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Protein

Coagulation factor X

Gene

F10

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

Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. EC:3.4.21.6

<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 and SERPINA10.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei276Charge relay system1
Active sitei322Charge relay system1
Active sitei419Charge relay system1

<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

  • calcium ion binding Source: InterPro
  • phospholipid binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: BHF-UCL

GO - Biological processi

  • blood coagulation Source: GO_Central
  • blood coagulation, extrinsic pathway Source: Reactome
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of protein kinase B signaling Source: BHF-UCL

<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

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS05000-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.4.21.6 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-140834 Extrinsic Pathway of Fibrin Clot Formation
R-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P00742

SIGNOR Signaling Network Open Resource

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SIGNORi
P00742

Protein family/group databases

MEROPS protease database

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MEROPSi
S01.216

<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 X (EC:3.4.21.6)
Alternative name(s):
Stuart factor
Stuart-Prower factor
Cleaved into the following 3 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:F10
<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 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000126218.11

Human Gene Nomenclature Database

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HGNCi
HGNC:3528 F10

Online Mendelian Inheritance in Man (OMIM)

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MIMi
613872 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P00742

<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 X deficiency (FA10D)21 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.
See also OMIM:227600
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_06542847E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 PublicationCorresponds to variant dbSNP:rs121964943Ensembl.1
Natural variantiVAR_06542951G → V in FA10D. 1 PublicationCorresponds to variant dbSNP:rs751782758Ensembl.1
Natural variantiVAR_06543054E → G in FA10D; Ketchikan. 1 PublicationCorresponds to variant dbSNP:rs121964944Ensembl.1
Natural variantiVAR_06543154E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 PublicationsCorresponds to variant dbSNP:rs121964939Ensembl.1
Natural variantiVAR_06543272E → Q in FA10D; Tokyo. 1 PublicationCorresponds to variant dbSNP:rs121964945Ensembl.1
Natural variantiVAR_06543391E → K in FA10D; Riyadh. 1 Publication1
Natural variantiVAR_065434142E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 PublicationsCorresponds to variant dbSNP:rs61753266EnsemblClinVar.1
Natural variantiVAR_065435149C → Y in FA10D. 1 Publication1
Natural variantiVAR_065436151C → Y in FA10D. 1 Publication1
Natural variantiVAR_075212176 – 186Missing in FA10D; unknown pathological significance. 1 PublicationAdd BLAST11
Natural variantiVAR_075213262G → D in FA10D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1393705267Ensembl.1
Natural variantiVAR_065437289G → R in FA10D; may affect splicing. 1 PublicationCorresponds to variant dbSNP:rs121964946Ensembl.1
Natural variantiVAR_065438304E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs747292771Ensembl.1
Natural variantiVAR_065439322D → N in FA10D; Stockton; 50% decrease in specific activity. 2 PublicationsCorresponds to variant dbSNP:rs121964942Ensembl.1
Natural variantiVAR_065440327R → W in FA10D. 1 PublicationCorresponds to variant dbSNP:rs770119164Ensembl.1
Natural variantiVAR_065441338V → M in FA10D. 1 PublicationCorresponds to variant dbSNP:rs121964947Ensembl.1
Natural variantiVAR_065442350E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs372309538Ensembl.1
Natural variantiVAR_065443358T → M in FA10D; Roma. 2 PublicationsCorresponds to variant dbSNP:rs768222784Ensembl.1
Natural variantiVAR_065444363G → S in FA10D. 1 Publication1
Natural variantiVAR_065445366R → C in FA10D; San Antonio. 1 PublicationCorresponds to variant dbSNP:rs104894392EnsemblClinVar.1
Natural variantiVAR_065446374S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 PublicationsCorresponds to variant dbSNP:rs121964941Ensembl.1
Natural variantiVAR_072751382V → A in FA10D; partial loss of activity. 2 Publications1
Natural variantiVAR_065447383P → S in FA10D; Friuli. 1 PublicationCorresponds to variant dbSNP:rs121964940Ensembl.1
Natural variantiVAR_065448390C → F in FA10D; Padua 4. 1 PublicationCorresponds to variant dbSNP:rs199778916Ensembl.1
Natural variantiVAR_065449404C → R in FA10D. 1 Publication1
Natural variantiVAR_065450406G → S in FA10D; almost complete loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs376163818Ensembl.1
Natural variantiVAR_065451420G → R in FA10D; Padua 3. 1 PublicationCorresponds to variant dbSNP:rs750759634Ensembl.1
Natural variantiVAR_072752421G → D in FA10D; significant loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs758726161Ensembl.1
Natural variantiVAR_065452448K → N in FA10D; San Giovanni Rotondo. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2159

