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Protein

Coagulation factor IX

Gene

F9

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 IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ ions, phospholipids, and factor VIIIa.6 Publications

Miscellaneous

In 1952, one of the earliest researchers of the disease, Dr. R.G. Macfarlane used the patient's surname, Christmas, to refer to the disease and also to refer to the clotting factor which he called the 'Christmas Factor' At the time Stephen Christmas was a 5-year-old boy. He died in 1993 at the age of 46 from acquired immunodeficiency syndrome contracted through treatment with blood products.

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi47Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi48Calcium 2Combined sources1 Publication1
Metal bindingi53Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi53Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi54Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi54Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi61Calcium 4 or magnesium 1; via 4-carboxyglutamateCombined sourcesBy similarity1 Publication1
Metal bindingi63Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi63Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi66Calcium 4 or magnesium 1; via 4-carboxyglutamateCombined sourcesBy similarity1 Publication1
Metal bindingi67Calcium 1; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi72Calcium 5 or magnesium 2; via 4-carboxyglutamateCombined sourcesBy similarity1 Publication1
Metal bindingi73Calcium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi73Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi76Calcium 3; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi76Calcium 5 or magnesium 2; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi76Calcium 5; via 4-carboxyglutamateCombined sources1 Publication1
Metal bindingi82Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi86Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity1
Metal bindingi93Calcium 7Combined sources1 Publication1
Metal bindingi94Calcium 7; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi96Calcium 7Combined sources1 Publication1
Metal bindingi110Calcium 7Combined sources1 Publication1
Metal bindingi111Calcium 7; via carbonyl oxygenCombined sources1 Publication1
<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 sitei267Charge relay system2 Publications1
Metal bindingi281Calcium 8Combined sources5 Publications1
Metal bindingi283Calcium 8; via carbonyl oxygenCombined sources5 Publications1
Metal bindingi286Calcium 8; via carbonyl oxygenCombined sources5 Publications1
Metal bindingi288Calcium 8Combined sources5 Publications1
Metal bindingi291Calcium 8Combined sources5 Publications1
Active sitei315Charge relay system1 Publication1
Active sitei411Charge relay system2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.4.21.22 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-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
P00740

SIGNOR Signaling Network Open Resource

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SIGNORi
P00740

Protein family/group databases

MEROPS protease database

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MEROPSi
S01.214

<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 IX1 Publication (EC:3.4.21.224 Publications)
Alternative name(s):
Christmas factor
Plasma thromboplastin component
Short name:
PTC
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:F9
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000101981.10

Human Gene Nomenclature Database

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HGNCi
HGNC:3551 F9

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300746 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P00740

