Fibrinogen alpha chain

Details

Name

Fibrinogen alpha chain

Synonyms

• Fibrinogen alpha chain precursor

Gene Name

FGA

Organism

Humans

Amino acid sequence

>lcl|BSEQ0001074|Fibrinogen alpha chain
MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDW
NYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSA
NNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSC
RGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQ
LQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSS
GPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTW
NPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNV
SPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTK
EVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEF
VSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKS
YKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFS
VYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQR
GSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSH
NNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENG
VVWVSFRGADYSLRAVRMKIRPLVTQ

Number of residues

866

Molecular Weight

94972.455

Theoretical pI

5.87

GO Classification

Functions

structural molecule activity

Processes

acute-phase response / adaptive immune response / blood coagulation / blood coagulation, common pathway / blood coagulation, fibrin clot formation / cell-matrix adhesion / cellular protein complex assembly / cellular protein metabolic process / cellular response to granulocyte colony-stimulating factor / cellular response to interleukin-6 / cellular response to organic cyclic compound / extracellular matrix organization / fibrinolysis / induction of bacterial agglutination / innate immune response / liver regeneration / negative regulation of blood coagulation, common pathway / negative regulation of endothelial cell apoptotic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / plasminogen activation / platelet activation / platelet aggregation / platelet degranulation / positive regulation of ERK1 and ERK2 cascade / positive regulation of exocytosis / positive regulation of heterotypic cell-cell adhesion / positive regulation of peptide hormone secretion / positive regulation of protein secretion / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of vasoconstriction / protein complex assembly / protein polymerization / response to calcium ion / response to cycloheximide / response to estradiol / response to genistein / response to morphine / signal transduction

Components

blood microparticle / cell cortex / cell surface / external side of plasma membrane / extracellular exosome / extracellular region / extracellular space / extracellular vesicle / fibrinogen complex / plasma membrane / platelet alpha granule / platelet alpha granule lumen / rough endoplasmic reticulum

General Function

Structural molecule activity

Specific Function

Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.

Pfam Domain Function

• Fibrinogen_C (PF00147)
• Fib_alpha (PF08702)
• Fibrinogen_aC (PF12160)

