ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P02679


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FIBG_HUMAN
Primary accession number P02679
Secondary accession numbers P04469 P04470 Q96A14 Q96KJ3
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on April 16, 2002 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 124)
Name and origin of the protein
Protein name Fibrinogen gamma chain [Precursor]
Synonyms None
Gene name
Name: FGG
ORFNames: PRO2061
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
DOI=10.1021/bi00329a041; PubMed=2990550 [NCBI, ExPASy, EBI, Israel, Japan]
Rixon M.W., Chung D.W., Davie E.W.;
"Nucleotide sequence of the gene for the gamma chain of human fibrinogen.";
Biochemistry 24:2077-2086(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1021/bi00282a033; PubMed=6688357 [NCBI, ExPASy, EBI, Israel, Japan]
Chung D.W., Chan W.-Y., Davie E.W.;
"Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen.";
Biochemistry 22:3250-3256(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-140 AND ARG-191.
SeattleSNPs program for genomic applications;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F.;
"Functional prediction of the coding sequences of 33 new genes deduced by analysis of cDNA clones from human fetal liver.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
TISSUE=Skeletal muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PROTEIN SEQUENCE OF 27-437.
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 75-286.
TISSUE=Liver;
PubMed=1685103 [NCBI, ExPASy, EBI, Israel, Japan]
Marchetti L., Zanelli T., Malcovati M., Tenchini M.L.;
"Polymorphism of the human gamma chain fibrinogen gene.";
DNA Seq. 1:419-422(1991).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-437 (ISOFORMS GAMMA-A AND GAMMA-B).
PubMed=6092346 [NCBI, ExPASy, EBI, Israel, Japan]
Fornace A.J. Jr., Cummings D.E., Comeau C.M., Kant J.A., Crabtree G.R.;
"Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near the 3' end of the gene produces gamma A and gamma B forms of gamma-fibrinogen.";
J. Biol. Chem. 259:12826-12830(1984).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 209-270.
DOI=10.1093/nar/11.21.7427; PubMed=6689067 [NCBI, ExPASy, EBI, Israel, Japan]
Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S.;
"Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen.";
Nucleic Acids Res. 11:7427-7434(1983).
[10]
PROTEIN SEQUENCE OF 411-453 (ISOFORM GAMMA-B).
DOI=10.1021/bi00524a036; PubMed=7306501 [NCBI, ExPASy, EBI, Israel, Japan]
Wolfenstein-Todel C., Mosesson M.W.;
"Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma').";
Biochemistry 20:6146-6149(1981).
[11]
REVIEW, AND DISULFIDE BONDS.
PubMed=6575689 [NCBI, ExPASy, EBI, Israel, Japan]
Henschen A., Lottspeich F., Kehl M., Southan C.;
"Covalent structure of fibrinogen.";
Ann. N. Y. Acad. Sci. 408:28-43(1983).
[12]
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).
[13]
DISULFIDE BONDS.
DOI=10.1016/0049-3848(76)90245-0; PubMed=936108 [NCBI, ExPASy, EBI, Israel, Japan]
Blombaeck B., Hessel B., Hogg D.;
"Disulfide bridges in NH2-terminal part of human fibrinogen.";
Thromb. Res. 8:639-658(1976).
[14]
QUATERNARY STRUCTURE, AND DISULFIDE BONDS.
DOI=10.1021/bi00278a003; PubMed=6860649 [NCBI, ExPASy, EBI, Israel, Japan]
Hoeprich P.D., Doolittle R.F.;
"Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation.";
Biochemistry 22:2049-2055(1983).
[15]
SULFATION.
DOI=10.1021/bi00103a004; PubMed=1892842 [NCBI, ExPASy, EBI, Israel, Japan]
Farrel D.H., Mulvihill E.R., Huang S., Chung D.W., Davie E.W.;
"Recombinant human fibrinogen and sulfation of the gamma' chain.";
Biochemistry 30:9414-9420(1991).
[16]
SULFATION AT TYR-444 AND TYR-448.
PubMed=11307817 [NCBI, ExPASy, EBI, Israel, Japan]
Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., Mosesson M.W.;
"The amino acid sequence in fibrin responsible for high affinity thrombin binding.";
Thromb. Haemost. 85:470-474(2001).
[17]
REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, AND LIGANDS.
PubMed=6383194 [NCBI, ExPASy, EBI, Israel, Japan]
Doolittle R.F.;
"Fibrinogen and fibrin.";
Annu. Rev. Biochem. 53:195-229(1984).
