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Entry version 236 (13 Feb 2019)
Sequence version 2 (01 Oct 1996)
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Protein

Fibrinogen alpha chain

Gene

FGA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi791CalciumCombined sources1 Publication1
Metal bindingi793CalciumCombined sources1 Publication1
Metal bindingi795Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi797Calcium; via carbonyl oxygenCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processAdaptive immunity, Blood coagulation, Hemostasis, Immunity, Innate immunity
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
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-8957275 Post-translational protein phosphorylation
R-HSA-977225 Amyloid fiber formation

SIGNOR Signaling Network Open Resource

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SIGNORi
P02671

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fibrinogen alpha chain
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FGA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000171560.14

Human Gene Nomenclature Database

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HGNCi
HGNC:3661 FGA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
134820 gene+phenotype

neXtProt; the human protein knowledge platform

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neXtProti
NX_P02671

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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 dbSNP:rs121909612EnsemblClinVar.1
Natural variantiVAR_010732573R → L in AMYL8. 1 PublicationCorresponds to variant dbSNP:rs78506343EnsemblClinVar.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 dbSNP:rs121909606EnsemblClinVar.1
Natural variantiVAR_002401573R → C in DYSFIBRIN; fibrinogen Dusart/Paris-5. 1 PublicationCorresponds to variant dbSNP:rs121909613EnsemblClinVar.1

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
2243

MalaCards human disease database

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MalaCardsi
FGA
MIMi105200 phenotype
134820 gene+phenotype
202400 phenotype
616004 phenotype

Open Targets

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OpenTargetsi
ENSG00000171560

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
93562 AFib amyloidosis
98880 Familial afibrinogenemia
98881 Familial dysfibrinogenemia
248408 Familial hypodysfibrinogenemia
101041 Familial hypofibrinogenemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA429

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2364709

Drug and drug target database

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DrugBanki
DB04919 Alfimeprase
DB00009 Alteplase
DB05099 Ancrod
DB00029 Anistreplase
DB05675 EP-2104R
DB00015 Reteplase
DB00364 Sucralfate
DB00031 Tenecteplase

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FGA

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1706799

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 193 PublicationsAdd BLAST19
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000000902120 – 35Fibrinopeptide AAdd BLAST16
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000902236 – 866Fibrinogen alpha chainAdd BLAST831

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei22PhosphoserineCombined sources1
Modified residuei45Phosphoserine; by FAM20CCombined sources1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi320O-linked (GalNAc...) threonine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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...) serine1 Publication1
Modified residuei364Phosphoserine; by FAM20C1 Publication1
Cross-linki385Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Modified residuei412PhosphothreonineCombined sources1
Modified residuei451PhosphoserineCombined sources1
Glycosylationi453N-linked (GlcNAc...) asparagine; in variant Caracas-21 Publication1
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...) asparagine3 Publications1
Disulfide bondi799 ↔ 812Combined sources1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P02671

MaxQB - The MaxQuant DataBase

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MaxQBi
P02671

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P02671

PeptideAtlas

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PeptideAtlasi
P02671

PRoteomics IDEntifications database

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PRIDEi
P02671

ProteomicsDB human proteome resource

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ProteomicsDBi
51542
51543 [P02671-2]

2D gel databases

USC-OGP 2-DE database

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OGPi
P02671

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P02671

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P02671

GlyConnect protein glycosylation platform

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GlyConnecti
1238
157

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P02671

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P02671

SwissPalm database of S-palmitoylation events

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SwissPalmi
P02671

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P02671

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P02671

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000171560 Expressed in 113 organ(s), highest expression level in liver

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P02671 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P02671 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB016776
HPA051370
HPA064755

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108534, 33 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1922 Fibrinogen

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P02671

Database of interacting proteins

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DIPi
DIP-29643N

Protein interaction database and analysis system

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IntActi
P02671, 23 interactors