Transmembrane Regions

Not Available

Cellular Location

Secreted

Gene sequence

>lcl|BSEQ0021267|Fibrinogen alpha chain (FGA)
ATGTTTTCCATGAGGATCGTCTGCCTGGTCCTAAGTGTGGTGGGCACAGCATGGACTGCA
GATAGTGGTGAAGGTGACTTTCTAGCTGAAGGAGGAGGCGTGCGTGGCCCAAGGGTTGTG
GAAAGACATCAATCTGCCTGCAAAGATTCAGACTGGCCCTTCTGCTCTGATGAAGACTGG
AACTACAAATGCCCTTCTGGCTGCAGGATGAAAGGGTTGATTGATGAAGTCAATCAAGAT
TTTACAAACAGAATAAATAAGCTCAAAAATTCACTATTTGAATATCAGAAGAACAATAAG
GATTCTCATTCGTTGACCACTAATATAATGGAAATTTTGAGAGGCGATTTTTCCTCAGCC
AATAACCGTGATAATACCTACAACCGAGTGTCAGAGGATCTGAGAAGCAGAATTGAAGTC
CTGAAGCGCAAAGTCATAGAAAAAGTACAGCATATCCAGCTTCTGCAGAAAAATGTTAGA
GCTCAGTTGGTTGATATGAAACGACTGGAGGTGGACATTGATATTAAGATCCGATCTTGT
CGAGGGTCATGCAGTAGGGCTTTAGCTCGTGAAGTAGATCTGAAGGACTATGAAGATCAG
CAGAAGCAACTTGAACAGGTCATTGCCAAAGACTTACTTCCCTCTAGAGATAGGCAACAC
TTACCACTGATAAAAATGAAACCAGTTCCAGACTTGGTTCCCGGAAATTTTAAGAGCCAG
CTTCAGAAGGTACCCCCAGAGTGGAAGGCATTAACAGACATGCCGCAGATGAGAATGGAG
TTAGAGAGACCTGGTGGAAATGAGATTACTCGAGGAGGCTCCACCTCTTATGGAACCGGA
TCAGAGACGGAAAGCCCCAGGAACCCTAGCAGTGCTGGAAGCTGGAACTCTGGGAGCTCT
GGACCTGGAAGTACTGGAAACCGAAACCCTGGGAGCTCTGGGACTGGAGGGACTGCAACC
TGGAAACCTGGGAGCTCTGGACCTGGAAGTACTGGAAGCTGGAACTCTGGGAGCTCTGGA
ACTGGAAGTACTGGAAACCAAAACCCTGGGAGCCCTAGACCTGGTAGTACCGGAACCTGG
AATCCTGGCAGCTCTGAACGCGGAAGTGCTGGGCACTGGACCTCTGAGAGCTCTGTATCT
GGTAGTACTGGACAATGGCACTCTGAATCTGGAAGTTTTAGGCCAGATAGCCCAGGCTCT
GGGAACGCGAGGCCTAACAACCCAGACTGGGGCACATTTGAAGAGGTGTCAGGAAATGTA
AGTCCAGGGACAAGGAGAGAGTACCACACAGAAAAACTGGTCACTTCTAAAGGAGATAAA
GAGCTCAGGACTGGTAAAGAGAAGGTCACCTCTGGTAGCACAACCACCACGCGTCGTTCA
TGCTCTAAAACCGTTACTAAGACTGTTATTGGTCCTGATGGTCACAAAGAAGTTACCAAA
GAAGTGGTGACCTCCGAAGATGGTTCTGACTGTCCCGAGGCAATGGATTTAGGCACATTG
TCTGGCATAGGTACTCTGGATGGGTTCCGCCATAGGCACCCTGATGAAGCTGCCTTCTTC
GACACTGCCTCAACTGGAAAAACATTCCCAGGTTTCTTCTCACCTATGTTAGGAGAGTTT
GTCAGTGAGACTGAGTCTAGGGGCTCAGAATCTGGCATCTTCACAAATACAAAGGAATCC
AGTTCTCATCACCCTGGGATAGCTGAATTCCCTTCCCGTGGTAAATCTTCAAGTTACAGC
AAACAATTTACTAGTAGCACGAGTTACAACAGAGGAGACTCCACATTTGAAAGCAAGAGC
TATAAAATGGCAGATGAGGCCGGAAGTGAAGCCGATCATGAAGGAACACATAGCACCAAG
AGAGGCCATGCTAAATCTCGCCCTGTCAGAGACTGTGATGATGTCCTCCAAACACATCCT
TCAGGTACCCAAAGTGGCATTTTCAATATCAAGCTACCGGGATCCAGTAAGATTTTTTCT
GTTTATTGCGATCAAGAGACCAGTTTGGGAGGATGGCTTTTGATCCAGCAAAGAATGGAT
GGATCACTGAATTTTAACCGGACCTGGCAAGACTACAAGAGAGGTTTCGGCAGCCTGAAT
GACGAGGGGGAAGGAGAATTCTGGCTAGGCAATGACTACCTCCACTTACTAACCCAAAGG
GGCTCTGTTCTTAGGGTTGAATTAGAGGACTGGGCTGGGAATGAAGCTTATGCAGAATAT
CACTTCCGGGTAGGCTCTGAGGCTGAAGGCTATGCCCTCCAAGTCTCCTCCTATGAAGGC
ACTGCGGGTGATGCTCTGATTGAGGGTTCCGTAGAGGAAGGGGCAGAGTACACCTCTCAC
AACAACATGCAGTTCAGCACCTTTGACAGGGATGCAGACCAGTGGGAAGAGAACTGTGCA
GAAGTCTATGGGGGAGGCTGGTGGTATAATAACTGCCAAGCAGCCAATCTCAATGGAATC
TACTACCCTGGGGGCTCCTATGACCCAAGGAATAACAGTCCTTATGAGATTGAGAATGGA
GTGGTCTGGGTTTCCTTTAGAGGGGCAGATTATTCCCTCAGGGCTGTTCGCATGAAAATT
AGGCCCCTTGTGACCCAATAG

Chromosome Location

4

Locus

4q28

External Identifiers

Resource	Link
UniProtKB ID	P02671
UniProtKB Entry Name	FIBA_HUMAN
GenBank Protein ID	13591824
GenBank Gene ID	AF361104
GenAtlas ID	FGA
HGNC ID	HGNC:3661

