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UniProtKB/Swiss-Prot entry P02671


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

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Entry information
Entry name FIBA_HUMAN
Primary accession number P02671
Secondary accession numbers Q9BX62 Q9UCH2
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 127)
Name and origin of the protein
Protein name Fibrinogen alpha chain [Precursor]
Synonyms None
Contains Fibrinopeptide A
Gene name
Name: FGA
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 (ISOFORM 1).
DOI=10.1021/bi00163a002; PubMed=1457396 [NCBI, ExPASy, EBI, Israel, Japan]
Fu Y., Weissbach L., Plant P.W., Oddoux C., Cao Y., Liang T.J., Roy S.N., Redman C.M., Grieninger G.;
"Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits.";
Biochemistry 31:11968-11972(1992).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Chung D.W., Grieninger G.;
"Fibrinogen DNA and protein sequences.";
(In) Ebert R.F. (eds.); Index of variant human fibrinogens, pp.13-24, CRC Press, Boca Raton (1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-6; ALA-331 AND ALA-456.
SeattleSNPs program for genomic applications;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE OF 1-655 (ISOFORM 1).
TISSUE=Liver;
PubMed=2102623 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=6575389 [NCBI, ExPASy, EBI, Israel, Japan]
Kant J.A., Lord S.T., Crabtree G.R.;
"Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications.";
Proc. Natl. Acad. Sci. U.S.A. 80:3953-3957(1983).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-629.
DOI=10.1021/bi00282a031; PubMed=6688355 [NCBI, ExPASy, EBI, Israel, Japan]
Rixon M.W., Chan W.-Y., Davie E.W., Chung D.W.;
"Characterization of a complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen.";
Biochemistry 22:3237-3244(1983).
[7]
PROTEIN SEQUENCE OF 20-629.
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).
[8]
PROTEIN SEQUENCE OF 20-629, AND DISULFIDE BONDS.
DOI=10.1021/bi00591a024; PubMed=518846 [NCBI, ExPASy, EBI, Israel, Japan]
Watt K.W.K., Cottrell B.A., Strong D.D., Doolittle R.F.;
"Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence.";
Biochemistry 18:5410-5416(1979).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 110-156.
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]
NUCLEOTIDE SEQUENCE OF 605-644 (ISOFORM 2).
PubMed=6575700 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PROTEIN SEQUENCE OF 20-35.
Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M.;
"Studies on fibrinopeptides from primates.";
Acta Chem. Scand. 19:1788-1789(1965).
[12]
CROSS-LINKING ACCEPTOR SITES.
DOI=10.1021/bi00591a023; PubMed=518845 [NCBI, ExPASy, EBI, Israel, Japan]
Cottrell B.A., Strong D.D., Watt K.W.K., Doolittle R.F.;
"Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites.";
Biochemistry 18:5405-5410(1979).
[13]
CROSS-LINKING ACCEPTOR SITES.
PubMed=632262 [NCBI, ExPASy, EBI, Israel, Japan]
Fretto L.J., Ferguson E.W., Steinman H.M., McKee P.A.;
"Localization of the alpha-chain cross-link acceptor sites of human fibrin.";
J. Biol. Chem. 253:2184-2195(1978).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686, 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).
[15]
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).
[16]
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).
[17]
CROSS-LINKING SITE FOR ALPHA-2-PLASMIN INHIBITOR.
PubMed=2877981 [NCBI, ExPASy, EBI, Israel, Japan]
Kimura S., Aoki N.;
"Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor.";
J. Biol. Chem. 261:15591-15595(1986).
[18]
PHOSPHORYLATION.
DOI=10.1016/0006-291X(83)91247-0; PubMed=6318767 [NCBI, ExPASy, EBI, Israel, Japan]
Itarte E., Plana M., Guasch M.D., Martos C.;
"Phosphorylation of fibrinogen by casein kinase 1.";
Biochem. Biophys. Res. Commun. 117:631-636(1983).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS SPECTROMETRY.
TISSUE=Pituitary;
DOI=10.1007/s11102-006-8916-x; PubMed=16807684 [NCBI, ExPASy, EBI, Israel, Japan]
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-277, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; THR-412; SER-524; SER-549 AND SER-609, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-39.
