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UniProtKB - P02675 (FIBB_HUMAN)

Protein

Fibrinogen beta chain

Gene

FGB

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 alpha (FGA) 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. 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

<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

  • chaperone binding Source: BHF-UCL
  • extracellular matrix structural constituent Source: BHF-UCL
  • signaling receptor binding Source: InterPro
  • structural molecule activity Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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

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-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

SIGNOR Signaling Network Open Resource

More...SIGNORi		P02675

<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 beta chain
Cleaved into the following 2 chains:
Fibrinopeptide B
Fibrinogen beta 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:FGB
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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:ENSG00000171564.11

Human Gene Nomenclature Database

More...HGNCi		HGNC:3662 FGB

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		134830 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P02675

<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; 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)4 Publications
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_07272495C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_016908196R → C in CAFBN; fibrinogen Longmont. 1 PublicationCorresponds to variant dbSNP:rs121909623EnsemblClinVar.1
Natural variantiVAR_072620202L → Q in CAFBN. 1 PublicationCorresponds to variant dbSNP:rs121909624EnsemblClinVar.1
Natural variantiVAR_016909383L → R in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant dbSNP:rs121909621EnsemblClinVar.1
Natural variantiVAR_072725407T → K in CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_016910430G → D in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant dbSNP:rs121909622EnsemblClinVar.1
Dysfibrinogenemia, congenital (DYSFIBRIN)1 Publication
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_00240698A → T in DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 PublicationCorresponds to variant dbSNP:rs121909620EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		2244

MalaCards human disease database

More...MalaCardsi		FGB
MIMi202400 phenotype
616004 phenotype

Open Targets

More...OpenTargetsi		ENSG00000171564

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		PA163

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2048

Drug and drug target database

More...DrugBanki		DB04919 Alfimeprase
DB00364 Sucralfate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FGB

Domain mapping of disease mutations (DMDM)

More...DMDMi		399492

<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 – 304 PublicationsAdd BLAST30
<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_000000907031 – 44Fibrinopeptide B1 PublicationAdd BLAST14
<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_000000907145 – 491Fibrinogen beta chainAdd BLAST447

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 residuei31Pyrrolidone carboxylic acid1 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 bondi95Interchain (with C-55 in alpha chain)1 Publication
Disulfide bondi106Interchain (with C-68 in alpha chain)1 Publication
Disulfide bondi110Interchain (with C-45 in gamma chain)1 Publication
Disulfide bondi223Interchain (with C-184 in alpha chain)Combined sources4 Publications
Disulfide bondi227Interchain (with C-161 in gamma chain)
Disulfide bondi231 ↔ 316Combined sources4 Publications
Disulfide bondi241 ↔ 270Combined sources4 Publications
<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>Glycosylationi394N-linked (GlcNAc...) asparagine6 Publications1
Disulfide bondi424 ↔ 437Combined sources4 Publications

<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

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>Sitei44 – 45Cleavage; by thrombin; to release fibrinopeptide B2
Sitei152 – 153Cleavage; by plasmin; to break down fibrin clots2
Sitei160 – 161Cleavage; by hementin; to prevent blood coagulation2
Sitei163 – 164Cleavage; by plasmin; to break down fibrin clots2

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P02675

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02675

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

More...PaxDbi		P02675

PeptideAtlas

More...PeptideAtlasi		P02675

PRoteomics IDEntifications database

More...PRIDEi		P02675

ProteomicsDB human proteome resource

More...ProteomicsDBi		51544

2D gel databases

DOSAC-COBS 2D-PAGE database

More...DOSAC-COBS-2DPAGEi		P02675

USC-OGP 2-DE database

More...OGPi		P02675

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00298497
P02675

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

More...SWISS-2DPAGEi		P02675

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P02675

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P02675

GlyConnect protein glycosylation platform

More...GlyConnecti		157
159

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02675

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

More...PhosphoSitePlusi		P02675

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P02675

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P02675

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P02675

<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		ENSG00000171564 Expressed in 108 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...CleanExi		HS_FGB

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P02675 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P02675 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB008624
HPA001900
HPA001901

<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.4 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
P279584EBI-1034445,EBI-6377335From Hepatitis C virus genotype 1a (isolate H).

