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Protein

Coagulation factor V

Gene

F5

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

Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by SERPINA5.4 Publications

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 bindingi139CalciumBy similarity1
Metal bindingi140CalciumBy similarity1
Metal bindingi1843CopperBy similarity1
Metal bindingi1845CopperBy similarity1

<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, Copper, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114608 Platelet degranulation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-204005 COPII-mediated vesicle transport
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-5694530 Cargo concentration in the ER
R-HSA-8957275 Post-translational protein phosphorylation

SIGNOR Signaling Network Open Resource

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SIGNORi
P12259

<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:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor
Proaccelerin, labile factor
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:F5
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000198734.10

Human Gene Nomenclature Database

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HGNCi
HGNC:3542 F5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
612309 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P12259

<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

Factor V deficiency (FA5D)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA blood coagulation disorder leading to a hemorrhagic diathesis known as parahemophilia.
See also OMIM:227400
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_0327001730Y → C in FA5D; Seoul 2. 2 PublicationsCorresponds to variant dbSNP:rs118203907EnsemblClinVar.1
Natural variantiVAR_0327012102R → C in FA5D; impairs both factor V secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs118203910EnsemblClinVar.1
Thrombophilia due to activated protein C resistance (THPH2)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemostatic disorder due to defective degradation of factor V by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.
See also OMIM:188055
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013621334R → T in THPH2; Cambridge. 1 PublicationCorresponds to variant dbSNP:rs118203906EnsemblClinVar.1
Natural variantiVAR_032698387I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 PublicationsCorresponds to variant dbSNP:rs118203911EnsemblClinVar.1
Natural variantiVAR_001213534R → Q in THPH2; factor V Leiden; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. 5 PublicationsCorresponds to variant dbSNP:rs6025EnsemblClinVar.1
Natural variantiVAR_032699613C → R in THPH2; Nijkerk. 1 PublicationCorresponds to variant dbSNP:rs1453479152Ensembl.1
Natural variantiVAR_0173292102R → H in THPH2. 1 Publication1
Budd-Chiari syndrome (BDCHS)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera.
See also OMIM:600880
Ischemic stroke (ISCHSTR)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
See also OMIM:601367
Pregnancy loss, recurrent, 1 (RPRGL1)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.
See also OMIM:614389

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNET

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DisGeNETi
2153

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
F5

MalaCards human disease database

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MalaCardsi
F5
MIMi188055 phenotype
227400 phenotype
600880 phenotype
601367 phenotype
614389 phenotype

Open Targets

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OpenTargetsi
ENSG00000198734

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

More...
Orphaneti
131 Budd-Chiari syndrome
329217 Cerebral sinovenous thrombosis
326 Congenital factor V deficiency
391320 East Texas bleeding disorder
64738 NON RARE IN EUROPE: Non rare thrombophilia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA159

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3618

Drug and drug target database

More...
DrugBanki
DB00055 Drotrecogin alfa
DB05777 Thrombomodulin Alfa

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
F5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
308153653

<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 – 28Add BLAST28
<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_000000297829 – 2224Coagulation factor VAdd BLAST2196
ChainiPRO_000000297929 – 737Coagulation factor V heavy chainAdd BLAST709
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000002980738 – 1573Activation peptide (connecting region)Add BLAST836
ChainiPRO_00000029811574 – 2224Coagulation factor V light chainAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi51N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi55N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi167 ↔ 193PROSITE-ProRule annotation
Glycosylationi239N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi248 ↔ 329PROSITE-ProRule annotation
Glycosylationi297N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi382N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi460N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi500 ↔ 526PROSITE-ProRule annotation
Glycosylationi554N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi603 ↔ 684PROSITE-ProRule annotation
<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 residuei640PhosphothreonineCombined sources1
Modified residuei693SulfotyrosineSequence analysis1
Modified residuei724SulfotyrosineSequence analysis1
Modified residuei726SulfotyrosineSequence analysis1
Glycosylationi741N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi752N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi760N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi776N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi782N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi821N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei859Phosphoserine; by FAM20C1 Publication1
Glycosylationi938N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi977N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1074N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1083N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1103N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1106N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1479N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1499N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1522SulfotyrosineSequence analysis1
Modified residuei1538SulfotyrosineSequence analysis1
Modified residuei1543SulfotyrosineSequence analysis1
Glycosylationi1559N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei1593SulfotyrosineSequence analysis1
Glycosylationi1703N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1725 ↔ 1751Curated
Disulfide bondi1907 ↔ 2061PROSITE-ProRule annotation
Glycosylationi2010N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2066 ↔ 2221PROSITE-ProRule annotation
Glycosylationi2209N-linked (GlcNAc...) asparagineSequence analysis1

