Reviewed, UniProtKB/Swiss-Prot P02671 (FIBA_HUMAN)

Names and origin

Protein names

Recommended name:
    Fibrinogen alpha chain
Cleaved into the following chain:
    1- Recommended name:
            Fibrinopeptide A

Gene names

Name:

FGA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	866 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Subunit structure	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. Ref.16
Subcellular location	Secreted.
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.
Post-translational modification	The alpha chain is not glycosylated. Ref.14 Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. About one-third of the alpha chains in the molecules in blood were found to be phosphorylated. Ref.18 Ref.19 Ref.20 Ref.21 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.
Involvement in 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. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias. Defects in FGA are a cause of amyloidois type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. Ref.33
Sequence similarities	Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Amyloid Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Amyloidosis Disease mutation
Domain	Coiled coil Signal
PTM	Disulfide bond Glycoprotein Isopeptide bond Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	platelet activation Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro response to calcium ion Inferred from direct assay. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	external side of plasma membrane Inferred from direct assay. Source: UniProtKB fibrinogen complex Traceable author statement. Source: ProtInc platelet alpha granule lumen Inferred from Experiment. Source: Reactome
Molecular function	eukaryotic cell surface binding Inferred from direct assay. Source: UniProtKB protein binding, bridging Inferred from electronic annotation. Source: InterPro receptor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT2	P48634	1	EBI-348571,EBI-347545

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02671-1) Also known as: Alpha-E; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P02671-2) Also known as: Alpha; The sequence of this isoform differs from the canonical sequence as follows:      631-644: DCDDVLQTHPSGTQ → GIHTSPLGKPSLSP      645-866: Missing.
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	640 – 644	5	PSLSP → LPCPPRLS in AAK31372. Ref.3

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.7 Ref.8 Ref.11

Peptide

20 – 35

16

Fibrinopeptide A

PRO_0000009021

Chain

36 – 866

831

Fibrinogen alpha chain

PRO_0000009022

Regions

Domain

623 – 864

242

Fibrinogen C-terminal

Region

36 – 38

3

Alpha-chain polymerization, binding distal domain of another fibrin gamma chain

Coiled coil

68 – 631

564

By similarity

Sites

Site

35 – 36

2

Cleavage; by thrombin; to release fibrinopeptide A

Amino acid modifications

Modified residue

22

1

Phosphoserine Ref.19

Modified residue

277

1

Phosphotyrosine Ref.20

Modified residue

364

1

Phosphoserine Ref.21

Modified residue

412

1

Phosphothreonine Ref.21

Modified residue

524

1

Phosphoserine Ref.21

Modified residue

549

1

Phosphoserine Ref.21

Modified residue

609

1

Phosphoserine Ref.21

Glycosylation

453

1

N-linked (GlcNAc...); in variant Caracas-2

Glycosylation

686

1

N-linked (GlcNAc...) Ref.14

Disulfide bond

47

Interchain Ref.8 Ref.15

Disulfide bond

55

Interchain (with C-95 in beta chain) Ref.8 Ref.15

Disulfide bond

64

Interchain (with C-49 in gamma chain) Ref.8 Ref.15

Disulfide bond

68

Interchain (with C-106 in beta chain) Ref.8 Ref.15

Disulfide bond

180

Interchain (with C-165 in gamma chain) Ref.8 Ref.15

Disulfide bond

184

Interchain (with C-223 in beta chain) Ref.8 Ref.15

Disulfide bond

461 ↔ 491

Ref.8 Ref.15

Cross-link

322

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-41 in alpha-2-antiplasmin)

Cross-link

347

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Cross-link

385

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Cross-link

527

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential

Cross-link

558

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential

Cross-link

575

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential

Cross-link

581

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential

Cross-link

599

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential

Natural variations

Alternative sequence

631 – 644

14

DCDDV…PSGTQ → GIHTSPLGKPSLSP in isoform 2.

VSP_001531

Alternative sequence

645 – 866

222

Missing in isoform 2.

VSP_001532

Natural variant

6

1

I → V: dbSNP rs2070025. Ref.3

VAR_011609

Natural variant

26

1

D → N in Lille-1.

