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P02679 (FIBG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 186. 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 gamma chain
Gene names
Name:FGG
ORF Names:PRO2061
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length453 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 By similarity. Ref.19 Ref.22 Ref.23 Ref.24

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

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.

Sulfation of C-terminal tyrosines increases affinity for thrombin.

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. Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.

Miscellaneous

The gamma-chain carries the main binding site for the platelet receptor.

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Sulfation
   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

Traceable author statement. Source: Reactome

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 Ref.56. 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

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Gamma-B (identifier: P02679-1)

Also known as: Gamma';

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.
Note: Present in about 10% of the fibrinogen molecules in plasma but absent from those in the platelets.
Isoform Gamma-A (identifier: P02679-2)

The sequence of this isoform differs from the canonical sequence as follows:
     434-453: VRPEHPAETEYDSLYPEDDL → AGDV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.9 Ref.10
Chain27 – 453427Fibrinogen gamma chain
PRO_0000009099

Regions

Domain170 – 416247Fibrinogen C-terminal
Calcium binding341 – 35515 Ref.27
Region400 – 42223Gamma-chain polymerization, binding amino end of another fibrin alpha chain
Region423 – 43715Platelet aggregation and Staphylococcus clumping

Sites

Site84 – 852Cleavage; by plasmin; to break down fibrin clots
Site88 – 892Cleavage; by plasmin; to break down fibrin clots
Site102 – 1032Cleavage; by hementin; to prevent blood coagulation

Amino acid modifications

Modified residue4441Sulfotyrosine Ref.21
Modified residue4481Sulfotyrosine Ref.21
Glycosylation781N-linked (GlcNAc...) (complex) Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34
Glycosylation3341N-linked (GlcNAc...); in variant Asahi
Disulfide bond34Interchain (with C-35) Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond35Interchain (with C-34) Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond45Interchain (with C-110 in beta chain) Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond49Interchain (with C-64 in alpha chain) Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond161Interchain (with C-227 in beta chain) Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond165Interchain (with C-180 in alpha chain) Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond179 ↔ 208 Ref.16 Ref.17 Ref.18 Ref.19
Disulfide bond352 ↔ 365 Ref.16 Ref.17 Ref.18 Ref.19
Cross-link424Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432)
Cross-link432Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424)

Natural variations

Alternative sequence434 – 45320VRPEH…PEDDL → AGDV in isoform Gamma-A.
VSP_001537
Natural variant771E → G.
Corresponds to variant rs11551835 [ dbSNP | Ensembl ].
VAR_049066
Natural variant1401Y → H. Ref.6
Corresponds to variant rs2066870 [ dbSNP | Ensembl ].
VAR_033930
Natural variant1911G → R in Milano-12. Ref.6 Ref.61 Ref.62
Corresponds to variant rs6063 [ dbSNP | Ensembl ].
VAR_014170
Natural variant3011R → C in Tochigi/Osaka-2/Milano-5/Villajoyosa. Ref.14 Ref.43 Ref.50 Ref.53 Ref.57
VAR_002409
Natural variant3011R → H in Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. Ref.14 Ref.54 Ref.59 Ref.60
VAR_002410
Natural variant3181G → V in Baltimore-1; impaired polymerization. Ref.44
VAR_002411
Natural variant3341N → I in Baltimore-3; impaired polymerization. Ref.45
Corresponds to variant rs121913090 [ dbSNP | Ensembl ].
VAR_002413
Natural variant3341N → K in Kyoto-1; causes accelerated cleavage by plasmin. Ref.43 Ref.47
VAR_002412
Natural variant3351G → D in Hillsborough; prolonged thrombin clotting time. Ref.64
VAR_015853
Natural variant3361M → T in Asahi; impaired polymerization. Ref.42 Ref.43
VAR_002414
Natural variant345 – 3462Missing in Vlissingen; defective calcium binding and impaired polymerization.
VAR_002415
Natural variant3551Q → R in Nagoya-1; impaired polymerization. Ref.52
VAR_002416
Natural variant3561D → V in Milano-1; impaired polymerization. Ref.49
VAR_002418
Natural variant3561D → Y in Kyoto-3; impaired polymerization. Ref.43 Ref.48
VAR_002417
Natural variant3631N → K in Bern-1; impaired polymerization. Ref.46
VAR_002419
Natural variant3771G → VMCGEALPMLKDPCYS in Paris-1; impaired polymerization.
VAR_002420
Natural variant3841S → C in Milano-7; impaired polymerization. Ref.51
VAR_002421
Natural variant4011R → G in Osaka-5. Ref.55
VAR_002422
Natural variant4101M → V. Ref.62
Corresponds to variant rs6061 [ dbSNP | Ensembl ].
VAR_014171