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108535, 130 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1922 Fibrinogen

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P02675

Database of interacting proteins

More...DIPi		DIP-385N

Protein interaction database and analysis system

More...IntActi		P02675, 16 interactors

Molecular INTeraction database

More...MINTi		P02675

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000306099

<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

1491
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
1FZAX-ray2.90B/E164-491[»]
1FZBX-ray2.90B/E164-491[»]
1FZCX-ray2.30B/E164-491[»]
1FZEX-ray3.00B/E164-491[»]
1FZFX-ray2.70B/E164-491[»]
M/N/S/T45-48[»]
1FZGX-ray2.50B/E164-491[»]
1LT9X-ray2.80B/E179-491[»]
1LTJX-ray2.80B/E179-491[»]
1N86X-ray3.20B/E164-491[»]
I/J45-51[»]
1N8EX-ray4.50B/E164-491[»]
1RE3X-ray2.45B/E179-491[»]
1RE4X-ray2.70B/E179-491[»]
1RF0X-ray2.81B/E179-491[»]
1RF1X-ray2.53B/E179-491[»]
2A45X-ray3.65H/K45-135[»]
2FFDX-ray2.89B/E179-491[»]
2H43X-ray2.70B/E164-491[»]
2HLOX-ray2.60B/E164-491[»]
2HODX-ray2.90B/E/H/K164-491[»]
2HPCX-ray2.90B/E/H/K164-491[»]
2OYHX-ray2.40B/E179-491[»]
2OYIX-ray2.70B/E179-491[»]
2Q9IX-ray2.80B/E164-491[»]
2XNXX-ray3.30B/E/H/K164-491[»]
2XNYX-ray7.50B/E164-491[»]
2Z4EX-ray2.70B/E164-489[»]
3BVHX-ray2.60B/E191-488[»]
3E1IX-ray2.30B/E164-491[»]
3GHGX-ray2.90B/E/H/K31-491[»]
3H32X-ray3.60B/E31-488[»]
3HUSX-ray3.04B/E179-491[»]
6ATZX-ray2.70E/F69-79[»]
6BIJX-ray2.10C69-81[»]
6BILX-ray2.40C69-81[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P02675

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

More...SMRi		P02675

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		P02675

<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>Domaini232 – 488Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST257

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>Regioni45 – 47Beta-chain polymerization, binding distal domain of another fibrin3

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 coili157 – 2223 PublicationsAdd BLAST66

<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.3 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		ENSGT00940000158122

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000059561

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005707

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02675

KEGG Orthology (KO)

More...KOi		K03904

Identification of Orthologs from Complete Genome Data

More...OMAi		WQKRQKQ

Database of Orthologous Groups

More...OrthoDBi		357340at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02675

TreeFam database of animal gene trees

More...TreeFami		TF336658

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
IPR037580 Fibrinogen_beta
IPR020837 Fibrinogen_CS

The PANTHER Classification System

More...PANTHERi		PTHR19143:SF332 PTHR19143:SF332, 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P02675-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRMVSWSFH KLKTMKHLLL LLLCVFLVKS QGVNDNEEGF FSARGHRPLD 
        60         70         80         90        100
KKREEAPSLR PAPPPISGGG YRARPAKAAA TQKKVERKAP DAGGCLHADP 
       110        120        130        140        150
DLGVLCPTGC QLQEALLQQE RPIRNSVDEL NNNVEAVSQT SSSSFQYMYL 
       160        170        180        190        200
LKDLWQKRQK QVKDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS 
       210        220        230        240        250
ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE 
       260        270        280        290        300
TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK 
       310        320        330        340        350
QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD 
       360        370        380        390        400
KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH 
       410        420        430        440        450
NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG 
       460        470        480        490 
QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q
Length:491
Mass (Da):55,928
Last modified:July 1, 1993 - 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:iB92FFB9976AB53C5
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6REL8D6REL8_HUMAN
Fibrinogen beta chain
FGB
272Annotation 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>
F8W6P4F8W6P4_HUMAN
Fibrinogen beta chain
FGB
45Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH07030 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