MalaCards human disease database

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MalaCardsi
F10
MIMi227600 phenotype

Open Targets

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OpenTargetsi
ENSG00000126218

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

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Orphaneti
328 Congenital factor X deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27940

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL244

Drug and drug target database

More...
DrugBanki
DB07211 (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE
DB08746 1-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-4-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINE
DB07974 1-{2-[(4-CHLOROPHENYL)AMINO]-2-OXOETHYL}-N-(1-ISOPROPYLPIPERIDIN-4-YL)-1H-INDOLE-2-CARBOXAMIDE
DB07277 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE
DB07278 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE
DB08487 3-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB08495 4-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB04673 4-[(5-CHLOROINDOL-2-YL)SULFONYL]-2-(2-METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN-2-YL]CARBONYL]PIPERAZINE
DB08745 4-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-1-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINONE
DB08173 5-CHLORO-N-(2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO)ETHYL)THIOPHENE-2-CARBOXAMIDE
DB07872 5-chloro-N-[(3R)-1-(2-{[2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl]amino}-2-oxoethyl)pyrrolidin-3-yl]thiophene-2-carboxamide
DB07843 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB07847 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-(4-MORPHOLINYL)-2-OXO ETHYL]-2-OXO-3-PYRROLIDINYL}-2-NAPHTHALENESULFONAMIDE
DB07844 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB00025 Antihemophilic Factor (Recombinant)
DB06605 Apixaban
DB00100 Coagulation Factor IX (Recombinant)
DB13150 Coagulation factor VII human
DB00036 Coagulation factor VIIa Recombinant Human
DB09075 Edoxaban
DB01225 Enoxaparin
DB00569 Fondaparinux sodium
DB03847 Gamma-Carboxy-Glutamic Acid
DB01109 Heparin
DB05713 LY-517717
DB00170 Menadione
DB07973 N-(1-ISOPROPYLPIPERIDIN-4-YL)-1-(3-METHOXYBENZYL)-1H-INDOLE-2-CARBOXAMIDE
DB07800 N-(2-(((5-CHLORO-2-PYRIDINYL)AMINO)SULFONYL)PHENYL)-4-(2-OXO-1(2H)-PYRIDINYL)BENZAMIDE
DB06228 Rivaroxaban
DB05362 SSR-126517E

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2359

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
F10

Domain mapping of disease mutations (DMDM)

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DMDMi
119761

<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 – 31Sequence analysisAdd BLAST31
<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_000002778632 – 401 Publication9
<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_000002778741 – 488Coagulation factor XAdd BLAST448
ChainiPRO_000002778841 – 179Factor X light chainAdd BLAST139
ChainiPRO_0000027789183 – 488Factor X heavy chainAdd BLAST306
PropeptideiPRO_0000027790183 – 234Activation peptideAdd BLAST52
ChainiPRO_0000027791235 – 488Activated factor Xa heavy chainAdd BLAST254

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 residuei464-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotation1 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 bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi90 ↔ 101
Disulfide bondi95 ↔ 110
Modified residuei103(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi112 ↔ 121
Disulfide bondi129 ↔ 140
Disulfide bondi136 ↔ 149
Disulfide bondi151 ↔ 164
Disulfide bondi172 ↔ 342Interchain (between light and heavy chains)
<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>Glycosylationi199O-linked (GalNAc...) threonine1 Publication1
Glycosylationi211O-linked (GalNAc...) threonine1 Publication1
GlycosylationiCAR_000012221N-linked (GlcNAc...) asparagine1 Publication1
GlycosylationiCAR_000013231N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi241 ↔ 246
Disulfide bondi261 ↔ 277
Disulfide bondi390 ↔ 404
Disulfide bondi415 ↔ 443

