Fibrinogen beta chain

Details

Name
Fibrinogen beta chain
Synonyms
  • Fibrinogen beta chain precursor
Gene Name
FGB
Organism
Humans
Amino acid sequence
>lcl|BSEQ0004100|Fibrinogen beta chain
MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLR
PAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQE
RPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQ
LYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKE
CEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYK
QGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFT
VQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDP
RKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKM
SMKIRPFFPQQ
Number of residues
491
Molecular Weight
55927.9
Theoretical pI
8.38
GO Classification
Functions
chaperone binding / structural molecule activity
Processes
adaptive immune response / blood coagulation / blood coagulation, fibrin clot formation / cell-matrix adhesion / cellular protein complex assembly / cellular response to interleukin-1 / cellular response to leptin stimulus / extracellular matrix organization / fibrinolysis / induction of bacterial agglutination / innate immune response / 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 polymerization / response to calcium ion / 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
General Function
Structural molecule activity
Specific Function
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) 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. 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 antibacterial immune response via both innate and T-cell mediated pathways.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0019235|Fibrinogen beta chain (FGB)
ATGAAAAGGATGGTTTCTTGGAGCTTCCACAAACTTAAAACCATGAAACATCTATTATTG
CTACTATTGTGTGTTTTTCTAGTTAAGTCCCAAGGTGTCAACGACAATGAGGAGGGTTTC
TTCAGTGCCCGTGGTCATCGACCCCTTGACAAGAAGAGAGAAGAGGCTTTGCTACAACAG
GAAAGGCCAATCAGAAATAGTGTTGATGAGTTAAATAACAATGTGGAAGCTGTTTCCCAG
ACCTCCTCTTCTTCCTTTCAGTACATGTATTTGCTGAAAGACCTGTGGCAAAAGAGGCAG
AAGCAAGTAAAAGATAATGAAAATGTAGTCAATGAGTACTCCTCAGAACTGGAAAAGCAC
CAATTATATATAGATGAGACTGTGAATAGCAATATCCCAACTAACCTTCGTGTGCTTCGT
TCAATCCTGGAAAACCTGAGAAGCAAAATACAAAAGTTAGAATCTGATGTCTCAGCTCAA
ATGGAATATTGTCGCACCCCATGCACTGTCAGTTGCAATATTCCTGTGGTGTCTGGCAAA
GAATGTGAGGAAATTATCAGGAAAGGAGGTGAAACATCTGAAATGTATCTCATTCAACCT
GACAGTTCTGTCAAACCGTATAGAGTATACTGTGACATGAATACAGAAAATGGAGGATGG
ACAGTGATTCAGAACCGTCAAGACGGTAGTGTTGACTTTGGCAGGAAATGGGATCCATAT
AAACAGGGATTTGGAAATGTTGCAACCAACACAGATGGGAAGAATTACTGTGGCCTACCA
GGTGAATATTGGCTTGGAAATGATAAAATTAGCCAGCTTACCAGGATGGGACCCACAGAA
CTTTTGATAGAAATGGAGGACTGGAAAGGAGACAAAGTAAAGGCTCACTATGGAGGATTC
ACTGTACAGAATGAAGCCAACAAATACCAGATCTCAGTGAACAAATACAGAGGAACAGCC
GGTAATGCCCTCATGGATGGAGCATCTCAGCTGATGGGAGAAAACAGGACCATGACCATT
CACAACGGCATGTTCTTCAGCACGTATGACAGAGACAATGACGGCTGGTTAACATCAGAT
CCCAGAAAACAGTGTTCTAAAGAAGACGGTGGTGGATGGTGGTATAATAGATGTCATGCA
GCCAATCCAAACGGCAGATACTACTGGGGTGGACAGTACACCTGGGACATGGCAAAGCAT
GGCACAGATGATGGTGTAGTATGGATGAATTGGAAGGGGTCATGGTACTCAATGAGGAAG
ATGAGTATGAAGATCAGGCCCTTCTTCCCACAGCAATAG
Chromosome Location
4
Locus
4q28
External Identifiers
ResourceLink
UniProtKB IDP02675
UniProtKB Entry NameFIBB_HUMAN
GenBank Protein ID182430
GenBank Gene IDJ00129
GenAtlas IDFGB
HGNC IDHGNC:3662
General References
  1. Chung DW, Que BG, Rixon MW, Mace M Jr, Davie EW: Characterization of complementary deoxyribonucleic acid and genomic deoxyribonucleic acid for the beta chain of human fibrinogen. Biochemistry. 1983 Jun 21;22(13):3244-50. [Article]
  2. 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]
  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. [Article]
  4. 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]
  5. 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]