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 conflicti138 – 139SQ → QS AA sequence (Ref. 11) Curated2
Sequence conflicti138 – 139SQ → QS AA sequence (PubMed:936108).Curated2
Sequence conflicti145 – 146FQ → QF AA sequence (PubMed:420779).Curated2
Sequence conflicti145 – 146FQ → QF AA sequence (Ref. 11) Curated2
Sequence conflicti145 – 146FQ → QF AA sequence (PubMed:936108).Curated2
Sequence conflicti192P → A in AAA52429 (PubMed:6688356).Curated1
Sequence conflicti245I → T in AAI07767 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0141692K → E1 PublicationCorresponds to variant dbSNP:rs6053EnsemblClinVar.1
Natural variantiVAR_00240239 – 102Missing in New York-1. 1 PublicationAdd BLAST64
Natural variantiVAR_00240344R → C in Christchurch-2, Seattle-1 and Ijmuiden. 1 PublicationCorresponds to variant dbSNP:rs121909616EnsemblClinVar.1
Natural variantiVAR_00240445G → R in Ise. 1 Publication1
Natural variantiVAR_00240574R → C in Nijmegen. 1 PublicationCorresponds to variant dbSNP:rs121909619EnsemblClinVar.1
Natural variantiVAR_07272495C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_00240698A → T in DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 PublicationCorresponds to variant dbSNP:rs121909620EnsemblClinVar.1
Natural variantiVAR_013091100P → S1 PublicationCorresponds to variant dbSNP:rs2227434Ensembl.1
Natural variantiVAR_013092170N → H1 PublicationCorresponds to variant dbSNP:rs2227409Ensembl.1
Natural variantiVAR_016908196R → C in CAFBN; fibrinogen Longmont. 1 PublicationCorresponds to variant dbSNP:rs121909623EnsemblClinVar.1
Natural variantiVAR_072620202L → Q in CAFBN. 1 PublicationCorresponds to variant dbSNP:rs121909624EnsemblClinVar.1
Natural variantiVAR_013093265P → L2 PublicationsCorresponds to variant dbSNP:rs6054EnsemblClinVar.1
Natural variantiVAR_002407365A → T in Pontoise-2. Corresponds to variant dbSNP:rs121909617EnsemblClinVar.1
Natural variantiVAR_016909383L → R in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant dbSNP:rs121909621EnsemblClinVar.1
Natural variantiVAR_072725407T → K in CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_016910430G → D in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant dbSNP:rs121909622EnsemblClinVar.1
Natural variantiVAR_002408478R → K in Baltimore-2. 3 PublicationsCorresponds to variant dbSNP:rs4220EnsemblClinVar.1

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
J00129 mRNA Translation: AAA52429.1
J00131, J00130 Genomic DNA Translation: AAA98115.1
J00132 Genomic DNA Translation: AAA98116.1
J00133 mRNA No translation available.
M64983 Genomic DNA Translation: AAA18024.2
AF388026 Genomic DNA Translation: AAK62470.1
AK312972 mRNA Translation: BAG35810.1
CH471056 Genomic DNA Translation: EAX04932.1
BC007030 mRNA Translation: AAH07030.1 Sequence problems.
BC106760 mRNA Translation: AAI06761.1
BC107766 mRNA Translation: AAI07767.1
AH002694 Genomic DNA Translation: AAA52445.1
X05018 Genomic DNA Translation: CAA28674.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3786.1

Protein sequence database of the Protein Information Resource

More...PIRi		B43568 FGHUB

NCBI Reference Sequences

More...RefSeqi		NP_001171670.1, NM_001184741.1
NP_005132.2, NM_005141.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.300774

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000302068; ENSP00000306099; ENSG00000171564

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2244

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2244

Keywords - Coding sequence diversityi

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
J00129 mRNA Translation: AAA52429.1
J00131, J00130 Genomic DNA Translation: AAA98115.1
J00132 Genomic DNA Translation: AAA98116.1
J00133 mRNA No translation available.
M64983 Genomic DNA Translation: AAA18024.2
AF388026 Genomic DNA Translation: AAK62470.1
AK312972 mRNA Translation: BAG35810.1
CH471056 Genomic DNA Translation: EAX04932.1
BC007030 mRNA Translation: AAH07030.1 Sequence problems.
BC106760 mRNA Translation: AAI06761.1
BC107766 mRNA Translation: AAI07767.1
AH002694 Genomic DNA Translation: AAA52445.1
X05018 Genomic DNA Translation: CAA28674.1
CCDSiCCDS3786.1
PIRiB43568 FGHUB
RefSeqiNP_001171670.1, NM_001184741.1
NP_005132.2, NM_005141.4
UniGeneiHs.300774

