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Protein

Fibrinogen gamma chain

Gene

FGG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi344CalciumCombined sources6 Publications1
Metal bindingi346CalciumCombined sources6 Publications1
Metal bindingi348Calcium; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi350Calcium; via carbonyl oxygenCombined sources6 Publications1

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • receptor binding Source: BHF-UCL
  • structural molecule activity Source: BHF-UCL

GO - Biological processi

  • blood coagulation Source: Reactome
  • blood coagulation, fibrin clot formation Source: UniProtKB
  • cell-matrix adhesion Source: BHF-UCL
  • cellular protein complex assembly Source: BHF-UCL
  • extracellular matrix organization Source: Reactome
  • fibrinolysis Source: UniProtKB
  • negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • plasminogen activation Source: UniProtKB
  • platelet aggregation Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of exocytosis Source: BHF-UCL
  • positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  • positive regulation of peptide hormone secretion Source: BHF-UCL
  • positive regulation of protein secretion Source: BHF-UCL
  • positive regulation of substrate adhesion-dependent cell spreading Source: BHF-UCL
  • positive regulation of vasoconstriction Source: BHF-UCL
  • protein polymerization Source: BHF-UCL
  • protein secretion Source: UniProtKB
  • response to calcium ion Source: BHF-UCL
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171557-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen gamma chain
Gene namesi
Name:FGG
ORF Names:PRO2061
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3694. FGG.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell cortex Source: Ensembl
  • cell surface Source: BHF-UCL
  • external side of plasma membrane Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • fibrinogen complex Source: UniProtKB
  • plasma membrane Source: Reactome
  • platelet alpha granule Source: BHF-UCL
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital afibrinogenemia (CAFBN)1 Publication
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.
Disease descriptionRare 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.
See also OMIM:202400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072726303T → P in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072727327D → H in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072728345N → D in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; decreased fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072729401R → W in CAFBN; hypofibrinogenemia; heterozygous. 1 PublicationCorresponds to variant rs75848804dbSNPEnsembl.1
Dysfibrinogenemia, congenital (DYSFIBRIN)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia).
See also OMIM:616004
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_002410301R → H in DYSFIBRIN; fibrinogen Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. 4 PublicationsCorresponds to variant rs121913088dbSNPEnsembl.1
Natural variantiVAR_002411318G → V in DYSFIBRIN; fibrinogen Baltimore-1; impaired polymerization. 1 PublicationCorresponds to variant rs121913089dbSNPEnsembl.1
Natural variantiVAR_002418356D → V in DYSFIBRIN; fibrinogen Milano-1; impaired polymerization. 1 PublicationCorresponds to variant rs121913094dbSNPEnsembl.1
Natural variantiVAR_072621404S → P in DYSFIBRIN; fibrinogen Philadelphia. 1 PublicationCorresponds to variant rs587777720dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2266.
MalaCardsiFGG.
MIMi202400. phenotype.
616004. phenotype.
OpenTargetsiENSG00000171557.
Orphaneti98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBiPA430.

Chemistry databases

ChEMBLiCHEMBL2364709.
DrugBankiDB00364. Sucralfate.

Polymorphism and mutation databases

BioMutaiFGG.
DMDMi20178280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 262 PublicationsAdd BLAST26
ChainiPRO_000000909927 – 453Fibrinogen gamma chainAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34Interchain (with C-35)Combined sources1 Publication
Disulfide bondi35Interchain (with C-34)Combined sources1 Publication
Disulfide bondi45Interchain (with C-110 in beta chain)1 Publication
Disulfide bondi49Interchain (with C-64 in alpha chain)1 Publication
Modified residuei68Phosphoserine; by FAM20C1 Publication1
Glycosylationi78N-linked (GlcNAc...) (complex)6 Publications1
Disulfide bondi161Interchain (with C-227 in beta chain)1 Publication
Disulfide bondi165Interchain (with C-180 in alpha chain)1 Publication
Disulfide bondi179 ↔ 208Combined sources6 Publications
Glycosylationi334N-linked (GlcNAc...); in variant Asahi1
Disulfide bondi352 ↔ 365Combined sources6 Publications
Cross-linki424Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432)
Cross-linki432Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424)
Modified residuei444Sulfotyrosine1 Publication1
Modified residuei448Sulfotyrosine1 Publication1

Post-translational modificationi

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.1 Publication
Sulfation of C-terminal tyrosines increases affinity for thrombin.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84 – 85Cleavage; by plasmin; to break down fibrin clots2
Sitei88 – 89Cleavage; by plasmin; to break down fibrin clots2
Sitei102 – 103Cleavage; by hementin; to prevent blood coagulation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP02679.
PaxDbiP02679.
PeptideAtlasiP02679.
PRIDEiP02679.

2D gel databases

DOSAC-COBS-2DPAGEP02679.
OGPiP02679.
REPRODUCTION-2DPAGEIPI00219713.
P02679.
SWISS-2DPAGEP02679.

PTM databases

iPTMnetiP02679.
PhosphoSitePlusiP02679.
UniCarbKBiP02679.

Miscellaneous databases

PMAP-CutDBP02679.

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level).3 Publications

Gene expression databases

BgeeiENSG00000171557.
CleanExiHS_FGG.
ExpressionAtlasiP02679. baseline and differential.
GenevisibleiP02679. HS.

Organism-specific databases

HPAiCAB033120.
HPA027529.

Interactioni

Subunit structurei

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.7 Publications

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108557. 24 interactors.
DIPiDIP-29644N.
IntActiP02679. 5 interactors.
MINTiMINT-5004002.
STRINGi9606.ENSP00000336829.

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 33Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi44 – 46Combined sources3
Helixi49 – 94Combined sources46
Turni96 – 98Combined sources3
Turni115 – 118Combined sources4
Turni119 – 122Combined sources4
Turni124 – 128Combined sources5
Helixi129 – 160Combined sources32
Beta strandi161 – 163Combined sources3
Beta strandi166 – 168Combined sources3
Beta strandi171 – 178Combined sources8
Helixi179 – 184Combined sources6
Beta strandi191 – 195Combined sources5
Turni198 – 200Combined sources3
Beta strandi204 – 210Combined sources7
Beta strandi212 – 214Combined sources3
Beta strandi216 – 226Combined sources11
Helixi234 – 239Combined sources6
Beta strandi241 – 244Combined sources4
Beta strandi246 – 248Combined sources3
Beta strandi252 – 254Combined sources3
Helixi256 – 263Combined sources8
Helixi265 – 267Combined sources3
Beta strandi270 – 277Combined sources8
Beta strandi279 – 281Combined sources3
Beta strandi283 – 290Combined sources8
Helixi296 – 298Combined sources3
Beta strandi301 – 303Combined sources3
Beta strandi305 – 309Combined sources5
Helixi315 – 317Combined sources3
Beta strandi322 – 324Combined sources3
Helixi327 – 331Combined sources5
Beta strandi341 – 343Combined sources3
Beta strandi346 – 350Combined sources5
Helixi352 – 356Combined sources5
Beta strandi358 – 360Combined sources3
Beta strandi363 – 365Combined sources3
Beta strandi367 – 369Combined sources3
Beta strandi370 – 373Combined sources4
Beta strandi376 – 379Combined sources4
Helixi382 – 384Combined sources3
Beta strandi385 – 387Combined sources3
Beta strandi392 – 395Combined sources4
Turni396 – 398Combined sources3
Beta strandi406 – 414Combined sources9
Helixi415 – 417Combined sources3
Beta strandi420 – 424Combined sources5
Beta strandi426 – 433Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.59C426-435[»]
2VDRX-ray2.40C428-452[»]
2VR3X-ray1.95C/D425-436[»]
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[»]
ProteinModelPortaliP02679.
SMRiP02679.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02679.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini170 – 416Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST247

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni400 – 422Gamma-chain polymerization, binding amino end of another fibrin alpha chainAdd BLAST23
Regioni423 – 437Platelet aggregation and Staphylococcus clumpingAdd BLAST15

Domaini

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.2 Publications

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00760000118809.
HOVERGENiHBG099783.
InParanoidiP02679.
KOiK03905.
PhylomeDBiP02679.
TreeFamiTF336658.