<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

Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus).
Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity.3 Publications
Activated protein C inactivates factor V and factor Va by proteolytic degradation.1 Publication
Phosphorylated by FAM20C in the extracellular medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei334 – 335Cleavage; by activated protein C1 Publication2
Sitei534 – 535Cleavage; by activated protein C1 Publication2
Sitei707 – 708Cleavage; by activated protein C1 Publication2
Sitei737 – 738Cleavage; by thrombin1 Publication2
Sitei1022 – 1023Cleavage; by activated protein C1 Publication2
Sitei1046 – 1047Cleavage; by thrombin1 Publication2
Sitei1573 – 1574Cleavage; by thrombin1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P12259

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

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PaxDbi
P12259

PeptideAtlas

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PeptideAtlasi
P12259

PRoteomics IDEntifications database

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PRIDEi
P12259

ProteomicsDB human proteome resource

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ProteomicsDBi
52838

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P12259

GlyConnect protein glycosylation platform

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GlyConnecti
1120

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P12259

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

More...
PhosphoSitePlusi
P12259

<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

Plasma.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000198734 Expressed in 160 organ(s), highest expression level in right lobe of liver

CleanEx database of gene expression profiles

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CleanExi
HS_F5

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P12259 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P12259 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA002036

<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

Factor Va, the activated form of factor V, is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. Forms heterodimer with SERPINA5.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108452, 13 interactors

Database of interacting proteins

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DIPi
DIP-47331N

Protein interaction database and analysis system

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IntActi
P12259, 3 interactors

Molecular INTeraction database

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MINTi
P12259

STRING: functional protein association networks

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STRINGi
9606.ENSP00000356771

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P12259

<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

12224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P12259

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

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SMRi
P12259

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P12259

<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>Domaini30 – 329F5/8 type A 1Add BLAST300
Domaini30 – 193Plastocyanin-like 1Add BLAST164
Domaini203 – 329Plastocyanin-like 2Add BLAST127
Domaini348 – 684F5/8 type A 2Add BLAST337
Domaini348 – 526Plastocyanin-like 3Add BLAST179
Domaini536 – 684Plastocyanin-like 4Add BLAST149
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati895 – 9111-1Add BLAST17
Repeati912 – 9281-2Add BLAST17
Repeati1185 – 11932-19
Repeati1194 – 12022-29
Repeati1203 – 12112-39
Repeati1212 – 12202-49
Repeati1221 – 12292-59
Repeati1230 – 12382-69
Repeati1239 – 12472-79
Repeati1248 – 12562-89
Repeati1257 – 12652-99
Repeati1266 – 12742-109
Repeati1275 – 12832-119
Repeati1284 – 12922-129
Repeati1293 – 13012-139
Repeati1302 – 13102-149
Repeati1311 – 13192-159
Repeati1320 – 13282-169
Repeati1329 – 13372-179
Repeati1338 – 13462-189
Repeati1347 – 13552-199
Repeati1356 – 13642-209
Repeati1365 – 13732-219
Repeati1374 – 13822-229
Repeati1383 – 13912-239
Repeati1392 – 14002-249
Repeati1401 – 14092-259
Repeati1410 – 14182-269
Repeati1419 – 14272-279
Repeati1428 – 14362-289
Repeati1437 – 14452-299
Repeati1446 – 14542-309
Repeati1455 – 14632-319
Repeati1464 – 14722-329
Repeati1473 – 14812-339
Repeati1482 – 14902-349
Repeati1493 – 15012-359
Domaini1578 – 1907F5/8 type A 3Add BLAST330
Domaini1578 – 1751Plastocyanin-like 5Add BLAST174
Domaini1761 – 1907Plastocyanin-like 6Add BLAST147
Domaini1907 – 2061F5/8 type C 1PROSITE-ProRule annotationAdd BLAST155
Domaini2066 – 2221F5/8 type C 2PROSITE-ProRule annotationAdd BLAST156

