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P02671 (FIBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrinogen alpha chain

Cleaved into the following 2 chains:

  1. Fibrinopeptide A
  2. Fibrinogen alpha chain
Gene names
Name:FGA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length866 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.19

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.28

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.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.

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.38

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentAmyloid
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAmyloidosis
Disease mutation
   DomainCoiled coil
Signal
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Isopeptide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

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_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell cortex

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

external side of plasma membrane

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

fibrinogen complex

Traceable author statement PubMed 10467729. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

platelet alpha granule lumen

Traceable author statement. Source: Reactome

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.10 Ref.11 Ref.14
Peptide20 – 3516Fibrinopeptide A Ref.14
PRO_0000009021
Chain36 – 866831Fibrinogen alpha chain
PRO_0000009022

Regions

Domain623 – 864242Fibrinogen C-terminal
Region36 – 383Alpha-chain polymerization, binding distal domain of another fibrin gamma chain
Coiled coil68 – 631564 By similarity

Sites

Site35 – 362Cleavage; by thrombin; to release fibrinopeptide A
Site100 – 1012Cleavage; by plasmin; to break down fibrin clots
Site121 – 1222Cleavage; by hementin; to prevent blood coagulation
Site123 – 1242Cleavage; by plasmin; to break down fibrin clots

Amino acid modifications

Modified residue221Phosphoserine Ref.22
Modified residue4121Phosphothreonine Ref.23
Modified residue56514-hydroxyproline; by P4HA1 Ref.24
Modified residue6091Phosphoserine Ref.23
Glycosylation3201O-linked (GalNAc...) Ref.28
Glycosylation3511O-linked (GalNAc...) Ref.28
Glycosylation4531N-linked (GlcNAc...); in variant Caracas-2
Glycosylation6861N-linked (GlcNAc...) Ref.17 Ref.25
Disulfide bond47Interchain Ref.11 Ref.18
Disulfide bond55Interchain (with C-95 in beta chain) Ref.11 Ref.18
Disulfide bond64Interchain (with C-49 in gamma chain) Ref.11 Ref.18
Disulfide bond68Interchain (with C-106 in beta chain) Ref.11 Ref.18
Disulfide bond180Interchain (with C-165 in gamma chain) Ref.11 Ref.18
Disulfide bond184Interchain (with C-223 in beta chain) Ref.11 Ref.18
Disulfide bond461 ↔ 491 Ref.11 Ref.18
Cross-link322Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-41 in alpha-2-antiplasmin)
Cross-link347Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-link385Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Cross-link527Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential
Cross-link558Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential
Cross-link575Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential
Cross-link581Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential
Cross-link599Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Potential

Natural variations

Alternative sequence631 – 64414DCDDV…PSGTQ → GIHTSPLGKPSLSP in isoform 2.
VSP_001531
Alternative sequence645 – 866222Missing in isoform 2.
VSP_001532
Natural variant61I → V. Ref.3
Corresponds to variant rs2070025 [ dbSNP | Ensembl ].
VAR_011609
Natural variant261D → N in Lille-1.
VAR_002390
Natural variant311G → V in Rouen-1.
VAR_002391
Natural variant351R → C.
VAR_002392
Natural variant351R → H. Ref.39
VAR_002393
Natural variant371P → L in Kyoto-2. Ref.34
VAR_002394
Natural variant381R → G in Aarhus-1.
VAR_002397
Natural variant381R → N in Munich-1; requires 2 nucleotide substitutions.
VAR_002395
Natural variant381R → S in Detroit-1.
VAR_002396
Natural variant391V → D in Canterbury. Ref.40
VAR_010730
Natural variant661S → T.
VAR_002398
Natural variant1601R → S in Lima. Ref.35
VAR_002399
Natural variant3311T → A. Ref.3 Ref.4 Ref.41
Corresponds to variant rs6050 [ dbSNP | Ensembl ].
VAR_011610
Natural variant4461K → E. Ref.41
Corresponds to variant rs6052 [ dbSNP | Ensembl ].
VAR_014168
Natural variant4531S → N in Caracas-2. Ref.36
VAR_002400
Natural variant4561T → A. Ref.3
Corresponds to variant rs2070031 [ dbSNP | Ensembl ].
VAR_011611
Natural variant5451E → V in AMYL8.
VAR_010731
Natural variant5731R → C in Dusart/Paris-5. Ref.37
VAR_002401
Natural variant5731R → L in AMYL8. Ref.38
VAR_010732

Experimental info

Sequence conflict1771I → V in BAF83248. Ref.4
Sequence conflict1841C → W in AAA52426. Ref.9
Sequence conflict215 – 2162SR → RS AA sequence Ref.10
Sequence conflict2991S → G AA sequence Ref.10
Sequence conflict3041S → G AA sequence Ref.10
Sequence conflict317 – 3182GT → SG AA sequence Ref.11
Isoform 2:
Sequence conflict640 – 6445PSLSP → LPCPPRLS in AAK31372. Ref.3

Secondary structure

............................................................. 866
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha-E) [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: EA73A81204D8AEC4

FASTA86694,973
        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 

« Hide

Isoform 2 (Alpha) [UniParc].

