UniProtKB - P08709 (FA7_HUMAN)
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>sp|P08709|FA7_HUMAN Coagulation factor VII OS=Homo sapiens OX=9606 GN=F7 PE=1 SV=1 MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRR ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGS CKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGG TLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTN HDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVL NVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTG IVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFPCommunity curation ()Add a publicationFeedback
Coagulation factor VII
F7
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>Select a section on the left to see content.
<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
Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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-|-Ile bond in factor X to form factor Xa. EC:3.4.21.21
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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>Sitei | 113 | Important for S-112 for O-xylosylation | 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei | 253 | Charge relay systemBy similarity | 1 | |
Active sitei | 302 | Charge relay systemBy similarity | 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 398 | SubstrateBy similarity | 1 | |
Active sitei | 404 | Charge relay systemBy similarity | 1 |
<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
- serine-type endopeptidase activity Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.2"Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation."
O'Hara P.J., Grant F.J., Haldeman B.A., Gray C.L., Insley M.Y., Hagen F.S., Murray M.J.
Proc. Natl. Acad. Sci. U.S.A. 84:5158-5162(1987) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
- serine-type peptidase activity Source: ProtIncTraceable author statementi
- Ref.2"Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation."
O'Hara P.J., Grant F.J., Haldeman B.A., Gray C.L., Insley M.Y., Hagen F.S., Murray M.J.
Proc. Natl. Acad. Sci. U.S.A. 84:5158-5162(1987) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
- signaling receptor binding Source: Ensembl
GO - Biological processi
- animal organ regeneration Source: Ensembl
- blood coagulation Source: BHF-UCL
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- "Structural integrity of the gamma-carboxyglutamic acid domain of human blood coagulation factor IXa Is required for its binding to cofactor VIIIa."
Larson P.J., Stanfield-Oakley S.A., VanDusen W.J., Kasper C.K., Smith K.J., Monroe D.M., High K.A.
J Biol Chem 271:3869-3876(1996) [PubMed] [Europe PMC] [Abstract]
- circadian rhythm Source: Ensembl
- positive regulation of blood coagulation Source: Ensembl
- positive regulation of cell migration Source: BHF-UCLTraceable author statementi
- "Formation of tissue factor-factor VIIa-factor Xa complex induces activation of the mTOR pathway which regulates migration of human breast cancer cells."
Jiang X., Zhu S., Panetti T.S., Bromberg M.E.
Thromb Haemost 100:127-133(2008) [PubMed] [Europe PMC] [Abstract]
- positive regulation of leukocyte chemotaxis Source: BHF-UCLInferred from direct assayi
- "TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC."
Siegbahn A., Johnell M., Nordin A., Aberg M., Velling T.
Arterioscler Thromb Vasc Biol 28:135-141(2008) [PubMed] [Europe PMC] [Abstract]
- positive regulation of platelet-derived growth factor receptor signaling pathway Source: BHF-UCLInferred from direct assayi
- "TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC."
Siegbahn A., Johnell M., Nordin A., Aberg M., Velling T.
Arterioscler Thromb Vasc Biol 28:135-141(2008) [PubMed] [Europe PMC] [Abstract]
- positive regulation of positive chemotaxis Source: BHF-UCLInferred from direct assayi
- "TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC."
Siegbahn A., Johnell M., Nordin A., Aberg M., Velling T.
Arterioscler Thromb Vasc Biol 28:135-141(2008) [PubMed] [Europe PMC] [Abstract]
- positive regulation of protein kinase B signaling Source: BHF-UCLInferred from direct assayi
- "Formation of tissue factor-factor VIIa-factor Xa complex induces activation of the mTOR pathway which regulates migration of human breast cancer cells."
Jiang X., Zhu S., Panetti T.S., Bromberg M.E.
Thromb Haemost 100:127-133(2008) [PubMed] [Europe PMC] [Abstract]
- protein processing Source: BHF-UCLInferred from direct assayi
- proteolysis Source: ComplexPortalInferred from direct assayi
- "Mechanism of the Ca2+-induced enhancement of the intrinsic factor VIIa activity."
Bjelke J.R., Olsen O.H., Fodje M., Svensson L.A., Bang S., Bolt G., Kragelund B.B., Persson E.
J Biol Chem 283:25863-25870(2008) [PubMed] [Europe PMC] [Abstract]
- response to 2,3,7,8-tetrachlorodibenzodioxine Source: Ensembl
- response to anticoagulant Source: Ensembl
- response to astaxanthin Source: Ensembl
- response to carbon dioxide Source: Ensembl
- response to cholesterol Source: Ensembl
- response to estradiol Source: Ensembl
- response to estrogen Source: Ensembl
- response to genistein Source: Ensembl
- response to growth hormone Source: Ensembl
- response to hypoxia Source: Ensembl
- response to Thyroid stimulating hormone Source: Ensembl
- response to thyrotropin-releasing hormone Source: Ensembl
- response to thyroxine Source: Ensembl
- response to vitamin K Source: Ensembl
<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 function | Hydrolase, Protease, Serine protease |
Biological process | Blood coagulation, Hemostasis |
Ligand | Calcium |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.21.21, 2681 |
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | P08709 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1368108, BMAL1:CLOCK,NPAS2 activates circadian gene expression R-HSA-140834, Extrinsic 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 More...SABIO-RKi | P08709 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P08709 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P08709 |
Protein family/group databases
MEROPS protease database More...MEROPSi | S01.215 |
<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%5Fand%5Ftaxonomy%5Fsection">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 VII (EC:3.4.21.21
Alternative name(s): Proconvertin Serum prothrombin conversion accelerator Short name: SPCA INN: Eptacog alfa Cleaved into the following 2 chains: |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:F7 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>Organismi | Homo sapiens (Human) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri | 9606 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:3544, F7 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613878, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08709 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000057593 |
<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
Endoplasmic reticulum
- endoplasmic reticulum lumen Source: Reactome
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
Golgi apparatus
- Golgi lumen Source: Reactome
Plasma Membrane
- plasma membrane Source: Reactome
Other locations
- collagen-containing extracellular matrix Source: BHF-UCLInferred from high throughput direct assayi
- "Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver."