[18]
POLYMERIZATION SITE.
PubMed=6592597 [NCBI, ExPASy, EBI, Israel, Japan]
Horwitz B.H., Varadi A., Scheraga H.A.;
"Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen.";
Proc. Natl. Acad. Sci. U.S.A. 81:5980-5984(1984).
[19]
POLYMERIZATION SITE.
PubMed=6451630 [NCBI, ExPASy, EBI, Israel, Japan]
Olexa S.A., Budzynski A.Z.;
"Localization of a fibrin polymerization site.";
J. Biol. Chem. 256:3544-3549(1981).
[20]
PLATELET AGGREGATION SITE.
DOI=10.1021/bi00303a028; PubMed=6326808 [NCBI, ExPASy, EBI, Israel, Japan]
Kloczewiak M., Timmons S., Lukas T.J., Hawiger J.;
"Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain.";
Biochemistry 23:1767-1774(1984).
[21]
PLATELET AGGREGATION SITE.
PubMed=6325435 [NCBI, ExPASy, EBI, Israel, Japan]
Plow E.F., Srouji A.H., Meyer D., Marguerie G., Ginsberg M.H.;
"Evidence that three adhesive proteins interact with a common recognition site on activated platelets.";
J. Biol. Chem. 259:5388-5391(1984).
[22]
CALCIUM-BINDING SITE.
PubMed=3160702 [NCBI, ExPASy, EBI, Israel, Japan]
Dang C.V., Ebert R.F., Bell W.R.;
"Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence.";
J. Biol. Chem. 260:9713-9719(1985).
[23]
CHROMATOGRAPHIC COMPARISON OF GAMMA-A AND GAMMA-B CHAINS.
PubMed=6933547 [NCBI, ExPASy, EBI, Israel, Japan]
Wolfenstein-Todel C., Mosesson M.W.;
"Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma').";
Proc. Natl. Acad. Sci. U.S.A. 77:5069-5073(1980).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan]
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.";
Proteomics 4:454-465(2004).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[27]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
DOI=10.1016/S0969-2126(97)00171-8; PubMed=9016719 [NCBI, ExPASy, EBI, Israel, Japan]
Yee V.C., Pratt K.P., Cote H.C.F., le Trong I., Chung D.W., Davie E.W., Stenkamp R.E., Teller D.C.;
"Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen.";
Structure 5:125-138(1997).
[28]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
DOI=10.1073/pnas.94.14.7176; PubMed=9207064 [NCBI, ExPASy, EBI, Israel, Japan]
Pratt K.P., Cote H.C.F., Chung D.W., Stenkamp R.E., Davie E.W.;
"The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro.";
Proc. Natl. Acad. Sci. U.S.A. 94:7176-7181(1997).
[29]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 114-432.
DOI=10.1038/38947; PubMed=9333233 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[30]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 114-432.
DOI=10.1021/bi9804129; PubMed=9628725 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[31]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-432.
DOI=10.1021/bi982626w; PubMed=10074346 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[32]
VARIANT ASAHI THR-336.
PubMed=2496144 [NCBI, ExPASy, EBI, Israel, Japan]
Yamazumi K., Shimura K., Terukina S., Takahashi N., Matsuda M.;
"A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi.";
J. Clin. Invest. 83:1590-1597(1989).
[33]
VARIANTS ASAHI; KYOTO-1; KYOTO-3 AND OSAKA-2.
PubMed=1421174 [NCBI, ExPASy, EBI, Israel, Japan]
Mimuro J., Muramatsu S., Maekawa H., Sakata Y., Kaneko M., Yoshitake S., Okuma M., Ito Y., Takeda Y., Matsuda M.;
"Gene analyses of abnormal fibrinogens with a mutation in the gamma chain.";
Int. J. Hematol. 56:129-134(1992).
[34]
VARIANT BALTIMORE-1 VAL-318.
PubMed=2257302 [NCBI, ExPASy, EBI, Israel, Japan]
Bantia S., Mane S.M., Bell W.R., Dang C.V.;
"Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly-->Val (GGC-->GTC) mutation.";
Blood 76:2279-2283(1990).
[35]
VARIANT BALTIMORE-3 ILE-334.
PubMed=2328317 [NCBI, ExPASy, EBI, Israel, Japan]
Bantia S., Bell W.R., Dang C.V.;
"Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation.";
Blood 75:1659-1663(1990).
[36]
VARIANT BERN-1 LYS-363.