VAR_002390

Natural variant

31

1

G → V in Rouen-1.

VAR_002391

Natural variant

35

1

R → C Ref.34

VAR_002392

Natural variant

35

1

R → H Ref.34

VAR_002393

Natural variant

37

1

P → L in Kyoto-2.

VAR_002394

Natural variant

38

1

R → G in Aarhus-1.

VAR_002397

Natural variant

38

1

R → N in Munich-1; requires 2 nucleotide substitutions.

VAR_002395

Natural variant

38

1

R → S in Detroit-1.

VAR_002396

Natural variant

39

1

V → D in Canterbury.

VAR_010730

Natural variant

66

1

S → T

VAR_002398

Natural variant

160

1

R → S in Lima.

VAR_002399

Natural variant

331

1

T → A: dbSNP rs6050. Ref.3 Ref.36

VAR_011610

Natural variant

446

1

K → E: dbSNP rs6052. Ref.36

VAR_014168

Natural variant

453

1

S → N in Caracas-2.

VAR_002400

Natural variant

456

1

T → A: dbSNP rs2070031. Ref.3

VAR_011611

Natural variant

545

1

E → V in AMYL8.

VAR_010731

Natural variant

573

1

R → C in Dusart/Paris-5.

VAR_002401

Natural variant

573

1

R → L in AMYL8. Ref.33

VAR_010732

Experimental info

Sequence conflict

184

1

C → W in AAA52426. Ref.6

Sequence conflict

215 – 216

2

SR → RS AA sequence Ref.7

Sequence conflict

299

1

S → G AA sequence Ref.7

Sequence conflict

304

1

S → G AA sequence Ref.7

Sequence conflict

317 – 318

2

GT → SG AA sequence Ref.8

Secondary structure

1

.

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866

Helix Strand Turn

Details...