Experimental info

Sequence conflict1141K → I in AAB59530. Ref.2
Sequence conflict1141K → I in AAB59531. Ref.2
Sequence conflict4351R → Y AA sequence Ref.15
Sequence conflict4481Y → R AA sequence Ref.15

Secondary structure

....................................................................................... 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gamma-B (Gamma') [UniParc].

Last modified April 16, 2002. Version 3.
Checksum: 1787204904E0D4BB

FASTA45351,512
        10         20         30         40         50         60 
MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 

        70         80         90        100        110        120 
KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 

       130        140        150        160        170        180 
KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 

       190        200        210        220        230        240 
DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 

       250        260        270        280        290        300 
FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 

       310        320        330        340        350        360 
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 

       370        380        390        400        410        420 
WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 

       430        440        450 
GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE DDL 

« Hide

Isoform Gamma-A [UniParc].

Checksum: 3D73A7BC1E71381B
Show »

FASTA43749,497

References

« Hide 'large scale' references
[1]"Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen."
Chung D.W., Chan W.-Y., Davie E.W.
Biochemistry 22:3250-3256(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Nucleotide sequence of the gene for the gamma chain of human fibrinogen."
Rixon M.W., Chung D.W., Davie E.W.
Biochemistry 24:2077-2086(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
[3]"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] (ISOFORMS GAMMA-A AND GAMMA-B).
Tissue: Liver.
[4]"Functional prediction of the coding sequences of 33 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
Tissue: Fetal liver.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
[6]SeattleSNPs variation discovery resource
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-140 AND ARG-191.
[7]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].
[8]"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 GAMMA-A).
Tissue: Skeletal muscle.
[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 27-437.
[10]"Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets."
Bertagnolli M.E., Beckerle M.C.
J. Cell Biol. 121:1329-1342(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-41.
Tissue: Platelet.
[11]"Polymorphism of the human gamma chain fibrinogen gene."
Marchetti L., Zanelli T., Malcovati M., Tenchini M.L.
DNA Seq. 1:419-422(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-286.
Tissue: Liver.
[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 [GENOMIC DNA / MRNA] OF 209-270.
[13]"Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near the 3' end of the gene produces gamma A and gamma B forms of gamma-fibrinogen."
Fornace A.J. Jr., Cummings D.E., Comeau C.M., Kant J.A., Crabtree G.R.
J. Biol. Chem. 259:12826-12830(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-437 (ISOFORMS GAMMA-A AND GAMMA-B).
[14]"Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275-->His) and Villajoyosa (gamma Arg 275-->Cys)."
Borrell M., Gari M., Coll I., Vallve C., Tirado I., Soria J.M., Sala N., Munoz C., Oliver A., Garcia A.
Blood Coagul. Fibrinolysis 6:198-206(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 291-310, VARIANTS BARCELONA-3/BARCELONA-4 HIS-301 AND VILLAJOYOSA CYS-301.
Tissue: Blood.
[15]"Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma')."
Wolfenstein-Todel C., Mosesson M.W.
Biochemistry 20:6146-6149(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 411-453 (ISOFORM GAMMA-B).
[16]"Covalent structure of fibrinogen."
Henschen A., Lottspeich F., Kehl M., Southan C.
Ann. N. Y. Acad. Sci. 408:28-43(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, DISULFIDE BONDS.
[17]"The structures of fibrinogen and fibrin."
Doolittle R.F., Takagi T., Watt K.W.K., Bouma H. III, Cottrell B.A., Cassman K.G., Goldbaum D.M., Doolittle L.R., Friezner S.J.
(In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H. (eds.); Regulatory proteolytic enzymes and their inhibitors, pp.163-172, Pergamon Press, New York (1978)
Cited for: DISULFIDE BONDS.
[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]"Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation."
Hoeprich P.D., Doolittle R.F.
Biochemistry 22:2049-2055(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: QUATERNARY STRUCTURE, DISULFIDE BONDS.
[20]"Recombinant human fibrinogen and sulfation of the gamma' chain."
Farrel D.H., Mulvihill E.R., Huang S., Chung D.W., Davie E.W.
Biochemistry 30:9414-9420(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
[21]"The amino acid sequence in fibrin responsible for high affinity thrombin binding."
Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., Mosesson M.W.
Thromb. Haemost. 85:470-474(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-444 AND TYR-448.
[22]"Fibrinogen and fibrin."
Doolittle R.F.
Annu. Rev. Biochem. 53:195-229(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
[23]"Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen."
Horwitz B.H., Varadi A., Scheraga H.A.
Proc. Natl. Acad. Sci. U.S.A. 81:5980-5984(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMERIZATION SITE.
[24]"Localization of a fibrin polymerization site."
Olexa S.A., Budzynski A.Z.
J. Biol. Chem. 256:3544-3549(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMERIZATION SITE.
[25]"Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain."
Kloczewiak M., Timmons S., Lukas T.J., Hawiger J.
Biochemistry 23:1767-1774(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PLATELET AGGREGATION SITE.
[26]"Evidence that three adhesive proteins interact with a common recognition site on activated platelets."
Plow E.F., Srouji A.H., Meyer D., Marguerie G., Ginsberg M.H.
J. Biol. Chem. 259:5388-5391(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PLATELET AGGREGATION SITE.
[27]"Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence."
Dang C.V., Ebert R.F., Bell W.R.
J. Biol. Chem. 260:9713-9719(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING SITE.
[28]"Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma')."
Wolfenstein-Todel C., Mosesson M.W.
Proc. Natl. Acad. Sci. U.S.A. 77:5069-5073(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMATOGRAPHIC COMPARISON OF GAMMA-A AND GAMMA-B CHAINS.
[29]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
Tissue: Plasma.
[30]"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-78.
Tissue: Plasma.
[31]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
Tissue: Platelet.
[32]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
Tissue: Milk.
[33]"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-78.
Tissue: Liver.
[34]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-78.
[35]"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.
[36]"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].
[37]"Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen."
Yee V.C., Pratt K.P., Cote H.C.F., le Trong I., Chung D.W., Davie E.W., Stenkamp R.E., Teller D.C.
Structure 5:125-138(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
[38]"The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro."
Pratt K.P., Cote H.C.F., Chung D.W., Stenkamp R.E., Davie E.W.
Proc. Natl. Acad. Sci. U.S.A. 94:7176-7181(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
[39]"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 114-432.
[40]"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 114-432.
[41]"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 114-432.
[42]"A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi."
Yamazumi K., Shimura K., Terukina S., Takahashi N., Matsuda M.
J. Clin. Invest. 83:1590-1597(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASAHI THR-336.
[43]"Gene analyses of abnormal fibrinogens with a mutation in the gamma chain."
Mimuro J., Muramatsu S., Maekawa H., Sakata Y., Kaneko M., Yoshitake S., Okuma M., Ito Y., Takeda Y., Matsuda M.
Int. J. Hematol. 56:129-134(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3 TYR-356.
[44]"Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly-->Val (GGC-->GTC) mutation."
Bantia S., Mane S.M., Bell W.R., Dang C.V.
Blood 76:2279-2283(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BALTIMORE-1 VAL-318.
[45]"Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation."
Bantia S., Bell W.R., Dang C.V.
Blood 75:1659-1663(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BALTIMORE-3 ILE-334.
[46]"Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization."
Steinmann C., Reber P., Jungo M., Laemmle B., Heinemann G., Wermuth B., Furlan M.
Blood 82:2104-2108(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BERN-1 LYS-363.
[47]"Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site."
Yoshida N., Terukina S., Okuma M., Moroi M., Aoki N., Matsuda M.
J. Biol. Chem. 263:13848-13856(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KYOTO-1 LYS-334.
[48]"Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization."
Terukina S., Yamazumi K., Okamoto K., Yamashita H., Ito Y., Matsuda M.
Blood 74:2681-2687(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KYOTO-3 TYR-356.
[49]"Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp-->Val impairs fibrin polymerization."
Reber P., Furlan M., Rupp C., Kehl M., Henschen A., Mannucci P.M., Beck E.A.
Blood 67:1751-1756(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MILANO-1 VAL-356.
[50]"Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution."
Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M.
Blood Coagul. Fibrinolysis 5:463-471(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MILANO-5 CYS-301.
[51]"A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization."
Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M.
