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Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain]

 FIBB_HUMAN              Reviewed;         491 AA.
P02675; A0JLR9; B2R7G3; Q32Q65; Q3KPF2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 2.
25-OCT-2017, entry version 210.
RecName: Full=Fibrinogen beta chain;
Contains:
RecName: Full=Fibrinopeptide B;
Contains:
RecName: Full=Fibrinogen beta chain;
Flags: Precursor;
Name=FGB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6688356; DOI=10.1021/bi00282a032;
Chung D.W., Que B.G., Rixon M.W., Mace M. Jr., Davie E.W.;
"Characterization of complementary deoxyribonucleic acid and genomic
deoxyribonucleic acid for the beta chain of human fibrinogen.";
Biochemistry 22:3244-3250(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2102623;
Chung D.W., Harris J.E., Davie E.W.;
"Nucleotide sequences of the three genes coding for human
fibrinogen.";
Adv. Exp. Med. Biol. 281:39-48(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chung D.W., Harris J.E., Davie E.W.;
"Nucleotide sequences of the three genes coding for human
fibrinogen.";
(In) Liu C.Y., Chien S. (eds.);
Fibrinogen, thrombosis, coagulation and fibrinolysis, pp.39-48, Plenum
Press, New York (1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-100; HIS-170;
LEU-265 AND LYS-478.
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
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 T.-O., 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. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
PubMed=6575700; DOI=10.1111/j.1749-6632.1983.tb23265.x;
Chung D.W., Rixon M.W., Que B.G., Davie E.W.;
"Cloning of fibrinogen genes and their cDNA.";
Ann. N. Y. Acad. Sci. 408:449-456(1983).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
PubMed=3029722; DOI=10.1093/nar/15.4.1615;
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. 15:1615-1625(1987).
[10]
PROTEIN SEQUENCE OF 31-491, AND PYROGLUTAMATE FORMATION AT GLN-31.
PubMed=420779; DOI=10.1021/bi00568a011;
Watt K.W.K., Takagi T., Doolittle R.F.;
"Amino acid sequence of the beta chain of human fibrinogen.";
Biochemistry 18:68-76(1979).
[11]
PROTEIN SEQUENCE OF 31-491, AND GLYCOSYLATION AT ASN-394.
Henschen A., Lottspeich F., Southan C., Topfer-Petersen E.;
"Human fibrinogen: sequence, sulfur bridges, glycosylation and some
structural variants.";
(In) Peeters H. (eds.);
Protides of the biological fluids, Proc. 28th colloquium, pp.51-56,
Pergamon Press, Oxford (1980).
[12]
PROTEIN SEQUENCE OF 31-148, AND DISULFIDE BONDS.
PubMed=936108; DOI=10.1016/0049-3848(76)90245-0;
Blombaeck B., Hessel B., Hogg D.;
"Disulfide bridges in NH2-terminal part of human fibrinogen.";
Thromb. Res. 8:639-658(1976).
[13]
PROTEIN SEQUENCE OF 31-44.
Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M.;
"Studies on fibrinopeptides from primates.";
Acta Chem. Scand. 19:1788-1789(1965).
[14]
PROTEIN SEQUENCE OF 45-53.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[15]
PROTEIN SEQUENCE OF 54-72; 164-178 AND 225-239, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[16]
REVIEW, AND DISULFIDE BONDS.
PubMed=6575689; DOI=10.1111/j.1749-6632.1983.tb23232.x;
Henschen A., Lottspeich F., Kehl M., Southan C.;
"Covalent structure of fibrinogen.";
Ann. N. Y. Acad. Sci. 408:28-43(1983).
[17]
DISULFIDE BONDS.
PubMed=891553; DOI=10.1111/j.1432-1033.1977.tb11704.x;
Gaardlund B., Hessel B., Marguerie G., Murano G., Blombaeck B.;
"Primary structure of human fibrinogen. Characterization of disulfide-
containing cyanogen-bromide fragments.";
Eur. J. Biochem. 77:595-610(1977).
[18]
DISULFIDE BONDS.
Doolittle R.F., Takagi T., Watt K.W.K., Bouma H. III, Cottrell B.A.,
Cassman K.G., Goldbaum D.M., Doolittle L.R., Friezner S.J.;
"The structures of fibrinogen and fibrin.";
(In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H.