  6. Huber P, Dalmon J, Courtois G, Laurent M, Assouline Z, Marguerie G: Characterization of the 5'-flanking region for the human fibrinogen beta gene. Nucleic Acids Res. 1987 Feb 25;15(4):1615-25. [Article]
  7. Watt KW, Takagi T, Doolittle RF: Amino acid sequence of the beta chain of human fibrinogen. Biochemistry. 1979 Jan 9;18(1):68-76. [Article]
  8. Blomback B, Hessel B, Hogg D: Disulfide bridges in nh2 -terminal part of human fibrinogen. Thromb Res. 1976 May;8(5):639-58. [Article]
  9. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [Article]
  10. Henschen A, Lottspeich F, Kehl M, Southan C: Covalent structure of fibrinogen. Ann N Y Acad Sci. 1983 Jun 27;408:28-43. [Article]
  11. Gardlund B, Hessel B, Marguerie G, Murano G, Blomback B: Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments. Eur J Biochem. 1977 Aug 1;77(3):595-610. [Article]
  12. Doolittle RF: Fibrinogen and fibrin. Annu Rev Biochem. 1984;53:195-229. [Article]
  13. Tran H, Tanaka A, Litvinovich SV, Medved LV, Haudenschild CC, Argraves WS: The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis. J Biol Chem. 1995 Aug 18;270(33):19458-64. [Article]
  14. 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]
  15. Lewandrowski U, Moebius J, Walter U, Sickmann A: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol Cell Proteomics. 2006 Feb;5(2):226-33. Epub 2005 Oct 31. [Article]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. 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]
  23. 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]
  24. Schmelzer CH, Ebert RF, Bell WR: A polymorphism at B beta 448 of fibrinogen identified during structural studies of fibrinogen Baltimore II. Thromb Res. 1988 Oct 15;52(2):173-7. [Article]
  25. Yoshida N, Wada H, Morita K, Hirata H, Matsuda M, Yamazumi K, Asakura S, Shirakawa S: A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine. Blood. 1991 May 1;77(9):1958-63. [Article]
  26. Koopman J, Haverkate F, Lord ST, Grimbergen J, Mannucci PM: Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr. J Clin Invest. 1992 Jul;90(1):238-44. [Article]
  27. Koopman J, Haverkate F, Grimbergen J, Engesser L, Novakova I, Kerst AF, Lord ST: Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes. Proc Natl Acad Sci U S A. 1992 Apr 15;89(8):3478-82. [Article]
  28. Liu CY, Koehn JA, Morgan FJ: Characterization of fibrinogen New York 1. A dysfunctional fibrinogen with a deletion of B beta(9-72) corresponding exactly to exon 2 of the gene. J Biol Chem. 1985 Apr 10;260(7):4390-6. [Article]
  29. 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]
  30. Duga S, Asselta R, Santagostino E, Zeinali S, Simonic T, Malcovati M, Mannucci PM, Tenchini ML: Missense mutations in the human beta fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion. Blood. 2000 Feb 15;95(4):1336-41. [Article]
  31. Lounes KC, Lefkowitz JB, Henschen-Edman AH, Coates AI, Hantgan RR, Lord ST: The impaired polymerization of fibrinogen Longmont (Bbeta166Arg-->Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers. Blood. 2001 Aug 1;98(3):661-6. [Article]
  32. Asselta R, Duga S, Spena S, Peyvandi F, Castaman G, Malcovati M, Mannucci PM, Tenchini ML: Missense or splicing mutation? The case of a fibrinogen Bbeta-chain mutation causing severe hypofibrinogenemia. Blood. 2004 Apr 15;103(8):3051-4. Epub 2003 Dec 24. [Article]
  33. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB04919AlfimepraseinvestigationalunknownDetails
DB11311ProthrombinapprovedyescleavageDetails
DB13151Anti-inhibitor coagulant complexapproved, investigationalyescleavageDetails
DB11572Thrombin alfaapprovedyesactivatorDetails
DB11571Human thrombinapprovedyesactivatorDetails
DB11300Thrombinapproved, investigationalyesactivatorDetails
DB00364SucralfateapprovedunknownbinderprotectorDetails