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.2 Publications
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

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

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PaxDbi
P00742

PeptideAtlas

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PeptideAtlasi
P00742

PRoteomics IDEntifications database

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PRIDEi
P00742

ProteomicsDB human proteome resource

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ProteomicsDBi
51275

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
102

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00742

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

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PhosphoSitePlusi
P00742

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P00742

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P00742

<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; synthesized in the liver.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000126218 Expressed in 127 organ(s), highest expression level in right lobe of liver

CleanEx database of gene expression profiles

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CleanExi
HS_F10

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00742 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P00742 HS

<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

The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108457, 9 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P00742

Database of interacting proteins

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DIPi
DIP-29896N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P00742

Protein interaction database and analysis system

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IntActi
P00742, 12 interactors

Molecular INTeraction database

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MINTi
P00742

STRING: functional protein association networks

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STRINGi
9606.ENSP00000364709

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00742

<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

1488
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
P00742

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

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SMRi
P00742

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

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EvolutionaryTracei
P00742

<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>Domaini41 – 85GlaPROSITE-ProRule annotationAdd BLAST45
Domaini86 – 122EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini125 – 165EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini235 – 467Peptidase S1PROSITE-ProRule annotationAdd BLAST233

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>Regioni183 – 203O-glycosylated at one siteAdd BLAST21
Regioni476 – 485O-glycosylated at one site10

<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 peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IGPV Eukaryota
COG5640 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157694

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000251821

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG013304

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00742

KEGG Orthology (KO)

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KOi
K01314

Identification of Orthologs from Complete Genome Data

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OMAi
CAGYDAK

Database of Orthologous Groups

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OrthoDBi
EOG091G0AH5

Database for complete collections of gene phylogenies

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PhylomeDBi
P00742

TreeFam database of animal gene trees

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TreeFami
TF327329

Family and domain databases

Conserved Domains Database

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CDDi
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.740.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER

Pfam protein domain database

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Pfami
View protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001143 Factor_X, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00722 CHYMOTRYPSIN
PR00001 GLABLOOD

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 1 hit
PS01187 EGF_CA, 1 hit
PS00011 GLA_1, 1 hit
PS50998 GLA_2, 1 hit
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 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 3 potential isoforms that are computationally mapped.Show allAlign All