(eds.);
Regulatory proteolytic enzymes and their inhibitors, pp.163-172,
Pergamon Press, New York (1978).
[19]
REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, AND LIGANDS.
PubMed=6383194; DOI=10.1146/annurev.bi.53.070184.001211;
Doolittle R.F.;
"Fibrinogen and fibrin.";
Annu. Rev. Biochem. 53:195-229(1984).
[20]
INTERACTION WITH FBLN1.
PubMed=7642629; DOI=10.1074/jbc.270.33.19458;
Tran H., Tanaka A., Litvinovich S.V., Medved L.V., Haudenschild C.C.,
Argraves W.S.;
"The interaction of fibulin-1 with fibrinogen. A potential role in
hemostasis and thrombosis.";
J. Biol. Chem. 270:19458-19464(1995).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
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. 8:651-661(2009).
[24]
CLEAVAGE BY HEMENTIN AND PLASMIN.
PubMed=2143188;
Kirschbaum N.E., Budzynski A.Z.;
"A unique proteolytic fragment of human fibrinogen containing the A
alpha COOH-terminal domain of the native molecule.";
J. Biol. Chem. 265:13669-13676(1990).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[27]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 164-491, DISULFIDE BONDS,
AND SUBUNIT.
PubMed=9333233; DOI=10.1038/38947;
Spraggon G., Everse S.J., Doolittle R.F.;
"Crystal structures of fragment D from human fibrinogen and its
crosslinked counterpart from fibrin.";
Nature 389:455-462(1997).
[28]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 164-491 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, GLYCOSYLATION AT ASN-394, SUBUNIT, COILED
COIL DOMAIN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9628725; DOI=10.1021/bi9804129;
Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F.;
"Crystal structure of fragment double-D from human fibrin with two
different bound ligands.";
Biochemistry 37:8637-8642(1998).
[29]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 164-491 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, GLYCOSYLATION AT ASN-394, SUBUNIT,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND COILED COIL DOMAIN.
PubMed=10074346; DOI=10.1021/bi982626w;
Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F.;
"Conformational changes in fragments D and double-D from human
fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.";
Biochemistry 38:2941-2946(1999).
[30]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-491 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, GLYCOSYLATION AT ASN-394, SUBUNIT,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND COILED COIL DOMAIN.
PubMed=19296670; DOI=10.1021/bi802205g;
Kollman J.M., Pandi L., Sawaya M.R., Riley M., Doolittle R.F.;
"Crystal structure of human fibrinogen.";
Biochemistry 48:3877-3886(2009).
[31]
VARIANT BALTIMORE-2 LYS-478.
PubMed=3194892; DOI=10.1016/0049-3848(88)90096-5;
Schmelzer C.H., Ebert R.F., Bell W.R.;
"A polymorphism at B beta 448 of fibrinogen identified during
structural studies of fibrinogen Baltimore II.";
Thromb. Res. 52:173-177(1988).
[32]
VARIANT ISE ARG-45.
PubMed=2018836;
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 77:1958-1963(1991).
[33]
INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN THR-98.
PubMed=1634610; DOI=10.1172/JCI115841;
Koopman J., Haverkate F., Lord S.T., Grimbergen J., Mannucci P.M.;
"Molecular basis of fibrinogen Naples associated with defective
thrombin binding and thrombophilia. Homozygous substitution of B beta
68 Ala-->Thr.";
J. Clin. Invest. 90:238-244(1992).
[34]
VARIANTS IJMUIDEN CYS-44 AND NIJMEGEN CYS-74.
PubMed=1565641; DOI=10.1073/pnas.89.8.3478;
Koopman J., Haverkate F., Grimbergen J., Engesser L., Novakova I.,
Kerst A.F.J.A., Lord S.T.;
"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. 89:3478-3482(1992).
[35]
VARIANT NEW YORK-1 39-GLY--LEU-102 DEL.
PubMed=3156856;
Liu C.Y., Koehn J.A., Morgan F.J.;
"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. 260:4390-4396(1985).
[36]
VARIANTS GLU-2; LEU-265 AND LYS-478.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[37]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[38]
VARIANTS CAFBN ARG-383 AND ASP-430.