Turn

133 – 135

3

Turn

139 – 141

3

Helix

142 – 178

37

Turn

179 – 183

5

Helix

195 – 209

15

Beta strand

673 – 681

9

Helix

689 – 694

6

Helix

711 – 718

8

Beta strand

723 – 729

7

Beta strand

735 – 744

10

Turn

747 – 751

5

Beta strand

753 – 762

10

Turn

765 – 768

4

Turn

771 – 773

3

Helix

775 – 778

4

Beta strand

793 – 797

5

Helix

799 – 803

5

Beta strand

810 – 812

3

Beta strand

814 – 816

3

Beta strand

823 – 826

4

Helix

829 – 831

3

Beta strand

840 – 843

4

Helix

844 – 847

4

Beta strand

854 – 861

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha-E) [UniParc]. Last modified October 1, 1996. Version 2. Checksum: EA73A81204D8AEC4	FASTA	866	94,973
	10 20 30 40 50 60 MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS DWPFCSDEDW 70 80 90 100 110 120 NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK DSHSLTTNIM EILRGDFSSA 130 140 150 160 170 180 NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC 190 200 210 220 230 240 RGSCSRALAR EVDLKDYEDQ QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ 250 260 270 280 290 300 LQKVPPEWKA LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS 310 320 330 340 350 360 GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG SPRPGSTGTW 370 380 390 400 410 420 NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS GNARPNNPDW GTFEEVSGNV 430 440 450 460 470 480 SPGTRREYHT EKLVTSKGDK ELRTGKEKVT SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK 490 500 510 520 530 540 EVVTSEDGSD CPEAMDLGTL SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF 550 560 570 580 590 600 VSETESRGSE SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS 610 620 630 640 650 660 YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI KLPGSSKIFS 670 680 690 700 710 720 VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN DEGEGEFWLG NDYLHLLTQR 730 740 750 760 770 780 GSVLRVELED WAGNEAYAEY HFRVGSEAEG YALQVSSYEG TAGDALIEGS VEEGAEYTSH 790 800 810 820 830 840 NNMQFSTFDR DADQWEENCA EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG 850 860 VVWVSFRGAD YSLRAVRMKI RPLVTQ
	Isoform 2 (Alpha). Checksum: B9035F3DD864572A	FASTA	644	69,757
	10 20 30 40 50 60 MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS DWPFCSDEDW 70 80 90 100 110 120 NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK DSHSLTTNIM EILRGDFSSA 130 140 150 160 170 180 NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC 190 200 210 220 230 240 RGSCSRALAR EVDLKDYEDQ QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ 250 260 270 280 290 300 LQKVPPEWKA LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS 310 320 330 340 350 360 GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG SPRPGSTGTW 370 380 390 400 410 420 NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS GNARPNNPDW GTFEEVSGNV 430 440 450 460 470 480 SPGTRREYHT EKLVTSKGDK ELRTGKEKVT SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK 490 500 510 520 530 540 EVVTSEDGSD CPEAMDLGTL SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF 550 560 570 580 590 600 VSETESRGSE SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS 610 620 630 640 YKMADEAGSE ADHEGTHSTK RGHAKSRPVR GIHTSPLGKP SLSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits." Fu Y., Weissbach L., Plant P.W., Oddoux C., Cao Y., Liang T.J., Roy S.N., Redman C.M., Grieninger G. Biochemistry 31:11968-11972(1992) [PubMed: 1457396] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[2]	"Fibrinogen DNA and protein sequences." Chung D.W., Grieninger G. (In) Ebert R.F. (eds.); Index of variant human fibrinogens, pp.13-24, CRC Press, Boca Raton (1994) Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[3]	SeattleSNPs variation discovery resource Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-6; ALA-331 AND ALA-456.
[4]	"Nucleotide sequences of the three genes coding for human fibrinogen." Chung D.W., Harris J.E., Davie E.W. Adv. Exp. Med. Biol. 281:39-48(1990) [PubMed: 2102623] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-655 (ISOFORM 1). Tissue: Liver.
[5]	"Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications." Kant J.A., Lord S.T., Crabtree G.R. Proc. Natl. Acad. Sci. U.S.A. 80:3953-3957(1983) [PubMed: 6575389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[6]	"Characterization of a complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen." Rixon M.W., Chan W.-Y., Davie E.W., Chung D.W. Biochemistry 22:3237-3244(1983) [PubMed: 6688355] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-629.
[7]	"Human fibrinogen: sequence, sulfur bridges, glycosylation and some structural variants." Henschen A., Lottspeich F., Southan C., Topfer-Petersen E. (In) Peeters H. (eds.); Protides of the biological fluids, Proc. 28th colloquium, pp.51-56, Pergamon Press, Oxford (1980) Cited for: PROTEIN SEQUENCE OF 20-629.
[8]	"Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence." Watt K.W.K., Cottrell B.A., Strong D.D., Doolittle R.F. Biochemistry 18:5410-5416(1979) [PubMed: 518846] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-629, DISULFIDE BONDS.
[9]	"Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen." Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S. Nucleic Acids Res. 11:7427-7434(1983) [PubMed: 6689067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-156.