PubMed=8400260 [NCBI, ExPASy, EBI, Israel, Japan]
Steinmann C., Reber P., Jungo M., Laemmle B., Heinemann G., Wermuth B., Furlan M.;
"Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization.";
Blood 82:2104-2108(1993).
[37]
VARIANT KYOTO-1 LYS-334.
PubMed=2971046 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida N., Terukina S., Okuma M., Moroi M., Aoki N., Matsuda M.;
"Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site.";
J. Biol. Chem. 263:13848-13856(1988).
[38]
VARIANT KYOTO-3 TYR-356.
PubMed=2819242 [NCBI, ExPASy, EBI, Israel, Japan]
Terukina S., Yamazumi K., Okamoto K., Yamashita H., Ito Y., Matsuda M.;
"Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization.";
Blood 74:2681-2687(1989).
[39]
VARIANT MILANO-1 VAL-356.
PubMed=3708159 [NCBI, ExPASy, EBI, Israel, Japan]
Reber P., Furlan M., Rupp C., Kehl M., Henschen A., Mannucci P.M., Beck E.A.;
"Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp-->Val impairs fibrin polymerization.";
Blood 67:1751-1756(1986).
[40]
VARIANT MILANO-5 CYS-301.
PubMed=7841300 [NCBI, ExPASy, EBI, Israel, Japan]
Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M.;
"Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution.";
Blood Coagul. Fibrinolysis 5:463-471(1994).
[41]
VARIANT MILANO-7 CYS-384.
PubMed=8080993 [NCBI, ExPASy, EBI, Israel, Japan]
Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M.;
"A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization.";
Blood 84:1874-1880(1994).
[42]
VARIANT NAGOYA-1 ARG-355.
PubMed=2738036 [NCBI, ExPASy, EBI, Israel, Japan]
Miyata T., Furukawa K., Iwanaga S., Takamatsu J., Saito H.;
"Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer.";
J. Biochem. 105:10-14(1989).
[43]
VARIANT OSAKA-2 CYS-301.
PubMed=2971042 [NCBI, ExPASy, EBI, Israel, Japan]
Terukina S., Matsuda M., Hirata H., Takeda Y., Miyata T., Takao T., Shimonishi Y.;
"Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site.";
J. Biol. Chem. 263:13579-13587(1988).
[44]
VARIANT OSAKA-3 HIS-301.
PubMed=1455400 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida N., Imoka S., Hirata H., Matsuda M., Asakura S.;
"Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant.";
Thromb. Haemost. 68:534-538(1992).
[45]
VARIANT OSAKA-5 GLY-401.
PubMed=1733971 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida N., Hirata H., Morigami Y., Imaoka S., Matsuda M., Yamazumi K., Asakura S.;
"Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis.";
J. Biol. Chem. 267:2753-2759(1992).
[46]
VARIANT PARIS-1.
PubMed=8470043 [NCBI, ExPASy, EBI, Israel, Japan]
Rosenberg J.B., Newman P.J., Mosesson M.W., Guillin M.-C., Amrani D.L.;
"Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain.";
Thromb. Haemost. 69:217-220(1993).
[47]
VARIANT TOCHIGI CYS-301.
PubMed=3337908 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida N., Ota K., Moroi M., Matsuda M.;
"An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine.";
Blood 71:480-487(1988).
[48]
VARIANT VLISSINGEN 345-ASN-ASP-346 DEL.
PubMed=2071611 [NCBI, ExPASy, EBI, Israel, Japan]
Koopman J., Haverkate F., Briet E., Lord S.T.;
"A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization.";
J. Biol. Chem. 266:13456-13461(1991).
[49]
VARIANT BERGAMO-2/ESSEN/HAIFA/PERUGIA HIS-301.
PubMed=3563970 [NCBI, ExPASy, EBI, Israel, Japan]
Reber P., Furlan M., Henschen A., Kaudewitz H., Barbui T., Hilgard P., Nenci G.G., Berrettini M., Beck E.A.;
"Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and Perugia.";
Thromb. Haemost. 56:401-406(1986).
[50]
VARIANT SAGA HIS-301.
PubMed=2976995 [NCBI, ExPASy, EBI, Israel, Japan]
Yamazumi K., Terukina S., Onohara S., Matsuda M.;
"Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga' with an Arg-275 to His substitution.";
Thromb. Haemost. 60:476-480(1988).
[51]
VARIANT MILANO-12 ARG-191.
DOI=10.1182/blood.V98.2.351; PubMed=11435303 [NCBI, ExPASy, EBI, Israel, Japan]
Bolliger-Stucki B., Lord S.T., Furlan M.;
"Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, A-alpha R16C and gamma G165R.";
Blood 98:351-357(2001).