PubMed=10666208;
Duga S., Asselta R., Santagostino E., Zeinali S., Simonic T.,
Malcovati M., Mannucci P.M., Tenchini M.L.;
"Missense mutations in the human beta fibrinogen gene cause congenital
afibrinogenemia by impairing fibrinogen secretion.";
Blood 95:1336-1341(2000).
[39]
VARIANT CAFBN CYS-196.
PubMed=11468164; DOI=10.1182/blood.V98.3.661;
Lounes K.C., Lefkowitz J.B., Henschen-Edman A.H., Coates A.I.,
Hantgan R.R., Lord S.T.;
"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 98:661-666(2001).
[40]
VARIANT CAFBN GLN-202.
PubMed=15070683; DOI=10.1182/blood-2003-10-3725;
Asselta R., Duga S., Spena S., Peyvandi F., Castaman G., Malcovati M.,
Mannucci P.M., Tenchini M.L.;
"Missense or splicing mutation? The case of a fibrinogen Bbeta-chain
mutation causing severe hypofibrinogenemia.";
Blood 103:3051-3054(2004).
[41]
VARIANTS CAFBN ARG-95 AND LYS-407, AND CHARACTERIZATION OF VARIANTS
CAFBN ARG-95 AND LYS-407.
PubMed=25427968; DOI=10.1160/TH14-07-0629;
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. 113:567-576(2015).
-!- 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. {ECO:0000250|UniProtKB:E9PV24}.
-!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3
non-identical chains (alpha, beta and gamma). The 2 heterotrimers
are in head to head conformation with the N-termini in a small
central domain. {ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
-!- INTERACTION:
P27958:- (xeno); NbExp=4; IntAct=EBI-1034445, EBI-6377335;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
{ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9628725}.
-!- DOMAIN: A long coiled coil structure formed by 3 polypeptide
chains connects the central nodule to the C-terminal domains
(distal nodules). The long C-terminal ends of the alpha chains
fold back, contributing a fourth strand to the coiled coil
structure. {ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
-!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin,
which cleaves fibrinopeptides A and B from alpha and beta chains,
and thus exposes the N-terminal polymerization sites responsible
for the formation of the soft clot. The soft clot is converted
into the hard clot by factor XIIIA which catalyzes the epsilon-
(gamma-glutamyl)lysine cross-linking between gamma chains
(stronger) and between alpha chains (weaker) of different
monomers. {ECO:0000269|PubMed:2143188}.
-!- DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare
autosomal recessive disorder is characterized by bleeding that
varies from mild to severe and by complete absence or extremely
low levels of plasma and platelet fibrinogen.
{ECO:0000269|PubMed:10666208, ECO:0000269|PubMed:11468164,
ECO:0000269|PubMed:15070683, ECO:0000269|PubMed:25427968}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. Patients with congenital fibrinogen
abnormalities can manifest different clinical pictures. Some cases
are clinically silent, some show a tendency toward bleeding and
some show a predisposition for thrombosis with or without
bleeding.
-!- DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A
disorder characterized by qualitative abnormalities
(dysfibrinogenemia) of the circulating fibrinogen. Affected
individuals are frequently asymptomatic, but some patients have
bleeding diathesis, thromboembolic complications, or both. In some
cases, dysfibrinogenemia is associated with low circulating
fibrinogen levels (hypodysfibrinogenemia).
{ECO:0000269|PubMed:1634610}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH07030.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=FGB";
-!- WEB RESOURCE: Name=Wikipedia; Note=Fibrinogen entry;
URL="https://en.wikipedia.org/wiki/Fibrinogen";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/fgb/";
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EMBL; J00129; AAA52429.1; -; mRNA.
EMBL; J00131; AAA98115.1; -; Genomic_DNA.
EMBL; J00130; AAA98115.1; JOINED; Genomic_DNA.
EMBL; J00132; AAA98116.1; -; Genomic_DNA.
EMBL; J00133; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M64983; AAA18024.2; -; Genomic_DNA.
EMBL; AF388026; AAK62470.1; -; Genomic_DNA.
EMBL; AK312972; BAG35810.1; -; mRNA.
EMBL; CH471056; EAX04932.1; -; Genomic_DNA.
EMBL; BC007030; AAH07030.1; ALT_SEQ; mRNA.
EMBL; BC106760; AAI06761.1; -; mRNA.