PubMed=1560020 [NCBI, ExPASy, EBI, Israel, Japan]
Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P.;
"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. 267:7911-7920(1992).
[23]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 130-216.
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-216.
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).
[25]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 670-866.
DOI=10.1073/pnas.95.16.9099; PubMed=9689040 [NCBI, ExPASy, EBI, Israel, Japan]
Spraggon G., Applegate D., Everse S.J., Zhang J.Z., Veerapandian L., Redman C., Doolittle R.F., Grieninger G.;
"Crystal structure of a recombinant alphaEC domain from human fibrinogen-420.";
Proc. Natl. Acad. Sci. U.S.A. 95:9099-9104(1998).
[26]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 130-216.
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).
[27]
VARIANT KYOTO-2.
PubMed=2070049 [NCBI, ExPASy, EBI, Israel, Japan]
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 78:149-153(1991).
[28]
VARIANT LIMA.
PubMed=1634621 [NCBI, ExPASy, EBI, Israel, Japan]
Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H., Takahashi N., Arocha-Pinango C.L., Rodriguez S., Nagy H., Perez-Requejo J.L., Matsuda M.;
"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. 90:67-76(1992).
[29]
VARIANT CARACAS-2.
PubMed=1675636 [NCBI, ExPASy, EBI, Israel, Japan]
Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H., Takahashi N., de Bosch N.B., Carvajal Z., Ojeda A., Arocha-Pinango C.L., Matsuda M.;
"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. 266:11575-11581(1991).
[30]
VARIANT DUSART.
PubMed=8473507 [NCBI, ExPASy, EBI, Israel, Japan]
Koopman J., Haverkate F., Grimbergen J., Lord S.T., Mosesson M.W., Diorio J.P., Siebenlist K.S., Legrand C., Soria J., Soria C., Caen J.P.;
"Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia.";
J. Clin. Invest. 91:1637-1643(1993).
[31]
VARIANT RENAL AMYLOIDOSIS LEU-573.
DOI=10.1038/ng0393-252; PubMed=8097946 [NCBI, ExPASy, EBI, Israel, Japan]
Benson M.D., Liepnieks J., Uemichi T., Wheeler G., Correa R.;
"Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain.";
Nat. Genet. 3:252-255(1993).
[32]
VARIANT OSAKA IV HIS-35.
DOI=10.1007/BF00308999; PubMed=8461606 [NCBI, ExPASy, EBI, Israel, Japan]
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 23:45-50(1993).
[33]
VARIANT CANTERBURY.
PubMed=8675656 [NCBI, ExPASy, EBI, Israel, Japan]
Brennan S.O., Hammonds B., George P.M.;
"Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A-alpha 20 Val-to-Asp).";
J. Clin. Invest. 96:2854-2858(1995).
[34]
VARIANTS ALA-331 AND GLU-446.
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).
[35]
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).
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.
  • INTERACTION:
    P48634:BAT2; NbExp=1; IntAct=EBI-348571, EBI-347545;
  • SUBCELLULAR LOCATION: Secreted.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsAlpha-E
    Isoform IDP02671-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsAlpha
    Isoform IDP02671-2
    Note: Ref.3 (AAK31372) sequence is in conflict in positions: 640:PSLSP->LPCPPRLS.
    Features which should be applied to build the isoform sequence: VSP_001531, VSP_001532.
  • 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: The alpha chain is not glycosylated.
  • PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
  • PTM: About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.
  • 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.
  • DISEASE: Defects in FGA are a cause of congenital afibrinogenemia [MIM:202400]. This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. The majority of cases of afibrinogenemia are due to truncating mutations.
  • DISEASE: Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.
  • DISEASE: Defects in FGA are a cause of hereditary renal amyloidosis [MIM:105200].
  • SIMILARITY: Contains 1 fibrinogen C-terminal domain.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=FGA";.
  • 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=FGA";.
  • 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/fga/";.
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
M64982; AAA17056.1; -; Unassigned_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M64982; AAA17055.1; -; Unassigned_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M58569; AAC97142.1; -; Other_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M58569; AAC97143.1; -; Other_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF361104; AAK31372.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF361104; AAK31373.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00128; AAA52427.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00127; AAA52426.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02272; AAA52428.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M26878; AAA52444.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93956; FGHUA.
D44234; D44234.
RefSeq NP_000499.1; -.