Checksum: B9035F3DD864572A
Show »

FASTA64469,757

References

« Hide '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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-331.
Tissue: Heart.
[5]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. expand/collapse author list , 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].
[6]"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).
[7]"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.
[8]"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).
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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).
[14]"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.
[15]"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.
[16]"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.
[17]"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.
Tissue: Plasma.
[18]"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.
[19]"Fibrinogen and fibrin."
Doolittle R.F.
Annu. Rev. Biochem. 53:195-229(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
[20]"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.
[21]"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.
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[24]"Prolyl 4-hydroxylation of alpha-fibrinogen: a novel protein modification revealed by plasma proteomics."
Ono M., Matsubara J., Honda K., Sakuma T., Hashiguchi T., Nose H., Nakamori S., Okusaka T., Kosuge T., Sata N., Nagai H., Ioka T., Tanaka S., Tsuchida A., Aoki T., Shimahara M., Yasunami Y., Itoi T. expand/collapse author list , Moriyasu F., Negishi A., Kuwabara H., Shoji A., Hirohashi S., Yamada T.
J. Biol. Chem. 284:29041-29049(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT PRO-565.
[25]"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.
Tissue: Liver.
[26]"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.
[27]"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].
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]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.
AK290559 mRNA. Translation: BAF83248.1.
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.
PIRFGHUA. A93956.
D44234.
RefSeqNP_000499.1. NM_000508.3.
NP_068657.1. NM_021871.2.
UniGeneHs.351593.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBRX-ray2.30F/G/I26-35[»]
1DM4X-ray2.50C26-35[»]
1FZAX-ray2.90A/D130-216[»]
1FZBX-ray2.90A/D130-216[»]
1FZCX-ray2.30A/D130-216[»]
1FZDX-ray2.10A/B/C/D/E/F/G/H666-866[»]
1FZEX-ray3.00A/D130-216[»]
1FZFX-ray2.70A/D130-216[»]
1FZGX-ray2.50A/D130-216[»]
1LT9X-ray2.80A/D145-210[»]
1LTJX-ray2.80A/D145-210[»]
1N86X-ray3.20A/D130-216[»]
1N8EX-ray4.50A/D130-218[»]
1RE3X-ray2.45A/D145-210[»]
1RE4X-ray2.70A/D145-210[»]
1RF0X-ray2.81A/D145-210[»]
1RF1X-ray2.53A/D145-210[»]
1YCPX-ray2.50F/N20-42[»]
2A45X-ray3.65G/J36-92[»]
2FFDX-ray2.89A/D145-210[»]
2H43X-ray2.70A/D130-216[»]
2HLOX-ray2.60A/D130-216[»]
2HODX-ray2.90A/D/G/J130-216[»]
2HPCX-ray2.90A/D/G/J130-216[»]
2OYHX-ray2.40A/D145-210[»]
2OYIX-ray2.70A/D145-210[»]
2Q9IX-ray2.80A/D130-216[»]
2XNXX-ray3.30A/D/G/J130-216[»]
2XNYX-ray7.50A/D130-216[»]
2Z4EX-ray2.70A/D130-216[»]
3AT0X-ray2.50B332-347[»]
3BVHX-ray2.60A/D148-209[»]
3E1IX-ray2.30A/D130-216[»]
3GHGX-ray2.90A/D/G/J20-581[»]
3H32X-ray3.60A/D20-216[»]
3HUSX-ray3.04A/D145-210[»]
4F27X-ray1.92Q336-347[»]
ProteinModelPortalP02671.
SMRP02671. Positions 46-231, 411-866.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108534. 18 interactions.
DIPDIP-29643N.
IntActP02671. 12 interactions.
MINTMINT-1033042.
STRING9606.ENSP00000306361.

Chemistry

BindingDBP02671.
ChEMBLCHEMBL2364709.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00364. Sucralfate.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP02671.

Polymorphism databases

DMDM1706799.

2D gel databases

OGPP02671.
SWISS-2DPAGEP02671.

Proteomic databases

PaxDbP02671.
PeptideAtlasP02671.
PRIDEP02671.

Protocols and materials databases

DNASU2243.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302053; ENSP00000306361; ENSG00000171560. [P02671-1]
ENST00000403106; ENSP00000385981; ENSG00000171560. [P02671-2]
GeneID2243.
KEGGhsa:2243.
UCSCuc003iod.1. human. [P02671-1]
uc003ioe.1. human. [P02671-2]

Organism-specific databases

CTD2243.
GeneCardsGC04M155504.
HGNCHGNC:3661. FGA.
HPACAB016776.
HPA051370.
MIM105200. phenotype.
134820. gene+phenotype.
202400. phenotype.
neXtProtNX_P02671.
Orphanet98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
PharmGKBPA429.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG114889.
HOGENOMHOG000285947.
HOVERGENHBG005668.
InParanoidP02671.
KOK03903.
OMAYKCPSGC.
OrthoDBEOG7X9G60.
PhylomeDBP02671.
TreeFamTF351984.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02671.
BgeeP02671.
CleanExHS_FGA.
GenevestigatorP02671.

Family and domain databases

Gene3D3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR014716. 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]
PfamPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGA. human.
EvolutionaryTraceP02671.
GeneWikiFibrinogen_alpha_chain.
GenomeRNAi2243.
NextBio35464018.
PMAP-CutDBP02671.
PROP02671.
SOURCESearch...

Entry information

Entry nameFIBA_HUMAN
AccessionPrimary (citable) accession number: P02671
Secondary accession number(s): A8K3E4 expand/collapse secondary AC list , D3DP14, D3DP15, Q4QQH7, Q9BX62, Q9UCH2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM