Prothrombin

Details

Name
Prothrombin
Synonyms
  • 3.4.21.5
  • Coagulation factor II
Gene Name
F2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016004|Prothrombin
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC
VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV
NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE
CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA
QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG
DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI
DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN
DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP
VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST
RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY
GFYTHVFRLKKWIQKVIDQFGE
Number of residues
622
Molecular Weight
70036.295
Theoretical pI
5.7
GO Classification
Functions
calcium ion binding / growth factor activity / receptor binding / serine-type endopeptidase activity / thrombospondin receptor activity
Processes
acute-phase response / blood coagulation / blood coagulation, intrinsic pathway / cell surface receptor signaling pathway / cellular protein metabolic process / cellular response to mechanical stimulus / cytosolic calcium ion homeostasis / fibrinolysis / leukocyte migration / multicellular organismal development / negative regulation of astrocyte differentiation / negative regulation of fibrinolysis / negative regulation of platelet activation / negative regulation of proteolysis / peptidyl-glutamic acid carboxylation / platelet activation / positive regulation of blood coagulation / positive regulation of cell growth / positive regulation of cell proliferation / positive regulation of collagen biosynthetic process / positive regulation of phosphatidylinositol 3-kinase signaling / positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway / positive regulation of protein phosphorylation / positive regulation of reactive oxygen species metabolic process / positive regulation of release of sequestered calcium ion into cytosol / post-translational protein modification / proteolysis / regulation of blood coagulation / regulation of cell shape / regulation of gene expression / response to inactivity / response to wounding
Components
blood microparticle / cytosol / endoplasmic reticulum lumen / extracellular exosome / extracellular matrix / extracellular region / extracellular space / Golgi lumen / plasma membrane
General Function
Thrombospondin receptor activity
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0016005|Prothrombin (F2)
ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC
CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG
GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTGGAGCGAGAGTGC
GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG
GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT
GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG
AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT
GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC
GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA
TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA
GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG
TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA
CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC
TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT
GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA
GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC
CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT
CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC
GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG
CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG
GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT
GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACCAGGTACGAGCGAAACATTGAAAAG
ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC
CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT
GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG
GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC
AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC
CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA
GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC
CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT
GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT
GGAGAGTAG
Chromosome Location
11
Locus
11p11-q12
External Identifiers
ResourceLink
UniProtKB IDP00734
UniProtKB Entry NameTHRB_HUMAN
GenBank Protein ID339641
GenBank Gene IDM17262
GenAtlas IDF2
HGNC IDHGNC:3535
General References
  1. Degen SJ, Davie EW: Nucleotide sequence of the gene for human prothrombin. Biochemistry. 1987 Sep 22;26(19):6165-77. [PubMed:2825773]
  2. Wang W, Fu Q, Zhou R, Wu W, Ding Q, Hu Y, Wang X, Wang H, Wang Z: Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 by Gly. Haemophilia. 2004 Jan;10(1):94-7. [PubMed:14962227]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
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  5. Degen SJ, MacGillivray RT, Davie EW: Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin. Biochemistry. 1983 Apr 26;22(9):2087-97. [PubMed:6305407]
  6. Suzuki K, Moriyama M, Nakajima C, Kawamura K, Miyazawa K, Tsugawa R, Kikuchi N, Nagata K: Isolation and partial characterization of crystal matrix protein as a potent inhibitor of calcium oxalate crystal aggregation: evidence of activation peptide of human prothrombin. Urol Res. 1994;22(1):45-50. [PubMed:8073540]
  7. Walz DA, Hewett-Emmett D, Seegers WH: Amino acid sequence of human prothrombin fragments 1 and 2. Proc Natl Acad Sci U S A. 1977 May;74(5):1969-72. [PubMed:266717]
  8. Butkowski RJ, Elion J, Downing MR, Mann KG: Primary structure of human prethrombin 2 and alpha-thrombin. J Biol Chem. 1977 Jul 25;252(14):4942-57. [PubMed:873923]
  9. Suzuki K, Nishioka J, Kusumoto H, Hashimoto S: Mechanism of inhibition of activated protein C by protein C inhibitor. J Biochem. 1984 Jan;95(1):187-95. [PubMed:6323392]
  10. Rabiet MJ, Blashill A, Furie B, Furie BC: Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma. J Biol Chem. 1986 Oct 5;261(28):13210-5. [PubMed:3759958]
  11. Glenn KC, Frost GH, Bergmann JS, Carney DH: Synthetic peptides bind to high-affinity thrombin receptors and modulate thrombin mitogenesis. Pept Res. 1988 Nov-Dec;1(2):65-73. [PubMed:2856554]
  12. Pihusch R, Buchholz T, Lohse P, Rubsamen H, Rogenhofer N, Hasbargen U, Hiller E, Thaler CJ: Thrombophilic gene mutations and recurrent spontaneous abortion: prothrombin mutation increases the risk in the first trimester. Am J Reprod Immunol. 2001 Aug;46(2):124-31. [PubMed:11506076]
  13. Casas JP, Hingorani AD, Bautista LE, Sharma P: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. Arch Neurol. 2004 Nov;61(11):1652-61. [PubMed:15534175]
  14. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed:14760718]
  15. Li G, Cui Y, McIlmurray L, Allen WE, Wang H: rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce chemotaxis of human osteoblasts and microvascular endothelial cells. J Orthop Res. 2005 May;23(3):680-5. Epub 2005 Apr 7. [PubMed:15885491]
  16. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952]
  17. Fife C, Mader JT, Stone J, Brill L, Satterfield K, Norfleet A, Zwernemann A, Ryaby JT, Carney DH: Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a placebo-controlled phase I/II study. Wound Repair Regen. 2007 Jan-Feb;15(1):23-34. [PubMed:17244316]
  18. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218]
