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Protein

Prothrombin

Gene

F2

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

Functioni

Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.1 Publication

Catalytic activityi

Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.

Enzyme regulationi

Inhibited by SERPINA5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei406Charge relay system1
Active sitei462Charge relay system1
Active sitei568Charge relay system1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • growth factor activity Source: BHF-UCL
  • receptor binding Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB
  • thrombospondin receptor activity Source: BHF-UCL

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • blood coagulation Source: Reactome
  • blood coagulation, intrinsic pathway Source: Reactome
  • cell surface receptor signaling pathway Source: BHF-UCL
  • cellular protein metabolic process Source: Reactome
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • fibrinolysis Source: UniProtKB
  • leukocyte migration Source: Reactome
  • multicellular organism development Source: ProtInc
  • negative regulation of astrocyte differentiation Source: BHF-UCL
  • negative regulation of fibrinolysis Source: BHF-UCL
  • negative regulation of platelet activation Source: BHF-UCL
  • negative regulation of proteolysis Source: BHF-UCL
  • peptidyl-glutamic acid carboxylation Source: Reactome
  • platelet activation Source: BHF-UCL
  • positive regulation of blood coagulation Source: BHF-UCL
  • positive regulation of cell growth Source: Ensembl
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of collagen biosynthetic process Source: BHF-UCL
  • positive regulation of lipid kinase activity Source: BHF-UCL
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  • positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
  • positive regulation of protein localization to nucleus Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of reactive oxygen species metabolic process Source: UniProtKB
  • positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  • proteolysis Source: ProtInc
  • regulation of blood coagulation Source: UniProtKB
  • regulation of cell shape Source: Ensembl
  • regulation of cytosolic calcium ion concentration Source: BHF-UCL
  • regulation of gene expression Source: Ensembl
  • response to wounding Source: BHF-UCL
  • signal peptide processing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Acute phase, Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciZFISH:HS11470-MONOMER.
BRENDAi3.4.21.5. 2681.
ReactomeiR-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-HSA-416476. G alpha (q) signalling events.
R-HSA-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-HSA-76009. Platelet Aggregation (Plug Formation).
SABIO-RKP00734.
SIGNORiP00734.

Protein family/group databases

MEROPSiS01.217.

Names & Taxonomyi

Protein namesi
Recommended name:
Prothrombin (EC:3.4.21.5)
Alternative name(s):
Coagulation factor II
Cleaved into the following 4 chains:
Gene namesi
Name:F2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3535. F2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor II deficiency (FA2D)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.
See also OMIM:613679
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05523272E → G in FA2D; Shanghai. 1 Publication1
Natural variantiVAR_006711200E → K in FA2D; prothrombin type 3; variant confirmed at protein level. 2 PublicationsCorresponds to variant rs62623459dbSNPEnsembl.1
Natural variantiVAR_006712314R → C in FA2D; Barcelona/Madrid. 1 PublicationCorresponds to variant rs121918477dbSNPEnsembl.1
Natural variantiVAR_006713314R → H in FA2D; Padua-1. 1 PublicationCorresponds to variant rs754231232dbSNPEnsembl.1
Natural variantiVAR_006714380M → T in FA2D; Himi-1. 1 PublicationCorresponds to variant rs121918481dbSNPEnsembl.1
Natural variantiVAR_006715425R → C in FA2D; Quick-1. 1 PublicationCorresponds to variant rs121918479dbSNPEnsembl.1
Natural variantiVAR_006716431R → H in FA2D; Himi-2. 1 PublicationCorresponds to variant rs121918482dbSNPEnsembl.1
Natural variantiVAR_006717461R → W in FA2D; Tokushima. 3 PublicationsCorresponds to variant rs121918478dbSNPEnsembl.1
Natural variantiVAR_006718509E → A in FA2D; Salakta/Frankfurt. 2 Publications1
Natural variantiVAR_006719601G → V in FA2D; Quick-2. 1 PublicationCorresponds to variant rs121918480dbSNPEnsembl.1
Ischemic stroke (ISCHSTR)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
See also OMIM:601367
Thrombophilia due to thrombin defect (THPH1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis.
Disease descriptionA multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
See also OMIM:188050
Pregnancy loss, recurrent, 2 (RPRGL2)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.
See also OMIM:614390

Pharmaceutical usei

The peptide TP508 also known as Chrysalin (Orthologic) could be used to accelerate repair of both soft and hard tissues.

