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Protein

Coagulation factor IX

Gene

F9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

GO - Molecular functioni

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

GO - Biological processi

  • blood coagulation Source: UniProtKB
  • blood coagulation, extrinsic pathway Source: Reactome
  • blood coagulation, intrinsic pathway Source: Reactome
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • peptidyl-glutamic acid carboxylation Source: Reactome
  • proteolysis Source: UniProtKB
  • signal peptide processing Source: Reactome
  • zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS02329-MONOMER.
BRENDAi3.4.21.22. 2681.
ReactomeiR-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-RKP00740.

Protein family/group databases

MEROPSiS01.214.

Names & Taxonomyi

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:
Gene namesi
Name:F9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3551. F9.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi lumen Source: Reactome
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hemophilia B (HEMB)37 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
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 rs387906481dbSNPEnsembl.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 Publications1
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 rs137852225dbSNPEnsembl.1
Natural variantiVAR_00654273E → V in HEMB; severe; Chongqing; Gla mutant. 1 PublicationCorresponds to variant rs137852226dbSNPEnsembl.1
Natural variantiVAR_01730875R → Q in HEMB; mild. 1 PublicationCorresponds to variant rs137852228dbSNPEnsembl.1
Natural variantiVAR_01730979E → D in HEMB. 1 PublicationCorresponds to variant rs137852229dbSNPEnsembl.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 rs137852230dbSNPEnsembl.1
Natural variantiVAR_00654596Q → P in HEMB; severe; New London. Corresponds to variant rs137852231dbSNPEnsembl.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 rs137852233dbSNPEnsembl.1
Natural variantiVAR_006550108C → S in HEMB. 1
Natural variantiVAR_006551110D → N in HEMB; severe; Oxford-D1. Corresponds to variant rs137852274dbSNPEnsembl.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 Publication1
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 rs137852237dbSNPEnsembl.1
Natural variantiVAR_006568191R → H in HEMB; moderate; Chapel-Hill, Chicago-2. 2 PublicationsCorresponds to variant rs137852238dbSNPEnsembl.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 rs137852241dbSNPEnsembl.1
Natural variantiVAR_006570226R → W in HEMB; severe; Nagoya-1, Dernbach, Deventer, Idaho. 3 PublicationsCorresponds to variant rs137852240dbSNPEnsembl.1
Natural variantiVAR_006573227V → D in HEMB; mild. 1
Natural variantiVAR_017310227V → F in HEMB; Milano. 1 PublicationCorresponds to variant rs137852242dbSNPEnsembl.1
Natural variantiVAR_017311228V → F in HEMB; severe; Kashihara. 1 PublicationCorresponds to variant rs137852243dbSNPEnsembl.1
Natural variantiVAR_006574228V → L in HEMB; mild; Cardiff-2. 1 PublicationCorresponds to variant rs137852243dbSNPEnsembl.1
Natural variantiVAR_006575241Q → H in HEMB. 1 Publication1
Natural variantiVAR_017352241Q → K in HEMB. 1 Publication1
Natural variantiVAR_017312252C → S in HEMB; severe. 1 PublicationCorresponds to variant rs267606792dbSNPEnsembl.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 rs137852246dbSNPEnsembl.1
Natural variantiVAR_006579279A → T in HEMB; mild. 2 PublicationsCorresponds to variant rs137852247dbSNPEnsembl.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 rs137852279dbSNPEnsembl.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 rs137852249dbSNPEnsembl.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 rs137852251dbSNPEnsembl.1
Natural variantiVAR_006585316I → F in HEMB. 1 Publication1
Natural variantiVAR_017354318L → R in HEMB. 1 Publication1
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 rs137852254dbSNPEnsembl.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 rs137852275dbSNPEnsembl.1
Natural variantiVAR_017316357G → R in HEMB. 1 PublicationCorresponds to variant rs137852257dbSNPEnsembl.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 rs137852259dbSNPEnsembl.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 rs137852273dbSNPEnsembl.1
Natural variantiVAR_017317397A → P in HEMB; mild; Hong Kong-11. 1 PublicationCorresponds to variant rs137852281dbSNPEnsembl.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 rs137852278dbSNPEnsembl.1
Natural variantiVAR_017320411S → G in HEMB; Varel. 1 PublicationCorresponds to variant rs137852277dbSNPEnsembl.1
Natural variantiVAR_017319411S → I in HEMB; Schmallenberg. 1 PublicationCorresponds to variant rs137852276dbSNPEnsembl.1
Natural variantiVAR_017363412G → E in HEMB. 1 Publication1
Natural variantiVAR_006605413G → R in HEMB; moderate to severe. 2 Publications1
Natural variantiVAR_017321414P → T in HEMB; Bergamo; increased protein abundance; loss of function in blood coagulation. 3 PublicationsCorresponds to variant rs137852265dbSNPEnsembl.1
Natural variantiVAR_006606419V → E in HEMB; moderately severe. 2 PublicationsCorresponds to variant rs137852280dbSNPEnsembl.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 rs767828752dbSNPEnsembl.1
Natural variantiVAR_017364435C → Y in HEMB. 1 Publication1
Natural variantiVAR_006616436A → V in HEMB; moderately severe; Niigata. 1 PublicationCorresponds to variant rs137852266dbSNPEnsembl.1
Natural variantiVAR_017365442G → E in HEMB. 1 Publication1
Natural variantiVAR_017322442G → R in HEMB; severe; Angers. 1 PublicationCorresponds to variant rs137852267dbSNPEnsembl.1
Natural variantiVAR_017323443I → T in HEMB; moderately severe; Long Beach, Los Angeles and Vancouver. 2 PublicationsCorresponds to variant rs137852268dbSNPEnsembl.1
Natural variantiVAR_006617445T → TIYT in HEMB; severe; Lousada. 1
Natural variantiVAR_073983447V → VYKTV in HEMB; reduced protein abundance; loss of function in blood coagulation. 1 Publication1
Natural variantiVAR_006618449R → Q in HEMB; mild. 1 PublicationCorresponds to variant rs143018900dbSNPEnsembl.1
Natural variantiVAR_006619449R → W in HEMB; mild. 1 PublicationCorresponds to variant rs757996262dbSNPEnsembl.1
Natural variantiVAR_006620450Y → C in HEMB; severe. 1 Publication1
Natural variantiVAR_017324453W → R in HEMB. 1 PublicationCorresponds to variant rs137852269dbSNPEnsembl.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).