Molecular INTeraction database

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MINTi
P02671

STRING: functional protein association networks

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STRINGi
9606.ENSP00000306361

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1866
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P02671

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P02671

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P02671

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini623 – 864Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST242

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni36 – 38Alpha-chain polymerization, binding distal domain of another fibrin gamma chain3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili68 – 6311 PublicationAdd BLAST564

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2579 Eukaryota
ENOG410ZYS4 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157467

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000285947

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005668

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02671

KEGG Orthology (KO)

More...
KOi
K03903

Identification of Orthologs from Complete Genome Data

More...
OMAi
PGSTGTW

Database of Orthologous Groups

More...
OrthoDBi
1104340at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P02671

TreeFam database of animal gene trees

More...
TreeFami
TF351984

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00087 FReD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR012290 Fibrinogen_a/b/g_coil_dom
IPR021996 Fibrinogen_aC
IPR037579 Fibrinogen_alpha
IPR020837 Fibrinogen_CS

The PANTHER Classification System

More...
PANTHERi
PTHR19143:SF232 PTHR19143:SF232, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08702 Fib_alpha, 1 hit
PF12160 Fibrinogen_aC, 1 hit
PF00147 Fibrinogen_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00186 FBG, 1 hit
SM01212 Fib_alpha, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56496 SSF56496, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WUA0A0A087WUA0_HUMAN
Fibrinogen alpha chain
FGA
289Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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 → V1 PublicationCorresponds to variant dbSNP:rs2070025EnsemblClinVar.1
Natural variantiVAR_00239026D → N in Lille-1. Corresponds to variant dbSNP:rs121909604EnsemblClinVar.1
Natural variantiVAR_00239131G → V in Rouen-1. Corresponds to variant dbSNP:rs121909605EnsemblClinVar.1
Natural variantiVAR_00239235R → C in DYSFIBRIN; fibrinogen Metz 1/Hershey III. 1 PublicationCorresponds to variant dbSNP:rs121909606EnsemblClinVar.1
Natural variantiVAR_00239335R → H1 PublicationCorresponds to variant dbSNP:rs121909607EnsemblClinVar.1
Natural variantiVAR_00239437P → L in Kyoto-2. 1 PublicationCorresponds to variant dbSNP:rs121909609EnsemblClinVar.1
Natural variantiVAR_00239738R → G in Aarhus-1. Corresponds to variant dbSNP:rs121909608EnsemblClinVar.1
Natural variantiVAR_00239538R → N in Munich-1; requires 2 nucleotide substitutions. 1
Natural variantiVAR_00239638R → S in Detroit-1. Corresponds to variant dbSNP:rs1403508334Ensembl.1
Natural variantiVAR_01073039V → D in Canterbury. 1 PublicationCorresponds to variant dbSNP:rs121909614EnsemblClinVar.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 → A3 PublicationsCorresponds to variant dbSNP:rs6050EnsemblClinVar.1
Natural variantiVAR_014168446K → E1 PublicationCorresponds to variant dbSNP:rs6052Ensembl.1
Natural variantiVAR_002400453S → N in Caracas-2. 1 PublicationCorresponds to variant dbSNP:rs121909610EnsemblClinVar.1
Natural variantiVAR_011611456T → A1 PublicationCorresponds to variant dbSNP:rs2070031Ensembl.1
Natural variantiVAR_010731545E → V in AMYL8. Corresponds to variant dbSNP:rs121909612EnsemblClinVar.1
Natural variantiVAR_002401573R → C in DYSFIBRIN; fibrinogen Dusart/Paris-5. 1 PublicationCorresponds to variant dbSNP:rs121909613EnsemblClinVar.1
Natural variantiVAR_010732573R → L in AMYL8. 1 PublicationCorresponds to variant dbSNP:rs78506343EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3787.1 [P02671-1]
CCDS47152.1 [P02671-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A93956 FGHUA
D44234