Naba A., Clauser K.R., Whittaker C.A., Carr S.A., Tanabe K.K., Hynes R.O.
BMC Cancer 14:518-518(2014) [PubMed] [Europe PMC] [Abstract]
- membrane Source: ComplexPortal
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- "Mechanism of the Ca2+-induced enhancement of the intrinsic factor VIIa activity."
Bjelke J.R., Olsen O.H., Fodje M., Svensson L.A., Bang S., Bolt G., Kragelund B.B., Persson E.
J Biol Chem 283:25863-25870(2008) [PubMed] [Europe PMC] [Abstract]
- protein-containing complex Source: ComplexPortalInferred from physical interactioni
- "Design and Synthesis of Novel Meta-Linked Phenylglycine Macrocyclic FVIIa Inhibitors."
Richter J.M., Cheney D.L., Bates J.A., Wei A., Luettgen J.M., Rendina A.R., Harper T.M., Narayanan R., Wong P.C., Seiffert D., Wexler R.R., Priestley E.S.
ACS Med Chem Lett 8:67-72(2017) [PubMed] [Europe PMC] [Abstract]
- serine-type endopeptidase complex Source: ComplexPortalInferred from physical interactioni
- "Mechanism of the Ca2+-induced enhancement of the intrinsic factor VIIa activity."
Bjelke J.R., Olsen O.H., Fodje M., Svensson L.A., Bang S., Bolt G., Kragelund B.B., Persson E.
J Biol Chem 283:25863-25870(2008) [PubMed] [Europe PMC] [Abstract]
- serine-type peptidase complex Source: BHF-UCLInferred from physical interactioni
- vesicle Source: Ensembl
- collagen-containing extracellular matrix Source: BHF-UCLInferred from high throughput direct assayi
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 VII deficiency (FA7D)26 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.11"Molecular defects in CRM+ factor VII deficiencies: modelling of missense mutations in the catalytic domain of FVII."
Bernardi F., Liney D.L., Patracchini P., Gemmati D., Legnani C., Arcieri P., Pinotti M., Redaelli R., Ballerini G., Pemberton S., Wacey A.I., Mariani G., Tuddenham E.G.D., Marchetti G.
Br. J. Haematol. 86:610-618(1994) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-412, VARIANTS FA7D ILE-358; GLN-364; PHE-370 AND ARG-402, VARIANT GLN-413. - Ref.21"Purification and characterization of factor VII 304-Gln: a variant molecule with reduced activity isolated from a clinically unaffected male."
O'Brien D.P., Gale K.M., Anderson J.S., McVey J.H., Miller G.J., Meade T.W., Tuddenham E.G.D.
Blood 78:132-140(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D GLN-364. - Ref.22"Detection of two missense mutations and characterization of a repeat polymorphism in the factor VII gene (F7)."
Marchetti G., Patracchini P., Gemmati D., Derosa V., Pinotti M., Rodorigo G., Casonato A., Girolami A., Bernardi F.
Hum. Genet. 89:497-502(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D GLN-364 AND PHE-370. - Ref.23"A missense mutation (178Cys-->Tyr) and two neutral dimorphisms (115His and 333Ser) in the human coagulation factor VII gene."
Marchetti G., Ferrati M., Patracchini P., Redaelli R., Bernardi F.
Hum. Mol. Genet. 2:1055-1056(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D TYR-238. - Ref.24"Detection of missense mutations by single-strand conformational polymorphism (SSCP) analysis in five dysfunctional variants of coagulation factor VII."
Takamiya O., Kemball-Cook G., Martin D.M.A., Cooper D.N., von Felten A., Meili E., Hahn I., Prangnell D.R., Lumley H., Tuddenham E.G.D., McVey J.H.
Hum. Mol. Genet. 2:1355-1359(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D GLN-139; TRP-139; ARG-160; GLU-197 AND GLN-364. - Ref.25"Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor."
Chaing S., Clarke B., Sridhara S., Chu K., Friedman P., Vandusen W., Roberts H.R., Blajchman M., Monroe D.M., High K.A.
Blood 83:3524-3535(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D GLN-139 AND GLN-212. - Ref.27"Topologically equivalent mutations causing dysfunctional coagulation factors VII (294Ala-->Val) and X (334Ser-->Pro)."
Bernardi F., Castaman G., Redaelli R., Pinotti M., Lunghi B., Rodeghiero F., Marchetti G.