General References

1. Fu Y, Weissbach L, Plant PW, Oddoux C, Cao Y, Liang TJ, Roy SN, Redman CM, Grieninger G: Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits. Biochemistry. 1992 Dec 8;31(48):11968-72. [Article]
2. 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. [Article]
3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
4. Chung DW, Harris JE, Davie EW: Nucleotide sequences of the three genes coding for human fibrinogen. Adv Exp Med Biol. 1990;281:39-48. [Article]
5. Kant JA, Lord ST, Crabtree GR: Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications. Proc Natl Acad Sci U S A. 1983 Jul;80(13):3953-7. [Article]
6. Rixon MW, Chan WY, Davie EW, Chung DW: Characterization of a complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen. Biochemistry. 1983 Jun 21;22(13):3237-44. [Article]
7. Watt KW, Cottrell BA, Strong DD, Doolittle RF: Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence. Biochemistry. 1979 Nov 27;18(24):5410-6. [Article]
8. Imam AM, Eaton MA, Williamson R, Humphries S: Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen. Nucleic Acids Res. 1983 Nov 11;11(21):7427-34. [Article]
9. Chung DW, Rixon MW, Que BG, Davie EW: Cloning of fibrinogen genes and their cDNA. Ann N Y Acad Sci. 1983 Jun 27;408:449-56. [Article]
10. Bouma H, Takagi T, Doolittle RF: The arrangement of disulfide bonds in fragment D from human fibrinogen. Thromb Res. 1978 Sep;13(3):557-62. [Article]
11. Cottrell BA, Strong DD, Watt KW, Doolittle RF: Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites. Biochemistry. 1979 Nov 27;18(24):5405-10. [Article]
12. Fretto LJ, Ferguson EW, Steinman HM, McKee PA: Localization of the alpha-chain cross-link acceptor sites of human fibrin. J Biol Chem. 1978 Apr 10;253(7):2184-95. [Article]
13. 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. [Article]
14. Blomback B, Hessel B, Hogg D: Disulfide bridges in nh2 -terminal part of human fibrinogen. Thromb Res. 1976 May;8(5):639-58. [Article]
15. Doolittle RF: Fibrinogen and fibrin. Annu Rev Biochem. 1984;53:195-229. [Article]
16. Kimura S, Aoki N: Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor. J Biol Chem. 1986 Nov 25;261(33):15591-5. [Article]
17. Itarte E, Plana M, Guasch MD, Martos C: Phosphorylation of fibrinogen by casein kinase 1. Biochem Biophys Res Commun. 1983 Dec 16;117(2):631-6. [Article]
18. Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F: Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9(2):109-20. [Article]
19. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [Article]
20. Ono M, Matsubara J, Honda K, Sakuma T, Hashiguchi T, Nose H, Nakamori S, Okusaka T, Kosuge T, Sata N, Nagai H, Ioka T, Tanaka S, Tsuchida A, Aoki T, Shimahara M, Yasunami Y, Itoi T, Moriyasu F, Negishi A, Kuwabara H, Shoji A, Hirohashi S, Yamada T: Prolyl 4-hydroxylation of alpha-fibrinogen: a novel protein modification revealed by plasma proteomics. J Biol Chem. 2009 Oct 16;284(42):29041-9. doi: 10.1074/jbc.M109.041749. Epub 2009 Aug 20. [Article]
21. 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. [Article]
22. Kirschbaum NE, Budzynski AZ: A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule. J Biol Chem. 1990 Aug 15;265(23):13669-76. [Article]
23. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
24. Zauner G, Hoffmann M, Rapp E, Koeleman CA, Dragan I, Deelder AM, Wuhrer M, Hensbergen PJ: Glycoproteomic analysis of human fibrinogen reveals novel regions of O-glycosylation. J Proteome Res. 2012 Dec 7;11(12):5804-14. doi: 10.1021/pr3005937. Epub 2012 Oct 29. [Article]
25. Adamczyk B, Struwe WB, Ercan A, Nigrovic PA, Rudd PM: Characterization of fibrinogen glycosylation and its importance for serum/plasma N-glycome analysis. J Proteome Res. 2013 Jan 4;12(1):444-54. doi: 10.1021/pr300813h. Epub 2012 Nov 30. [Article]
26. 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. [Article]
27. Tagliabracci VS, Wiley SE, Guo X, Kinch LN, Durrant E, Wen J, Xiao J, Cui J, Nguyen KB, Engel JL, Coon JJ, Grishin N, Pinna LA, Pagliarini DJ, Dixon JE: A Single Kinase Generates the Majority of the Secreted Phosphoproteome. Cell. 2015 Jun 18;161(7):1619-32. doi: 10.1016/j.cell.2015.05.028. [Article]