P00742-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK
60 70 80 90 100
GHLERECMEE TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK
110 120 130 140 150
CKDGLGEYTC TCLEGFEGKN CELFTRKLCS LDNGDCDQFC HEEQNSVVCS
160 170 180 190 200
CARGYTLADN GKACIPTGPY PCGKQTLERR KRSVAQATSS SGEAPDSITW
210 220 230 240 250
KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE CKDGECPWQA
260 270 280 290 300
LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE
310 320 330 340 350
AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE
360 370 380 390 400
STLMTQKTGI VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ
410 420 430 440 450
NMFCAGYDTK QEDACQGDSG GPHVTRFKDT YFVTGIVSWG EGCARKGKYG
460 470 480
IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE VITSSPLK
Length:488
Mass (Da):54,732
Last modified:October 1, 1989 - 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:iF81D5746AF4797AF
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JVE8Q5JVE8_HUMAN
Coagulation factor X
F10
332Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B7ZBK1B7ZBK1_HUMAN
Coagulation factor X
F10
334Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8WBM7F8WBM7_HUMAN
Coagulation factor X
F10
130Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti285 – 288KVRV → E in AAA51984 (PubMed:3011603).Curated4
Sequence conflicti285 – 288KVRV → E in AAA52486 (PubMed:6587384).Curated4
Sequence conflicti442G → S in AAA52490 (PubMed:2582420).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0141627L → I1 PublicationCorresponds to variant dbSNP:rs5963Ensembl.1
Natural variantiVAR_01416330Q → H1 PublicationCorresponds to variant dbSNP:rs5961EnsemblClinVar.1
Natural variantiVAR_06542847E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 PublicationCorresponds to variant dbSNP:rs121964943Ensembl.1
Natural variantiVAR_06542951G → V in FA10D. 1 PublicationCorresponds to variant dbSNP:rs751782758Ensembl.1
Natural variantiVAR_06543054E → G in FA10D; Ketchikan. 1 PublicationCorresponds to variant dbSNP:rs121964944Ensembl.1
Natural variantiVAR_06543154E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 PublicationsCorresponds to variant dbSNP:rs121964939Ensembl.1
Natural variantiVAR_06543272E → Q in FA10D; Tokyo. 1 PublicationCorresponds to variant dbSNP:rs121964945Ensembl.1
Natural variantiVAR_06543391E → K in FA10D; Riyadh. 1 Publication1
Natural variantiVAR_065434142E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 PublicationsCorresponds to variant dbSNP:rs61753266EnsemblClinVar.1
Natural variantiVAR_065435149C → Y in FA10D. 1 Publication1
Natural variantiVAR_065436151C → Y in FA10D. 1 Publication1
Natural variantiVAR_020176152A → T1 PublicationCorresponds to variant dbSNP:rs3211772Ensembl.1
Natural variantiVAR_075212176 – 186Missing in FA10D; unknown pathological significance. 1 PublicationAdd BLAST11
Natural variantiVAR_020177192G → R1 PublicationCorresponds to variant dbSNP:rs3211783EnsemblClinVar.1
Natural variantiVAR_075213262G → D in FA10D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1393705267Ensembl.1
Natural variantiVAR_065437289G → R in FA10D; may affect splicing. 1 PublicationCorresponds to variant dbSNP:rs121964946Ensembl.1
Natural variantiVAR_065438304E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs747292771Ensembl.1
Natural variantiVAR_065439322D → N in FA10D; Stockton; 50% decrease in specific activity. 2 PublicationsCorresponds to variant dbSNP:rs121964942Ensembl.1
Natural variantiVAR_065440327R → W in FA10D. 1 PublicationCorresponds to variant dbSNP:rs770119164Ensembl.1
Natural variantiVAR_065441338V → M in FA10D. 1 PublicationCorresponds to variant dbSNP:rs121964947Ensembl.1
Natural variantiVAR_065442350E → K in FA10D. 1 PublicationCorresponds to variant dbSNP:rs372309538Ensembl.1
Natural variantiVAR_065443358T → M in FA10D; Roma. 2 PublicationsCorresponds to variant dbSNP:rs768222784Ensembl.1
Natural variantiVAR_065444363G → S in FA10D. 1 Publication1
Natural variantiVAR_065445366R → C in FA10D; San Antonio. 1 PublicationCorresponds to variant dbSNP:rs104894392EnsemblClinVar.1
Natural variantiVAR_065446374S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 PublicationsCorresponds to variant dbSNP:rs121964941Ensembl.1
Natural variantiVAR_072751382V → A in FA10D; partial loss of activity. 2 Publications1
Natural variantiVAR_065447383P → S in FA10D; Friuli. 1 PublicationCorresponds to variant dbSNP:rs121964940Ensembl.1
Natural variantiVAR_065448390C → F in FA10D; Padua 4. 1 PublicationCorresponds to variant dbSNP:rs199778916Ensembl.1
Natural variantiVAR_065449404C → R in FA10D. 1 Publication1
Natural variantiVAR_065450406G → S in FA10D; almost complete loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs376163818Ensembl.1
Natural variantiVAR_065451420G → R in FA10D; Padua 3. 1 PublicationCorresponds to variant dbSNP:rs750759634Ensembl.1
Natural variantiVAR_072752421G → D in FA10D; significant loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs758726161Ensembl.1
Natural variantiVAR_065452448K → N in FA10D; San Giovanni Rotondo. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K03194 mRNA Translation: AAA52490.1
M57285 mRNA Translation: AAA52421.1
AF503510 Genomic DNA Translation: AAM19347.1
BC046125 mRNA Translation: AAH46125.1
N00045
, L00390, L00391, L00392, L00393, L00394, L00395, L00396 Genomic DNA Translation: AAA52764.1
M22613 mRNA Translation: AAA51984.1
K01886 mRNA Translation: AAA52486.1
M33297 Genomic DNA Translation: AAA52636.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS9530.1