[52]
VARIANTS ARG-191 AND VAL-410.
DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[53]
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).
[54]
VARIANT HILLSBOROUGH ASP-335.
DOI=10.1182/blood.V99.10.3597; PubMed=11986213 [NCBI, ExPASy, EBI, Israel, Japan]
Mullin J.L., Brennan S.O., Ganly P.S., George P.M.;
"Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with impaired clotting.";
Blood 99:3597-3601(2002).
Comments
  • FUNCTION: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
  • 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 (By similarity).
  • SUBCELLULAR LOCATION: Secreted.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameGamma-B
    SynonymsGamma'
    Isoform IDP02679-1
    Note: Present in about 10% of the fibrinogen molecules in plasma but absent from those in the platelets.
    This is the isoform sequence displayed in this entry.
    NameGamma-A
    Isoform IDP02679-2
    Features which should be applied to build the isoform sequence: VSP_001537.
  • 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.
  • 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.
  • PTM: Sulfation of C-terminal tyrosines increases affinity for thrombin.
  • DISEASE: Defects in FGG are a cause of thrombophilia.
  • DISEASE: Defects in FGG are a cause of congenital afibrinogenemia [MIM:202400]. It is a rare autosomal recessive disorder characterized by complete absence of detectable fibrinogen.
  • MISCELLANEOUS: The gamma-chain carries the main binding site for the platelet receptor.
  • SIMILARITY: Contains 1 fibrinogen C-terminal domain.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=FGG";.
  • WEB RESOURCE: Name=Wikipedia; Note=Fibrinogen entry; URL="http://en.wikipedia.org/wiki/Fibrinogen";.
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/fgg/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M10014; AAB59531.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10014; AAB59530.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF350254; AAK19751.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF350254; AAK19752.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF118092; AAF22036.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007044; AAH07044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021674; AAH21674.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51473; CAA35837.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00086; CAA24944.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02569; AAA52430.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02569; AAA52431.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A90470; FGHUG.
A90494; FGHUGB.
RefSeq NP_000500.2; -.
NP_068656.2; -.
UniGene Hs.546255
3D structure databases
PDB
1DUG; X-ray; 1.80 A; A/B=-.[ExPASy / RCSB / EBI]
1FIB; X-ray; 2.10 A; A=169-433.[ExPASy / RCSB / EBI]
1FIC; X-ray; 2.50 A; A/B=169-433.[ExPASy / RCSB / EBI]
1FID; X-ray; 2.10 A; A=169-433.[ExPASy / RCSB / EBI]
1FZA; X-ray; 2.90 A; C/F=114-432.[ExPASy / RCSB / EBI]
1FZB; X-ray; 2.90 A; C/F=114-432.[ExPASy / RCSB / EBI]
1FZC; X-ray; 2.30 A; C/F=114-432.[ExPASy / RCSB / EBI]
1FZE; X-ray; 3.00 A; C/F=114-432.[ExPASy / RCSB / EBI]
1FZF; X-ray; 2.70 A; C/F=114-432.[ExPASy / RCSB / EBI]
1FZG; X-ray; 2.50 A; C/F=114-432.[ExPASy / RCSB / EBI]
1LT9; X-ray; 2.80 A; C/F=122-432.[ExPASy / RCSB / EBI]
1LTJ; X-ray; 2.80 A; C/F=122-432.[ExPASy / RCSB / EBI]
1N86; X-ray; 3.20 A; C/F=114-433.[ExPASy / RCSB / EBI]
1N8E; X-ray; 4.50 A; C/F=114-433.[ExPASy / RCSB / EBI]
1RE3; X-ray; 2.45 A; C/F=122-432.[ExPASy / RCSB / EBI]
1RE4; X-ray; 2.70 A; C/F=122-432.[ExPASy / RCSB / EBI]
1RF0; X-ray; 2.81 A; C/F=122-432.[ExPASy / RCSB / EBI]
1RF1; X-ray; 2.53 A; C/F=122-432.[ExPASy / RCSB / EBI]
2A45; X-ray; 3.65 A; I/L=27-71.[ExPASy / RCSB / EBI]
2FFD; X-ray; 2.89 A; C/F=122-432.[ExPASy / RCSB / EBI]
2FIB; X-ray; 2.01 A; A=169-433.[ExPASy / RCSB / EBI]
2H43; X-ray; 2.70 A; F=115-433.[ExPASy / RCSB / EBI]
2HOD; X-ray; 2.90 A; C/F/I/L=115-433.[ExPASy / RCSB / EBI]
2HPC; X-ray; 2.90 A; C/F/I/L=115-433.[ExPASy / RCSB / EBI]
2HWL; X-ray; 2.40 A; P=439-452.[ExPASy / RCSB / EBI]
2OYH; X-ray; 2.40 A; C/F=122-432.[ExPASy / RCSB / EBI]
2OYI; X-ray; 2.70 A; C/F=122-432.[ExPASy / RCSB / EBI]
3FIB; X-ray; 2.10 A; A=170-418.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DUG; -.