28. Martin PD, Robertson W, Turk D, Huber R, Bode W, Edwards BF: The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution. J Biol Chem. 1992 Apr 15;267(11):7911-20. [Article]
29. Spraggon G, Everse SJ, Doolittle RF: Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature. 1997 Oct 2;389(6650):455-62. [Article]
30. Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF: Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry. 1998 Jun 16;37(24):8637-42. [Article]
31. Spraggon G, Applegate D, Everse SJ, Zhang JZ, Veerapandian L, Redman C, Doolittle RF, Grieninger G: Crystal structure of a recombinant alphaEC domain from human fibrinogen-420. Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9099-104. [Article]
32. Everse SJ, Spraggon G, Veerapandian L, Doolittle RF: Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry. 1999 Mar 9;38(10):2941-6. [Article]
33. Kollman JM, Pandi L, Sawaya MR, Riley M, Doolittle RF: Crystal structure of human fibrinogen. Biochemistry. 2009 May 12;48(18):3877-86. doi: 10.1021/bi802205g. [Article]
34. Yoshida N, Okuma M, Hirata H, Matsuda M, Yamazumi K, Asakura S: Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine. Blood. 1991 Jul 1;78(1):149-53. [Article]
35. Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, Arocha-Pinango CL, Rodriguez S, Nagy H, Perez-Requejo JL, et al.: Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator. J Clin Invest. 1992 Jul;90(1):67-76. [Article]
36. Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, de Bosch NB, Carvajal Z, Ojeda A, Arocha-Pinango CL, et al.: An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation. J Biol Chem. 1991 Jun 25;266(18):11575-81. [Article]
37. Koopman J, Haverkate F, Grimbergen J, Lord ST, Mosesson MW, DiOrio JP, Siebenlist KS, Legrand C, Soria J, Soria C, et al.: Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia. J Clin Invest. 1993 Apr;91(4):1637-43. [Article]
38. Benson MD, Liepnieks J, Uemichi T, Wheeler G, Correa R: Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain. Nat Genet. 1993 Mar;3(3):252-5. [Article]
39. Yamazumi K, Terukina S, Matsuda M, Kanbayashi J, Sakon M, Tsujinaka T: Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution. Surg Today. 1993;23(1):45-50. [Article]
40. Brennan SO, Hammonds B, George PM: Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A alpha 20 Val --> Asp). J Clin Invest. 1995 Dec;96(6):2854-8. [Article]
41. 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. [Article]
42. Flood VH, Al-Mondhiry HA, Farrell DH: The fibrinogen Aalpha R16C mutation results in fibrinolytic resistance. Br J Haematol. 2006 Jul;134(2):220-6. [Article]
43. Asselta R, Plate M, Robusto M, Borhany M, Guella I, Solda G, Afrasiabi A, Menegatti M, Shamsi T, Peyvandi F, Duga S: Clinical and molecular characterisation of 21 patients affected by quantitative fibrinogen deficiency. Thromb Haemost. 2015 Mar;113(3):567-76. doi: 10.1160/TH14-07-0629. Epub 2014 Nov 27. [Article]

Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB00009	Alteplase	approved, investigational	yes	binder	Details
DB00015	Reteplase	approved, investigational	yes		Details
DB00029	Anistreplase	approved	yes		Details
DB00031	Tenecteplase	approved	yes		Details
DB04919	Alfimeprase	investigational	unknown		Details
DB05099	Ancrod	approved, investigational	unknown		Details
DB05675	EP-2104R	investigational	unknown		Details
DB06245	Lanoteplase	investigational	unknown		Details
DB11311	Prothrombin	approved	yes	cleavage	Details
DB13151	Anti-inhibitor coagulant complex	approved, investigational	yes	cleavage	Details
DB01593	Zinc	approved, investigational	unknown		Details
DB11572	Thrombin alfa	approved	yes	activator	Details
DB11571	Human thrombin	approved	yes	activator	Details
DB11300	Thrombin	approved, investigational	yes	activator	Details
DB14487	Zinc acetate	approved, investigational	unknown		Details
DB14533	Zinc chloride	approved, investigational	unknown	binder	Details
DB14548	Zinc sulfate, unspecified form	approved, experimental	unknown	binder	Details
DB00364	Sucralfate	approved	unknown	binder	Details