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNETi2147.
MalaCardsiF2.
MIMi188050. phenotype.
601367. phenotype.
613679. phenotype.
614390. phenotype.
OpenTargetsiENSG00000180210.
Orphaneti329217. Cerebral sinovenous thrombosis.
325. Congenital factor II deficiency.
64738. Non rare thrombophilia.
PharmGKBiPA157.

Chemistry databases

ChEMBLiCHEMBL204.
DrugBankiDB00025. Antihemophilic Factor (Recombinant).
DB00278. Argatroban.
DB05777. ART-123.
DB00006. Bivalirudin.
DB00100. Coagulation Factor IX.
DB06695. Dabigatran etexilate.
DB00055. Drotrecogin alfa.
DB00001. Lepirudin.
DB00170. Menadione.
DB01123. Proflavine.
DB04786. Suramin.
DB04898. Ximelagatran.
GuidetoPHARMACOLOGYi2362.

Polymorphism and mutation databases

BioMutaiF2.
DMDMi135807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002815925 – 432 PublicationsAdd BLAST19
ChainiPRO_000002816044 – 622ProthrombinAdd BLAST579
PeptideiPRO_000002816144 – 198Activation peptide fragment 1Add BLAST155
PeptideiPRO_0000028162199 – 327Activation peptide fragment 2Add BLAST129
ChainiPRO_0000028163328 – 363Thrombin light chainAdd BLAST36
ChainiPRO_0000028164364 – 622Thrombin heavy chainAdd BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei494-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei504-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei574-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi60 ↔ 65
Modified residuei624-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei634-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei684-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi90 ↔ 103
Disulfide bondi108 ↔ 186
Glycosylationi121N-linked (GlcNAc...) (complex)3 Publications1
Disulfide bondi129 ↔ 169
Glycosylationi143N-linked (GlcNAc...) (complex)3 Publications1
Disulfide bondi157 ↔ 181
Disulfide bondi213 ↔ 291
Disulfide bondi234 ↔ 274
Disulfide bondi262 ↔ 286
Disulfide bondi336 ↔ 482Interchain (between light and heavy chains)
Disulfide bondi391 ↔ 407
Glycosylationi416N-linked (GlcNAc...) (complex)5 Publications1
Disulfide bondi536 ↔ 550By similarity
Disulfide bondi564 ↔ 594By similarity

Post-translational modificationi

The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.2 Publications
N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei198 – 199Cleavage; by thrombin2
Sitei327 – 328Cleavage; by factor Xa2
Sitei363 – 364Cleavage; by factor Xa2

Keywords - PTMi

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

Proteomic databases

MaxQBiP00734.
PaxDbiP00734.
PeptideAtlasiP00734.
PRIDEiP00734.
TopDownProteomicsiP00734.

2D gel databases

SWISS-2DPAGEP00734.

PTM databases

iPTMnetiP00734.
PhosphoSitePlusiP00734.
UniCarbKBiP00734.

Miscellaneous databases

PMAP-CutDBP00734.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000180210.
CleanExiHS_F2.
ExpressionAtlasiP00734. baseline and differential.
GenevisibleiP00734. HS.

Organism-specific databases

HPAiCAB016780.
CAB018650.
HPA051476.
HPA054698.

Interactioni

Subunit structurei

Heterodimer (named alpha-thrombin) of a light and a heavy chain; disulfide-linked. Forms a heterodimer with SERPINA5.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q846V45EBI-297094,EBI-989571From a different organism.
THBDP072044EBI-297094,EBI-941422

GO - Molecular functioni

  • growth factor activity Source: BHF-UCL
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108447. 16 interactors.
DIPiDIP-6115N.
IntActiP00734. 10 interactors.
MINTiMINT-147273.
STRINGi9606.ENSP00000308541.

Chemistry databases

BindingDBiP00734.

