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Protein

Fibrinogen alpha chain

Gene

FGA

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

Functioni

Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin 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 immune response via both innate and T-cell mediated pathways.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi791CalciumCombined sources1 Publication1
Metal bindingi793CalciumCombined sources1 Publication1
Metal bindingi795Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi797Calcium; via carbonyl oxygenCombined sources1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • blood coagulation Source: Reactome
  • blood coagulation, common pathway Source: BHF-UCL
  • blood coagulation, fibrin clot formation Source: UniProtKB
  • cell-matrix adhesion Source: BHF-UCL
  • cellular protein complex assembly Source: BHF-UCL
  • cellular protein metabolic process Source: Reactome
  • extracellular matrix organization Source: Reactome
  • fibrinolysis Source: UniProtKB
  • induction of bacterial agglutination Source: CACAO
  • innate immune response Source: UniProtKB-KW
  • negative regulation of blood coagulation, common pathway Source: BHF-UCL
  • 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: UniProtKB
  • 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 complex assembly Source: UniProtKB
  • protein polymerization Source: BHF-UCL
  • response to calcium ion Source: BHF-UCL
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Blood coagulation, Hemostasis, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171560-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.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP02671.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen alpha chain
Cleaved into the following 2 chains:
Gene namesi
Name:FGA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3661. FGA.

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: UniProtKB
  • extracellular space Source: BHF-UCL
  • extracellular vesicle 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

Amyloid, Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital afibrinogenemia (CAFBN)1 Publication
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.
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_07272155C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072722129R → P in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072723184C → W in CAFBN; hypofibrinogenemia; heterozygous; impaired fibrinogen complex assembly. 1 Publication1
Amyloidosis 8 (AMYL8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of hereditary generalized amyloidosis. Clinical features include extensive visceral amyloid deposits, renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. There is no involvement of the nervous system.
See also OMIM:105200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010731545E → V in AMYL8. Corresponds to variant rs121909612dbSNPEnsembl.1
Natural variantiVAR_010732573R → L in AMYL8. 1 PublicationCorresponds to variant rs78506343dbSNPEnsembl.1
Dysfibrinogenemia, congenital (DYSFIBRIN)2 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_00239235R → C in DYSFIBRIN; fibrinogen Metz 1/Hershey III. 1 PublicationCorresponds to variant rs121909606dbSNPEnsembl.1
Natural variantiVAR_002401573R → C in DYSFIBRIN; fibrinogen Dusart/Paris-5. 1 PublicationCorresponds to variant rs121909613dbSNPEnsembl.1

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

DisGeNETi2243.
MalaCardsiFGA.
MIMi105200. phenotype.
134820. gene+phenotype.
202400. phenotype.
616004. phenotype.
OpenTargetsiENSG00000171560.
Orphaneti98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
PharmGKBiPA429.

Chemistry databases

ChEMBLiCHEMBL2364709.
DrugBankiDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00364. Sucralfate.
DB00031. Tenecteplase.

Polymorphism and mutation databases

BioMutaiFGA.
DMDMi1706799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 193 PublicationsAdd BLAST19
PeptideiPRO_000000902120 – 35Fibrinopeptide AAdd BLAST16
ChainiPRO_000000902236 – 866Fibrinogen alpha chainAdd BLAST831

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22PhosphoserineCombined sources1
Modified residuei45Phosphoserine; by FAM20CCombined sources1 Publication1
Disulfide bondi47Interchain1 Publication
Modified residuei50PhosphoserineCombined sources1
Disulfide bondi55Interchain (with C-95 in beta chain)1 Publication
Modified residuei56Phosphoserine; by FAM20C1 Publication1
Disulfide bondi64Interchain (with C-49 in gamma chain)1 Publication
Disulfide bondi68Interchain (with C-106 in beta chain)1 Publication
Disulfide bondi180Interchain (with C-165 in gamma chain)4 Publications
Disulfide bondi184Interchain (with C-223 in beta chain)4 Publications
Modified residuei281PhosphoserineCombined sources1
Modified residuei291PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1
Glycosylationi320O-linked (GalNAc...)1 Publication1
Cross-linki322Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-41 in alpha-2-antiplasmin)
Cross-linki347Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Glycosylationi351O-linked (GalNAc...)1 Publication1
Modified residuei364Phosphoserine; by FAM20C1 Publication1
Cross-linki385Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Modified residuei412PhosphothreonineCombined sources1
Modified residuei451PhosphoserineCombined sources1
Glycosylationi453N-linked (GlcNAc...); in variant Caracas-21
Disulfide bondi461 ↔ 491By similarity
Modified residuei501PhosphoserineCombined sources1
Modified residuei505PhosphothreonineCombined sources1
Modified residuei524Phosphoserine; by FAM20C1 Publication1
Cross-linki527Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence analysis
Cross-linki558Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence analysis
Modified residuei560Phosphoserine; by FAM20C1 Publication1
Modified residuei5654-hydroxyproline; by P4HA11 Publication1
Cross-linki575Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence analysis
Cross-linki581Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence analysis
Cross-linki599Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)Sequence analysis
Modified residuei609Phosphoserine; by FAM20CCombined sources1 Publication1
Glycosylationi686N-linked (GlcNAc...)3 Publications1
Disulfide bondi799 ↔ 812Combined sources1 Publication