EMBL; BC107766; AAI07767.1; -; mRNA.
EMBL; AH002694; AAA52445.1; -; Genomic_DNA.
EMBL; X05018; CAA28674.1; -; Genomic_DNA.
CCDS; CCDS3786.1; -.
PIR; B43568; FGHUB.
RefSeq; NP_001171670.1; NM_001184741.1.
RefSeq; NP_005132.2; NM_005141.4.
UniGene; Hs.300774; -.
PDB; 1FZA; X-ray; 2.90 A; B/E=164-491.
PDB; 1FZB; X-ray; 2.90 A; B/E=164-491.
PDB; 1FZC; X-ray; 2.30 A; B/E=164-491.
PDB; 1FZE; X-ray; 3.00 A; B/E=164-491.
PDB; 1FZF; X-ray; 2.70 A; B/E=164-491, M/N/S/T=45-48.
PDB; 1FZG; X-ray; 2.50 A; B/E=164-491.
PDB; 1LT9; X-ray; 2.80 A; B/E=179-491.
PDB; 1LTJ; X-ray; 2.80 A; B/E=179-491.
PDB; 1N86; X-ray; 3.20 A; B/E=164-491, I/J=45-51.
PDB; 1N8E; X-ray; 4.50 A; B/E=164-491.
PDB; 1RE3; X-ray; 2.45 A; B/E=179-491.
PDB; 1RE4; X-ray; 2.70 A; B/E=179-491.
PDB; 1RF0; X-ray; 2.81 A; B/E=179-491.
PDB; 1RF1; X-ray; 2.53 A; B/E=179-491.
PDB; 2A45; X-ray; 3.65 A; H/K=45-135.
PDB; 2FFD; X-ray; 2.89 A; B/E=179-491.
PDB; 2H43; X-ray; 2.70 A; B/E=164-491.
PDB; 2HLO; X-ray; 2.60 A; B/E=164-491.
PDB; 2HOD; X-ray; 2.90 A; B/E/H/K=164-491.
PDB; 2HPC; X-ray; 2.90 A; B/E/H/K=164-491.
PDB; 2OYH; X-ray; 2.40 A; B/E=179-491.
PDB; 2OYI; X-ray; 2.70 A; B/E=179-491.
PDB; 2Q9I; X-ray; 2.80 A; B/E=164-491.
PDB; 2XNX; X-ray; 3.30 A; B/E/H/K=164-491.
PDB; 2XNY; X-ray; 7.50 A; B/E=164-491.
PDB; 2Z4E; X-ray; 2.70 A; B/E=164-489.
PDB; 3BVH; X-ray; 2.60 A; B/E=191-488.
PDB; 3E1I; X-ray; 2.30 A; B/E=164-491.
PDB; 3GHG; X-ray; 2.90 A; B/E/H/K=31-491.
PDB; 3H32; X-ray; 3.60 A; B/E=31-488.
PDB; 3HUS; X-ray; 3.04 A; B/E=179-491.
PDBsum; 1FZA; -.
PDBsum; 1FZB; -.
PDBsum; 1FZC; -.
PDBsum; 1FZE; -.
PDBsum; 1FZF; -.
PDBsum; 1FZG; -.
PDBsum; 1LT9; -.
PDBsum; 1LTJ; -.
PDBsum; 1N86; -.
PDBsum; 1N8E; -.
PDBsum; 1RE3; -.
PDBsum; 1RE4; -.
PDBsum; 1RF0; -.
PDBsum; 1RF1; -.
PDBsum; 2A45; -.
PDBsum; 2FFD; -.
PDBsum; 2H43; -.
PDBsum; 2HLO; -.
PDBsum; 2HOD; -.
PDBsum; 2HPC; -.
PDBsum; 2OYH; -.
PDBsum; 2OYI; -.
PDBsum; 2Q9I; -.
PDBsum; 2XNX; -.
PDBsum; 2XNY; -.
PDBsum; 2Z4E; -.
PDBsum; 3BVH; -.
PDBsum; 3E1I; -.
PDBsum; 3GHG; -.
PDBsum; 3H32; -.
PDBsum; 3HUS; -.
ProteinModelPortal; P02675; -.
SMR; P02675; -.
BioGrid; 108535; 129.