Hum. Mol. Genet. 3:1175-1177(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D VAL-354. - Ref.28"Factor VII Mie: homozygous asymptomatic type I deficiency caused by an amino acid substitution of His (CAC) for Arg(247) (CGC) in the catalytic domain."
Ohiwa M., Hayashi T., Wada H., Minamikawa K., Shirakawa S., Suzuki K.
Thromb. Haemost. 71:773-777(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D HIS-307. - Ref.29"A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule."
Arbini A.A., Mannucci P.M., Bauer K.A.
Blood 87:5085-5094(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D MET-419. - Ref.30"Mutation pattern in clinically asymptomatic coagulation factor VII deficiency."
Bernardi F., Castaman G., Pinotti M., Ferraresi P., di Iasio M.G., Lunghi B., Rodeghiero F., Marchetti G.
Hum. Mutat. 8:108-115(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D TRP-283; LYS-325; VAL-358; GLN-364 AND GLU-402, VARIANT GLN-413. - Ref.31"Factor VII central. A novel mutation in the catalytic domain that reduces tissue factor binding, impairs activation by factor Xa, and abolishes amidolytic and coagulant activity."
Bharadwaj D., Iino M., Kontoyianni M., Smith K.J., Foster D.C., Kisiel W.
J. Biol. Chem. 271:30685-30691(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D SER-388, CHARACTERIZATION OF VARIANT FA7D SER-388. - Ref.32"Ala244Val is a common, probably ancient mutation causing factor VII deficiency in Moroccan and Iranian Jews."
Tamary H., Fromovich Y., Shalmon L., Reich Z., Dym O., Lanir N., Brenner B., Paz M., Luder A.S., Blau O., Korostishevsky M., Zaizov R., Seligsohn U.
Thromb. Haemost. 76:283-291(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D VAL-304. - Ref.33"Factor VII deficiency caused by a structural variant N57D of the first epidermal growth factor domain."
Leonard B.J., Chen Q., Blajchman M.A., Ofosu F.A., Sridhara S., Yang D., Clarke B.J.
Blood 91:142-148(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D ASP-117, CHARACTERIZATION OF VARIANT FA7D ASP-117. - Ref.34"Factor VII Morioka (FVII L-26P): a homozygous missense mutation in the signal sequence identified in a patient with factor VII deficiency."
Ozawa T., Takikawa Y., Niiya K., Ejiri N., Suzuki K., Sato S., Sakuragawa N.
Br. J. Haematol. 101:47-49(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D PRO-13. - Ref.35"Two new missense mutations (P134T and A244V) in the coagulation factor VII gene."
Alshinawi C., Scerri C., Galdies R., Aquilina A., Felice A.E.
Hum. Mutat. Suppl. 1:S189-S191(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D THR-194 AND VAL-304. - Ref.38"Two novel factor VII gene mutations in a Chinese family with factor VII deficiency."
Au W.Y., Lam C.C.K., Chan E.C., Kwong Y.L.
Br. J. Haematol. 111:143-145(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D GLY-389. - Ref.39"Molecular analysis of the genotype-phenotype relationship in factor VII deficiency."
Millar D.S., Kemball-Cook G., McVey J.H., Tuddenham E.G.D., Mumford A.D., Attock G.B., Reverter J.C., Lanir N., Parapia L.A., Reynaud J., Meili E., von Felton A., Martinowitz U., Prangnell D.R., Krawczak M., Cooper D.N.
Hum. Genet. 107:327-342(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D GLN-73; GLN-79; PHE-121; PRO-125; CYS-128; TRP-139; SER-151; VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302; THR-304; VAL-304; CYS-307; MET-332; VAL-354; ILE-358; PHE-370; GLY-389; SER-391 AND GLU-435. - Ref.40"Twenty two novel mutations of the factor VII gene in factor VII deficiency."
Wulff K., Herrmann F.H.
Hum. Mutat. 15:489-496(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D LEU-64; PRO-120; CYS-128; LYS-154; SER-157; ARG-160; ARG-195; GLN-212; ASP-216; TYR-254; THR-266; HIS-302; VAL-304; CYS-307; MET-312; LYS-325; PHE-341; VAL-354; ILE-358; ARG-363; PHE-370; HIS-403 AND MET-419. - Ref.42"Two double heterozygous mutations in the F7 gene show different manifestations."
Nagaizumi K., Inaba H., Suzuki T., Hatta Y., Hagiwara T., Amano K., Arai M., Fukutake K.
Br. J. Haematol. 119:1052-1058(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D LYS-85 AND GLN-408. - Ref.43"A patient homozygous for a Gly354Cys mutation in factor VII that results in severely impaired secretion of the molecule, but not complete deficiency."
Takamiya O., Hino K.
Br. J. Haematol. 124:336-342(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D CYS-414, CHARACTERIZATION OF VARIANT FA7D CYS-414. - Ref.44"Phenotypic and genotypic characterization of Factor VII deficiency patients from Western India."
Mota L., Shetty S., Idicula-Thomas S., Ghosh K.
Clin. Chim. Acta 409:106-111(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D ARG-82; ARG-177; THR-198; GLN-212; PRO-251; ARG-323; ARG-344; PHE-370; MET-384; GLU-398 AND ARG-408. - Ref.45"Factor VII deficiency: clinical manifestation of 717 subjects from Europe and Latin America with mutations in the factor 7 gene."