Post-translational modificationi

The alpha chain is normally not N-glycosylated (PubMed:23151259), even though glycosylation at Asn-686 was observed when a fragment of the protein was expressed in insect cells (PubMed:9689040). It is well known that heterologous expression of isolated domains can lead to adventitious protein modifications. Besides, glycosylation at Asn-686 is supported by large-scale glycoproteomics studies (PubMed:16335952 and PubMed:19159218), but the evidence is still quite tenuous. Most likely, Asn-686 is not glycosylated in the healthy human body, or only with low efficiency.Curated4 Publications
O-glycosylated.1 Publication
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.
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
Phosphorylated by FAM20C in the extracellular medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei35 – 36Cleavage; by thrombin; to release fibrinopeptide A2
Sitei100 – 101Cleavage; by plasmin; to break down fibrin clots2
Sitei121 – 122Cleavage; by hementin; to prevent blood coagulation2
Sitei123 – 124Cleavage; by plasmin; to break down fibrin clots2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein

Proteomic databases

MaxQBiP02671.
PaxDbiP02671.
PeptideAtlasiP02671.
PRIDEiP02671.

2D gel databases

OGPiP02671.
SWISS-2DPAGEP02671.

PTM databases

iPTMnetiP02671.
PhosphoSitePlusiP02671.
SwissPalmiP02671.
UniCarbKBiP02671.

Miscellaneous databases

PMAP-CutDBP02671.

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000171560.
CleanExiHS_FGA.
ExpressionAtlasiP02671. baseline and differential.
GenevisibleiP02671. HS.

Organism-specific databases

HPAiCAB016776.
HPA051370.
HPA064755.

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APOA1P026472EBI-348571,EBI-701692

Protein-protein interaction databases

BioGridi108534. 27 interactors.
DIPiDIP-29643N.
IntActiP02671. 16 interactors.
MINTiMINT-1033042.
STRINGi9606.ENSP00000306361.

Structurei

Secondary structure

1866
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni27 – 31Combined sources5
Beta strandi57 – 60Combined sources4
Beta strandi63 – 65Combined sources3
Helixi67 – 92Combined sources26
Helixi94 – 111Combined sources18
Helixi116 – 129Combined sources14
Turni133 – 135Combined sources3
Turni139 – 141Combined sources3
Helixi142 – 178Combined sources37
Turni179 – 183Combined sources5
Beta strandi184 – 186Combined sources3
Helixi195 – 209Combined sources15
Turni226 – 228Combined sources3
Beta strandi337 – 343Combined sources7
Beta strandi582 – 587Combined sources6
Beta strandi673 – 681Combined sources9
Helixi689 – 694Combined sources6
Helixi711 – 718Combined sources8
Beta strandi723 – 729Combined sources7
Beta strandi735 – 744Combined sources10
Turni747 – 751Combined sources5
Beta strandi753 – 762Combined sources10
Turni765 – 768Combined sources4
Turni771 – 773Combined sources3
Helixi775 – 778Combined sources4
Beta strandi793 – 797Combined sources5
Helixi799 – 803Combined sources5
Beta strandi810 – 812Combined sources3
Beta strandi814 – 816Combined sources3
Beta strandi823 – 826Combined sources4
Helixi829 – 831Combined sources3
Beta strandi840 – 843Combined sources4
Helixi844 – 847Combined sources4
Beta strandi854 – 861Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BBRX-ray2.30F/G/I26-35[»]
1DM4X-ray2.50C26-35[»]
1FPHX-ray2.50F26-35[»]
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[»]
5CFAX-ray1.45C/D580-594[»]
ProteinModelPortaliP02671.
SMRiP02671.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02671.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini623 – 864Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST242

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 38Alpha-chain polymerization, binding distal domain of another fibrin gamma chain3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili68 – 6311 PublicationAdd BLAST564

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.Curated2 Publications

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP02671.
KOiK03903.
OMAiPGSTGTW.
OrthoDBiEOG091G03M1.
PhylomeDBiP02671.
TreeFamiTF351984.