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 rs137852283dbSNPEnsembl.1

Pharmaceutical usei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi2158.
MalaCardsiF9.
MIMi300807. phenotype.
306900. phenotype.
OpenTargetsiENSG00000101981.
Orphaneti169799. Mild hemophilia B.
169796. Moderately severe hemophilia B.
169793. Severe hemophilia B.
177929. Symptomatic form of hemophilia B in female carriers.
PharmGKBiPA27954.

Protein family/group databases

Allergomei9616. Hom s Factor IX.

Chemistry databases

ChEMBLiCHEMBL2016.
DrugBankiDB00025. Antihemophilic Factor (Recombinant).
DB00170. Menadione.
GuidetoPHARMACOLOGYi2364.

Polymorphism and mutation databases

BioMutaiF9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000002775529 – 461 PublicationAdd BLAST18
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
Modified residuei534-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei634-carboxyglutamatePROSITE-ProRule annotationBy similarity1
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
Glycosylationi85O-linked (GalNAc...)1 Publication1
Modified residuei864-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi97 ↔ 108Combined sources2 Publications
GlycosylationiCAR_00000999O-linked (Glc...); alternate2 Publications1
Glycosylationi99O-linked (Xyl...); alternate1 Publication1
Disulfide bondi102 ↔ 117Combined sources2 Publications
GlycosylationiCAR_000010107O-linked (Fuc...)1 Publication1
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...)Sequence analysis1
Modified residuei204Phosphoserine2 Publications1
Modified residuei205Phosphothreonine; alternate1 Publication1
Glycosylationi205O-linked (GalNAc...); alternate2 Publications1
Glycosylationi213N-linked (GlcNAc...)Sequence analysis1
Glycosylationi215O-linked (GalNAc...)2 Publications1
Glycosylationi225O-linked (GalNAc...)1 Publication1
Disulfide bondi252 ↔ 268Combined sources4 Publications
Disulfide bondi382 ↔ 396Combined sources4 Publications
Disulfide bondi407 ↔ 435Combined sources4 Publications

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
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

PaxDbiP00740.
PeptideAtlasiP00740.
PRIDEiP00740.

PTM databases

iPTMnetiP00740.
PhosphoSitePlusiP00740.
UniCarbKBiP00740.

Miscellaneous databases

PMAP-CutDBP00740.

Expressioni

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

BgeeiENSG00000101981.
CleanExiHS_F9.
GenevisibleiP00740. HS.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi108456. 33 interactors.
DIPiDIP-58520N.
IntActiP00740. 1 interactor.
STRINGi9606.ENSP00000218099.

Chemistry databases

BindingDBiP00740.

Structurei

Secondary structure

1461
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 52Combined sources3
Helixi60 – 64Combined sources5
Beta strandi65 – 67Combined sources3
Helixi71 – 75Combined sources5
Beta strandi78 – 80Combined sources3
Helixi81 – 90Combined sources10
Turni96 – 99Combined sources4
Beta strandi102 – 105Combined sources4
Beta strandi107 – 111Combined sources5
Beta strandi114 – 118Combined sources5
Turni125 – 128Combined sources4
Turni134 – 136Combined sources3
Helixi137 – 140Combined sources4
Beta strandi142 – 148Combined sources7
Turni149 – 151Combined sources3
Beta strandi152 – 156Combined sources5
Beta strandi161 – 163Combined sources3
Beta strandi165 – 168Combined sources4
Beta strandi170 – 172Combined sources3
Beta strandi174 – 176Combined sources3
Beta strandi187 – 189Combined sources3
Beta strandi241 – 248Combined sources8
Beta strandi252 – 258Combined sources7
Beta strandi261 – 264Combined sources4
Helixi266 – 268Combined sources3
Beta strandi269 – 271Combined sources3
Beta strandi276 – 280Combined sources5
Beta strandi282 – 286Combined sources5
Beta strandi292 – 301Combined sources10
Turni303 – 306Combined sources4
Beta strandi307 – 310Combined sources4
Turni311 – 314Combined sources4
Beta strandi317 – 323Combined sources7
Helixi339 – 347Combined sources9
Beta strandi350 – 360Combined sources11
Beta strandi370 – 377Combined sources8
Helixi379 – 384Combined sources6
Beta strandi394 – 398Combined sources5
Beta strandi414 – 419Combined sources6
Beta strandi<