Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 236 (13 Feb 2019)
Sequence version 3 (16 Apr 2002)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Fibrinogen gamma chain

Gene

FGG

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

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

Miscellaneous

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

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 bindingi344CalciumCombined sources6 Publications1
Metal bindingi346CalciumCombined sources6 Publications1
Metal bindingi348Calcium; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi350Calcium; via carbonyl oxygenCombined sources6 Publications1

<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 processBlood coagulation, Hemostasis
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

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P02679

<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 gamma chain
<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:FGG
ORF Names:PRO2061
<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:ENSG00000171557.16

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3694 FGG

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
134850 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P02679

<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

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. 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
<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_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 dbSNP:rs75848804EnsemblClinVar.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 dbSNP:rs121913088EnsemblClinVar.1
Natural variantiVAR_002411318G → V in DYSFIBRIN; fibrinogen Baltimore-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913089EnsemblClinVar.1
Natural variantiVAR_002418356D → V in DYSFIBRIN; fibrinogen Milano-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913094EnsemblClinVar.1
Natural variantiVAR_072621404S → P in DYSFIBRIN; fibrinogen Philadelphia. 1 PublicationCorresponds to variant dbSNP:rs587777720EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2266

MalaCards human disease database

More...
MalaCardsi
FGG
MIMi202400 phenotype
616004 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000171557

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

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

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA430

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2364709

Drug and drug target database

More...
DrugBanki
DB00364 Sucralfate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FGG

Domain mapping of disease mutations (DMDM)

More...
DMDMi
20178280

<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 – 262 PublicationsAdd BLAST26
<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_000000909927 – 453Fibrinogen gamma chainAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 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
<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 residuei68Phosphoserine; by FAM20C1 Publication1
<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>Glycosylationi78N-linked (GlcNAc...) (complex) asparagine6 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...) asparagine; in variant Asahi1
Disulfide bondi352 ↔ 365Combined sources6 Publications
<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-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

<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

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
<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>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

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P02679

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P02679

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

More...
PaxDbi
P02679

PeptideAtlas

More...
PeptideAtlasi
P02679

PRoteomics IDEntifications database

More...
PRIDEi
P02679

ProteomicsDB human proteome resource

More...
ProteomicsDBi
51545
51546 [P02679-2]

2D gel databases

DOSAC-COBS 2D-PAGE database

More...
DOSAC-COBS-2DPAGEi
P02679

USC-OGP 2-DE database

More...
OGPi
P02679

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00219713
P02679

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

More...
SWISS-2DPAGEi
P02679

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P02679

GlyConnect protein glycosylation platform

More...
GlyConnecti
157
160

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P02679

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

More...
PhosphoSitePlusi
P02679

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P02679

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P02679

<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).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000171557 Expressed in 105 organ(s), highest expression level in liver

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P02679 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P02679 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB033120
HPA027529

<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.7 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

WithEntry#Exp.IntActNotes
gapAP753582EBI-1034422,EBI-2259469From Mycoplasma pneumoniae (strain ATCC 29342 / M129).

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108557, 28 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1922 Fibrinogen

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P02679

Database of interacting proteins

More...
DIPi
DIP-29644N

Protein interaction database and analysis system

More...
IntActi
P02679, 16 interactors

Molecular INTeraction database

More...
MINTi
P02679

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000336829

<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

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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-ray2.59C426-433[»]
2VDRX-ray2.40C428-433[»]
2VR3X-ray1.95C/D425-433[»]
2XNXX-ray3.30C/F/I/L114-432[»]
2XNYX-ray7.50C/F114-432[»]
2Y7LX-ray1.49B421-433[»]
2Z4EX-ray2.70C/F114-433[»]
3BVHX-ray2.60C/F128-420[»]
3E1IX-ray2.30C/F114-432[»]
3FIBX-ray2.10A170-418[»]
3GHGX-ray2.90C/F/I/L27-433[»]
3H32X-ray3.60C/F121-433[»]
3HUSX-ray3.04C/F122-432[»]
4B60X-ray1.83C/D421-433[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P02679

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

More...
SMRi
P02679

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
P02679

<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>Domaini170 – 416Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST247

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>Regioni400 – 422Gamma-chain polymerization, binding amino end of another fibrin alpha chainAdd BLAST23
Regioni423 – 437Platelet aggregation and Staphylococcus clumpingAdd BLAST15

<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.2 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
ENSGT00940000158467

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG099783

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02679

KEGG Orthology (KO)

More...
KOi
K03905

Database of Orthologous Groups

More...
OrthoDBi
751651at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P02679

TreeFam database of animal gene trees

More...
TreeFami
TF336658

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00087 FReD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.215.10, 1 hit
4.10.530.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036056 Fibrinogen-like_C
IPR014716 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
IPR037581 Fibrinogen_gamma

The PANTHER Classification System

More...
PANTHERi
PTHR19143:SF338 PTHR19143:SF338, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08702 Fib_alpha, 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 4 potential isoforms that are computationally mapped.Show allAlign All

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
<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: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

<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 are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JC84C9JC84_HUMAN
Fibrinogen gamma chain
FGG
461Annotation score:

Annotation score:2 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>
C9JEU5C9JEU5_HUMAN
Fibrinogen gamma chain
FGG
445Annotation score:

Annotation score:2 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>
C9JPQ9C9JPQ9_HUMAN
Fibrinogen gamma chain
FGG
119Annotation 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>
C9JU00C9JU00_HUMAN
Fibrinogen gamma chain
FGG
123Annotation 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 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 dbSNP:rs11551835Ensembl.1
Natural variantiVAR_033930140Y → H1 PublicationCorresponds to variant dbSNP:rs2066870EnsemblClinVar.1
Natural variantiVAR_014170191G → R in Milano-12. 3 PublicationsCorresponds to variant dbSNP:rs6063EnsemblClinVar.1
Natural variantiVAR_002409301R → C in Tochigi/Osaka-2/Milano-5/Villajoyosa. 5 PublicationsCorresponds to variant dbSNP:rs121913087EnsemblClinVar.1
Natural variantiVAR_002410301R → H in DYSFIBRIN; fibrinogen Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. 4 PublicationsCorresponds to variant dbSNP:rs121913088EnsemblClinVar.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 dbSNP:rs121913089EnsemblClinVar.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 dbSNP:rs121913090EnsemblClinVar.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 dbSNP:rs121913091EnsemblClinVar.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 dbSNP:rs121913092EnsemblClinVar.1
Natural variantiVAR_002418356D → V in DYSFIBRIN; fibrinogen Milano-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913094EnsemblClinVar.1
Natural variantiVAR_002417356D → Y in Kyoto-3; impaired polymerization. 2 PublicationsCorresponds to variant dbSNP:rs121913093EnsemblClinVar.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 dbSNP:rs75848804EnsemblClinVar.1
Natural variantiVAR_072729401R → W in CAFBN; hypofibrinogenemia; heterozygous. 1 PublicationCorresponds to variant dbSNP:rs75848804EnsemblClinVar.1
Natural variantiVAR_072621404S → P in DYSFIBRIN; fibrinogen Philadelphia. 1 PublicationCorresponds to variant dbSNP:rs587777720EnsemblClinVar.1
Natural variantiVAR_014171410M → V1 PublicationCorresponds to variant dbSNP:rs6061Ensembl.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_001537434 – 453VRPEH…PEDDL → AGDV in isoform Gamma-A. 5 PublicationsAdd BLAST20

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
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3788.1 [P02679-1]
CCDS47153.1 [P02679-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A90470 FGHUG
A90494 FGHUGB

NCBI Reference Sequences

More...
RefSeqi
NP_000500.2, NM_000509.5 [P02679-2]
NP_068656.2, NM_021870.2 [P02679-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.727584

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000336098; ENSP00000336829; ENSG00000171557 [P02679-1]
ENST00000404648; ENSP00000384860; ENSG00000171557 [P02679-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2266

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2266

UCSC genome browser

More...
UCSCi
uc003iog.4 human [P02679-1]

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

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-ray2.59C426-433[»]
2VDRX-ray2.40C428-433[»]
2VR3X-ray1.95C/D425-433[»]
2XNXX-ray3.30C/F/I/L114-432[»]
2XNYX-ray7.50C/F114-432[»]
2Y7LX-ray1.49B421-433[»]
2Z4EX-ray2.70C/F114-433[»]
3BVHX-ray2.60C/F128-420[»]
3E1IX-ray2.30C/F114-432[»]
3FIBX-ray2.10A170-418[»]
3GHGX-ray2.90C/F/I/L27-433[»]
3H32X-ray3.60C/F121-433[»]
3HUSX-ray3.04C/F122-432[»]
4B60X-ray1.83C/D421-433[»]
ProteinModelPortaliP02679
SMRiP02679
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108557, 28 interactors
ComplexPortaliCPX-1922 Fibrinogen
CORUMiP02679
DIPiDIP-29644N
IntActiP02679, 16 interactors
MINTiP02679
STRINGi9606.ENSP00000336829

Chemistry databases

ChEMBLiCHEMBL2364709
DrugBankiDB00364 Sucralfate

PTM databases

CarbonylDBiP02679
GlyConnecti157
160
iPTMnetiP02679
PhosphoSitePlusiP02679
UniCarbKBiP02679

Polymorphism and mutation databases

BioMutaiFGG
DMDMi20178280

2D gel databases

DOSAC-COBS-2DPAGEiP02679
OGPiP02679
REPRODUCTION-2DPAGEiIPI00219713
P02679
SWISS-2DPAGEiP02679

Proteomic databases

jPOSTiP02679
MaxQBiP02679
PaxDbiP02679
PeptideAtlasiP02679
PRIDEiP02679
ProteomicsDBi51545
51546 [P02679-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2266
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

Comparative Toxicogenomics Database

More...
CTDi
2266
DisGeNETi2266
EuPathDBiHostDB:ENSG00000171557.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FGG
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

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00940000158467
HOVERGENiHBG099783
InParanoidiP02679
KOiK03905
OrthoDBi751651at2759
PhylomeDBiP02679
TreeFamiTF336658

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
SIGNORiP02679

Miscellaneous databases

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

More...
ChiTaRSi
FGG human
EvolutionaryTraceiP02679

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
FGG

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

More...
GenomeRNAii
2266
PMAP-CutDBiP02679

Protein Ontology

More...
PROi
PR:P02679

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000171557 Expressed in 105 organ(s), highest expression level in liver
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
InterProiView protein in InterPro
IPR036056 Fibrinogen-like_C
IPR014716 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
IPR037581 Fibrinogen_gamma
PANTHERiPTHR19143:SF338 PTHR19143:SF338, 1 hit
PfamiView protein in Pfam
PF08702 Fib_alpha, 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

More...
ProtoNeti
Search...

<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 nameiFIBG_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: P02679
Secondary accession number(s): A8K057
, P04469, P04470, Q53Y18, Q96A14, Q96KJ3, Q9UC62, Q9UC63, Q9UCF3
<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: April 16, 2002
Last modified: February 13, 2019
This is version 236 of the entry and version 3 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again