Family and domain databases

CDDicd00087. FReD. 1 hit.
Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. 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]
PfamiPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
SM01212. Fib_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Gamma-B (identifier: P02679-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG
60 70 80 90 100
IADFLSTYQT KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS
110 120 130 140 150
KPNMIDAATL KSRKMLEEIM KYEASILTHD SSIRYLQEIY NSNNQKIVNL
160 170 180 190 200
KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ DIANKGAKQS GLYFIKPLKA
210 220 230 240 250
NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG FGHLSPTGTT
260 270 280 290 300
EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY
310 320 330 340 350
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG
360 370 380 390 400
NCAEQDGSGW WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT
410 420 430 440 450
RWYSMKKTTM KIIPFNRLTI GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE

DDL
Note: Present in about 10% of the fibrinogen molecules in plasma but absent from those in the platelets.
Length:453
Mass (Da):51,512
Last modified:April 16, 2002 - v3
Checksum:i1787204904E0D4BB
GO
Isoform Gamma-A (identifier: P02679-2) [UniParc]FASTAAdd to basket

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

Show »
Length:437
Mass (Da):49,497
Checksum:i3D73A7BC1E71381B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti114K → I in AAB59530 (PubMed:2990550).Curated1
Sequence conflicti114K → I in AAB59531 (PubMed:2990550).Curated1
Sequence conflicti435R → Y AA sequence (PubMed:7306501).Curated1
Sequence conflicti448Y → R AA sequence (PubMed:7306501).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04906677E → G.Corresponds to variant rs11551835dbSNPEnsembl.1
Natural variantiVAR_033930140Y → H.1 PublicationCorresponds to variant rs2066870dbSNPEnsembl.1
Natural variantiVAR_014170191G → R in Milano-12. 3 PublicationsCorresponds to variant rs6063dbSNPEnsembl.1
Natural variantiVAR_002409301R → C in Tochigi/Osaka-2/Milano-5/Villajoyosa. 5 PublicationsCorresponds to variant rs121913087dbSNPEnsembl.1
Natural variantiVAR_002410301R → H in DYSFIBRIN; fibrinogen Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. 4 PublicationsCorresponds to variant rs121913088dbSNPEnsembl.1
Natural variantiVAR_072726303T → P in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_002411318G → V in DYSFIBRIN; fibrinogen Baltimore-1; impaired polymerization. 1 PublicationCorresponds to variant rs121913089dbSNPEnsembl.1
Natural variantiVAR_072727327D → H in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_002413334N → I in Baltimore-3; impaired polymerization. 1 PublicationCorresponds to variant rs121913090dbSNPEnsembl.1
Natural variantiVAR_002412334N → K in Kyoto-1; causes accelerated cleavage by plasmin. 2 Publications1
Natural variantiVAR_015853335G → D in Hillsborough; prolonged thrombin clotting time. 1 Publication1
Natural variantiVAR_002414336M → T in Asahi; impaired polymerization. 2 PublicationsCorresponds to variant rs121913091dbSNPEnsembl.1
Natural variantiVAR_002415345 – 346Missing in Vlissingen; defective calcium binding and impaired polymerization. 1 Publication2
Natural variantiVAR_072728345N → D in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; decreased fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_002416355Q → R in Nagoya-1; impaired polymerization. 1 PublicationCorresponds to variant rs121913092dbSNPEnsembl.1
Natural variantiVAR_002418356D → V in DYSFIBRIN; fibrinogen Milano-1; impaired polymerization. 1 PublicationCorresponds to variant rs121913094dbSNPEnsembl.1
Natural variantiVAR_002417356D → Y in Kyoto-3; impaired polymerization. 2 PublicationsCorresponds to variant rs121913093dbSNPEnsembl.1
Natural variantiVAR_002419363N → K in Bern-1; impaired polymerization. 1 Publication1
Natural variantiVAR_002420377G → VMCGEALPMLKDPCYS in Paris-1; impaired polymerization. 1 Publication1
Natural variantiVAR_002421384S → C in Milano-7; impaired polymerization. 1 Publication1
Natural variantiVAR_002422401R → G in Osaka-5. 1 PublicationCorresponds to variant rs75848804dbSNPEnsembl.1
Natural variantiVAR_072729401R → W in CAFBN; hypofibrinogenemia; heterozygous. 1 PublicationCorresponds to variant rs75848804dbSNPEnsembl.1
Natural variantiVAR_072621404S → P in DYSFIBRIN; fibrinogen Philadelphia. 1 PublicationCorresponds to variant rs587777720dbSNPEnsembl.1
Natural variantiVAR_014171410M → V.1 PublicationCorresponds to variant rs6061dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001537434 – 453VRPEH…PEDDL → AGDV in isoform Gamma-A. 5 PublicationsAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3788.1. [P02679-1]
CCDS47153.1. [P02679-2]
PIRiA90470. FGHUG.
A90494. FGHUGB.
RefSeqiNP_000500.2. NM_000509.5. [P02679-2]
NP_068656.2. NM_021870.2. [P02679-1]
UniGeneiHs.727584.