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FZAX-ray2.90B/E164-491[»]
1FZBX-ray2.90B/E164-491[»]
1FZCX-ray2.30B/E164-491[»]
1FZEX-ray3.00B/E164-491[»]
1FZFX-ray2.70B/E164-491[»]
M/N/S/T45-48[»]
1FZGX-ray2.50B/E164-491[»]
1LT9X-ray2.80B/E179-491[»]
1LTJX-ray2.80B/E179-491[»]
1N86X-ray3.20B/E164-491[»]
I/J45-51[»]
1N8EX-ray4.50B/E164-491[»]
1RE3X-ray2.45B/E179-491[»]
1RE4X-ray2.70B/E179-491[»]
1RF0X-ray2.81B/E179-491[»]
1RF1X-ray2.53B/E179-491[»]
2A45X-ray3.65H/K45-135[»]
2FFDX-ray2.89B/E179-491[»]
2H43X-ray2.70B/E164-491[»]
2HLOX-ray2.60B/E164-491[»]
2HODX-ray2.90B/E/H/K164-491[»]
2HPCX-ray2.90B/E/H/K164-491[»]
2OYHX-ray2.40B/E179-491[»]
2OYIX-ray2.70B/E179-491[»]
2Q9IX-ray2.80B/E164-491[»]
2XNXX-ray3.30B/E/H/K164-491[»]
2XNYX-ray7.50B/E164-491[»]
2Z4EX-ray2.70B/E164-489[»]
3BVHX-ray2.60B/E191-488[»]
3E1IX-ray2.30B/E164-491[»]
3GHGX-ray2.90B/E/H/K31-491[»]
3H32X-ray3.60B/E31-488[»]
3HUSX-ray3.04B/E179-491[»]
6ATZX-ray2.70E/F69-79[»]
6BIJX-ray2.10C69-81[»]
6BILX-ray2.40C69-81[»]
ProteinModelPortaliP02675
SMRiP02675
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108535, 130 interactors
ComplexPortaliCPX-1922 Fibrinogen
CORUMiP02675
DIPiDIP-385N
IntActiP02675, 16 interactors
MINTiP02675
STRINGi9606.ENSP00000306099

Chemistry databases

ChEMBLiCHEMBL2048
DrugBankiDB04919 Alfimeprase
DB00364 Sucralfate

PTM databases

CarbonylDBiP02675
GlyConnecti157
159
iPTMnetiP02675
PhosphoSitePlusiP02675
SwissPalmiP02675
UniCarbKBiP02675

Polymorphism and mutation databases

BioMutaiFGB
DMDMi399492

2D gel databases

DOSAC-COBS-2DPAGEiP02675
OGPiP02675
REPRODUCTION-2DPAGEiIPI00298497
P02675
SWISS-2DPAGEiP02675
UCD-2DPAGEiP02675

Proteomic databases

EPDiP02675
jPOSTiP02675
PaxDbiP02675
PeptideAtlasiP02675
PRIDEiP02675
ProteomicsDBi51544

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302068; ENSP00000306099; ENSG00000171564
GeneIDi2244
KEGGihsa:2244

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2244
DisGeNETi2244
EuPathDBiHostDB:ENSG00000171564.11

GeneCards: human genes, protein and diseases

More...GeneCardsi		FGB
HGNCiHGNC:3662 FGB
HPAiCAB008624
HPA001900
HPA001901
MalaCardsiFGB
MIMi134830 gene
202400 phenotype
616004 phenotype
neXtProtiNX_P02675
OpenTargetsiENSG00000171564
Orphaneti98880 Familial afibrinogenemia
98881 Familial dysfibrinogenemia
248408 Familial hypodysfibrinogenemia
101041 Familial hypofibrinogenemia
PharmGKBiPA163

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00940000158122
HOGENOMiHOG000059561
HOVERGENiHBG005707
InParanoidiP02675
KOiK03904
OMAiWQKRQKQ
OrthoDBi357340at2759
PhylomeDBiP02675
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-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
SIGNORiP02675

Miscellaneous databases

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

More...ChiTaRSi		FGB human
EvolutionaryTraceiP02675

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Fibrinogen_beta_chain

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

More...GenomeRNAii		2244
PMAP-CutDBiP02675

Protein Ontology

More...PROi		PR:P02675

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000171564 Expressed in 108 organ(s), highest expression level in liver
CleanExiHS_FGB
ExpressionAtlasiP02675 baseline and differential
GenevisibleiP02675 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
IPR037580 Fibrinogen_beta
IPR020837 Fibrinogen_CS
PANTHERiPTHR19143:SF332 PTHR19143:SF332, 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 nameiFIBB_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: P02675
Secondary accession number(s): A0JLR9
, B2R7G3, Q32Q65, Q3KPF2
<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: July 1, 1993
Last modified: January 16, 2019
This is version 222 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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 chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
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