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>Regioni692 – 1573BAdd BLAST882
Regioni895 – 9282 X 17 AA tandem repeatsAdd BLAST34
Regioni1185 – 150135 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-TAdd BLAST317

<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

Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA repeats.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IJ6Y Eukaryota
ENOG4111F6G LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158556

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005631

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P12259

KEGG Orthology (KO)

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KOi
K03902

Database for complete collections of gene phylogenies

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PhylomeDBi
P12259

TreeFam database of animal gene trees

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TreeFami
TF329807

Family and domain databases

Conserved Domains Database

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CDDi
cd00057 FA58C, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.260, 2 hits
2.60.40.420, 5 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011707 Cu-oxidase_3
IPR033138 Cu_oxidase_CS
IPR008972 Cupredoxin
IPR000421 FA58C
IPR024715 Factor_5/8_like
IPR008979 Galactose-bd-like_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF07732 Cu-oxidase_3, 2 hits
PF00754 F5_F8_type_C, 2 hits

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000354 Factors_V_VIII, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00231 FA58C, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49503 SSF49503, 6 hits
SSF49785 SSF49785, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01285 FA58C_1, 2 hits
PS01286 FA58C_2, 2 hits
PS50022 FA58C_3, 2 hits
PS00079 MULTICOPPER_OXIDASE1, 2 hits

<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 1 potential isoform that is computationally mapped.Show allAlign All