<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

Hemophilia B (HEMB)38 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma.
See also OMIM:306900
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_00652117I → N in HEMB; severe; UK 22. 1
Natural variantiVAR_07397520L → S in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation. 1 Publication1
Natural variantiVAR_00652228C → R in HEMB; moderate; HB130. Corresponds to variant dbSNP:rs387906481EnsemblClinVar.1
Natural variantiVAR_01734328C → Y in HEMB; decreased protein abundance; decreased function in blood coagulation. 2 Publications1
Natural variantiVAR_00652330V → I in HEMB. 1
Natural variantiVAR_00652543R → L in HEMB; severe; Bendorf, Beuten, Gleiwitz; impairs removal of propeptide. 2 Publications1
Natural variantiVAR_00652443R → Q in HEMB; severe; San Dimas, Oxford-3, Strasbourg-2; impairs removal of propeptide. 6 PublicationsCorresponds to variant dbSNP:rs1275708479Ensembl.1
Natural variantiVAR_00652643R → W in HEMB; severe; Boxtel, Heiden, Lienen; impairs removal of propeptide. 3 Publications1
Natural variantiVAR_00652745K → N in HEMB; severe; Seattle E. 1
Natural variantiVAR_00652846R → S in HEMB; severe; Cambridge; impaired processing of the propeptide; impaired gamma-carboxylation; decreased protein abundance; loss of function in blood coagulation. 1 Publication1
Natural variantiVAR_00652946R → T in HEMB; severe. 1 Publication1
Natural variantiVAR_00653048N → I in HEMB; severe; Calgary-16. 1
Natural variantiVAR_00653149S → P in HEMB. 1
Natural variantiVAR_01734452L → S in HEMB; severe; Gla mutant. 1 Publication1
Natural variantiVAR_00653253E → A in HEMB; severe; Oxford-B2; Gla mutant. 1
Natural variantiVAR_07397654E → D in HEMB; unknown pathological significance; no effect on protein abundance; loss of function in blood coagulation. 1 Publication1
Natural variantiVAR_00653354E → G in HEMB; severe; HB151; Gla mutant. 1
Natural variantiVAR_00653455F → C in HEMB. 1
Natural variantiVAR_00653558G → A in HEMB; severe; Hong Kong-1. 1
Natural variantiVAR_07397758G → E in HEMB; unknown pathological significance; no effect on protein abundance; loss of function in blood coagulation. 1 Publication1
Natural variantiVAR_00653658G → R in HEMB; severe; Los Angeles-4. 1
Natural variantiVAR_00653762 – 63Missing in HEMB; severe. 2
Natural variantiVAR_00653866E → V in HEMB; moderate. 1
Natural variantiVAR_00653967E → K in HEMB; severe; Nagoya-4; Gla mutant. 1
Natural variantiVAR_00654071F → S in HEMB; severe. 1
Natural variantiVAR_00654173E → K in HEMB; severe; Seattle-3; Gla mutant. 1 PublicationCorresponds to variant dbSNP:rs137852225Ensembl.1
Natural variantiVAR_00654273E → V in HEMB; severe; Chongqing; Gla mutant. 1 PublicationCorresponds to variant dbSNP:rs137852226EnsemblClinVar.1
Natural variantiVAR_01730875R → Q in HEMB; mild. 1 PublicationCorresponds to variant dbSNP:rs137852228EnsemblClinVar.1
Natural variantiVAR_01730979E → D in HEMB. 1 PublicationCorresponds to variant dbSNP:rs137852229EnsemblClinVar.1
Natural variantiVAR_01734584T → R in HEMB; decreased protein abundance; loss of function in blood coagulation. 2 Publications1
Natural variantiVAR_00654391Y → C in HEMB; moderate. 1
Natural variantiVAR_00654493D → G in HEMB; moderate; Alabama. 1 PublicationCorresponds to variant dbSNP:rs137852230EnsemblClinVar.1
Natural variantiVAR_00654596Q → P in HEMB; severe; New London. Corresponds to variant dbSNP:rs137852231EnsemblClinVar.1
Natural variantiVAR_00654697C → S in HEMB. 1
Natural variantiVAR_006547101P → R in HEMB. 1
Natural variantiVAR_006548102C → R in HEMB; severe; Basel. 1
Natural variantiVAR_017346106G → D in HEMB. 1 Publication1
Natural variantiVAR_006549106G → S in HEMB; mild; Durham. 2 PublicationsCorresponds to variant dbSNP:rs137852233EnsemblClinVar.1
Natural variantiVAR_006550108C → S in HEMB. 1
Natural variantiVAR_006551110D → N in HEMB; severe; Oxford-D1. Corresponds to variant dbSNP:rs137852274EnsemblClinVar.1
Natural variantiVAR_006552112I → S in HEMB. 1
Natural variantiVAR_006553113N → K in HEMB; mild. 1 Publication1
Natural variantiVAR_006554115Y → C in HEMB; severe. 1 Publication1
Natural variantiVAR_006555119C → F in HEMB; severe. 1
Natural variantiVAR_006556119C → R in HEMB; Iran. 1 Publication1
Natural variantiVAR_017347124E → K in HEMB. 1 Publication1
Natural variantiVAR_006557125G → E in HEMB. 1
Natural variantiVAR_017348125G → R in HEMB. 1 Publication1
Natural variantiVAR_006558125G → V in HEMB. 1 Publication1
Natural variantiVAR_006559129 – 130Missing in HEMB. 2
Natural variantiVAR_017349134C → Y in HEMB. 1 Publication1
Natural variantiVAR_006560136I → T in HEMB; mild. 1
Natural variantiVAR_073978138N → H in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation. 1 Publication1