Genome annotation databases

EnsembliENST00000336098; ENSP00000336829; ENSG00000171557. [P02679-1]
ENST00000404648; ENSP00000384860; ENSG00000171557. [P02679-2]
GeneIDi2266.
KEGGihsa:2266.
UCSCiuc003iog.4. human. [P02679-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Fibrinogen entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3788.1. [P02679-1]
CCDS47153.1. [P02679-2]
PIRiA90470. FGHUG.
A90494. FGHUGB.
RefSeqiNP_000500.2. NM_000509.5. [P02679-2]
NP_068656.2. NM_021870.2. [P02679-1]
UniGeneiHs.727584.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.59C426-435[»]
2VDRX-ray2.40C428-452[»]
2VR3X-ray1.95C/D425-436[»]
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[»]
ProteinModelPortaliP02679.
SMRiP02679.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108557. 24 interactors.
DIPiDIP-29644N.
IntActiP02679. 5 interactors.
MINTiMINT-5004002.
STRINGi9606.ENSP00000336829.

Chemistry databases

ChEMBLiCHEMBL2364709.
DrugBankiDB00364. Sucralfate.

PTM databases

iPTMnetiP02679.
PhosphoSitePlusiP02679.
UniCarbKBiP02679.

Polymorphism and mutation databases

BioMutaiFGG.
DMDMi20178280.

2D gel databases

DOSAC-COBS-2DPAGEP02679.
OGPiP02679.
REPRODUCTION-2DPAGEIPI00219713.
P02679.
SWISS-2DPAGEP02679.

Proteomic databases

MaxQBiP02679.
PaxDbiP02679.
PeptideAtlasiP02679.
PRIDEiP02679.

Protocols and materials databases

DNASUi2266.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336098; ENSP00000336829; ENSG00000171557. [P02679-1]
ENST00000404648; ENSP00000384860; ENSG00000171557. [P02679-2]
GeneIDi2266.
KEGGihsa:2266.
UCSCiuc003iog.4. human. [P02679-1]

Organism-specific databases

CTDi2266.
DisGeNETi2266.
GeneCardsiFGG.
HGNCiHGNC:3694. FGG.
HPAiCAB033120.
HPA027529.
MalaCardsiFGG.
MIMi134850. gene.
202400. phenotype.
616004. phenotype.
neXtProtiNX_P02679.
OpenTargetsiENSG00000171557.
Orphaneti98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBiPA430.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00760000118809.
HOVERGENiHBG099783.
InParanoidiP02679.
KOiK03905.
PhylomeDBiP02679.
TreeFamiTF336658.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171557-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.

Miscellaneous databases

ChiTaRSiFGG. human.
EvolutionaryTraceiP02679.
GeneWikiiFGG.
GenomeRNAii2266.
PMAP-CutDBP02679.
PROiP02679.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171557.
CleanExiHS_FGG.
ExpressionAtlasiP02679. baseline and differential.
GenevisibleiP02679. HS.

Family and domain databases

CDDicd00087. FReD. 1 hit.
Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. 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]
PfamiPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
SM01212. Fib_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFIBG_HUMAN
AccessioniPrimary (citable) accession number: P02679
Secondary accession number(s): A8K057
, P04469, P04470, Q53Y18, Q96A14, Q96KJ3, Q9UC62, Q9UC63, Q9UCF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: November 30, 2016
This is version 214 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.