CORUM; P02675; -.
DIP; DIP-385N; -.
IntAct; P02675; 16.
STRING; 9606.ENSP00000306099; -.
ChEMBL; CHEMBL2048; -.
DrugBank; DB04919; Alfimeprase.
DrugBank; DB00364; Sucralfate.
iPTMnet; P02675; -.
PhosphoSitePlus; P02675; -.
SwissPalm; P02675; -.
UniCarbKB; P02675; -.
BioMuta; FGB; -.
DMDM; 399492; -.
DOSAC-COBS-2DPAGE; P02675; -.
OGP; P02675; -.
REPRODUCTION-2DPAGE; IPI00298497; -.
REPRODUCTION-2DPAGE; P02675; -.
SWISS-2DPAGE; P02675; -.
UCD-2DPAGE; P02675; -.
PaxDb; P02675; -.
PeptideAtlas; P02675; -.
PRIDE; P02675; -.
Ensembl; ENST00000302068; ENSP00000306099; ENSG00000171564.
GeneID; 2244; -.
KEGG; hsa:2244; -.
CTD; 2244; -.
DisGeNET; 2244; -.
EuPathDB; HostDB:ENSG00000171564.11; -.
GeneCards; FGB; -.
HGNC; HGNC:3662; FGB.
HPA; CAB008624; -.
HPA; HPA001900; -.
HPA; HPA001901; -.
MalaCards; FGB; -.
MIM; 134830; gene.
MIM; 202400; phenotype.
MIM; 616004; phenotype.
neXtProt; NX_P02675; -.
OpenTargets; ENSG00000171564; -.
Orphanet; 98880; Familial afibrinogenemia.
Orphanet; 98881; Familial dysfibrinogenemia.
Orphanet; 248408; Familial hypodysfibrinogenemia.
Orphanet; 101041; Familial hypofibrinogenemia.
PharmGKB; PA163; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00760000118809; -.
HOGENOM; HOG000059561; -.
HOVERGEN; HBG005707; -.
InParanoid; P02675; -.
KO; K03904; -.
OMA; TIHNGMF; -.
OrthoDB; EOG091G03M1; -.
PhylomeDB; P02675; -.
TreeFam; TF336658; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
SIGNOR; P02675; -.
ChiTaRS; FGB; human.
EvolutionaryTrace; P02675; -.
GeneWiki; Fibrinogen_beta_chain; -.
GenomeRNAi; 2244; -.
PMAP-CutDB; P02675; -.
PRO; PR:P02675; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000171564; -.
CleanEx; HS_FGB; -.
ExpressionAtlas; P02675; baseline and differential.
Genevisible; P02675; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005577; C:fibrinogen complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031091; C:platelet alpha granule; IDA:BHF-UCL.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0030674; F:protein binding, bridging; IEA:InterPro.
GO; GO:0005102; F:receptor binding; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IDA:BHF-UCL.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0043623; P:cellular protein complex assembly; IDA:BHF-UCL.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
GO; GO:0043152; P:induction of bacterial agglutination; IDA:CACAO.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0045921; P:positive regulation of exocytosis; IDA:BHF-UCL.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; NAS:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:BHF-UCL.
GO; GO:0051258; P:protein polymerization; IDA:BHF-UCL.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
CDD; cd00087; FReD; 1.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR020837; Fibrinogen_CS.
Pfam; PF08702; Fib_alpha; 1.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SMART; SM01212; Fib_alpha; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00514; FIBRINOGEN_C_1; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Blood coagulation; Coiled coil;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Hemostasis; Immunity; Innate immunity;
Polymorphism; Pyrrolidone carboxylic acid; Reference proteome;
Secreted; Signal.
SIGNAL 1 30 {ECO:0000269|PubMed:420779,
ECO:0000269|PubMed:936108,
ECO:0000269|Ref.11, ECO:0000269|Ref.13}.
PEPTIDE 31 44 Fibrinopeptide B.
{ECO:0000269|PubMed:12665801}.
/FTId=PRO_0000009070.
CHAIN 45 491 Fibrinogen beta chain.
/FTId=PRO_0000009071.
DOMAIN 232 488 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
REGION 45 47 Beta-chain polymerization, binding distal
domain of another fibrin.