Natural variantiVAR_006561139G → D in HEMB; severe. 1
Natural variantiVAR_006562139G → S in HEMB. 1
Natural variantiVAR_006563155C → F in HEMB; severe. 1 PublicationCorresponds to variant dbSNP:rs1330705989Ensembl.1
Natural variantiVAR_006564160G → E in HEMB; mild. 1
Natural variantiVAR_006565167Q → H in HEMB; mild. 1
Natural variantiVAR_017350169S → C in HEMB. 1 Publication1
Natural variantiVAR_017351170C → F in HEMB. 1 Publication1
Natural variantiVAR_006566178C → R in HEMB. 1
Natural variantiVAR_006567178C → W in HEMB; severe. 1
Natural variantiVAR_006569191R → C in HEMB; moderate; Albuquerque, Cardiff-1. 1 PublicationCorresponds to variant dbSNP:rs137852237EnsemblClinVar.1
Natural variantiVAR_006568191R → H in HEMB; moderate; Chapel-Hill, Chicago-2. 2 PublicationsCorresponds to variant dbSNP:rs137852238EnsemblClinVar.1
Natural variantiVAR_006571226R → G in HEMB; severe; Madrid. 2 Publications1
Natural variantiVAR_006572226R → Q in HEMB; severe; Hilo and Novara; no effect on protein abundance; loss of function in blood coagulation. 4 PublicationsCorresponds to variant dbSNP:rs137852241EnsemblClinVar.1
Natural variantiVAR_006570226R → W in HEMB; severe; Nagoya-1, Dernbach, Deventer, Idaho. 3 PublicationsCorresponds to variant dbSNP:rs137852240EnsemblClinVar.1
Natural variantiVAR_006573227V → D in HEMB; mild. 1
Natural variantiVAR_017310227V → F in HEMB; Milano. 1 PublicationCorresponds to variant dbSNP:rs137852242Ensembl.1
Natural variantiVAR_017311228V → F in HEMB; severe; Kashihara. 1 PublicationCorresponds to variant dbSNP:rs137852243EnsemblClinVar.1
Natural variantiVAR_006574228V → L in HEMB; mild; Cardiff-2. 1 PublicationCorresponds to variant dbSNP:rs137852243EnsemblClinVar.1
Natural variantiVAR_006575241Q → H in HEMB. 1 PublicationCorresponds to variant dbSNP:rs1182648920Ensembl.1
Natural variantiVAR_017352241Q → K in HEMB. 1 Publication1
Natural variantiVAR_017312252C → S in HEMB; severe. 1 PublicationCorresponds to variant dbSNP:rs267606792EnsemblClinVar.1
Natural variantiVAR_017353252C → Y in HEMB. 1 Publication1
Natural variantiVAR_006576253G → E in HEMB; severe. 1
Natural variantiVAR_006577253G → R in HEMB; severe; Luanda. 1 Publication1
Natural variantiVAR_006578265A → T in HEMB; mild. 1
Natural variantiVAR_017313268C → W in HEMB; moderate. 1 PublicationCorresponds to variant dbSNP:rs137852246EnsemblClinVar.1
Natural variantiVAR_006579279A → T in HEMB; mild. 2 PublicationsCorresponds to variant dbSNP:rs137852247EnsemblClinVar.1
Natural variantiVAR_006580283N → D in HEMB; severe. 1
Natural variantiVAR_073979284Missing in HEMB; severe; decreased protein abundance; loss of function in blood coagulation. 1 Publication1
Natural variantiVAR_006581286Missing in HEMB; severe. 1
Natural variantiVAR_017314291E → V in HEMB; Monschau. 1 PublicationCorresponds to variant dbSNP:rs137852279EnsemblClinVar.1
Natural variantiVAR_006582294R → G in HEMB; severe. 1
Natural variantiVAR_006583294R → Q in HEMB; mild to moderate; Dreihacken, Penafiel and Seattle-4. 5 PublicationsCorresponds to variant dbSNP:rs137852249EnsemblClinVar.1
Natural variantiVAR_073980296V → M in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation. 1 Publication1
Natural variantiVAR_006584302H → R in HEMB. 1 Publication1
Natural variantiVAR_017315306N → S in HEMB; mild. 1 PublicationCorresponds to variant dbSNP:rs137852251EnsemblClinVar.1
Natural variantiVAR_006585316I → F in HEMB. 1 Publication1
Natural variantiVAR_017354318L → R in HEMB. 1 PublicationCorresponds to variant dbSNP:rs1222227572Ensembl.1
Natural variantiVAR_006586321L → Q in HEMB; severe. 1
Natural variantiVAR_073981328N → K in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation. 1 Publication1
Natural variantiVAR_073982328N → Y in HEMB; moderate; decreased protein abundance; decreased function in blood coagulation. 1 Publication1
Natural variantiVAR_006587333P → H in HEMB; severe. 1
Natural variantiVAR_017355333P → T in HEMB. 1 Publication1
Natural variantiVAR_006588342T → K in HEMB; mild. 1
Natural variantiVAR_006589342T → M in HEMB; moderate. 3 PublicationsCorresponds to variant dbSNP:rs137852254EnsemblClinVar.1
Natural variantiVAR_017356344I → L in HEMB. 1 Publication1
Natural variantiVAR_006590351G → D in HEMB. 1
Natural variantiVAR_006591356W → C in HEMB; severe. 1
Natural variantiVAR_006592357G → E in HEMB; severe; Amagasaki. 1 PublicationCorresponds to variant dbSNP:rs137852275EnsemblClinVar.1
Natural variantiVAR_017316357G → R in HEMB. 1 PublicationCorresponds to variant dbSNP:rs137852257EnsemblClinVar.1
Natural variantiVAR_006593362K → E in HEMB; moderate. 1
Natural variantiVAR_006594363G → W in HEMB. 1
Natural variantiVAR_006595366A → D in HEMB. 1