Herrmann F.H., Wulff K., Auerswald G., Schulman S., Astermark J., Batorova A., Kreuz W., Pollmann H., Ruiz-Saez A., De Bosch N., Salazar-Sanchez L.
Haemophilia 15:267-280(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D LEU-64; GLN-73; PHE-82; PHE-84 DEL; GLY-88; PRO-88; PRO-120; CYS-128; ASP-138; GLN-139; LYS-154; SER-156; SER-157; ARG-160; PHE-171; PRO-181; ASN-183; PHE-186; SER-189; LEU-194; THR-194; ARG-195; GLN-212; ASP-216; ASN-241; THR-251; ARG-254; TYR-254; PRO-264; THR-266; ASN-272; ASN-277; TRP-283; ILE-298; GLN-301; ASN-302; HIS-302; THR-304; VAL-304; CYS-307; HIS-307; MET-312; PHE-321; LYS-325; GLN-326; CYS-337; PHE-341; SER-343; SER-345; CYS-350; VAL-354; ILE-358; PRO-360; ARG-363; HIS-363; GLN-364; TRP-364; PHE-370; TRP-375; MET-384; THR-387; VAL-387; SER-388; CYS-391; SER-391; GLU-401; HIS-403; ASN-404; GLY-413; MET-419; PHE-422; ALA-425; CYS-425; THR-429; ASP-432; GLU-435 AND PHE-437. - Ref.46"Familial factor VII deficiency with foetal and neonatal fatal cerebral haemorrhage associated with homozygosis to Gly180Arg mutation."
Landau D., Rosenberg N., Zivelin A., Staretz-Chacham O., Kapelushnik J.
Haemophilia 15:774-778(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FA7D ARG-240. - Ref.47"Recurrent mutations and genotype-phenotype correlations in hereditary factor VII deficiency in Korea."
Kwon M.J., Yoo K.Y., Lee K.O., Kim S.H., Kim H.J.
Blood Coagul. Fibrinolysis 22:102-105(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FA7D ARG-59 INS; VAL-314; SER-343 AND GLY-389.
Bernardi F., Liney D.L., Patracchini P., Gemmati D., Legnani C., Arcieri P., Pinotti M., Redaelli R., Ballerini G., Pemberton S., Wacey A.I., Mariani G., Tuddenham E.G.D., Marchetti G.
Br. J. Haematol. 86:610-618(1994) [PubMed] [Europe PMC] [Abstract]
O'Brien D.P., Gale K.M., Anderson J.S., McVey J.H., Miller G.J., Meade T.W., Tuddenham E.G.D.
Blood 78:132-140(1991) [PubMed] [Europe PMC] [Abstract]
Marchetti G., Patracchini P., Gemmati D., Derosa V., Pinotti M., Rodorigo G., Casonato A., Girolami A., Bernardi F.
Hum. Genet. 89:497-502(1992) [PubMed] [Europe PMC] [Abstract]
Marchetti G., Ferrati M., Patracchini P., Redaelli R., Bernardi F.
Hum. Mol. Genet. 2:1055-1056(1993) [PubMed] [Europe PMC] [Abstract]
Takamiya O., Kemball-Cook G., Martin D.M.A., Cooper D.N., von Felten A., Meili E., Hahn I., Prangnell D.R., Lumley H., Tuddenham E.G.D., McVey J.H.
Hum. Mol. Genet. 2:1355-1359(1993) [PubMed] [Europe PMC] [Abstract]
Chaing S., Clarke B., Sridhara S., Chu K., Friedman P., Vandusen W., Roberts H.R., Blajchman M., Monroe D.M., High K.A.
Blood 83:3524-3535(1994) [PubMed] [Europe PMC] [Abstract]
Bernardi F., Castaman G., Redaelli R., Pinotti M., Lunghi B., Rodeghiero F., Marchetti G.
Hum. Mol. Genet. 3:1175-1177(1994) [PubMed] [Europe PMC] [Abstract]
Ohiwa M., Hayashi T., Wada H., Minamikawa K., Shirakawa S., Suzuki K.
Thromb. Haemost. 71:773-777(1994) [PubMed] [Europe PMC] [Abstract]
Arbini A.A., Mannucci P.M., Bauer K.A.
Blood 87:5085-5094(1996) [PubMed] [Europe PMC] [Abstract]
Bernardi F., Castaman G., Pinotti M., Ferraresi P., di Iasio M.G., Lunghi B., Rodeghiero F., Marchetti G.
Hum. Mutat. 8:108-115(1996) [PubMed] [Europe PMC] [Abstract]
Bharadwaj D., Iino M., Kontoyianni M., Smith K.J., Foster D.C., Kisiel W.
J. Biol. Chem. 271:30685-30691(1996) [PubMed] [Europe PMC] [Abstract]
Tamary H., Fromovich Y., Shalmon L., Reich Z., Dym O., Lanir N., Brenner B., Paz M., Luder A.S., Blau O., Korostishevsky M., Zaizov R., Seligsohn U.
Thromb. Haemost. 76:283-291(1996) [PubMed] [Europe PMC] [Abstract]
Leonard B.J., Chen Q., Blajchman M.A., Ofosu F.A., Sridhara S., Yang D., Clarke B.J.