P12259-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT
60 70 80 90 100
NSSLNLSVTS FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV
110 120 130 140 150
HFKNKADKPL SIHPQGIRYS KLSEGASYLD HTFPAEKMDD AVAPGREYTY
160 170 180 190 200
EWSISEDSGP THDDPPCLTH IYYSHENLIE DFNSGLIGPL LICKKGTLTE
210 220 230 240 250
GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG TMPDITVCAH
260 270 280 290 300
DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV
310 320 330 340 350
GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW
360 370 380 390 400
EYFIAAEEVI WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE
410 420 430 440 450
DESFTKHTVN PNMKEDGILG PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV
460 470 480 490 500
TFSPYEDEVN SSFTSGRNNT MIRAVQPGET YTYKWNILEF DEPTENDAQC
510 520 530 540 550
LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA DIEQQAVFAV
560 570 580 590 600
FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL
610 620 630 640 650
GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES
660 670 680 690 700
VTVTMDNVGT WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE
710 720 730 740 750
STVMATRKMH DRLEPEDEES DADYDYQNRL AAALGIRSFR NSSLNQEEEE
760 770 780 790 800
FNLTALALEN GTEFVSSNTD IIVGSNYSSP SNISKFTVNN LAEPQKAPSH
810 820 830 840 850
QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL QPDVTGIRLL
860 870 880 890 900
SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS
910 920 930 940 950
PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA
960 970 980 990 1000
SEKGSYEIIQ DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK
1010 1020 1030 1040 1050
FPRVRHKSLQ VRQDGGKSRL KKSQFLIKTR KKKKEKHTHH APLSPRTFHP
1060 1070 1080 1090 1100
LRSEAYNTFS ERRLKHSLVL HKSNETSLPT DLNQTLPSMD FGWIASLPDH
1110 1120 1130 1140 1150
NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS TSDPSHRSSS
1160 1170 1180 1190 1200
PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS
1210 1220 1230 1240 1250
QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS
1260 1270 1280 1290 1300
LDLSQTNLSP ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH
1310 1320 1330 1340 1350
MTLSPELSQT NLSPALGQMP ISPDLSHTTL SLDFSQTNLS PELSQTNLSP
1360 1370 1380 1390 1400
ALGQMPLSPD PSHTTLSLDL SQTNLSPELS QTNLSPDLSE MPLFADLSQI
1410 1420 1430 1440 1450
PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP DISDTTLLPD
1460 1470 1480 1490 1500
LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND
1510 1520 1530 1540 1550
TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY
1560 1570 1580 1590 1600
KTDVRTNINS SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE
1610 1620 1630 1640 1650
TDIEDSDDIP EDTTYKKVVF RKYLDSTFTK RDPRGEYEEH LGILGPIIRA
1660 1670 1680 1690 1700
EVDDVIQVRF KNLASRPYSL HAHGLSYEKS SEGKTYEDDS PEWFKEDNAV
1710 1720 1730 1740 1750
QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI HSGLIGPLLI
1760 1770 1780 1790 1800
CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK
1810 1820 1830 1840 1850
KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL
1860 1870 1880 1890 1900
ENGNKQHQLG VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF
1910 1920 1930 1940 1950
LIMDRDCRMP MGLSTGIISD SQIKASEFLG YWEPRLARLN NGGSYNAWSV
1960 1970 1980 1990 2000
EKLAAEFASK PWIQVDMQKE VIITGIQTQG AKHYLKSCYT TEFYVAYSSN
2010 2020 2030 2040 2050
QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY IRISPTRAYN
2060 2070 2080 2090 2100
RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR
2110 2120 2130 2140 2150
ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV
2160 2170 2180 2190 2200
KSYTIHYSEQ GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF
2210 2220
IRVIPKTWNQ SIALRLELFG CDIY
Length:2,224
Mass (Da):251,703
Last modified:October 5, 2010 - v4
<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:i24AEF3FEA7332E37
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MRJ7A0A0A0MRJ7_HUMAN
Coagulation factor V
F5
2,229Annotation 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 ABD23003 differs from that shown. Reason: Erroneous gene model prediction.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 conflicti741N → S in ABD23003 (Ref. 7) Curated1
Sequence conflicti908E → K in AAA52424 (PubMed:3110773).Curated1
Sequence conflicti908E → K in CAC82573 (PubMed:11758222).Curated1
Sequence conflicti991K → E in BAF84302 (PubMed:14702039).Curated1
Sequence conflicti2213A → T in AAA52424 (PubMed:3110773).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02129715G → S1 PublicationCorresponds to variant dbSNP:rs9332485EnsemblClinVar.1
Natural variantiVAR_013886107D → H2 PublicationsCorresponds to variant dbSNP:rs6019EnsemblClinVar.1
Natural variantiVAR_013620334R → G in Hong Kong; does not predispose to clinical thrombosis. 2 PublicationsCorresponds to variant dbSNP:rs118203905EnsemblClinVar.1
Natural variantiVAR_013621334R → T in THPH2; Cambridge. 1 PublicationCorresponds to variant dbSNP:rs118203906EnsemblClinVar.1
Natural variantiVAR_032698387I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 PublicationsCorresponds to variant dbSNP:rs118203911EnsemblClinVar.1
Natural variantiVAR_013887413M → T2 PublicationsCorresponds to variant dbSNP:rs6033EnsemblClinVar.1
Natural variantiVAR_013622513R → K4 PublicationsCorresponds to variant dbSNP:rs6020EnsemblClinVar.1
Natural variantiVAR_001213534R → Q in THPH2; factor V Leiden; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. 5 PublicationsCorresponds to variant dbSNP:rs6025EnsemblClinVar.1
Natural variantiVAR_032699613C → R in THPH2; Nijkerk. 1 PublicationCorresponds to variant dbSNP:rs1453479152Ensembl.1
Natural variantiVAR_035817775S → A in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_047740781S → R. Corresponds to variant dbSNP:rs13306350Ensembl.1
Natural variantiVAR_013888809P → S2 PublicationsCorresponds to variant dbSNP:rs6031EnsemblClinVar.1
Natural variantiVAR_013889817N → T2 PublicationsCorresponds to variant dbSNP:rs6018EnsemblClinVar.1
Natural variantiVAR_001214858K → R5 PublicationsCorresponds to variant dbSNP:rs4524EnsemblClinVar.1
Natural variantiVAR_001215865H → R5 PublicationsCorresponds to variant dbSNP:rs4525EnsemblClinVar.1
Natural variantiVAR_021298915T → S1 PublicationCorresponds to variant dbSNP:rs9332695EnsemblClinVar.1
Natural variantiVAR_013890925K → E5 PublicationsCorresponds to variant dbSNP:rs6032EnsemblClinVar.1
Natural variantiVAR_021299969N → S1 PublicationCorresponds to variant dbSNP:rs9332604EnsemblClinVar.1
Natural variantiVAR_021300980R → L1 PublicationCorresponds to variant dbSNP:rs9332605Ensembl.1
Natural variantiVAR_0138911146H → Q2 PublicationsCorresponds to variant dbSNP:rs6005EnsemblClinVar.1
Natural variantiVAR_0138921285L → I3 PublicationsCorresponds to variant dbSNP:rs1046712EnsemblClinVar.1
Natural variantiVAR_0138931327H → R2 PublicationsCorresponds to variant dbSNP:rs1800595EnsemblClinVar.1
Natural variantiVAR_0477411397L → F2 PublicationsCorresponds to variant dbSNP:rs13306334EnsemblClinVar.1
Natural variantiVAR_0213011404P → S1 PublicationCorresponds to variant dbSNP:rs9332608EnsemblClinVar.1
Natural variantiVAR_0138941530E → A2 PublicationsCorresponds to variant dbSNP:rs6007Ensembl.1
Natural variantiVAR_0138951685T → S1 PublicationCorresponds to variant dbSNP:rs6011EnsemblClinVar.1
Natural variantiVAR_0327001730Y → C in FA5D; Seoul 2. 2 PublicationsCorresponds to variant dbSNP:rs118203907EnsemblClinVar.1
Natural variantiVAR_0138961749L → V1 PublicationCorresponds to variant dbSNP:rs6034Ensembl.1
Natural variantiVAR_0138971764M → V3 PublicationsCorresponds to variant dbSNP:rs6030EnsemblClinVar.1
Natural variantiVAR_0138981820M → I1 PublicationCorresponds to variant dbSNP:rs6026EnsemblClinVar.1
Natural variantiVAR_0327012102R → C in FA5D; impairs both factor V secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs118203910EnsemblClinVar.1
Natural variantiVAR_0173292102R → H in THPH2. 1 Publication1
Natural variantiVAR_0213022148M → T1 PublicationCorresponds to variant dbSNP:rs9332701EnsemblClinVar.1
Natural variantiVAR_0346032185K → R. Corresponds to variant dbSNP:rs6679078Ensembl.1
Natural variantiVAR_0138992222D → G1 PublicationCorresponds to variant dbSNP:rs6027EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M16967 mRNA Translation: AAA52424.1
L32779
, L32755, L32756, L32757, L32758, L32759, L32760, L32761, L32762, L32763, L32764, L32765, L32766, L32767, L32768, L32769, L32770, L32771, L32772, L32773, L32774, L32775, L32776, L32777, L32778 Genomic DNA Translation: AAB59401.1
AY364535 Genomic DNA Translation: AAQ55063.1
Z99572 Genomic DNA No translation available.
AK291613 mRNA Translation: BAF84302.1
M14335 mRNA Translation: AAB59532.1
DQ377944 Genomic DNA Translation: ABD23003.1 Sequence problems.
AJ297255 mRNA Translation: CAC82573.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1281.1