Natural variantiVAR_006596379R → G in HEMB; moderate. 1 Publication1
Natural variantiVAR_006597379R → Q in HEMB; severe; Iceland-1, London and Sesimbra. 3 PublicationsCorresponds to variant dbSNP:rs137852259EnsemblClinVar.1
Natural variantiVAR_006598382C → Y in HEMB. 1
Natural variantiVAR_017358383L → F in HEMB. 1 Publication1
Natural variantiVAR_017357383L → I in HEMB. 1 Publication1
Natural variantiVAR_006599387K → E in HEMB; mild. 1 Publication1
Natural variantiVAR_006600390I → F in HEMB; severe. 1
Natural variantiVAR_006601394M → K in HEMB. 1
Natural variantiVAR_017359395F → I in HEMB. 1 Publication1
Natural variantiVAR_017360395F → L in HEMB. 1 Publication1
Natural variantiVAR_017361396C → F in HEMB. 1 Publication1
Natural variantiVAR_006602396C → S in HEMB; severe. Corresponds to variant dbSNP:rs137852273EnsemblClinVar.1
Natural variantiVAR_017317397A → P in HEMB; mild; Hong Kong-11. 1 PublicationCorresponds to variant dbSNP:rs137852281EnsemblClinVar.1
Natural variantiVAR_006603404R → T in HEMB. 1
Natural variantiVAR_017362407C → R in HEMB. 1 Publication1
Natural variantiVAR_006604407C → S in HEMB; severe. 1
Natural variantiVAR_017318410D → H in HEMB; Mechtal. 1 PublicationCorresponds to variant dbSNP:rs137852278EnsemblClinVar.1
Natural variantiVAR_017320411S → G in HEMB; Varel. 1 PublicationCorresponds to variant dbSNP:rs137852277EnsemblClinVar.1
Natural variantiVAR_017319411S → I in HEMB; Schmallenberg. 1 PublicationCorresponds to variant dbSNP:rs137852276EnsemblClinVar.1
Natural variantiVAR_017363412G → E in HEMB. 1 PublicationCorresponds to variant dbSNP:rs1233706534Ensembl.1
Natural variantiVAR_006605413G → R in HEMB; moderate to severe. 2 PublicationsCorresponds to variant dbSNP:rs1306658513Ensembl.1
Natural variantiVAR_017321414P → T in HEMB; Bergamo; increased protein abundance; loss of function in blood coagulation. 3 PublicationsCorresponds to variant dbSNP:rs137852265EnsemblClinVar.1
Natural variantiVAR_006606419V → E in HEMB; moderately severe. 2 PublicationsCorresponds to variant dbSNP:rs137852280EnsemblClinVar.1
Natural variantiVAR_006607424F → V in HEMB. 1 Publication1
Natural variantiVAR_006608426T → P in HEMB; severe; Barcelos. 1 Publication1
Natural variantiVAR_006609430S → T in HEMB. 1
Natural variantiVAR_006610431W → G in HEMB. 1
Natural variantiVAR_006611431W → R in HEMB; moderate. 1
Natural variantiVAR_006612432G → S in HEMB; severe. 1
Natural variantiVAR_006613432G → V in HEMB; severe. 1 Publication1
Natural variantiVAR_006614433E → A in HEMB. 1
Natural variantiVAR_006615433E → K in HEMB. Corresponds to variant dbSNP:rs767828752Ensembl.1
Natural variantiVAR_017364435C → Y in HEMB. 1 Publication1
Natural variantiVAR_006616436A → V in HEMB; moderately severe; Niigata. 1 PublicationCorresponds to variant dbSNP:rs137852266EnsemblClinVar.1
Natural variantiVAR_017365442G → E in HEMB. 1 Publication1
Natural variantiVAR_017322442G → R in HEMB; severe; Angers. 1 PublicationCorresponds to variant dbSNP:rs137852267EnsemblClinVar.1
Natural variantiVAR_017323443I → T in HEMB; moderately severe; Long Beach, Los Angeles and Vancouver. 2 PublicationsCorresponds to variant dbSNP:rs137852268EnsemblClinVar.1
Natural variantiVAR_006617445T → TIYT in HEMB; severe; Lousada. 1
Natural variantiVAR_073983447V → VYTKV in HEMB; reduced protein abundance; loss of function in blood coagulation. 1 Publication1
Natural variantiVAR_006618449R → Q in HEMB; mild. 1 PublicationCorresponds to variant dbSNP:rs143018900Ensembl.1
Natural variantiVAR_006619449R → W in HEMB; mild. 1 PublicationCorresponds to variant dbSNP:rs757996262Ensembl.1
Natural variantiVAR_006620450Y → C in HEMB; severe. 1 Publication1
Natural variantiVAR_017324453W → R in HEMB. 1 PublicationCorresponds to variant dbSNP:rs137852269EnsemblClinVar.1
Natural variantiVAR_006621454I → T in HEMB; Italy. 1 Publication1
Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide (PubMed:12588353, PubMed:2738071, PubMed:3009023, PubMed:8295821, PubMed:9169594, PubMed:9600455, PubMed:25251685). Mutation in position 93 (Alabama) probably fails to bind to cell membranes (PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent cleavage of the activation peptide (PubMed:6603618, PubMed:8076946, PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493).12 Publications
Thrombophilia, X-linked, due to factor IX defect (THPH8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemostatic disorder characterized by a tendency to thrombosis.
See also OMIM:300807
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_062999384R → L in THPH8; factor IX Padua; higher specific activity than wild-type. 1 PublicationCorresponds to variant dbSNP:rs137852283EnsemblClinVar.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