Protein sequence database of the Protein Information Resource

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PIRi
A24478 EXHU

NCBI Reference Sequences

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RefSeqi
NP_000495.1, NM_000504.3
NP_001299603.1, NM_001312674.1
NP_001299604.1, NM_001312675.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.361463

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000375559; ENSP00000364709; ENSG00000126218

Database of genes from NCBI RefSeq genomes

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GeneIDi
2159

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2159

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 X entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03194 mRNA Translation: AAA52490.1
M57285 mRNA Translation: AAA52421.1
AF503510 Genomic DNA Translation: AAM19347.1
BC046125 mRNA Translation: AAH46125.1
N00045
, L00390, L00391, L00392, L00393, L00394, L00395, L00396 Genomic DNA Translation: AAA52764.1
M22613 mRNA Translation: AAA51984.1
K01886 mRNA Translation: AAA52486.1
M33297 Genomic DNA Translation: AAA52636.1
CCDSiCCDS9530.1
PIRiA24478 EXHU
RefSeqiNP_000495.1, NM_000504.3
NP_001299603.1, NM_001312674.1
NP_001299604.1, NM_001312675.1
UniGeneiHs.361463

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
1C5MX-ray1.95D235-488[»]
F84-179[»]
1EZQX-ray2.20A235-488[»]
B46-179[»]
1F0RX-ray2.10A235-488[»]
B46-179[»]
1F0SX-ray2.10A235-488[»]
B46-179[»]
1FAXX-ray3.00A235-488[»]
L84-179[»]
1FJSX-ray1.92A235-468[»]
L127-178[»]
1FXYX-ray2.15A235-344[»]
1G2LX-ray1.90A235-469[»]
B86-179[»]
1G2MX-ray3.02A235-469[»]
B86-179[»]
1HCGX-ray2.20A235-475[»]
B129-179[»]
1IOEX-ray2.90A235-469[»]
L84-179[»]
1IQEX-ray2.90A235-469[»]
L84-179[»]
1IQFX-ray3.20A235-469[»]
L84-179[»]
1IQGX-ray2.60A235-469[»]
L84-179[»]
1IQHX-ray3.00A235-469[»]
L84-179[»]
1IQIX-ray2.90A235-469[»]
L84-179[»]
1IQJX-ray3.00A235-469[»]
L84-179[»]
1IQKX-ray3.20A235-469[»]
L84-179[»]
1IQLX-ray2.70A235-469[»]
L84-179[»]
1IQMX-ray2.60A235-469[»]
L84-179[»]
1IQNX-ray2.60A235-469[»]
L84-179[»]
1KSNX-ray2.10A235-488[»]
B46-179[»]
1LPGX-ray2.00A46-179[»]
B235-488[»]
1LPKX-ray2.20A46-179[»]
B235-488[»]
1LPZX-ray2.40A46-179[»]
B235-488[»]
1LQDX-ray2.70A46-179[»]
B235-488[»]