  19. Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [PubMed:19139490]
  20. Nilsson J, Ruetschi U, Halim A, Hesse C, Carlsohn E, Brinkmalm G, Larson G: Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009 Nov;6(11):809-11. doi: 10.1038/nmeth.1392. Epub 2009 Oct 18. [PubMed:19838169]
  21. Halim A, Nilsson J, Ruetschi U, Hesse C, Larson G: Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD. Mol Cell Proteomics. 2012 Apr;11(4):M111.013649. doi: 10.1074/mcp.M111.013649. Epub 2011 Dec 14. [PubMed:22171320]
  22. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  23. Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J: The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989 Nov;8(11):3467-75. [PubMed:2583108]
  24. Grutter MG, Priestle JP, Rahuel J, Grossenbacher H, Bode W, Hofsteenge J, Stone SR: Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition. EMBO J. 1990 Aug;9(8):2361-5. [PubMed:2369893]
  25. Rydel TJ, Ravichandran KG, Tulinsky A, Bode W, Huber R, Roitsch C, Fenton JW 2nd: The structure of a complex of recombinant hirudin and human alpha-thrombin. Science. 1990 Jul 20;249(4966):277-80. [PubMed:2374926]
  26. Priestle JP, Rahuel J, Rink H, Tones M, Grutter MG: Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms. Protein Sci. 1993 Oct;2(10):1630-42. [PubMed:8251938]
  27. Rydel TJ, Yin M, Padmanabhan KP, Blankenship DT, Cardin AD, Correa PE, Fenton JW 2nd, Tulinsky A: Crystallographic structure of human gamma-thrombin. J Biol Chem. 1994 Sep 2;269(35):22000-6. [PubMed:8071320]
  28. van de Locht A, Bode W, Huber R, Le Bonniec BF, Stone SR, Esmon CT, Stubbs MT: The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin. EMBO J. 1997 Jun 2;16(11):2977-84. [PubMed:9214615]
  29. Guinto ER, Caccia S, Rose T, Futterer K, Waksman G, Di Cera E: Unexpected crucial role of residue 225 in serine proteases. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1852-7. [PubMed:10051558]
  30. Skordalakes E, Dodson GG, Green DS, Goodwin CA, Scully MF, Hudson HR, Kakkar VV, Deadman JJ: Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate. J Mol Biol. 2001 Aug 17;311(3):549-55. [PubMed:11493008]
  31. Schweizer E, Hoffmann-Roder A, Olsen JA, Seiler P, Obst-Sander U, Wagner B, Kansy M, Banner DW, Diederich F: Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors. Org Biomol Chem. 2006 Jun 21;4(12):2364-75. Epub 2006 May 10. [PubMed:16763681]
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  35. Board PG, Shaw DC: Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site. Br J Haematol. 1983 Jun;54(2):245-54. [PubMed:6405779]
  36. Rabiet MJ, Furie BC, Furie B: Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273. J Biol Chem. 1986 Nov 15;261(32):15045-8. [PubMed:3771562]
  37. Miyata T, Morita T, Inomoto T, Kawauchi S, Shirakami A, Iwanaga S: Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima. Biochemistry. 1987 Feb 24;26(4):1117-22. [PubMed:3567158]
  38. Inomoto T, Shirakami A, Kawauchi S, Shigekiyo T, Saito S, Miyoshi K, Morita T, Iwanaga S: Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin. Blood. 1987 Feb;69(2):565-9. [PubMed:3801671]
  39. Henriksen RA, Mann KG: Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382. Biochemistry. 1988 Dec 27;27(26):9160-5. [PubMed:3242619]
  40. Henriksen RA, Mann KG: Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity. Biochemistry. 1989 Mar 7;28(5):2078-82. [PubMed:2719946]
  41. Miyata T, Aruga R, Umeyama H, Bezeaud A, Guillin MC, Iwanaga S: Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity. Biochemistry. 1992 Aug 25;31(33):7457-62. [PubMed:1354985]
  42. Morishita E, Saito M, Kumabashiri I, Asakura H, Matsuda T, Yamaguchi K: Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337-->Thr and Arg-388-->His). Blood. 1992 Nov 1;80(9):2275-80. [PubMed:1421398]