Available under the name BeneFix (Baxter and American Home Products). Used to treat hemophilia B.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi305Y → F: Strongly increases enzyme activity with a synthetic peptide substrate; when associated with T-311; A-365 and T-391. 1 Publication1
Mutagenesisi311K → T: Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; A-365 and T-391. 1 Publication1
Mutagenesisi312Y → A: Strongly decreases enzyme activity with a synthetic peptide substrate. 1 Publication1
Mutagenesisi391Y → T: Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; T-311 and A-365. 1 Publication1

Keywords - Diseasei

Disease mutation, Hemophilia, Thrombophilia

Organism-specific databases

DisGeNET

More...
DisGeNETi
2158

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

More...
GeneReviewsi
F9

MalaCards human disease database

More...
MalaCardsi
F9
MIMi300807 phenotype
306900 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000101981

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

More...
Orphaneti
169799 Mild hemophilia B
169796 Moderately severe hemophilia B
169793 Severe hemophilia B
177929 Symptomatic form of hemophilia B in female carriers

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27954

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
9616 Hom s Factor IX

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2016

Drug and drug target database

More...
DrugBanki
DB00025 Antihemophilic Factor (Recombinant)
DB13150 Coagulation factor VII human
DB00170 Menadione
DB05131 TTP889

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2364

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
F9

<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 – 28Sequence analysisAdd BLAST28
<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_000002775529 – 461 PublicationAdd BLAST18
<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_000002775647 – 461Coagulation factor IXAdd BLAST415
ChainiPRO_000002775747 – 191Coagulation factor IXa light chainAdd BLAST145
PropeptideiPRO_0000027758192 – 226Activation peptideAdd BLAST35
ChainiPRO_0000027759227 – 461Coagulation factor IXa heavy chainAdd BLAST235