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.
IPR021996. Fibrinogen_aC.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 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 1 (identifier: P02671-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS
60 70 80 90 100
DWPFCSDEDW NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK
110 120 130 140 150
DSHSLTTNIM EILRGDFSSA NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ
160 170 180 190 200
HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC RGSCSRALAR EVDLKDYEDQ
210 220 230 240 250
QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ LQKVPPEWKA
260 270 280 290 300
LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS
310 320 330 340 350
GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG
360 370 380 390 400
SPRPGSTGTW NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS
410 420 430 440 450
GNARPNNPDW GTFEEVSGNV SPGTRREYHT EKLVTSKGDK ELRTGKEKVT
460 470 480 490 500
SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK EVVTSEDGSD CPEAMDLGTL
510 520 530 540 550
SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF VSETESRGSE
560 570 580 590 600
SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS
610 620 630 640 650
YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI
660 670 680 690 700
KLPGSSKIFS VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN
710 720 730 740 750
DEGEGEFWLG NDYLHLLTQR GSVLRVELED WAGNEAYAEY HFRVGSEAEG
760 770 780 790 800
YALQVSSYEG TAGDALIEGS VEEGAEYTSH NNMQFSTFDR DADQWEENCA
810 820 830 840 850
EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG VVWVSFRGAD
860
YSLRAVRMKI RPLVTQ
Length:866
Mass (Da):94,973
Last modified:October 1, 1996 - v2
Checksum:iEA73A81204D8AEC4
GO
Isoform 2 (identifier: P02671-2) [UniParc]FASTAAdd to basket
Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     631-644: DCDDVLQTHPSGTQ → GIHTSPLGKPSLSP
     645-866: Missing.

Show »
Length:644
Mass (Da):69,757
Checksum:iB9035F3DD864572A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti177I → V in BAF83248 (PubMed:14702039).Curated1
Sequence conflicti215 – 216SR → RS AA sequence (Ref. 10) Curated2
Sequence conflicti299S → G AA sequence (Ref. 10) Curated1
Sequence conflicti304S → G AA sequence (Ref. 10) Curated1
Sequence conflicti317 – 318GT → SG AA sequence (PubMed:518846).Curated2
Isoform 2 (identifier: P02671-2)
Sequence conflicti640 – 644PSLSP → LPCPPRLS in AAK31372 (Ref. 3) Curated5

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0116096I → V.1 PublicationCorresponds to variant rs2070025dbSNPEnsembl.1
Natural variantiVAR_00239026D → N in Lille-1. Corresponds to variant rs121909604dbSNPEnsembl.1
Natural variantiVAR_00239131G → V in Rouen-1. Corresponds to variant rs121909605dbSNPEnsembl.1
Natural variantiVAR_00239235R → C in DYSFIBRIN; fibrinogen Metz 1/Hershey III. 1 PublicationCorresponds to variant rs121909606dbSNPEnsembl.1
Natural variantiVAR_00239335R → H.1 PublicationCorresponds to variant rs121909607dbSNPEnsembl.1
Natural variantiVAR_00239437P → L in Kyoto-2. 1 PublicationCorresponds to variant rs121909609dbSNPEnsembl.1
Natural variantiVAR_00239738R → G in Aarhus-1. Corresponds to variant rs121909608dbSNPEnsembl.1
Natural variantiVAR_00239538R → N in Munich-1; requires 2 nucleotide substitutions. 1
Natural variantiVAR_00239638R → S in Detroit-1. 1
Natural variantiVAR_01073039V → D in Canterbury. 1 PublicationCorresponds to variant rs121909614dbSNPEnsembl.1
Natural variantiVAR_07272155C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_00239866S → T.1
Natural variantiVAR_072722129R → P in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_002399160R → S in Lima. 1 Publication1
Natural variantiVAR_072723184C → W in CAFBN; hypofibrinogenemia; heterozygous; impaired fibrinogen complex assembly. 1 Publication1
Natural variantiVAR_011610331T → A.3 PublicationsCorresponds to variant rs6050dbSNPEnsembl.1
Natural variantiVAR_014168446K → E.1 PublicationCorresponds to variant rs6052dbSNPEnsembl.1
Natural variantiVAR_002400453S → N in Caracas-2. 1 PublicationCorresponds to variant rs121909610dbSNPEnsembl.1
Natural variantiVAR_011611456T → A.1 PublicationCorresponds to variant rs2070031dbSNPEnsembl.1
Natural variantiVAR_010731545E → V in AMYL8. Corresponds to variant rs121909612dbSNPEnsembl.1
Natural variantiVAR_002401573R → C in DYSFIBRIN; fibrinogen Dusart/Paris-5. 1 PublicationCorresponds to variant rs121909613dbSNPEnsembl.1
Natural variantiVAR_010732573R → L in AMYL8. 1 PublicationCorresponds to variant rs78506343dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001531631 – 644DCDDV…PSGTQ → GIHTSPLGKPSLSP in isoform 2. 3 PublicationsAdd BLAST14
Alternative sequenceiVSP_001532645 – 866Missing in isoform 2. 3 PublicationsAdd BLAST222