1MQ5X-ray2.10A235-467[»]
L127-177[»]
1MQ6X-ray2.10A235-467[»]
L127-177[»]
1MSXmodel-A235-469[»]
1NFUX-ray2.05A235-488[»]
B46-240[»]
1NFWX-ray2.10A235-488[»]
B46-179[»]
1NFXX-ray2.15A235-488[»]
B46-179[»]
1NFYX-ray2.10A235-488[»]
B46-179[»]
1NL8model-F235-469[»]
L41-179[»]
1P0SX-ray2.80H235-488[»]
L41-178[»]
1V3XX-ray2.20A235-467[»]
B127-178[»]
1WU1X-ray2.30A235-467[»]
B85-179[»]
1XKAX-ray2.30C235-469[»]
L85-179[»]
1XKBX-ray2.40A/B85-179[»]
C/D235-469[»]
1Z6EX-ray1.80A235-468[»]
L127-178[»]
2BMGX-ray2.70A126-178[»]
B235-468[»]
2BOHX-ray2.20A46-179[»]
B235-488[»]
2BOKX-ray1.64A235-475[»]
L126-180[»]
2BQ6X-ray3.00A126-177[»]
B220-468[»]
2BQ7X-ray2.20A126-177[»]
B220-468[»]
2BQWX-ray2.95A126-177[»]
B220-468[»]
2CJIX-ray2.10A235-488[»]
B46-179[»]
2D1JX-ray2.20A235-467[»]
B125-178[»]
2EI6X-ray2.30A235-467[»]
B125-178[»]
2EI7X-ray2.30A235-467[»]
B125-178[»]
2EI8X-ray2.10A235-467[»]
B125-178[»]
2FZZX-ray2.20A235-468[»]
L127-178[»]
2G00X-ray2.10A235-468[»]
L127-178[»]
2GD4X-ray3.30A/L126-182[»]
B/H235-475[»]
2H9EX-ray2.20H235-467[»]
L86-234[»]
2J2UX-ray1.90A235-488[»]
B46-179[»]
2J34X-ray2.01A235-488[»]
B46-179[»]
2J38X-ray2.10A235-488[»]
B46-179[»]
2J4IX-ray1.80A235-488[»]
B46-179[»]
2J94X-ray2.10A235-488[»]
B46-179[»]
2J95X-ray2.01A235-488[»]
B46-179[»]
2JKHX-ray1.25A235-475[»]
L126-180[»]
2P16X-ray2.30A235-468[»]
L127-178[»]
2P3FX-ray3.10H235-469[»]
L125-178[»]
2P3TX-ray1.92A127-178[»]
B235-467[»]
2P3UX-ray1.62A127-178[»]
B235-467[»]
2P93X-ray1.90A235-468[»]
L127-178[»]
2P94X-ray1.80A235-468[»]
L127-178[»]
2P95X-ray2.20A235-468[»]
L127-178[»]
2PHBX-ray2.30A235-468[»]
B128-178[»]
2PR3X-ray1.50A235-468[»]
B128-178[»]
2Q1JX-ray1.90A235-468[»]
B128-178[»]
2RA0X-ray2.30A235-468[»]
L128-178[»]
2UWLX-ray1.90A235-488[»]
B46-179[»]
2UWOX-ray1.75A235-488[»]
B46-179[»]
2UWPX-ray1.75A235-488[»]
B46-179[»]
2VH0X-ray1.70A235-488[»]
B46-179[»]
2VH6X-ray1.95A235-488[»]
B46-177[»]
2VVCX-ray1.95A/B235-475[»]
K/L126-180[»]
2VVUX-ray2.30A235-475[»]
L126-180[»]
2VVVX-ray1.73A235-475[»]
L126-180[»]
2VWLX-ray1.80A235-475[»]
L126-180[»]
2VWMX-ray1.96A/B235-475[»]
K/L126-180[»]
2VWNX-ray1.61A235-475[»]
L126-180[»]
2VWOX-ray1.60A235-475[»]
L126-180[»]
2W26X-ray2.08A235-468[»]
B129-177[»]
2W3IX-ray1.90A235-468[»]
B128-178[»]
2W3KX-ray2.05A235-468[»]
