P02671 (FIBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibrinogen alpha chain

Cleaved into the following 2 chains:

1. Fibrinopeptide A
2. Fibrinogen alpha chain

Gene names

Name:

FGA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.18
Subcellular location	Secreted.
Tissue specificity	Plasma.
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.26 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.20 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. Phosphorylation sites are present in the extracellular medium.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. 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. Amyloidosis 8 (AMYL8) [MIM:105200]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.36
Sequence similarities	Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
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 Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome protein polymerization Inferred from electronic annotation. Source: InterPro response to calcium ion Inferred from direct assay PubMed 6777381. Source: BHF-UCL signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cell cortex Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from direct assay PubMed 6777381. Source: BHF-UCL fibrinogen complex Traceable author statement PubMed 10467729. Source: ProtInc platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	eukaryotic cell surface binding Inferred from direct assay PubMed 6777381. Source: BHF-UCL
Complete GO annotation...

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

Molecule processing

Signal peptide

1 – 19

19

Ref.9 Ref.10 Ref.13

Peptide

20 – 35

16

Fibrinopeptide A Ref.13

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

Site

100 – 101

2

Cleavage; by plasmin; to break down fibrin clots

Site

121 – 122

2

Cleavage; by hementin; to prevent blood coagulation

Site

123 – 124

2

Cleavage; by plasmin; to break down fibrin clots

Amino acid modifications

Modified residue

22

1

Phosphoserine Ref.21

Modified residue

412

1

Phosphothreonine Ref.22

Modified residue

609

1

Phosphoserine Ref.22

Glycosylation

320

1

O-linked (GalNAc...) Ref.26

Glycosylation

351

1

O-linked (GalNAc...) Ref.26

Glycosylation

453

1

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

Glycosylation

686

1

N-linked (GlcNAc...) Ref.16 Ref.23

Disulfide bond

47

Interchain Ref.10 Ref.17

Disulfide bond

55

Interchain (with C-95 in beta chain) Ref.10 Ref.17

Disulfide bond

64

Interchain (with C-49 in gamma chain) Ref.10 Ref.17

Disulfide bond

68

Interchain (with C-106 in beta chain) Ref.10 Ref.17

Disulfide bond

180

Interchain (with C-165 in gamma chain) Ref.10 Ref.17

Disulfide bond

184

Interchain (with C-223 in beta chain) Ref.10 Ref.17

Disulfide bond

461 ↔ 491

Ref.10 Ref.17

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. Ref.3
Corresponds to variant rs2070025 [ dbSNP | Ensembl ].

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.

VAR_002392

Natural variant

35

1

R → H. Ref.37

VAR_002393

Natural variant

37

1

P → L in Kyoto-2. Ref.32

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. Ref.38

VAR_010730

Natural variant

66

1

S → T.

VAR_002398

Natural variant

160

1

R → S in Lima. Ref.33

VAR_002399

Natural variant

331

1

T → A. Ref.3 Ref.39
Corresponds to variant rs6050 [ dbSNP | Ensembl ].

VAR_011610

Natural variant

446

1

K → E. Ref.39
Corresponds to variant rs6052 [ dbSNP | Ensembl ].

VAR_014168

Natural variant

453

1

S → N in Caracas-2. Ref.34

VAR_002400

Natural variant

456

1

T → A. Ref.3
Corresponds to variant rs2070031 [ dbSNP | Ensembl ].

VAR_011611

Natural variant

545

1

E → V in AMYL8.

VAR_010731

Natural variant

573

1

R → C in Dusart/Paris-5. Ref.35

VAR_002401

Natural variant

573

1

R → L in AMYL8. Ref.36

VAR_010732

Experimental info

Sequence conflict

184

1

C → W in AAA52426. Ref.8

Sequence conflict

215 – 216

2

SR → RS AA sequence Ref.9

Sequence conflict

299

1

S → G AA sequence Ref.9

Sequence conflict

304

1

S → G AA sequence Ref.9

Sequence conflict

317 – 318

2

GT → SG AA sequence Ref.10

Isoform 2:

Sequence conflict

640 – 644

5

PSLSP → LPCPPRLS in AAK31372. Ref.3

Secondary structure

1

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866

Helix Strand Turn

Details...