[10]	"Cloning of fibrinogen genes and their cDNA." Chung D.W., Rixon M.W., Que B.G., Davie E.W. Ann. N. Y. Acad. Sci. 408:449-456(1983) [PubMed: 6575700] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 605-644 (ISOFORM 2).
[11]	"Studies on fibrinopeptides from primates." Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M. Acta Chem. Scand. 19:1788-1789(1965) Cited for: PROTEIN SEQUENCE OF 20-35.
[12]	"Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites." Cottrell B.A., Strong D.D., Watt K.W.K., Doolittle R.F. Biochemistry 18:5405-5410(1979) [PubMed: 518845] [Abstract] Cited for: CROSS-LINKING ACCEPTOR SITES.
[13]	"Localization of the alpha-chain cross-link acceptor sites of human fibrin." Fretto L.J., Ferguson E.W., Steinman H.M., McKee P.A. J. Biol. Chem. 253:2184-2195(1978) [PubMed: 632262] [Abstract] Cited for: CROSS-LINKING ACCEPTOR SITES.
[14]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686, MASS SPECTROMETRY. Tissue: Plasma.
[15]	"Disulfide bridges in NH2-terminal part of human fibrinogen." Blombaeck B., Hessel B., Hogg D. Thromb. Res. 8:639-658(1976) [PubMed: 936108] [Abstract] Cited for: DISULFIDE BONDS.
[16]	"Fibrinogen and fibrin." Doolittle R.F. Annu. Rev. Biochem. 53:195-229(1984) [PubMed: 6383194] [Abstract] Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
[17]	"Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor." Kimura S., Aoki N. J. Biol. Chem. 261:15591-15595(1986) [PubMed: 2877981] [Abstract] Cited for: CROSS-LINKING SITE FOR ALPHA-2-PLASMIN INHIBITOR.
[18]	"Phosphorylation of fibrinogen by casein kinase 1." Itarte E., Plana M., Guasch M.D., Martos C. Biochem. Biophys. Res. Commun. 117:631-636(1983) [PubMed: 6318767] [Abstract] Cited for: PHOSPHORYLATION.
[19]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY. Tissue: Pituitary.
[20]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-277, MASS SPECTROMETRY.
[21]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; THR-412; SER-524; SER-549 AND SER-609, MASS SPECTROMETRY. Tissue: Platelet.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686, MASS SPECTROMETRY. Tissue: Liver.
[24]	"The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution." Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P. J. Biol. Chem. 267:7911-7920(1992) [PubMed: 1560020] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-39.
[25]	"Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin." Spraggon G., Everse S.J., Doolittle R.F. Nature 389:455-462(1997) [PubMed: 9333233] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 130-216.
[26]	"Crystal structure of fragment double-D from human fibrin with two different bound ligands." Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F. Biochemistry 37:8637-8642(1998) [PubMed: 9628725] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-216.
[27]	"Crystal structure of a recombinant alphaEC domain from human fibrinogen-420." Spraggon G., Applegate D., Everse S.J., Zhang J.Z., Veerapandian L., Redman C., Doolittle R.F., Grieninger G. Proc. Natl. Acad. Sci. U.S.A. 95:9099-9104(1998) [PubMed: 9689040] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 670-866.
[28]	"Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide." Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F. Biochemistry 38:2941-2946(1999) [PubMed: 10074346] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 130-216.
[29]	"Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine." Yoshida N., Okuma M., Hirata H., Matsuda M., Yamazumi K., Asakura S. Blood 78:149-153(1991) [PubMed: 2070049] [Abstract] Cited for: VARIANT KYOTO-2.
[30]	"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." 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. J. Clin. Invest. 90:67-76(1992) [PubMed: 1634621] [Abstract] Cited for: VARIANT LIMA.
[31]	"An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation." 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. J. Biol. Chem. 266:11575-11581(1991) [PubMed: 1675636] [Abstract] Cited for: VARIANT CARACAS-2.
[32]	"Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia." 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. J. Clin. Invest. 91:1637-1643(1993) [PubMed: 8473507] [Abstract] Cited for: VARIANT DUSART.
[33]	"Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain." Benson M.D., Liepnieks J., Uemichi T., Wheeler G., Correa R. Nat. Genet. 3:252-255(1993) [PubMed: 8097946] [Abstract] Cited for: VARIANT AMYL8 LEU-573.
[34]	"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." Yamazumi K., Terukina S., Matsuda M., Kanbayashi J., Sakon M., Tsujinaka T. Surg. Today 23:45-50(1993) [PubMed: 8461606] [Abstract] Cited for: VARIANT OSAKA IV HIS-35.
[35]	"Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A-alpha 20 Val-to-Asp)." Brennan S.O., Hammonds B., George P.M. J. Clin. Invest. 96:2854-2858(1995) [PubMed: 8675656] [Abstract] Cited for: VARIANT CANTERBURY.
[36]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." 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. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANTS ALA-331 AND GLU-446.
[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)
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Fibrinogen entry