COILED 157 222 {ECO:0000305|PubMed:10074346,
ECO:0000305|PubMed:19296670,
ECO:0000305|PubMed:9628725}.
SITE 44 45 Cleavage; by thrombin; to release
fibrinopeptide B.
SITE 152 153 Cleavage; by plasmin; to break down
fibrin clots.
SITE 160 161 Cleavage; by hementin; to prevent blood
coagulation.
SITE 163 164 Cleavage; by plasmin; to break down
fibrin clots.
MOD_RES 31 31 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:420779}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9628725,
ECO:0000269|Ref.11}.
DISULFID 95 95 Interchain (with C-55 in alpha chain).
{ECO:0000269|PubMed:19296670}.
DISULFID 106 106 Interchain (with C-68 in alpha chain).
{ECO:0000269|PubMed:19296670}.
DISULFID 110 110 Interchain (with C-45 in gamma chain).
{ECO:0000305|PubMed:6575689}.
DISULFID 223 223 Interchain (with C-184 in alpha chain).
{ECO:0000244|PDB:1FZC,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
DISULFID 227 227 Interchain (with C-161 in gamma chain).
DISULFID 231 316 {ECO:0000244|PDB:1FZC,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
DISULFID 241 270 {ECO:0000244|PDB:1FZC,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
DISULFID 424 437 {ECO:0000244|PDB:1FZC,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
VARIANT 2 2 K -> E (in dbSNP:rs6053).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014169.
VARIANT 39 102 Missing (in New York-1).
{ECO:0000269|PubMed:3156856}.
/FTId=VAR_002402.
VARIANT 44 44 R -> C (in Christchurch-2, Seattle-1 and
Ijmuiden; dbSNP:rs121909616).
{ECO:0000269|PubMed:1565641}.
/FTId=VAR_002403.
VARIANT 45 45 G -> R (in Ise).
{ECO:0000269|PubMed:2018836}.
/FTId=VAR_002404.
VARIANT 74 74 R -> C (in Nijmegen; dbSNP:rs121909619).
{ECO:0000269|PubMed:1565641}.
/FTId=VAR_002405.
VARIANT 95 95 C -> R (in CAFBN; hypofibrinogenemia;
heterozygous; decreased fibrinogen
complex assembly; no effect on fibrinogen
complex secretion).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072724.
VARIANT 98 98 A -> T (in DYSFIBRIN; fibrinogen Naples
and Milano-2; associated with defective
thrombin binding and thrombophilia;
dbSNP:rs121909620).
{ECO:0000269|PubMed:1634610}.
/FTId=VAR_002406.
VARIANT 100 100 P -> S (in dbSNP:rs2227434).
{ECO:0000269|Ref.4}.
/FTId=VAR_013091.
VARIANT 170 170 N -> H (in dbSNP:rs2227409).
{ECO:0000269|Ref.4}.
/FTId=VAR_013092.
VARIANT 196 196 R -> C (in CAFBN; fibrinogen Longmont;
dbSNP:rs121909623).
{ECO:0000269|PubMed:11468164}.
/FTId=VAR_016908.
VARIANT 202 202 L -> Q (in CAFBN; dbSNP:rs121909624).
{ECO:0000269|PubMed:15070683}.
/FTId=VAR_072620.
VARIANT 265 265 P -> L (in dbSNP:rs6054).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.4}.
/FTId=VAR_013093.
VARIANT 365 365 A -> T (in Pontoise-2;
dbSNP:rs121909617).
/FTId=VAR_002407.
VARIANT 383 383 L -> R (in CAFBN; abolishes fibrinogen
secretion; dbSNP:rs121909621).
{ECO:0000269|PubMed:10666208}.
/FTId=VAR_016909.
VARIANT 407 407 T -> K (in CAFBN; homozygous;
heterozygous; no effect on fibrinogen
complex assembly; impaired fibrinogen
complex secretion).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072725.
VARIANT 430 430 G -> D (in CAFBN; abolishes fibrinogen
secretion; dbSNP:rs121909622).
{ECO:0000269|PubMed:10666208}.
/FTId=VAR_016910.
VARIANT 478 478 R -> K (in Baltimore-2; dbSNP:rs4220).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:3194892,
ECO:0000269|Ref.4}.
/FTId=VAR_002408.