Protein sequence database of the Protein Information Resource

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PIRi
A56172 KFHU5

NCBI Reference Sequences

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RefSeqi
NP_000121.2, NM_000130.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.30054

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000367797; ENSP00000356771; ENSG00000198734

Database of genes from NCBI RefSeq genomes

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GeneIDi
2153

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2153

UCSC genome browser

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UCSCi
uc001ggg.2 human

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

Wikipedia

Factor V entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16967 mRNA Translation: AAA52424.1
L32779
, L32755, L32756, L32757, L32758, L32759, L32760, L32761, L32762, L32763, L32764, L32765, L32766, L32767, L32768, L32769, L32770, L32771, L32772, L32773, L32774, L32775, L32776, L32777, L32778 Genomic DNA Translation: AAB59401.1
AY364535 Genomic DNA Translation: AAQ55063.1
Z99572 Genomic DNA No translation available.
AK291613 mRNA Translation: BAF84302.1
M14335 mRNA Translation: AAB59532.1
DQ377944 Genomic DNA Translation: ABD23003.1 Sequence problems.
AJ297255 mRNA Translation: CAC82573.1
CCDSiCCDS1281.1
PIRiA56172 KFHU5
RefSeqiNP_000121.2, NM_000130.4
UniGeneiHs.30054