NP_068657.1; -.
UniGene Hs.351593
3D structure databases
PDB
1BBR; X-ray; 2.30 A; F/G/I=26-35.[ExPASy / RCSB / EBI]
1FZA; X-ray; 2.90 A; A/D=130-216.[ExPASy / RCSB / EBI]
1FZB; X-ray; 2.90 A; A/D=130-216.[ExPASy / RCSB / EBI]
1FZC; X-ray; 2.30 A; A/D=130-216.[ExPASy / RCSB / EBI]
1FZD; X-ray; 2.10 A; A/B/C/D/E/F/G/H=666-866.[ExPASy / RCSB / EBI]
1FZE; X-ray; 3.00 A; A/D=130-216.[ExPASy / RCSB / EBI]
1FZF; X-ray; 2.70 A; A/D=130-216.[ExPASy / RCSB / EBI]
1FZG; X-ray; 2.50 A; A/D=130-216.[ExPASy / RCSB / EBI]
1LT9; X-ray; 2.80 A; A/D=145-210.[ExPASy / RCSB / EBI]
1LTJ; X-ray; 2.80 A; A/D=145-210.[ExPASy / RCSB / EBI]
1N86; X-ray; 3.20 A; A/D=130-216, G/H=36-38.[ExPASy / RCSB / EBI]
1N8E; X-ray; 4.50 A; A/D=130-218.[ExPASy / RCSB / EBI]
1RE3; X-ray; 2.45 A; A/D=145-210.[ExPASy / RCSB / EBI]
1RE4; X-ray; 2.70 A; A/D=145-210.[ExPASy / RCSB / EBI]
1RF0; X-ray; 2.81 A; A/D=145-210.[ExPASy / RCSB / EBI]
1RF1; X-ray; 2.53 A; A/D=145-210.[ExPASy / RCSB / EBI]
2A45; X-ray; 3.65 A; G/J=36-92.[ExPASy / RCSB / EBI]
2FFD; X-ray; 2.89 A; A/D=145-210.[ExPASy / RCSB / EBI]
2H43; X-ray; 2.70 A; A/D=130-216.[ExPASy / RCSB / EBI]
2HLO; X-ray; 2.60 A; A/D=130-216.[ExPASy / RCSB / EBI]
2HOD; X-ray; 2.90 A; A/D/G/J=130-216.[ExPASy / RCSB / EBI]
2HPC; X-ray; 2.90 A; A/D/G/J=130-216.[ExPASy / RCSB / EBI]
2OYH; X-ray; 2.40 A; A/D=145-210.[ExPASy / RCSB / EBI]
2OYI; X-ray; 2.70 A; A/D=145-210.[ExPASy / RCSB / EBI]
2Q9I; X-ray; 2.80 A; A/D=130-216.[ExPASy / RCSB / EBI]
2Z4E; X-ray; 2.70 A; A/D=130-216.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BBR; -.
1FZA; -.
1FZB; -.
1FZC; -.
1FZD; -.
1FZE; -.
1FZF; -.
1FZG; -.
1LT9; -.
1LTJ; -.
1N86; -.
1N8E; -.
1RE3; -.
1RE4; -.
1RF0; -.
1RF1; -.
2A45; -.
2FFD; -.
2H43; -.
2HLO; -.
2HOD; -.
2HPC; -.
2OYH; -.
2OYI; -.
2Q9I; -.
2Z4E; -.
ModBase P02671.
Protein-protein interaction databases
IntAct P02671; -.
PTM databases
PhosphoSite P02671; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
2D gel databases
SWISS-2DPAGE P02671; -.
OGP P02671; -.
Siena-2DPAGE P02671; -.
Organism-specific databases
H-InvDB HIX0031437; -.
HGNC HGNC:3661; FGA.
GenAtlas FGA.
HPA CAB016776; -.
MIM 105200; phenotype. [NCBI / EBI]
134820; gene+phenotype. [NCBI / EBI]
202400; phenotype. [NCBI / EBI]
Orphanet 85450; Amyloid nephropathy, familial.
69; Amyloidosis.
335; Fibrinogen deficiency, congenital.
PharmGKB PA429; -.
GeneCards P02671.
Gene expression databases
ArrayExpress P02671; -.
CleanEx HS_FGA; -.
