW7", "database": "PDB", "url": "" }, { "id": "1NRQ", "database": "PDB", "url": "" }, { "id": "PAR1_HUMAN", "database": "ZINC - Predictions - Purchasable", "url": "" }, { "id": "P25116", "database": "GeneCards", "url": "" }, { "id": "ENSG00000181104", "database": "Ensembl", "url": "" }, { "id": "P25116", "database": "Pharos - Targets", "url": "" }, { "id": "ENSP00000321326", "database": "Ensembl", "url": "" }, { "id": "24523", "database": "Orphanet", "url": "" }, { "id": "PAR1_HUMAN", "database": "ZINC - FDA approved", "url": "" }, { "id": "3LU9", 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"name": "homologset.mgi", "label": "MGI Homologs" }, { "name": "homologset.oma", "label": "OMA Homologs" } ], "sequence_features": { "n_linked_sites": [ 121, 143, 260, 416 ], "o_linked_sites": [ 78, 145, 192, 199, 207, 315, 317 ], "snv_sites": [ 78, 109, 123, 144, 161, 315, 440 ], "glycation_sites": [], "phosphorylation_sites": [ 539, 540 ], "sequon_annotation_sites": [ { "start_pos": 121, "end_pos": 123 }, { "start_pos": 143, "end_pos": 145 }, { "start_pos": 205, "end_pos": 207 }, { "start_pos": 416, "end_pos": 418 } ] }, "section_stats": [ { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 90 }, { "field": "total_sites", "count": 11 }, { "field": "n_linked_glycans", "count": 53 }, { "field": "n_linked_glycan_sites", "count": 7 }, { "field": "o_linked_glycans", "count": 2 }, { "field": "o_linked_glycan_sites", "count": 7 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 3 }, { "field": "total_sites", "count": 3 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 3 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 87 }, { "field": "total_sites", "count": 11 }, { "field": "n_linked_glycans", "count": 53 }, { "field": "n_linked_glycan_sites", "count": 4 }, { "field": "o_linked_glycans", "count": 2 }, { "field": "o_linked_glycan_sites", "count": 7 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 2 }, { "field": "total_sites", "count": 2 } ], "sort_fields": [ "start_pos", "end_pos", "kinase_uniprot_canonical_ac", "kinase_gene_name", "residue", "comment", "site_lbl" ] }, { "table_id": "snv", "table_stats": [ { "field": "total", "count": 9 }, { "field": "total_sites", "count": 7 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl", "subjects_tested", "subjects_positive", "frequency" ] }, { "table_id": "snv_disease", "table_stats": [ { "field": "total", "count": 2 }, { "field": "total_sites", "count": 2 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl", "subjects_tested", "subjects_positive", "frequency" ] }, { "table_id": "snv_non_disease", "table_stats": [ { "field": "total", "count": 7 }, { "field": "total_sites", "count": 5 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl", "subjects_tested", "subjects_positive", "frequency" ] }, { "table_id": "publication", "table_stats": [ { "field": "total", "count": 478 } ], "sort_fields": [ "title", "journal", "date", "authors" ] } ] }