Blood 91:142-148(1998) [PubMed] [Europe PMC] [Abstract]
Ozawa T., Takikawa Y., Niiya K., Ejiri N., Suzuki K., Sato S., Sakuragawa N.
Br. J. Haematol. 101:47-49(1998) [PubMed] [Europe PMC] [Abstract]
Alshinawi C., Scerri C., Galdies R., Aquilina A., Felice A.E.
Hum. Mutat. Suppl. 1:S189-S191(1998) [PubMed] [Europe PMC] [Abstract]
Au W.Y., Lam C.C.K., Chan E.C., Kwong Y.L.
Br. J. Haematol. 111:143-145(2000) [PubMed] [Europe PMC] [Abstract]
Millar D.S., Kemball-Cook G., McVey J.H., Tuddenham E.G.D., Mumford A.D., Attock G.B., Reverter J.C., Lanir N., Parapia L.A., Reynaud J., Meili E., von Felton A., Martinowitz U., Prangnell D.R., Krawczak M., Cooper D.N.
Hum. Genet. 107:327-342(2000) [PubMed] [Europe PMC] [Abstract]
Wulff K., Herrmann F.H.
Hum. Mutat. 15:489-496(2000) [PubMed] [Europe PMC] [Abstract]
Nagaizumi K., Inaba H., Suzuki T., Hatta Y., Hagiwara T., Amano K., Arai M., Fukutake K.
Br. J. Haematol. 119:1052-1058(2002) [PubMed] [Europe PMC] [Abstract]
Takamiya O., Hino K.
Br. J. Haematol. 124:336-342(2004) [PubMed] [Europe PMC] [Abstract]
Mota L., Shetty S., Idicula-Thomas S., Ghosh K.
Clin. Chim. Acta 409:106-111(2009) [PubMed] [Europe PMC] [Abstract]
Herrmann F.H., Wulff K., Auerswald G., Schulman S., Astermark J., Batorova A., Kreuz W., Pollmann H., Ruiz-Saez A., De Bosch N., Salazar-Sanchez L.
Haemophilia 15:267-280(2009) [PubMed] [Europe PMC] [Abstract]
Landau D., Rosenberg N., Zivelin A., Staretz-Chacham O., Kapelushnik J.
Haemophilia 15:774-778(2009) [PubMed] [Europe PMC] [Abstract]
Kwon M.J., Yoo K.Y., Lee K.O., Kim S.H., Kim H.J.
Blood Coagul. Fibrinolysis 22:102-105(2011) [PubMed] [Europe PMC] [Abstract]
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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_014391 | 13 | L → P in FA7D; Morioka. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065369 | 59 | R → RR in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015135 | 64 | F → L in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014405 | 73 | L → Q in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014406 | 79 | E → Q in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065370 | 82 | C → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065371 | 82 | C → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065372 | 84 | Missing in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065373 | 85 | E → K in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065374 | 88 | R → G in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065375 | 88 | R → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065376 | 117 | N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015136 | 120 | S → P in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014407 | 121 | C → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014408 | 125 | L → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014409 | 128 | Y → C in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065377 | 138 | G → D in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006497 | 139 | R → K in FA7D. | 1 | |
Natural variantiVAR_006498 | 139 | R → Q in FA7D; Charlotte. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006499 | 139 | R → W in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014410 | 151 | C → S in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015137 | 154 | E → K in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065378 | 156 | G → S in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006501 | 157 | G → C in FA7D. | 1 | |
Natural variantiVAR_006500 | 157 | G → S in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014411 | 157 | G → V in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006502 | 160 | Q → R in FA7D. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065379 | 171 | S → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065380 | 177 | G → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065381 | 181 | L → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065382 | 183 | D → N in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065383 | 186 | S → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065384 | 189 | P → S in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065385 | 194 | P → L in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006503 | 194 | P → T in FA7D; Malta-I. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014412 | 195 | C → R in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006504 | 197 | K → E in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065386 | 198 | I → T in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006505 | 212 | R → Q in FA7D; Charlotte. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015138 | 216 | G → D in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006506 | 238 | C → Y in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065387 | 240 | G → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014413 | 241 | T → N in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065388 | 250 | S → F in FA7D. 1 Publication Manual assertion based on experiment ini | 1 | |
Natural variantiVAR_065389 | 251 | A → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065390 | 251 | A → T in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065391 | 254 | C → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015139 | 254 | C → Y in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065392 | 264 | L → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015140 | 266 | A → T in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065393 | 272 | D → N in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065394 | 277 | D → N in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006507 | 283 | R → W in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065395 | 298 | T → I in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065396 | 301 | H → Q in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014414 | 302 | D → H in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014415 | 302 | D → N in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014416 | 304 | A → T in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006508 | 304 | A → V in FA7D; Malta-II. 5 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014417 | 307 | R → C in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006509 | 307 | R → H in FA7D; Mie. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015141 | 312 | V → M in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065397 | 314 | L → V in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065398 | 321 | L → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065399 | 323 | L → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006510 | 325 | E → K in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065400 | 326 | R → Q in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014418 | 332 | T → M in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065401 | 337 | R → C in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015142 | 341 | V → F in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065402 | 343 | G → S in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_076570 | 344 | W → G in FA7D. 1 Publication Manual assertion based on experiment ini | 1 | |