CONFLICT 138 139 SQ -> QS (in Ref. 11; AA sequence and 12;
AA sequence). {ECO:0000305}.
CONFLICT 145 146 FQ -> QF (in Ref. 10; AA sequence, 11; AA
sequence and 12; AA sequence).
{ECO:0000305}.
CONFLICT 192 192 P -> A (in Ref. 1; AAA52429).
{ECO:0000305}.
CONFLICT 245 245 I -> T (in Ref. 7; AAI07767).
{ECO:0000305}.
TURN 100 102 {ECO:0000244|PDB:3GHG}.
HELIX 109 145 {ECO:0000244|PDB:3GHG}.
HELIX 147 167 {ECO:0000244|PDB:3GHG}.
HELIX 172 180 {ECO:0000244|PDB:3GHG}.
TURN 182 189 {ECO:0000244|PDB:1FZC}.
HELIX 190 222 {ECO:0000244|PDB:1FZC}.
STRAND 224 226 {ECO:0000244|PDB:2HOD}.
STRAND 233 235 {ECO:0000244|PDB:1FZC}.
STRAND 238 240 {ECO:0000244|PDB:1FZC}.
HELIX 241 246 {ECO:0000244|PDB:1FZC}.
STRAND 253 257 {ECO:0000244|PDB:1FZC}.
STRAND 261 263 {ECO:0000244|PDB:2OYH}.
STRAND 266 271 {ECO:0000244|PDB:1FZC}.
HELIX 274 276 {ECO:0000244|PDB:1FZC}.
STRAND 279 288 {ECO:0000244|PDB:1FZC}.
HELIX 296 301 {ECO:0000244|PDB:1FZC}.
STRAND 302 304 {ECO:0000244|PDB:1FZF}.
STRAND 306 308 {ECO:0000244|PDB:1FZC}.
STRAND 311 315 {ECO:0000244|PDB:2H43}.
STRAND 321 323 {ECO:0000244|PDB:1FZC}.
HELIX 326 334 {ECO:0000244|PDB:1FZC}.
STRAND 335 337 {ECO:0000244|PDB:2HOD}.
STRAND 339 345 {ECO:0000244|PDB:1FZC}.
STRAND 347 349 {ECO:0000244|PDB:1FZA}.
STRAND 351 361 {ECO:0000244|PDB:1FZC}.
HELIX 364 366 {ECO:0000244|PDB:1FZC}.
STRAND 370 379 {ECO:0000244|PDB:1FZC}.
HELIX 382 385 {ECO:0000244|PDB:1FZC}.
STRAND 388 390 {ECO:0000244|PDB:2HPC}.
HELIX 392 396 {ECO:0000244|PDB:1FZC}.
STRAND 404 407 {ECO:0000244|PDB:2HOD}.
STRAND 408 410 {ECO:0000244|PDB:1FZB}.
HELIX 420 422 {ECO:0000244|PDB:2OYI}.
TURN 424 428 {ECO:0000244|PDB:1FZC}.
STRAND 435 437 {ECO:0000244|PDB:1FZC}.
STRAND 439 441 {ECO:0000244|PDB:3E1I}.
STRAND 448 451 {ECO:0000244|PDB:3BVH}.
TURN 454 456 {ECO:0000244|PDB:1FZC}.
STRAND 457 461 {ECO:0000244|PDB:3HUS}.
STRAND 464 467 {ECO:0000244|PDB:3E1I}.
HELIX 468 471 {ECO:0000244|PDB:1FZC}.
STRAND 473 475 {ECO:0000244|PDB:2OYH}.
STRAND 478 485 {ECO:0000244|PDB:1FZC}.
SEQUENCE 491 AA; 55928 MW; B92FFB9976AB53C5 CRC64;
MKRMVSWSFH KLKTMKHLLL LLLCVFLVKS QGVNDNEEGF FSARGHRPLD KKREEAPSLR
PAPPPISGGG YRARPAKAAA TQKKVERKAP DAGGCLHADP DLGVLCPTGC QLQEALLQQE
RPIRNSVDEL NNNVEAVSQT SSSSFQYMYL LKDLWQKRQK QVKDNENVVN EYSSELEKHQ
LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE
CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK
QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT
VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP
RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM
SMKIRPFFPQ Q


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