B128-178[»]
2WYGX-ray1.88A235-487[»]
B46-179[»]
2WYJX-ray2.38A235-488[»]
B46-179[»]
2XBVX-ray1.66A235-475[»]
L126-180[»]
2XBWX-ray1.72A235-475[»]
L126-180[»]
2XBXX-ray1.85A235-475[»]
L126-180[»]
2XBYX-ray2.02A235-475[»]
L126-180[»]
2XC0X-ray2.05A235-475[»]
L126-180[»]
2XC4X-ray1.67A235-475[»]
L126-180[»]
2XC5X-ray1.70A235-475[»]
L126-180[»]
2Y5FX-ray1.29A235-468[»]
L127-180[»]
2Y5GX-ray1.29A235-468[»]
L127-180[»]
2Y5HX-ray1.33A235-468[»]
L127-180[»]
2Y7XX-ray1.90A235-488[»]
B46-179[»]
2Y7ZX-ray1.84A235-488[»]
B46-179[»]
2Y80X-ray1.90A235-488[»]
B46-179[»]
2Y81X-ray1.70A235-488[»]
B46-179[»]
2Y82X-ray2.20A235-488[»]
B46-179[»]
3CENX-ray1.60A235-468[»]
L127-178[»]
3CS7X-ray2.20A235-468[»]
L127-178[»]
3ENSX-ray2.30A/C85-178[»]
B/D235-472[»]
3FFGX-ray1.54A235-468[»]
L127-178[»]
3HPTX-ray2.19A/C85-178[»]
B/D235-472[»]
3IITX-ray1.80A235-467[»]
B125-178[»]
3K9XX-ray1.90A/C85-178[»]
B/D235-472[»]
3KL6X-ray1.45A235-475[»]
B126-179[»]
3KQBX-ray2.25A235-468[»]
L127-178[»]
3KQCX-ray2.20A235-468[»]
L127-178[»]
3KQDX-ray2.75A235-468[»]
L127-178[»]
3KQEX-ray2.35A235-468[»]
L127-178[»]
3LIWX-ray2.22A235-468[»]
B128-178[»]
3M36X-ray2.15A235-468[»]
L127-178[»]
3M37X-ray1.90A235-468[»]
L127-178[»]
3Q3KX-ray2.00A235-467[»]
B125-178[»]
3SW2X-ray2.42A85-178[»]
B235-472[»]
3TK5X-ray2.20A235-467[»]
B125-178[»]
3TK6X-ray1.80A235-467[»]
B125-178[»]
4A7IX-ray2.40A84-179[»]
B235-488[»]
4BTIX-ray2.30A/E84-179[»]
B/F235-488[»]
4BTTX-ray2.59A/E84-179[»]
B/F235-488[»]
4BTUX-ray2.37A/E84-179[»]
B/F235-488[»]
4Y6DX-ray1.55A235-488[»]
B46-179[»]
4Y71X-ray1.80A235-488[»]
B46-179[»]
4Y76X-ray2.00A235-488[»]
B46-179[»]
4Y79X-ray2.10A235-488[»]
B46-179[»]
4Y7AX-ray1.99A235-488[»]
B46-179[»]
4Y7BX-ray1.79A235-488[»]
B46-179[»]
4ZH8X-ray1.80A235-488[»]
B46-179[»]
4ZHAX-ray1.86A235-488[»]
B46-179[»]
5JQYX-ray1.99B86-124[»]
5JTCX-ray2.24B86-124[»]
5JZ8X-ray2.10B86-124[»]
5JZUX-ray2.50B86-111[»]
5JZZX-ray2.29B102-119[»]
5K0HX-ray2.20A235-468[»]
B128-178[»]
5VOEX-ray2.00H235-467[»]
L128-178[»]
5VOFX-ray2.25H235-467[»]
L128-178[»]
ProteinModelPortaliP00742
SMRiP00742
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108457, 9 interactors
CORUMiP00742
DIPiDIP-29896N
ELMiP00742
IntActiP00742, 12 interactors
MINTiP00742
STRINGi9606.ENSP00000364709