Natural variantiVAR_065403 | 344 | W → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065404 | 345 | G → S in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065405 | 350 | R → C in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006511 | 354 | A → V in FA7D. 5 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006512 | 358 | M → I in FA7D. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006513 | 358 | M → V in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065406 | 360 | L → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065407 | 363 | P → H in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015143 | 363 | P → R in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006514 | 364 | R → Q in FA7D; Harrow/Padua. 6 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065408 | 364 | R → W in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006515 | 370 | C → F in FA7D. 6 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065409 | 375 | R → W in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065410 | 384 | T → M in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065411 | 387 | M → T in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065412 | 387 | M → V in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065413 | 388 | F → S in FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014392 | 389 | C → G in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065414 | 391 | G → C in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014419 | 391 | G → S in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065415 | 398 | D → E in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065416 | 401 | K → E in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006517 | 402 | G → E in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006516 | 402 | G → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015144 | 403 | D → H in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065417 | 404 | S → N in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065418 | 408 | H → Q in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065419 | 408 | H → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065420 | 413 | R → G in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065421 | 414 | G → C in FA7D; results in severely impaired protein secretion. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006519 | 419 | T → M in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065422 | 422 | V → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065423 | 425 | G → A in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065424 | 425 | G → C in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065425 | 429 | A → T in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065426 | 432 | G → D in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014420 | 435 | G → E in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065427 | 437 | Y → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This subsection of the 'Pathology and Biotech' section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 112 | S → A: Complete loss of O-glycosylation and O-xylosylation by POGLUT1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 113 | S → A: No effect on O-glycosylation by POGLUT1. Drastic decrease in O-xylosylation. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNET More...DisGeNETi | 2155 |
MalaCards human disease database More...MalaCardsi | F7 |
MIMi | 227500, phenotype |
Open Targets More...OpenTargetsi | ENSG00000057593 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 327, Congenital factor VII deficiency |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA160 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | P08709, Tchem |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3991 |
Drug and drug target database More...DrugBanki | DB04590, (2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACID DB07207, 2-(4-HYDROXY-5-PHENYL-1H-PYRAZOL-3-YL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE DB04758, 2-[2-ETHANESULFONYLAMINO-3-(1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIM IDOYL-BENZYLAMIDE) DB04606, 2-[2-ETHANESULFONYLAMINO-3-(5-PROPOXY-1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIMIDOYL-BENZYLAMIDE) DB04593, 3-({1-[3-CARBAMIMIDOYL-1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-PROPYLCARBAMOYL]-2-METHYL-BUTYLSULFAMOYL}-METHYL)-BENZOIC ACID DB07376, 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID) DB07247, [2'-HYDROXY-3'-(1H-PYRROLO[3,2-C]PYRIDIN-2-YL)-BIPHENYL-3-YLMETHYL]-UREA DB08232, [5-(5-Amino-1H-pyrrolo[3,2-b]pyridin-2-yl)-6-hydroxy-3'-nitro-3-biphenylyl]acetic acid DB13151, Anti-inhibitor coagulant complex DB00100, Coagulation Factor IX (Recombinant) DB13152, Coagulation Factor IX Human DB00036, Coagulation factor VIIa Recombinant Human DB09332, Kappadione DB04767, N-[1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-3-METHYLSULFANYL-PROPYL]-3-HYDROXY-2-PROPOXYAMINO-BUTYRAMID DB13933, Nonacog beta pegol DB06552, rNAPc2 |
DrugCentral More...DrugCentrali | P08709 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2363 |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | F7 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 119766 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 peptidei | 1 – 20 | Sequence analysisAdd BLAST | 20 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_0000027729 | 21 – 60 | 1 Publication Manual assertion based on experiment ini
| 40 | |
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000027730 | 61 – 212 | Factor VII light chainAdd BLAST | 152 | |
ChainiPRO_0000027731 | 213 – 466 | Factor VII heavy chainAdd BLAST | 254 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 residuei | 66 | 4-carboxyglutamatePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Modified residuei | 67 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Modified residuei | 74 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Modified residuei | 76 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
<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 bondi | 77 ↔ 82 | |||
Modified residuei | 79 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| 1 | |
Modified residuei | 80 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Modified residuei | 85 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Modified residuei | 86 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Modified residuei | 89 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Modified residuei | 95 | 4-carboxyglutamatePROSITE-ProRule annotation Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
Disulfide bondi | 110 ↔ 121 | |||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>GlycosylationiCAR_000007 | 112 | O-linked (Glc...) serine; alternate4 Publications Manual assertion based on experiment ini
| 1 | |
Glycosylationi | 112 | O-linked (Xyl...) serine; alternate4 Publications Manual assertion based on experiment ini
| 1 | |
Disulfide bondi | 115 ↔ 130 | |||
GlycosylationiCAR_000180 | 120 | O-linked (Fuc) serine2 Publications Manual assertion based on experiment ini
| 1 | |
Modified residuei | 123 | (3R)-3-hydroxyaspartate1 Publication Manual assertion based on experiment ini
| 1 | |
Disulfide bondi | 132 ↔ 141 | |||
Disulfide bondi | 151 ↔ 162 | |||
Disulfide bondi | 158 ↔ 172 | |||
Disulfide bondi | 174 ↔ 187 | |||
Disulfide bondi | 195 ↔ 322 | |||
Glycosylationi | 205 | N-linked (GlcNAc...) asparagine2 Publications Manual assertion based on experiment ini
| 1 | |
Disulfide bondi | 219 ↔ 224 | |||
Disulfide bondi | 238 ↔ 254 | |||
Disulfide bondi | 370 ↔ 389 | |||
Glycosylationi | 382 | N-linked (GlcNAc...) asparagine2 Publications Manual assertion based on experiment ini
| 1 | |
Disulfide bondi | 400 ↔ 428 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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
Manual assertion based on experiment ini
- Ref.10"Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells."