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 residuei534-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei634-carboxyglutamatePROSITE-ProRule annotationBy similarity1
<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 bondi64 ↔ 69By similarity
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei824-carboxyglutamatePROSITE-ProRule annotationBy similarity1
<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>Glycosylationi85O-linked (GalNAc...) threonine1 Publication1
Modified residuei864-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi97 ↔ 108Combined sources2 Publications
GlycosylationiCAR_00000999O-linked (Glc...) serine; alternate4 Publications1
Glycosylationi99O-linked (Xyl...) serine; alternate3 Publications1
Disulfide bondi102 ↔ 117Combined sources2 Publications
GlycosylationiCAR_000010107O-linked (Fuc...) serine2 Publications1
Modified residuei110(3R)-3-hydroxyaspartate1 Publication1
Modified residuei114Phosphoserine1 Publication1
Disulfide bondi119 ↔ 128Combined sources2 Publications
Disulfide bondi134 ↔ 145Combined sources4 Publications
Disulfide bondi141 ↔ 155Combined sources4 Publications
Disulfide bondi157 ↔ 170Combined sources4 Publications
Disulfide bondi178 ↔ 335Interchain (between light and heavy chains)Combined sources4 Publications
Modified residuei201Sulfotyrosine1 Publication1
Glycosylationi203N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei204Phosphoserine2 Publications1
Modified residuei205Phosphothreonine; alternate1 Publication1
Glycosylationi205O-linked (GalNAc...) threonine; alternate2 Publications1
Glycosylationi213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi215O-linked (GalNAc...) threonine2 Publications1
Glycosylationi225O-linked (GalNAc...) threonine1 Publication1
Disulfide bondi252 ↔ 268Combined sources4 Publications
Disulfide bondi382 ↔ 396Combined sources4 Publications
Disulfide bondi407 ↔ 435Combined sources4 Publications

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

Activated by factor XIa, which excises the activation peptide (PubMed:9169594, PubMed:1730085). The propeptide can also be removed by snake venom protease (PubMed:20004170, PubMed:20080729).6 Publications
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication
Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro. Xylosylation at this site is minor.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei191 – 192Cleavage; by factor XIa2
Sitei226 – 227Cleavage; by factor XIa2

Keywords - PTMi

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

Proteomic databases

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

More...
PaxDbi
P00740

PeptideAtlas

More...
PeptideAtlasi
P00740

PRoteomics IDEntifications database

More...
PRIDEi
P00740

ProteomicsDB human proteome resource

More...
ProteomicsDBi
51274

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
96

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00740

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

More...
PhosphoSitePlusi
P00740

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P00740

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P00740

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in blood plasma (at protein level) (PubMed:3857619, PubMed:8295821, PubMed:2592373, PubMed:9169594, PubMed:19846852). Synthesized primarily in the liver and secreted in plasma.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000101981 Expressed in 31 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_F9

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P00740 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

Heterodimer of a light chain and a heavy chain; disulfide-linked (PubMed:20121198, PubMed:20121197, PubMed:20080729). Interacts with SERPINC1.5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108456, 39 interactors

Database of interacting proteins

More...
DIPi
DIP-58520N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P00740

Protein interaction database and analysis system

More...
IntActi
P00740, 4 interactors

Molecular INTeraction database

More...
MINTi
P00740

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000218099

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00740

<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

1461
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00740

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

More...
SMRi
P00740

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00740

<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>Domaini47 – 92GlaPROSITE-ProRule annotationAdd BLAST46
Domaini93 – 129EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini130 – 171EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini227 – 459Peptidase S1PROSITE-ProRule annotationAdd BLAST233

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain (PubMed:6425296). Under physiological ion concentrations, Ca2+ is displaced by Mg2+ from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein (By similarity).By similarity3 Publications

<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

More...
eggNOGi
ENOG410IGPV Eukaryota
COG5640 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159516

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000251821

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG013304

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00740

KEGG Orthology (KO)

More...
KOi
K01321

Identification of Orthologs from Complete Genome Data

More...
OMAi
SYECWCQ

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0AH5

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00740

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
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
IPR035694 Coagulation_factor_IX
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

The PANTHER Classification System

More...
PANTHERi
PTHR44064:SF4 PTHR44064:SF4, 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, 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>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P00740-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG
60 70 80 90 100
KLEEFVQGNL ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGSCKD DINSYECWCP FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD
160 170 180 190 200
NKVVCSCTEG YRLAENQKSC EPAVPFPCGR VSVSQTSKLT RAETVFPDVD
210 220 230 240 250
YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW QVVLNGKVDA
260 270 280 290 300
FCGGSIVNEK WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRII
310 320 330 340 350
PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS
360 370 380 390 400
GYVSGWGRVF HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH
410 420 430 440 450
EGGRDSCQGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY
460
VNWIKEKTKL T
Length:461
Mass (Da):51,778
Last modified:June 7, 2005 - 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:iC4720C1234477EF5
GO
Isoform 2 (identifier: P00740-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-130: Missing.

Show »
Length:423