Turn

27 – 31

5

Beta strand

57 – 60

4

Beta strand

63 – 65

3

Helix

67 – 92

26

Helix

94 – 111

18

Helix

116 – 129

14

Turn

133 – 135

3

Turn

139 – 141

3

Helix

142 – 178

37

Turn

179 – 183

5

Beta strand

184 – 186

3

Helix

195 – 209

15

Beta strand

337 – 343

7

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) [UniParc]. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
[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]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-655 (ISOFORM 1). Tissue: Liver.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-629.
[9]	"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.
[10]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-629, DISULFIDE BONDS.
[11]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-156.
[12]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 605-644 (ISOFORM 2).
[13]	"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.
[14]	"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] [Europe PMC] [Abstract] Cited for: CROSS-LINKING ACCEPTOR SITES.
[15]	"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] [Europe PMC] [Abstract] Cited for: CROSS-LINKING ACCEPTOR SITES.
[16]	"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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686, MASS SPECTROMETRY. Tissue: Plasma.
[17]	"Disulfide bridges in NH2-terminal part of human fibrinogen." Blombaeck B., Hessel B., Hogg D. Thromb. Res. 8:639-658(1976) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[18]	"Fibrinogen and fibrin." Doolittle R.F. Annu. Rev. Biochem. 53:195-229(1984) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
[19]	"Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor." Kimura S., Aoki N. J. Biol. Chem. 261:15591-15595(1986) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING SITE FOR ALPHA-2-PLASMIN INHIBITOR.
[20]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[21]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY. Tissue: Pituitary.
[22]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-412 AND SER-609, MASS SPECTROMETRY. Tissue: Platelet.
[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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686, MASS SPECTROMETRY. Tissue: Liver.
[24]	"A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule." Kirschbaum N.E., Budzynski A.Z. J. Biol. Chem. 265:13669-13676(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY HEMENTIN AND PLASMIN.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"Glycoproteomic analysis of human fibrinogen reveals novel regions of O-glycosylation." Zauner G., Hoffmann M., Rapp E., Koeleman C.A., Dragan I., Deelder A.M., Wuhrer M., Hensbergen P.J. J. Proteome Res. 11:5804-5814(2012) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-320 AND SER-351.
[27]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-39.
[28]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 130-216.
[29]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-216.
[30]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 670-866.
[31]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 130-216.
[32]	"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] [Europe PMC] [Abstract] Cited for: VARIANT KYOTO-2 LEU-37.
[33]	"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] [Europe PMC] [Abstract] Cited for: VARIANT LIMA SER-160.
[34]	"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] [Europe PMC] [Abstract] Cited for: VARIANT CARACAS-2 ASN-453.
[35]	"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] [Europe PMC] [Abstract] Cited for: VARIANT DUSART/PARIS-5 CYS-573.
[36]	"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] [Europe PMC] [Abstract] Cited for: VARIANT AMYL8 LEU-573.
[37]	"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] [Europe PMC] [Abstract] Cited for: VARIANT OSAKA IV HIS-35.
[38]	"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] [Europe PMC] [Abstract] Cited for: VARIANT CANTERBURY ASP-39.
[39]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS ALA-331 AND GLU-446.
[40]	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

EMBL
GenBank
DDBJ

M64982 Genomic DNA. Translation: AAA17056.1.
M64982 Genomic DNA. 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.
CH471056 Genomic DNA. Translation: EAX04925.1.
CH471056 Genomic DNA. Translation: EAX04926.1.
CH471056 Genomic DNA. Translation: EAX04927.1.
CH471056 Genomic DNA. Translation: EAX04928.1.
BC098280 mRNA. Translation: AAH98280.1.
BC099706 mRNA. Translation: AAH99706.1.
BC099720 mRNA. Translation: AAH99720.1.
BC101935 mRNA. Translation: AAI01936.1.
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. NM_000508.3.
NP_068657.1. NM_021871.2.

UniGene

Hs.351593.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BBR	X-ray	2.30	F/G/I	26-35	[»]
1DM4	X-ray	2.50	C	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	[»]
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	[»]
2XNX	X-ray	3.30	A/D/G/J	130-216	[»]
2XNY	X-ray	7.50	A/D	130-216	[»]
2Z4E	X-ray	2.70	A/D	130-216	[»]
3AT0	X-ray	2.50	B	332-347	[»]
3BVH	X-ray	2.60	A/D	148-209	[»]
3E1I	X-ray	2.30	A/D	130-216	[»]
3GHG	X-ray	2.90	A/D/G/J	20-581	[»]
3H32	X-ray	3.60	A/D	20-216	[»]
3HUS	X-ray	3.04	A/D	145-210	[»]
4F27	X-ray	1.92	Q	336-347	[»]

ProteinModelPortal

P02671.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29643N.

IntAct

P02671. 10 interactions.

MINT

MINT-1033042.

STRING

9606.ENSP00000306361.

PTM databases

PhosphoSite

P02671.

Polymorphism databases

DMDM

1706799.

2D gel databases

OGP

P02671.

SWISS-2DPAGE

P02671.

Proteomic databases

PaxDb

P02671.

PeptideAtlas

P02671.

PRIDE

P02671.

Protocols and materials databases

DNASU

2243.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302053; ENSP00000306361; ENSG00000171560.
ENST00000403106; ENSP00000385981; ENSG00000171560.

GeneID

2243.

KEGG

hsa:2243.

UCSC

uc003iod.1. human.
uc003ioe.1. human.

Organism-specific databases

CTD

2243.

GeneCards

GC04M155504.

HGNC

HGNC:3661. FGA.

HPA

CAB016776.

MIM

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

neXtProt

NX_P02671.

Orphanet

98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.

PharmGKB

PA429.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG114889.

HOGENOM

HOG000285947.

HOVERGEN

HBG005668.

InParanoid

P02671.

KO

K03903.

OMA

YKCPSGC.

OrthoDB

EOG4XPQFB.

PhylomeDB

P02671.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02671.

Bgee

P02671.

CleanEx

HS_FGA.

Genevestigator

P02671.

GermOnline

ENSG00000171560. Homo sapiens.

Family and domain databases

Gene3D

3.90.215.10. 1 hit.
4.10.530.10. 1 hit.

InterPro

IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR021996. Fibrinogen_aC.
IPR020837. Fibrinogen_CS.
[Graphical view]

Pfam

PF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]

SMART

SM00186. FBG. 1 hit.
[Graphical view]

SUPFAM

SSF56496. Fibrinogen_a/b/g_C. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

P02671.

ChEMBL

CHEMBL1831.

ChiTaRS

FGA. human.

DrugBank

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

EvolutionaryTrace

P02671.

GenomeRNAi

2243.

NextBio

9073.

PMAP-CutDB

P02671.

SOURCE

Search...

Entry information

Entry name

FIBA_HUMAN

Accession

Primary (citable) accession number: P02671
Secondary accession number(s): D3DP14 , D3DP15, Q4QQH7, Q9BX62, Q9UCH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 177 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.