Thim L., Bjoern S., Christensen M., Nicolaisen E.M., Lund-Hansen T., Pedersen A.H., Hedner U.
Biochemistry 27:7785-7793(1988) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 61-466, GAMMA-CARBOXYGLUTAMATION AT GLU-66; GLU-67; GLU-74; GLU-76; GLU-79; GLU-80; GLU-85; GLU-86; GLU-89 AND GLU-95, HYDROXYLATION AT ASP-123, GLYCOSYLATION AT ASN-205 AND ASN-382.
Manual assertion based on experiment ini
- Ref.10"Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells."
Thim L., Bjoern S., Christensen M., Nicolaisen E.M., Lund-Hansen T., Pedersen A.H., Hedner U.
Biochemistry 27:7785-7793(1988) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 61-466, GAMMA-CARBOXYGLUTAMATION AT GLU-66; GLU-67; GLU-74; GLU-76; GLU-79; GLU-80; GLU-85; GLU-86; GLU-89 AND GLU-95, HYDROXYLATION AT ASP-123, GLYCOSYLATION AT ASN-205 AND ASN-382. - Ref.14"Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine."
Bjoern S., Foster D.C., Thim L., Wiberg F.C., Christensen M., Komiyama Y., Pedersen A.H., Kisiel W.
J. Biol. Chem. 266:11051-11057(1991) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT SER-112 AND SER-120. - Ref.15"Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains."
Wang Y., Lee G.F., Kelley R.F., Spellman M.W.
Glycobiology 6:837-842(1996) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.16"Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms."
Ruiz-Canada C., Kelleher D.J., Gilmore R.
Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT ASN-205 AND ASN-382. - Ref.17"Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase."
Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A., Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A., Jafar-Nejad H., Haltiwanger R.S.
Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT SER-112, MUTAGENESIS OF SER-112 AND SER-113.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 212 – 213 | Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, ZymogenProteomic databases
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | P08709 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P08709 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08709 |
PeptideAtlas More...PeptideAtlasi | P08709 |
PRoteomics IDEntifications database More...PRIDEi | P08709 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 52160 [P08709-1] 52161 [P08709-2] |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 98, 4 O-Linked glycans (2 sites) |
GlyGen: Computational and Informatics Resources for Glycoscience More...GlyGeni | P08709, 5 sites, 9 N-linked glycans (2 sites), 4 O-linked glycans (3 sites) |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08709 |
MetOSite database of methionine sulfoxide sites More...MetOSitei | P08709 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08709 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000057593, Expressed in right lobe of liver and 141 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P08709, baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08709, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000057593, Tissue enriched (liver) |
<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Heterodimer of a light chain and a heavy chain linked by a disulfide bond.
2 PublicationsManual assertion based on experiment ini
- Ref.18"The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor."
Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H., Nemreson Y., Kirchhofer D.
Nature 380:41-46(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF. - Ref.19"Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant."
Zhang E., St Charles R., Tulinsky A.
J. Mol. Biol. 285:2089-2104(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
P08709
With | #Exp. | IntAct |
---|---|---|
F3 [P13726] | 7 | EBI-355972,EBI-1040727 |
GO - Molecular functioni
- signaling receptor binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 108453, 16 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-2808, Coagulation factor VIIa - tissue factor complex CPX-6211, Coagulation factor VIIa complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P08709 |
Database of interacting proteins More...DIPi | DIP-6135N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P08709 |
Protein interaction database and analysis system More...IntActi | P08709, 13 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000364731 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P08709 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | P08709, protein |
<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
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 66 – 68 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 73 – 77 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 84 – 91 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 94 – 104 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 109 – 112 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 116 – 118 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 120 – 124 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 127 – 131 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 136 – 138 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 145 – 147 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 148 – 150 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 151 – 153 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 154 – 157 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 159 – 165 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 166 – 168 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 169 – 173 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 178 – 180 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 187 – 189 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 191 – 193 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 199 – 205 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 220 – 222 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 227 – 232 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 235 – 242 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 244 – 250 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 252 – 255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 261 – 263 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 264 – 269 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 272 – 274 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 281 – 291 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 298 – 301 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 304 – 310 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 326 – 331 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 333 – 335 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 338 – 344 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 346 – 348 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 352 – 355 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 358 – 365 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 367 – 373 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 376 – 378 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 380 – 382 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 383 – 386 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 387 – 391 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 393 – 398 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 401 – 403 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 407 – 412 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 415 – 422 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 427 – 429 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 435 – 439 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 440 – 443 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 444 – 451 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 457 – 463 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08709 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P08709 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini | 61 – 105 | GlaPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 45 | |