Blood 84:1874-1880(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MILANO-7 CYS-384.
[52]"Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer."
Miyata T., Furukawa K., Iwanaga S., Takamatsu J., Saito H.
J. Biochem. 105:10-14(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NAGOYA-1 ARG-355.
[53]"Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site."
Terukina S., Matsuda M., Hirata H., Takeda Y., Miyata T., Takao T., Shimonishi Y.
J. Biol. Chem. 263:13579-13587(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OSAKA-2 CYS-301.
[54]"Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant."
Yoshida N., Imoka S., Hirata H., Matsuda M., Asakura S.
Thromb. Haemost. 68:534-538(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OSAKA-3 HIS-301.
[55]"Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis."
Yoshida N., Hirata H., Morigami Y., Imaoka S., Matsuda M., Yamazumi K., Asakura S.
J. Biol. Chem. 267:2753-2759(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OSAKA-5 GLY-401.
[56]"Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain."
Rosenberg J.B., Newman P.J., Mosesson M.W., Guillin M.-C., Amrani D.L.
Thromb. Haemost. 69:217-220(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PARIS-1 GLY-377 DELINS VAL-MET-CYS-GLY-GLU-ALA-LEU-PRO-MET-LEU-LYS-ASP-PRO-CYS-TYR-SER.
[57]"An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine."
Yoshida N., Ota K., Moroi M., Matsuda M.
Blood 71:480-487(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TOCHIGI CYS-301.
[58]"A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization."
Koopman J., Haverkate F., Briet E., Lord S.T.
J. Biol. Chem. 266:13456-13461(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VLISSINGEN 345-ASN-ASP-346 DEL.
[59]"Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and Perugia."
Reber P., Furlan M., Henschen A., Kaudewitz H., Barbui T., Hilgard P., Nenci G.G., Berrettini M., Beck E.A.
Thromb. Haemost. 56:401-406(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BERGAMO-2/ESSEN/HAIFA/PERUGIA HIS-301.
[60]"Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga' with an Arg-275 to His substitution."
Yamazumi K., Terukina S., Onohara S., Matsuda M.
Thromb. Haemost. 60:476-480(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SAGA HIS-301.
[61]"Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, A-alpha R16C and gamma G165R."
Bolliger-Stucki B., Lord S.T., Furlan M.
Blood 98:351-357(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MILANO-12 ARG-191.
[62]"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 ARG-191 AND VAL-410.
[63]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)
[64]"Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with impaired clotting."
Mullin J.L., Brennan S.O., Ganly P.S., George P.M.
Blood 99:3597-3601(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HILLSBOROUGH ASP-335.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10014 Genomic DNA. Translation: AAB59530.1.
M10014 Genomic DNA. Translation: AAB59531.1.
AF118092 mRNA. Translation: AAF22036.1.
AF350254 Genomic DNA. Translation: AAK19751.2.
AF350254 Genomic DNA. Translation: AAK19752.2.
AK289422 mRNA. Translation: BAF82111.1.
AK290824 mRNA. Translation: BAF83513.1.
BT007081 mRNA. Translation: AAP35744.1.
CH471056 Genomic DNA. Translation: EAX04917.1.
CH471056 Genomic DNA. Translation: EAX04919.1.
BC007044 mRNA. Translation: AAH07044.1.
BC021674 mRNA. Translation: AAH21674.1.
X51473 mRNA. Translation: CAA35837.1.
X00086 mRNA. Translation: CAA24944.1.
K02569 Genomic DNA. Translation: AAA52430.1.
K02569 Genomic DNA. Translation: AAA52431.1.
PIRFGHUG. A90470.
FGHUGB. A90494.
RefSeqNP_000500.2. NM_000509.4.
NP_068656.2. NM_021870.2.
UniGeneHs.727584.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DUGX-ray1.80A/B424-433[»]
1FIBX-ray2.10A169-433[»]
1FICX-ray2.50A/B169-433[»]
1FIDX-ray2.10A169-433[»]
1FZAX-ray2.90C/F114-432[»]
1FZBX-ray2.90C/F114-432[»]
1FZCX-ray2.30C/F114-432[»]
1FZEX-ray3.00C/F114-432[»]
1FZFX-ray2.70C/F114-432[»]
1FZGX-ray2.50C/F114-432[»]
1LT9X-ray2.80C/F122-432[»]
1LTJX-ray2.80C/F122-432[»]
1N86X-ray3.20C/F114-433[»]
1N8EX-ray4.50C/F114-433[»]
1RE3X-ray2.45C/F122-432[»]
1RE4X-ray2.70C/F122-432[»]
1RF0X-ray2.81C/F122-432[»]
1RF1X-ray2.53C/F122-432[»]
2A45X-ray3.65I/L27-71[»]
2FFDX-ray2.89C/F122-432[»]
2FIBX-ray2.01A169-433[»]
2H43X-ray2.70C/F115-433[»]
2HLOX-ray2.60C/F114-433[»]
2HODX-ray2.90C/F/I/L115-433[»]
2HPCX-ray2.90C/F/I/L115-433[»]
2HWLX-ray2.40P439-452[»]
2OYHX-ray2.40C/F122-432[»]
2OYIX-ray2.70C/F122-432[»]
2Q9IX-ray2.80C/F114-433[»]
2VDOX-ray2.51C426-433[»]
2VDPX-ray2.80C428-433[»]
2VDQX-ray2.59C426-433[»]
2VDRX-ray2.40C428-433[»]
2VR3X-ray1.95C/D425-433[»]
2XNXX-ray3.30C/F/I/L114-432[»]
2XNYX-ray7.50C/F114-432[»]
2Y7LX-ray1.49B421-433[»]
2Z4EX-ray2.70C/F114-433[»]
3BVHX-ray2.60C/F128-420[»]
3E1IX-ray2.30C/F114-432[»]
3FIBX-ray2.10A170-418[»]
3GHGX-ray2.90C/F/I/L27-433[»]
3H32X-ray3.60C/F121-433[»]
3HUSX-ray3.04C/F122-432[»]
4B60X-ray1.83C/D421-433[»]
ProteinModelPortalP02679.
SMRP02679. Positions 28-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108557. 7 interactions.
DIPDIP-29644N.
IntActP02679. 2 interactions.
MINTMINT-5004002.