GermOnline ENSG00000171560; Homo sapiens.
Ontologies
GO
GO:0009897; Cellular component: external side of plasma membrane (inferred from direct assay from UniProtKB).
GO:0005577; Cellular component: fibrinogen complex (traceable author statement from ProtInc).
GO:0031093; Cellular component: platelet alpha granule lumen (inferred from experiment from Reactome).
GO:0043499; Molecular function: eukaryotic cell surface binding (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0051592; Biological process: response to calcium ion (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002181; Fibrinogen_a/b/g_C.
IPR014716; Fibrinogen_a/b/g_C_1.
IPR012290; Fibrinogen_a/b/g_coil.
IPR014814; Fibrinogen_alpha_N.
Graphical view of domain structure.
Gene3D G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
G3DSA:1.20.5.50; Fibrinogen_a/b/g_coil; 1.
Pfam PF08702; Fib_alpha; 1.
PF00147; Fibrinogen_C; 1.
Pfam graphical view of domain structure.
SMART SM00186; FBG; 1.
SMART graphical view of domain structure.
PROSITE PS00514; FIBRINOGEN_C_1; 1.
PS51406; FIBRINOGEN_C_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P02671.
ProtoNet P02671.
Proteomic databases
PeptideAtlas P02671; -.
Genome annotation databases
Ensembl ENSG00000171560; Homo sapiens. [Contig view]
GeneID 2243; -.
KEGG hsa:2243; -.
NMPDR fig|9606.3.peg.24776; -.
Phylogenomic databases
HOGENOM P02671; -.
HOVERGEN P02671; -.
Other
DrugBank DB00009; Alteplase.
DB00029; Anistreplase.
DB00015; Reteplase.
DB00364; Sucralfate.
DB00031; Tenecteplase.
LinkHub P02671; -.
NextBio 9073; -.
SOURCE FGA; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Blood coagulation; Coiled coil; Direct protein sequencing; Disease mutation; Glycoprotein; Phosphoprotein; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19      
PEPTIDE   20    35  16     Fibrinopeptide A. PRO_0000009021
CHAIN   36   866  831     Fibrinogen alpha chain. PRO_0000009022
DOMAIN   623   864  242     Fibrinogen C-terminal. 
REGION   36    38  3     Alpha-chain polymerization, binding distal domain of another fibrin gamma chain. 
COILED   68   631  564     By similarity. 
SITE   35    36  2     Cleavage; by thrombin; to release fibrinopeptide A. 
MOD_RES   22    22        Phosphoserine. 
MOD_RES   277   277        Phosphotyrosine. 
MOD_RES   364   364        Phosphoserine. 
MOD_RES   412   412        Phosphothreonine. 
MOD_RES   524   524        Phosphoserine. 
MOD_RES   549   549        Phosphoserine. 
MOD_RES   609   609        Phosphoserine. 
CARBOHYD   453   453        N-linked (GlcNAc...); in variant Caracas-2. 
CARBOHYD   686   686        N-linked (GlcNAc...). 
DISULFID   47    47        Interchain. 
DISULFID   55    55        Interchain (with C-95 in beta chain). 
DISULFID   64    64        Interchain (with C-49 in gamma chain). 
DISULFID   68    68        Interchain (with C-106 in beta chain). 
DISULFID   180   180        Interchain (with C-165 in gamma chain). 
DISULFID   184   184        Interchain (with C-223 in beta chain). 
DISULFID   461   491         
CROSSLNK   322   322        Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-41 in alpha-2-antiplasmin). 
CROSSLNK   347   347        Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?). 
CROSSLNK   385   385        Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?). 
CROSSLNK   527   527        Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) (Potential). 
CROSSLNK   558   558        Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) (Potential). 
CROSSLNK   575   575        Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) (Potential). 
CROSSLNK   581   581        Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) (Potential). 
CROSSLNK   599   599        Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) (Potential). 
VAR_SEQ   631   644        DCDDVLQTHPSGTQ -> GIHTSPLGKPSLSP (in isoform 2). VSP_001531
VAR_SEQ   645   866        Missing (in isoform 2). VSP_001532
VARIANT   6     6  1     I -> V (in dbSNP:rs2070025 [NCBI]). VAR_011609 
VARIANT   26    26  1     D -> N (in Lille-1). VAR_002390 
VARIANT &n