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M64982 Unassigned RNA. Translation: AAA17056.1.
M64982 Unassigned RNA. Translation: AAA17055.1.
M58569 Transcribed RNA. Translation: AAC97142.1.
M58569 Transcribed RNA. Translation: AAC97143.1.
AF361104 Genomic DNA. Translation: AAK31372.1.
AF361104 Genomic DNA. Translation: AAK31373.1.
J00128 mRNA. Translation: AAA52427.1.
J00127 mRNA. Translation: AAA52426.1.
K02272 mRNA. Translation: AAA52428.1.
M26878 mRNA. Translation: AAA52444.1.

IPI

IPI00021885.
IPI00029717.

PIR

FGHUA. A93956.
D44234.

RefSeq

NP_000499.1.
NP_068657.1.

UniGene

Hs.351593

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BBR	X-ray	2.30	F/G/I	26-35	[»]
1FZA	X-ray	2.90	A/D	130-216	[»]
1FZB	X-ray	2.90	A/D	130-216	[»]
1FZC	X-ray	2.30	A/D	130-216	[»]
1FZD	X-ray	2.10	A/B/C/D/E/F/G/H	666-866	[»]
1FZE	X-ray	3.00	A/D	130-216	[»]
1FZF	X-ray	2.70	A/D	130-216	[»]
1FZG	X-ray	2.50	A/D	130-216	[»]
1LT9	X-ray	2.80	A/D	145-210	[»]
1LTJ	X-ray	2.80	A/D	145-210	[»]
1N86	X-ray	3.20	A/D	130-216	[»]
			G/H	36-38	[»]
1N8E	X-ray	4.50	A/D	130-218	[»]
1RE3	X-ray	2.45	A/D	145-210	[»]
1RE4	X-ray	2.70	A/D	145-210	[»]
1RF0	X-ray	2.81	A/D	145-210	[»]
1RF1	X-ray	2.53	A/D	145-210	[»]
1YCP	X-ray	2.50	F/N	20-42	[»]
2A45	X-ray	3.65	G/J	36-92	[»]
2FFD	X-ray	2.89	A/D	145-210	[»]
2H43	X-ray	2.70	A/D	130-216	[»]
2HLO	X-ray	2.60	A/D	130-216	[»]
2HOD	X-ray	2.90	A/D/G/J	130-216	[»]
2HPC	X-ray	2.90	A/D/G/J	130-216	[»]
2OYH	X-ray	2.40	A/D	145-210	[»]
2OYI	X-ray	2.70	A/D	145-210	[»]
2Q9I	X-ray	2.80	A/D	130-216	[»]
2Z4E	X-ray	2.70	A/D	130-216	[»]
3BVH	X-ray	2.60	A/D	148-209	[»]
3E1I	X-ray	2.30	A/D	130-216	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02671. 8 interactions.

PTM databases

PhosphoSite

P02671.

2-D gel databases

SWISS-2DPAGE

P02671.

OGP

P02671.

Siena-2DPAGE

P02671.

Proteomic databases

PeptideAtlas

P02671.

PRIDE

P02671.

Genome annotation databases

Ensembl

ENSG00000171560. Homo sapiens. [Contig view]

GeneID

2243.

KEGG

hsa:2243.

NMPDR

fig|9606.3.peg.24776.

Organism-specific databases

GeneCards

GC04M155723.

H-InvDB

HIX0031437.

HGNC

HGNC:3661. FGA.

HPA

CAB016776.

MIM

105200. phenotype.
134820. gene+phenotype.
202400. phenotype.

Orphanet

85450. Amyloid nephropathy, familial.
69. Amyloidosis.
335. Congenital fibrinogen deficiency.

PharmGKB

PA429.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P02671.

HOVERGEN

P02671.

OMA

P02671. SSYEGTA.

Enzyme and pathway databases

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02671.

Bgee

P02671.

CleanEx

HS_FGA.

GermOnline

ENSG00000171560. Homo sapiens.

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]

Gene3D

G3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit.
G3DSA:1.20.5.50. Fibrinogen_a/b/g_coil. 1 hit.

Pfam

PF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]

SMART

SM00186. FBG. 1 hit.
[Graphical view]

PROSITE

PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00364. Sucralfate.
DB00031. Tenecteplase.

NextBio

9073.

PMAP-CutDB

P02671.

SOURCE

Search...

Entry information

Entry name

FIBA_HUMAN

Accession

Primary (citable) accession number: P02671
Secondary accession number(s): Q9BX62, Q9UCH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)