NCBI Reference Sequences

More...
RefSeqi
NP_000499.1, NM_000508.4 [P02671-1]
NP_068657.1, NM_021871.3 [P02671-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.351593
Hs.612036

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000302053; ENSP00000306361; ENSG00000171560 [P02671-1]
ENST00000403106; ENSP00000385981; ENSG00000171560 [P02671-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2243

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2243

UCSC genome browser

More...
UCSCi
uc003iod.2 human [P02671-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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, 33 interactors
ComplexPortaliCPX-1922 Fibrinogen
CORUMiP02671
DIPiDIP-29643N
IntActiP02671, 23 interactors
MINTiP02671
STRINGi9606.ENSP00000306361

Chemistry databases

ChEMBLiCHEMBL2364709
DrugBankiDB04919 Alfimeprase
DB00009 Alteplase
DB05099 Ancrod
DB00029 Anistreplase
DB05675 EP-2104R
DB00015 Reteplase
DB00364 Sucralfate
DB00031 Tenecteplase

PTM databases

CarbonylDBiP02671
GlyConnecti1238
157
iPTMnetiP02671
PhosphoSitePlusiP02671
SwissPalmiP02671
UniCarbKBiP02671

Polymorphism and mutation databases

BioMutaiFGA
DMDMi1706799

2D gel databases

OGPiP02671
SWISS-2DPAGEiP02671

Proteomic databases

jPOSTiP02671
MaxQBiP02671
PaxDbiP02671
PeptideAtlasiP02671
PRIDEiP02671
ProteomicsDBi51542
51543 [P02671-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2243
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

Comparative Toxicogenomics Database

More...
CTDi
2243
DisGeNETi2243
EuPathDBiHostDB:ENSG00000171560.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FGA
HGNCiHGNC:3661 FGA
HPAiCAB016776
HPA051370
HPA064755
MalaCardsiFGA
MIMi105200 phenotype
134820 gene+phenotype
202400 phenotype
616004 phenotype
neXtProtiNX_P02671
OpenTargetsiENSG00000171560
Orphaneti93562 AFib amyloidosis
98880 Familial afibrinogenemia
98881 Familial dysfibrinogenemia
248408 Familial hypodysfibrinogenemia
101041 Familial hypofibrinogenemia
PharmGKBiPA429

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00940000157467
HOGENOMiHOG000285947
HOVERGENiHBG005668
InParanoidiP02671
KOiK03903
OMAiPGSTGTW
OrthoDBi1104340at2759
PhylomeDBiP02671
TreeFamiTF351984

Enzyme and pathway databases

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-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
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-8957275 Post-translational protein phosphorylation
R-HSA-977225 Amyloid fiber formation
SIGNORiP02671

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
FGA human
EvolutionaryTraceiP02671

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Fibrinogen_alpha_chain

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
2243
PMAP-CutDBiP02671

Protein Ontology

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PROi
PR:P02671

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000171560 Expressed in 113 organ(s), highest expression level in liver
ExpressionAtlasiP02671 baseline and differential
GenevisibleiP02671 HS

Family and domain databases

CDDicd00087 FReD, 1 hit
InterProiView protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR012290 Fibrinogen_a/b/g_coil_dom
IPR021996 Fibrinogen_aC
IPR037579 Fibrinogen_alpha
IPR020837 Fibrinogen_CS
PANTHERiPTHR19143:SF232 PTHR19143:SF232, 2 hits
PfamiView protein in Pfam
PF08702 Fib_alpha, 1 hit
PF12160 Fibrinogen_aC, 1 hit
PF00147 Fibrinogen_C, 1 hit
SMARTiView protein in SMART
SM00186 FBG, 1 hit
SM01212 Fib_alpha, 1 hit
SUPFAMiSSF56496 SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFIBA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P02671
Secondary accession number(s): A8K3E4
, D3DP14, D3DP15, Q4QQH7, Q9BX62, Q9UCH2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: February 13, 2019
This is version 236 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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 polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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