Chemistry databases

BindingDBiP00742
ChEMBLiCHEMBL244
DrugBankiDB07211 (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE
DB08746 1-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-4-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINE
DB07974 1-{2-[(4-CHLOROPHENYL)AMINO]-2-OXOETHYL}-N-(1-ISOPROPYLPIPERIDIN-4-YL)-1H-INDOLE-2-CARBOXAMIDE
DB07277 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE
DB07278 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE
DB08487 3-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB08495 4-({4-[(6-CHLORO-1-BENZOTHIEN-2-YL)SULFONYL]-2-OXOPIPERAZIN-1-YL}METHYL)BENZENECARBOXIMIDAMIDE
DB04673 4-[(5-CHLOROINDOL-2-YL)SULFONYL]-2-(2-METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN-2-YL]CARBONYL]PIPERAZINE
DB08745 4-[[(1E)-2-(4-CHLOROPHENYL)ETHENYL]SULFONYL]-1-[[1-(4-PYRIDINYL)-4-PIPERIDINYL]METHYL]PIPERAZINONE
DB08173 5-CHLORO-N-(2-(4-(2-OXOPYRIDIN-1(2H)-YL)BENZAMIDO)ETHYL)THIOPHENE-2-CARBOXAMIDE
DB07872 5-chloro-N-[(3R)-1-(2-{[2-fluoro-4-(2-oxopyridin-1(2H)-yl)phenyl]amino}-2-oxoethyl)pyrrolidin-3-yl]thiophene-2-carboxamide
DB07843 5-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB07847 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-(4-MORPHOLINYL)-2-OXO ETHYL]-2-OXO-3-PYRROLIDINYL}-2-NAPHTHALENESULFONAMIDE
DB07844 6-CHLORO-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}-1-BENZOTHIOPHENE-2-SULFONAMIDE
DB00025 Antihemophilic Factor (Recombinant)
DB06605 Apixaban
DB00100 Coagulation Factor IX (Recombinant)
DB13150 Coagulation factor VII human
DB00036 Coagulation factor VIIa Recombinant Human
DB09075 Edoxaban
DB01225 Enoxaparin
DB00569 Fondaparinux sodium
DB03847 Gamma-Carboxy-Glutamic Acid
DB01109 Heparin
DB05713 LY-517717
DB00170 Menadione
DB07973 N-(1-ISOPROPYLPIPERIDIN-4-YL)-1-(3-METHOXYBENZYL)-1H-INDOLE-2-CARBOXAMIDE
DB07800 N-(2-(((5-CHLORO-2-PYRIDINYL)AMINO)SULFONYL)PHENYL)-4-(2-OXO-1(2H)-PYRIDINYL)BENZAMIDE
DB06228 Rivaroxaban
DB05362 SSR-126517E
GuidetoPHARMACOLOGYi2359

Protein family/group databases

MEROPSiS01.216

PTM databases

GlyConnecti102
iPTMnetiP00742
PhosphoSitePlusiP00742
UniCarbKBiP00742

Polymorphism and mutation databases

BioMutaiF10
DMDMi119761

Proteomic databases

PaxDbiP00742
PeptideAtlasiP00742
PRIDEiP00742
ProteomicsDBi51275

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375559; ENSP00000364709; ENSG00000126218
GeneIDi2159
KEGGihsa:2159

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2159
DisGeNETi2159
EuPathDBiHostDB:ENSG00000126218.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
F10
HGNCiHGNC:3528 F10
MalaCardsiF10
MIMi227600 phenotype
613872 gene
neXtProtiNX_P00742
OpenTargetsiENSG00000126218
Orphaneti328 Congenital factor X deficiency
PharmGKBiPA27940

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IGPV Eukaryota
COG5640 LUCA
GeneTreeiENSGT00940000157694
HOGENOMiHOG000251821
HOVERGENiHBG013304
InParanoidiP00742
KOiK01314
OMAiCAGYDAK
OrthoDBiEOG091G0AH5
PhylomeDBiP00742
TreeFamiTF327329

Enzyme and pathway databases

BioCyciMetaCyc:HS05000-MONOMER
BRENDAi3.4.21.6 2681
ReactomeiR-HSA-140834 Extrinsic Pathway of Fibrin Clot Formation
R-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
SABIO-RKiP00742
SIGNORiP00742

Miscellaneous databases

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

More...
ChiTaRSi
F10 human
EvolutionaryTraceiP00742

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Factor_X

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

More...
GenomeRNAii
2159
PMAP-CutDBiP00742

Protein Ontology

More...
PROi
PR:P00742

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000126218 Expressed in 127 organ(s), highest expression level in right lobe of liver
CleanExiHS_F10
ExpressionAtlasiP00742 baseline and differential
GenevisibleiP00742 HS

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 1 hit
PS01187 EGF_CA, 1 hit
PS00011 GLA_1, 1 hit
PS50998 GLA_2, 1 hit
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 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 nameiFA10_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: P00742
Secondary accession number(s): Q14340
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: December 5, 2018
This is version 249 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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