  43. Iwahana H, Yoshimoto K, Shigekiyo T, Shirakami A, Saito S, Itakura M: Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia. Int J Hematol. 1992 Feb;55(1):93-100. [PubMed:1349838]
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  46. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed:10391209]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00001LepirudinapprovedyesinhibitorDetails
DB00006Bivalirudinapproved, investigationalyesinhibitorDetails
DB00278Argatrobanapproved, investigationalyesinhibitorDetails
DB00170Menadioneapproved, nutraceuticalunknownactivatorDetails
DB01123Proflavineapprovednoother/unknownDetails
DB027234-Oxo-2-Phenylmethanesulfonyl-Octahydro-Pyrrolo[1,2-a]Pyrazine-6-Carboxylic Acid [1-(N-Hydroxycarbamimidoyl)-Piperidin-4-Ylmethyl]-AmideexperimentalunknownDetails
DB03847Gamma-Carboxy-Glutamic AcidexperimentalunknownDetails
DB04136LysophosphotidylserineexperimentalunknownDetails
DB00055Drotrecogin alfaapproved, investigational, withdrawnunknownDetails
DB00100Coagulation Factor IX (Recombinant)approved, investigationalunknownDetails
DB04898Ximelagatranapproved, investigational, withdrawnyesinhibitorDetails
DB04591N-{2,2-DIFLUORO-2-[(2R)-PIPERIDIN-2-YL]ETHYL}-2-[2-(1H-1,2,4-TRIAZOL-1-YL)BENZYL][1,3]OXAZOLO[4,5-C]PYRIDIN-4-AMINEexperimentalunknownDetails
DB04697TRANS-4-(GUANIDINOMETHYL)-CYCLOHEXANE-L-YL-D-3-CYCLOHEXYLALANYL-L-AZETIDINE-2-YL-D-TYROSINYL-L-HOMOARGININAMIDEexperimentalunknownDetails
DB047222-(3-CHLORO-6-{[2,2-DIFLUORO-2-(1-OXIDOPYRIDIN-2-YL)ETHYL]AMINO}-1-OXIDOPYRIDIN-2-YL)-N-[1-(3-CHLOROPHENYL)ETHYL]ACETAMIDEexperimentalunknownDetails
DB047711-GUANIDINO-4-(N-NITRO-BENZOYLAMINO-L-LEUCYL-L-PROLYLAMINO)BUTANEexperimentalunknownDetails
DB047721-GUANIDINO-4-(N-PHENYLMETHANESULFONYL-L-LEUCYL-L-PROLYLAMINO)BUTANEexperimentalunknownDetails
DB04786SuramininvestigationalunknowninhibitorDetails
DB05777Thrombomodulin Alfaapproved, investigationalyesinhibitorDetails
DB05714FlovagatraninvestigationalunknownDetails
DB06695Dabigatran etexilateapprovedyesinhibitorDetails
DB06838methyl L-phenylalaninateexperimentalunknownDetails
DB06841D-phenylalanyl-N-[(1S)-4-{[amino(iminio)methyl]amino}-1-(chloroacetyl)butyl]-L-prolinamideexperimentalunknownDetails
DB06845(S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamideexperimentalunknownDetails
DB06850(S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamideexperimentalunknownDetails
DB06853N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamideexperimentalunknownDetails
DB017252-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamideexperimentalunknownDetails
DB038656-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-CarboxamidineexperimentalunknownDetails
DB06858N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamideexperimentalunknownDetails
DB06859N-ALLYL-5-AMIDINOAMINOOXY-PROPYLOXY-3-CHLORO-N-CYCLOPENTYLBENZAMIDEexperimentalunknownDetails
DB068616-(2-HYDROXY-CYCLOPENTYL)-7-OXO-HEPTANAMIDINEexperimentalunknownDetails
DB068656-CARBAMIMIDOYL-2-[2-HYDROXY-6-(4-HYDROXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACIDexperimentalunknownDetails
DB068666-CARBAMIMIDOYL-2-[2-HYDROXY-5-(3-METHOXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACIDexperimentalunknownDetails
DB06868N-(3-chlorobenzyl)-1-(4-methylpentanoyl)-L-prolinamideexperimentalunknownDetails
DB068691-[2-AMINO-2-CYCLOHEXYL-ACETYL]-PYRROLIDINE-3-CARBOXYLIC ACID 5-CHLORO-2-(2-ETHYLCARBAMOYL-ETHOXY)-BENZYLAMIDEexperimentalunknownDetails
DB068781-[(2R)-2-aminobutanoyl]-N-(3-chlorobenzyl)-L-prolinamideexperimentalunknownDetails
DB06911D-leucyl-N-(3-chlorobenzyl)-L-prolinamideexperimentalunknownDetails