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CZSX-ray1.90A2065-2224[»]
1CZTX-ray1.87A2065-2224[»]
1CZVX-ray2.40A/B2065-2224[»]
1FV4model-H29-691[»]
L1574-2224[»]
1Y61model-H29-737[»]
L1574-2224[»]
3P6ZX-ray1.70C/I685-737[»]
3P70X-ray2.55M/N/O/P685-737[»]
3S9CX-ray1.80B1561-1574[»]
ProteinModelPortaliP12259
SMRiP12259
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108452, 13 interactors
DIPiDIP-47331N
IntActiP12259, 3 interactors
MINTiP12259
STRINGi9606.ENSP00000356771

Chemistry databases

BindingDBiP12259
ChEMBLiCHEMBL3618
DrugBankiDB00055 Drotrecogin alfa
DB05777 Thrombomodulin Alfa

PTM databases

CarbonylDBiP12259
GlyConnecti1120
iPTMnetiP12259
PhosphoSitePlusiP12259

Polymorphism and mutation databases

BioMutaiF5
DMDMi308153653

Proteomic databases

MaxQBiP12259
PaxDbiP12259
PeptideAtlasiP12259
PRIDEiP12259
ProteomicsDBi52838

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2153
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367797; ENSP00000356771; ENSG00000198734
GeneIDi2153
KEGGihsa:2153
UCSCiuc001ggg.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2153
DisGeNETi2153
EuPathDBiHostDB:ENSG00000198734.10

GeneCards: human genes, protein and diseases

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GeneCardsi
F5
GeneReviewsiF5
HGNCiHGNC:3542 F5
HPAiHPA002036
MalaCardsiF5
MIMi188055 phenotype
227400 phenotype
600880 phenotype
601367 phenotype
612309 gene
614389 phenotype
neXtProtiNX_P12259
OpenTargetsiENSG00000198734
Orphaneti131 Budd-Chiari syndrome
329217 Cerebral sinovenous thrombosis
326 Congenital factor V deficiency
391320 East Texas bleeding disorder
64738 NON RARE IN EUROPE: Non rare thrombophilia
PharmGKBiPA159

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IJ6Y Eukaryota
ENOG4111F6G LUCA
GeneTreeiENSGT00940000158556
HOVERGENiHBG005631
InParanoidiP12259
KOiK03902
PhylomeDBiP12259
TreeFamiTF329807

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-204005 COPII-mediated vesicle transport
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-5694530 Cargo concentration in the ER
R-HSA-8957275 Post-translational protein phosphorylation
SIGNORiP12259

Miscellaneous databases

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

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ChiTaRSi
F5 human
EvolutionaryTraceiP12259

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Factor_V

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

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GenomeRNAii
2153

Protein Ontology

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PROi
PR:P12259

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000198734 Expressed in 160 organ(s), highest expression level in right lobe of liver
CleanExiHS_F5
ExpressionAtlasiP12259 baseline and differential
GenevisibleiP12259 HS

Family and domain databases

CDDicd00057 FA58C, 2 hits
Gene3Di2.60.120.260, 2 hits
2.60.40.420, 5 hits
InterProiView protein in InterPro
IPR011707 Cu-oxidase_3
IPR033138 Cu_oxidase_CS
IPR008972 Cupredoxin
IPR000421 FA58C
IPR024715 Factor_5/8_like
IPR008979 Galactose-bd-like_sf
PfamiView protein in Pfam
PF07732 Cu-oxidase_3, 2 hits
PF00754 F5_F8_type_C, 2 hits
PIRSFiPIRSF000354 Factors_V_VIII, 1 hit
SMARTiView protein in SMART
SM00231 FA58C, 2 hits
SUPFAMiSSF49503 SSF49503, 6 hits
SSF49785 SSF49785, 2 hits
PROSITEiView protein in PROSITE
PS01285 FA58C_1, 2 hits
PS01286 FA58C_2, 2 hits
PS50022 FA58C_3, 2 hits
PS00079 MULTICOPPER_OXIDASE1, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiFA5_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: P12259
Secondary accession number(s): A8K6E8
, Q14285, Q2EHR5, Q5R346, Q5R347, Q6UPU6, Q8WWQ6
<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: October 1, 1989
Last sequence update: October 5, 2010
Last modified: December 5, 2018
This is version 223 of the entry and version 4 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, Reference proteome

Documents

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