Domaini | 106 – 142 | EGF-like 1; calcium-bindingPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 37 | |
Domaini | 147 – 188 | EGF-like 2PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 42 | |
Domaini | 213 – 452 | Peptidase S1PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 240 |
<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
Manual assertion according to rulesi
Keywords - Domaini
EGF-like domain, Repeat, SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG502QRGI, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00940000154474 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_006842_19_5_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08709 |
Identification of Orthologs from Complete Genome Data More...OMAi | MAIDVPR |
Database of Orthologous Groups More...OrthoDBi | 265965at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08709 |
TreeFam database of animal gene trees More...TreeFami | TF327329 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00190, Tryp_SPc, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.10.10, 2 hits 4.10.740.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR017857, Coagulation_fac-like_Gla_dom IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR033190, F7 IPR035972, GLA-like_dom_SF IPR000294, GLA_domain IPR012224, Pept_S1A_FX IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001314, Peptidase_S1A IPR001254, Trypsin_dom IPR018114, TRYPSIN_HIS IPR033116, TRYPSIN_SER |
The PANTHER Classification System More...PANTHERi | PTHR24278:SF26, PTHR24278:SF26, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00008, EGF, 1 hit PF00594, Gla, 1 hit PF00089, Trypsin, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF001143, Factor_X, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00722, CHYMOTRYPSIN PR00001, GLABLOOD |
Simple Modular Architecture Research Tool; a protein domain database More...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 More...SUPFAMi | SSF50494, SSF50494, 1 hit SSF57630, SSF57630, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 1 hit PS00022, EGF_1, 1 hit PS01186, EGF_2, 1 hit 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basketThis entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE
60 70 80 90 100
AHGVLHRRRR ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF
110 120 130 140 150
WISYSDGDQC ASSPCQNGGS CKDQLQSYIC FCLPAFEGRN CETHKDDQLI
160 170 180 190 200
CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL LADGVSCTPT VEYPCGKIPI
210 220 230 240 250
LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG TLINTIWVVS
260 270 280 290 300
AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN
310 320 330 340 350
HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR
360 370 380 390 400
GATALELMVL NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC
410 420 430 440 450
KGDSGGPHAT HYRGTWYLTG IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL
460
MRSEPRPGVL LRAPFP
The sequence of this isoform differs from the canonical sequence as follows:
22-43: Missing.
10 20 30 40 50
MVSQALRLLC LLLGLQGCLA AVFVTQEEAH GVLHRRRRAN AFLEELRPGS
60 70 80 90 100
LERECKEEQC SFEEAREIFK DAERTKLFWI SYSDGDQCAS SPCQNGGSCK
110 120 130 140 150
DQLQSYICFC LPAFEGRNCE THKDDQLICV NENGGCEQYC SDHTGTKRSC
160 170 180 190 200
RCHEGYSLLA DGVSCTPTVE YPCGKIPILE KRNASKPQGR IVGGKVCPKG
210 220 230 240 250
ECPWQVLLLV NGAQLCGGTL INTIWVVSAA HCFDKIKNWR NLIAVLGEHD
260 270 280 290 300
LSEHDGDEQS RRVAQVIIPS TYVPGTTNHD IALLRLHQPV VLTDHVVPLC
310 320 330 340 350
LPERTFSERT LAFVRFSLVS GWGQLLDRGA TALELMVLNV PRLMTQDCLQ
360 370 380 390 400
QSRKVGDSPN ITEYMFCAGY SDGSKDSCKG DSGGPHATHY RGTWYLTGIV
410 420 430 440
SWGQGCATVG HFGVYTRVSQ YIEWLQKLMR SEPRPGVLLR APFP
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketEntry | Entry name | Protein names | Gene names | Length | Annotation | ||
---|---|---|---|---|---|---|---|
F5H8B0 | F5H8B0_HUMAN | Coagulation factor VII Coagulation factor VII | F7 | 382 | Annotation 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> | ||
E9PH36 | E9PH36_HUMAN | Coagulation factor VII Coagulation factor VII | F7 | 74 | Annotation 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> |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_014391 | 13 | L → P in FA7D; Morioka. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065369 | 59 | R → RR in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015135 | 64 | F → L in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014405 | 73 | L → Q in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014406 | 79 | E → Q in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065370 | 82 | C → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065371 | 82 | C → R in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065372 | 84 | Missing in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065373 | 85 | E → K in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065374 | 88 | R → G in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065375 | 88 | R → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065376 | 117 | N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015136 | 120 | S → P in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014407 | 121 | C → F in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014408 | 125 | L → P in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014409 | 128 | Y → C in FA7D. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065377 | 138 | G → D in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006497 | 139 | R → K in FA7D. | 1 | |
Natural variantiVAR_006498 | 139 | R → Q in FA7D; Charlotte. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006499 | 139 | R → W in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014410 | 151 | C → S in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015137 | 154 | E → K in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_065378 | 156 | G → S in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006501 | 157 | G → C in FA7D. | 1 | |
Natural variantiVAR_006500 | 157 | G → S in FA7D. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_014411 | 157 | G → V in FA7D. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_006502 | 160 | Q → R in FA7D. 4 Publications Manual assertion based on experiment ini
|