DB06919D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamideexperimentalunknownDetails
DB069291-butanoyl-N-(4-carbamimidoylbenzyl)-L-prolinamideexperimentalunknownDetails
DB06936N-(4-carbamimidoylbenzyl)-1-(4-methylpentanoyl)-L-prolinamideexperimentalunknownDetails
DB06942N-(4-carbamimidoylbenzyl)-1-(3-phenylpropanoyl)-L-prolinamideexperimentalunknownDetails
DB069471-[(2R)-2-aminobutanoyl]-N-(4-carbamimidoylbenzyl)-L-prolinamideexperimentalunknownDetails
DB06996D-leucyl-N-(4-carbamimidoylbenzyl)-L-prolinamideexperimentalunknownDetails
DB07005D-phenylalanyl-N-{4-[amino(iminio)methyl]benzyl}-L-prolinamideexperimentalunknownDetails
DB07016(3R)-8-(dioxidosulfanyl)-3-methyl-1,2,3,4-tetrahydroquinolineexperimentalunknownDetails
DB07027D-phenylalanyl-N-(3-fluorobenzyl)-L-prolinamideexperimentalunknownDetails
DB07083beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamideexperimentalunknownDetails
DB07088(S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamideexperimentalunknownDetails
DB07091(S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamideexperimentalunknownDetails
DB07095(S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamideexperimentalunknownDetails
DB071052-[2-(4-CHLORO-PHENYLSULFANYL)-ACETYLAMINO]-3-(4-GUANIDINO-PHENYL)-PROPIONAMIDEexperimentalunknownDetails
DB07120N4-(N,N-DIPHENYLCARBAMOYL)-AMINOGUANIDINEexperimentalunknownDetails
DB07128N7-BUTYL-N2-(5-CHLORO-2-METHYLPHENYL)-5-METHYL[1,2,4]TRIAZOLO[1,5-A]PYRIMIDINE-2,7-DIAMINEexperimentalunknownDetails
DB07131(S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamideexperimentalunknownDetails
DB07133D-phenylalanyl-N-(3-methylbenzyl)-L-prolinamideexperimentalunknownDetails
DB07143D-phenylalanyl-N-benzyl-L-prolinamideexperimentalunknownDetails
DB07165N-(5-CHLORO-BENZO[B]THIOPHEN-3-YLMETHYL)-2-[6-CHLORO-OXO-3-(2-PYRIDIN-2-YL-ETHYLAMINO)-2H-PYRAZIN-1-YL]-ACETAMIDEexperimentalunknownDetails
DB071903-cyclohexyl-D-alanyl-N-(3-chlorobenzyl)-L-prolinamideexperimentalunknownDetails
DB03159CRA_8696experimentalunknownDetails
DB07211(2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDEexperimentalunknownDetails
DB072772-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDEexperimentalunknownDetails
DB072782-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDEexperimentalunknownDetails
DB07279N-ETHYL-N-ISOPROPYL-3-METHYL-5-{[(2S)-2-(PYRIDIN-4-YLAMINO)PROPYL]OXY}BENZAMIDEexperimentalunknownDetails
DB073534-(2,5-DIAMINO-5-HYDROXY-PENTYL)-PHENOLexperimentalunknownDetails
DB073662-[N'-(4-AMINO-BUTYL)-HYDRAZINOCARBONYL]-PYRROLIDINE-1-CARBOXYLIC ACID BENZYL ESTERexperimentalunknownDetails
DB073765-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID)experimentalunknownDetails
DB074001-ETHOXYCARBONYL-D-PHE-PRO-2(4-AMINOBUTYL)HYDRAZINEexperimentalunknownDetails
DB01767Hemi-BabimexperimentalunknownDetails
DB074404-TERT-BUTYLBENZENESULFONIC ACIDexperimentalunknownDetails
DB074613-AMINO-3-BENZYL-9-CARBOXAMIDE[4.3.0]BICYCLO-1,6-DIAZANONAN-2-ONEexperimentalunknownDetails
DB022872-(2-Hydroxy-Phenyl)-3h-Benzoimidazole-5-CarboxamidineexperimentalunknownDetails
DB075084-(5-BENZENESULFONYLAMINO-1-METHYL-1H-BENZOIMIDAZOL-2-YLMETHYL)-BENZAMIDINEexperimentalunknownDetails
DB075151-(2-{[(6-AMINO-2-METHYLPYRIDIN-3-YL)METHYL]AMINO}ETHYL)-6-CHLORO-3-[(2,2-DIFLUORO-2-PYRIDIN-2-YLETHYL)AMINO]-1,4-DIHYDROPYRAZIN-2-OLexperimentalunknownDetails
DB075216-CHLORO-1-(2-{[(5-CHLORO-1-BENZOTHIEN-3-YL)METHYL]AMINO}ETHYL)-3-[(2-PYRIDIN-2-YLETHYL)AMINO]-1,4-DIHYDROPYRAZIN-2-OLexperimentalunknownDetails
DB07522N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]NAPHTHALENE-2-SULFONAMIDEexperimentalunknownDetails
DB07527N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]-4-METHOXY-2,3,6-TRIMETHYLBENZENESULFONAMIDEexperimentalunknownDetails