Chemistry

BindingDBP02679.
ChEMBLCHEMBL2364709.
DrugBankDB00364. Sucralfate.

PTM databases

PhosphoSiteP02679.

Polymorphism databases

DMDM20178280.

2D gel databases

DOSAC-COBS-2DPAGEP02679.
OGPP02679.
REPRODUCTION-2DPAGEIPI00219713.
P02679.
SWISS-2DPAGEP02679.

Proteomic databases

PaxDbP02679.
PeptideAtlasP02679.
PRIDEP02679.

Protocols and materials databases

DNASU2266.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336098; ENSP00000336829; ENSG00000171557. [P02679-1]
ENST00000404648; ENSP00000384860; ENSG00000171557. [P02679-2]
GeneID2266.
KEGGhsa:2266.
UCSCuc003iog.3. human. [P02679-2]
uc003ioj.3. human. [P02679-1]

Organism-specific databases

CTD2266.
GeneCardsGC04M155525.
HGNCHGNC:3694. FGG.
HPAHPA027529.
MIM134850. gene.
202400. phenotype.
neXtProtNX_P02679.
Orphanet98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBPA430.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269667.
HOVERGENHBG099783.
KOK03905.
OrthoDBEOG7X9G60.
PhylomeDBP02679.
TreeFamTF336658.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP02679.
BgeeP02679.
CleanExHS_FGG.
GenevestigatorP02679.

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.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamPF08702. Fib_alpha. 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

ChiTaRSFGG. human.
EvolutionaryTraceP02679.
GeneWikiFGG.
GenomeRNAi2266.
NextBio9205.
PMAP-CutDBP02679.
PROP02679.
SOURCESearch...

Entry information

Entry nameFIBG_HUMAN
AccessionPrimary (citable) accession number: P02679
Secondary accession number(s): A8K057 expand/collapse secondary AC list , P04469, P04470, Q53Y18, Q96A14, Q96KJ3, Q9UC62, Q9UC63, Q9UCF3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: April 16, 2014
This is version 186 of the entry and version 3 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