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3787.1. [P02671-1]
CCDS47152.1. [P02671-2]
PIRiA93956. FGHUA.
D44234.
RefSeqiNP_000499.1. NM_000508.4. [P02671-1]
NP_068657.1. NM_021871.3. [P02671-2]
UniGeneiHs.351593.
Hs.612036.

Genome annotation databases

EnsembliENST00000302053; ENSP00000306361; ENSG00000171560. [P02671-1]
ENST00000403106; ENSP00000385981; ENSG00000171560. [P02671-2]
GeneIDi2243.
KEGGihsa:2243.
UCSCiuc003iod.2. human. [P02671-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Fibrinogen entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3787.1. [P02671-1]
CCDS47152.1. [P02671-2]
PIRiA93956. FGHUA.
D44234.
RefSeqiNP_000499.1. NM_000508.4. [P02671-1]
NP_068657.1. NM_021871.3. [P02671-2]
UniGeneiHs.351593.
Hs.612036.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BBRX-ray2.30F/G/I26-35[»]
1DM4X-ray2.50C26-35[»]
1FPHX-ray2.50F26-35[»]
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[»]
5CFAX-ray1.45C/D580-594[»]
ProteinModelPortaliP02671.
SMRiP02671.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108534. 27 interactors.
DIPiDIP-29643N.
IntActiP02671. 16 interactors.
MINTiMINT-1033042.
STRINGi9606.ENSP00000306361.

Chemistry databases

ChEMBLiCHEMBL2364709.
DrugBankiDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00364. Sucralfate.
DB00031. Tenecteplase.

PTM databases

iPTMnetiP02671.
PhosphoSitePlusiP02671.
SwissPalmiP02671.
UniCarbKBiP02671.

Polymorphism and mutation databases

BioMutaiFGA.
DMDMi1706799.

2D gel databases

OGPiP02671.
SWISS-2DPAGEP02671.

Proteomic databases

MaxQBiP02671.
PaxDbiP02671.
PeptideAtlasiP02671.
PRIDEiP02671.

Protocols and materials databases

DNASUi2243.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302053; ENSP00000306361; ENSG00000171560. [P02671-1]
ENST00000403106; ENSP00000385981; ENSG00000171560. [P02671-2]
GeneIDi2243.
KEGGihsa:2243.
UCSCiuc003iod.2. human. [P02671-1]

Organism-specific databases

CTDi2243.
DisGeNETi2243.
GeneCardsiFGA.
HGNCiHGNC:3661. FGA.
HPAiCAB016776.
HPA051370.
HPA064755.
MalaCardsiFGA.
MIMi105200. phenotype.
134820. gene+phenotype.
202400. phenotype.
616004. phenotype.
neXtProtiNX_P02671.
OpenTargetsiENSG00000171560.
Orphaneti98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
PharmGKBiPA429.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP02671.
KOiK03903.
OMAiPGSTGTW.
OrthoDBiEOG091G03M1.
PhylomeDBiP02671.
TreeFamiTF351984.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171560-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.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP02671.

Miscellaneous databases

ChiTaRSiFGA. human.
EvolutionaryTraceiP02671.
GeneWikiiFibrinogen_alpha_chain.
GenomeRNAii2243.
PMAP-CutDBP02671.
PROiP02671.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171560.
CleanExiHS_FGA.
ExpressionAtlasiP02671. baseline and differential.
GenevisibleiP02671. 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.
IPR021996. Fibrinogen_aC.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 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 nameiFIBA_HUMAN
AccessioniPrimary (citable) accession number: P02671
Secondary accession number(s): A8K3E4
, D3DP14, D3DP15, Q4QQH7, Q9BX62, Q9UCH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 214 of the entry and version 2 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

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.