1FIB; -.
1FIC; -.
1FID; -.
1FZA; -.
1FZB; -.
1FZC; -.
1FZE; -.
1FZF; -.
1FZG; -.
1LT9; -.
1LTJ; -.
1N86; -.
1N8E; -.
1RE3; -.
1RE4; -.
1RF0; -.
1RF1; -.
2A45; -.
2FFD; -.
2FIB; -.
2H43; -.
2HOD; -.
2HPC; -.
2HWL; -.
2OYH; -.
2OYI; -.
3FIB; -.
ModBase P02679.
Protein-protein interaction databases
IntAct P02679; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
2D gel databases
SWISS-2DPAGE P02679; -.
Cornea-2DPAGE P02679; -.
DOSAC-COBS-2DPAGE P02679; -.
OGP P02679; -.
REPRODUCTION-2DPAGE IPI00219713; -.
P02679; -.
Siena-2DPAGE P02679; -.
Organism-specific databases
H-InvDB HIX0004586; -.
HGNC HGNC:3694; FGG.
GenAtlas FGG.
MIM 134850; gene. [NCBI / EBI]
202400; phenotype. [NCBI / EBI]
Orphanet 335; Fibrinogen deficiency, congenital.
PharmGKB PA430; -.
GeneCards P02679.
Gene expression databases
ArrayExpress P02679; -.
CleanEx HS_FGG; -.
GermOnline ENSG00000171557; Homo sapiens.
Ontologies
GO
GO:0005577; Cellular component: fibrinogen complex (traceable author statement from ProtInc).
GO:0005886; Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0031093; Cellular component: platelet alpha granule lumen (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR002181; Fibrinogen_a/b/g_C.
IPR014716; Fibrinogen_a/b/g_C_1.
IPR014715; Fibrinogen_a/b/g_C_2.
IPR012290; Fibrinogen_a/b/g_coil.
Graphical view of domain structure.
Gene3D G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
G3DSA:4.10.530.10; Fibrinogen_a/b/g_C_2; 1.
G3DSA:1.20.5.50; Fibrinogen_a/b/g_coil; 1.
Pfam PF00147; Fibrinogen_C; 1.
Pfam graphical view of domain structure.
SMART SM00186; FBG; 1.
SMART graphical view of domain structure.
PROSITE PS00514; FIBRIN_AG_C_DOMAIN; 1.
BLOCKS P02679.
Proteomic databases
PeptideAtlas P02679; -.
Genome annotation databases
Ensembl ENSG00000171557; Homo sapiens. [Contig view]
GeneID 2266; -.
KEGG hsa:2266; -.
Phylogenomic databases
HOGENOM P02679; -.
HOVERGEN P02679; -.
Other
DrugBank DB00364; Sucralfate.
LinkHub P02679; -.
SOURCE FGG; Homo sapiens.
ProtoNet P02679.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Blood coagulation; Calcium; Coiled coil; Direct protein sequencing; Disease mutation; Glycoprotein; Polymorphism; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    26  26      
CHAIN   27   453  427     Fibrinogen gamma chain. PRO_0000009099
DOMAIN   175   415  241     Fibrinogen C-terminal. 
CA_BIND   341   355  15      
REGION   400   422  23     Gamma-chain polymerization, binding amino end of another fibrin alpha chain. 
REGION   423   437  15     Platelet aggregation and Staphylococcus clumping. 
MOD_RES   444   444        Sulfotyrosine. 
MOD_RES   448   448        Sulfotyrosine. 
CARBOHYD   78    78        N-linked (GlcNAc...). 
CARBOHYD   334   334        N-linked (GlcNAc...); in variant Asahi. 
DISULFID   34    34        Interchain (with C-35). 
DISULFID   35    35        Interchain (with C-34). 
DISULFID   45    45        Interchain (with C-110 in beta chain). 
DISULFID   49    49        Interchain (with C-64 in alpha chain).