DB075482-(6-CHLORO-3-{[2,2-DIFLUORO-2-(2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUORO-6-PYRIDINYL)METHYL]ACETAMIDEexperimentalunknownDetails
DB075492-(6-CHLORO-3-{[2,2-DIFLUORO-2-(2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUORO-3-METHYL-6-PYRIDINYL)METHYL]ACETAMIDEexperimentalunknownDetails
DB075502-(6-CHLORO-3-{[2,2-DIFLUORO-2-(1-OXIDO-2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUOROPHENYL)METHYL]ACETAMIDEexperimentalunknownDetails
DB076393-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID ETHYL ESTERexperimentalunknownDetails
DB07658AC-(D)PHE-PRO-BOROLYS-OHexperimentalunknownDetails
DB07659AC-(D)PHE-PRO-BOROHOMOLYS-OHexperimentalunknownDetails
DB07660AC-(D)PHE-PRO-BOROHOMOORNITHINE-OHexperimentalunknownDetails
DB07665N-[2-(carbamimidamidooxy)ethyl]-2-{6-cyano-3-[(2,2-difluoro-2-pyridin-2-ylethyl)amino]-2-fluorophenyl}acetamideexperimentalunknownDetails
DB077183-(4-HYDROXY-PHENYL)PYRUVIC ACIDexperimentalunknownDetails
DB031364-Iodobenzo[B]Thiophene-2-CarboxamidineexperimentalunknownDetails
DB077414-(1R,3AS,4R,8AS,8BR)-[1-DIFLUOROMETHYL-2-(4-FLUOROBENZYL)-3-OXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZAMIDINEexperimentalunknownDetails
DB07796(3ASR,4RS,8ASR,8BRS)-4-(2-(4-FLUOROBENZYL)-1,3-DIOXODEACAHYDROPYRROLO[3,4-A] PYRROLIZIN-4-YL)BENZAMIDINEexperimentalunknownDetails
DB078094-({[4-(3-METHYLBENZOYL)PYRIDIN-2-YL]AMINO}METHYL)BENZENECARBOXIMIDAMIDEexperimentalunknownDetails
DB078971-(HYDROXYMETHYLENEAMINO)-8-HYDROXY-OCTANEexperimentalunknownDetails
DB07934[[CYCLOHEXANESULFONYL-GLYCYL]-3[PYRIDIN-4-YL-AMINOMETHYL]ALANYL]PIPERIDINEexperimentalunknownDetails
DB07944N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDEexperimentalunknownDetails
DB07946N-[2-({[amino(imino)methyl]amino}oxy)ethyl]-2-{6-chloro-3-[(2,2-difluoro-2-phenylethyl)amino]-2-fluorophenyl}acetamideexperimentalunknownDetails
DB080614-[3-(4-CHLOROPHENYL)-1H-PYRAZOL-5-YL]PIPERIDINEexperimentalunknownDetails
DB080623-(4-CHLOROPHENYL)-5-(METHYLTHIO)-4H-1,2,4-TRIAZOLEexperimentalunknownDetails
DB08152{(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetateexperimentalunknownDetails
DB08187METHYL-PHE-PRO-AMINO-CYCLOHEXYLGLYCINEexperimentalunknownDetails
DB01766Beta-(2-Naphthyl)-AlanineexperimentalunknownDetails
DB082542-NAPHTHALENESULFONIC ACIDexperimentalunknownDetails
DB08422[PHENYLALANINYL-PROLINYL]-[2-(PYRIDIN-4-YLAMINO)-ETHYL]-AMINEexperimentalunknownDetails
DB085464-[(3AS,4R,7R,8AS,8BR)-2-(1,3-BENZODIOXOL-5-YLMETHYL)-7-HYDROXY-1,3-DIOXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZENECARBOXIMIDAMIDEexperimentalunknownDetails
DB08624BENZOTHIAZOLEexperimentalunknownDetails
DB00025Antihemophilic factor, human recombinantapproved, investigationalunknownactivatorDetails
DB06404Human C1-esterase inhibitorapprovedunknowninhibitorDetails
DB09228Conestat alfaapproved, investigationalyesinhibitorDetails
DB11166Antithrombin Alfaapproved, investigationalyesinhibitorDetails
DB12831GabexateinvestigationalyesinhibitorDetails
DB12598NafamostatinvestigationalyesinhibitorDetails
DB13152Coagulation Factor IX HumanapprovedunknownDetails
DB13151Anti-inhibitor coagulant complexapproved, investigationalyesagonistDetails
DB13151Anti-inhibitor coagulant complexapproved, investigationalyessubstrateDetails
DB09130Copperapproved, investigationalunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB12364Betrixabanapproved, investigationalyesinhibitorDetails
DB09109Turoctocog alfaapproved, investigationalyesbinderDetails
DB09332KappadioneapprovedunknownagonistDetails
DB13998Lonoctocog alfaapproved, investigationalunknownactivatorDetails
DB13999Moroctocog alfaapprovedunknownactivatorDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails
DB14738Turoctocog alfa pegolapprovedyesbinderDetails