Structurei

Secondary structure

1622
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi47 – 60Combined sources14
Helixi67 – 74Combined sources8
Helixi77 – 89Combined sources13
Turni90 – 92Combined sources3
Helixi97 – 105Combined sources9
Beta strandi107 – 109Combined sources3
Turni112 – 115Combined sources4
Beta strandi124 – 126Combined sources3
Beta strandi128 – 130Combined sources3
Turni144 – 146Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi167 – 173Combined sources7
Beta strandi177 – 180Combined sources4
Turni186 – 188Combined sources3
Beta strandi191 – 193Combined sources3
Beta strandi211 – 214Combined sources4
Helixi216 – 218Combined sources3
Beta strandi229 – 231Combined sources3
Beta strandi233 – 235Combined sources3
Beta strandi237 – 239Combined sources3
Helixi240 – 246Combined sources7
Beta strandi247 – 249Combined sources3
Beta strandi253 – 255Combined sources3
Beta strandi273 – 275Combined sources3
Beta strandi277 – 279Combined sources3
Beta strandi283 – 285Combined sources3
Helixi295 – 297Combined sources3
Beta strandi322 – 324Combined sources3
Helixi326 – 329Combined sources4
Beta strandi330 – 332Combined sources3
Turni334 – 337Combined sources4
Turni340 – 342Combined sources3
Helixi343 – 345Combined sources3
Helixi352 – 358Combined sources7
Turni360 – 362Combined sources3
Beta strandi367 – 369Combined sources3
Beta strandi372 – 375Combined sources4
Beta strandi378 – 383Combined sources6
Turni384 – 387Combined sources4
Beta strandi388 – 395Combined sources8
Beta strandi397 – 403Combined sources7
Helixi405 – 407Combined sources3
Beta strandi408 – 410Combined sources3
Helixi411 – 413Combined sources3
Helixi419 – 421Combined sources3
Beta strandi422 – 427Combined sources6
Beta strandi430 – 433Combined sources4
Turni436 – 438Combined sources3
Beta strandi440 – 449Combined sources10
Turni455 – 458Combined sources4
Beta strandi464 – 470Combined sources7
Beta strandi475 – 477Combined sources3
Helixi486 – 492Combined sources7
Beta strandi495 – 497Combined sources3
Beta strandi498 – 504Combined sources7
Beta strandi507 – 510Combined sources4
Turni513 – 515Combined sources3
Beta strandi516 – 518Combined sources3
Beta strandi524 – 530Combined sources7
Helixi533 – 538Combined sources6
Beta strandi540 – 542Combined sources3
Beta strandi548 – 551Combined sources4
Helixi555 – 557Combined sources3
Turni565 – 569Combined sources5
Beta strandi571 – 575Combined sources5
Turni577 – 579Combined sources3
Beta strandi582 – 590Combined sources9
Beta strandi592 – 595Combined sources4
Beta strandi596 – 598Combined sources3
Beta strandi601 – 605Combined sources5
Helixi607 – 609Combined sources3
Helixi610 – 619Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2CX-ray2.10H364-622[»]
L328-363[»]
1A3BX-ray1.80H364-622[»]
L328-363[»]
1A3EX-ray1.85H364-622[»]
L328-363[»]
1A46X-ray2.12H364-622[»]
L328-363[»]
1A4WX-ray1.80H364-622[»]
L328-363[»]
1A5GX-ray2.06H364-622[»]
L328-363[»]
1A61X-ray2.20H364-622[»]
L328-363[»]
1ABIX-ray2.30H364-622[»]
L328-363[»]
1ABJX-ray2.40H364-622[»]
L328-363[»]
1AD8X-ray2.00H364-622[»]
L328-363[»]
1AE8X-ray2.00H364-622[»]
L328-363[»]
1AFEX-ray2.00H364-622[»]
L328-363[»]
1AHTX-ray1.60H364-622[»]
L328-363[»]
1AI8X-ray1.85H364-622[»]
L328-363[»]
1AIXX-ray2.10H364-622[»]
L328-363[»]
1AWFX-ray2.20H364-622[»]
L328-363[»]
1AWHX-ray3.00A/C328-363[»]
B/D364-622[»]
1AY6X-ray1.80H364-622[»]
L328-363[»]
1B5GX-ray2.07H364-622[»]
L328-363[»]
1B7XX-ray2.10A328-363[»]
B364-622[»]
1BA8X-ray1.80A328-363[»]
B364-622[»]
1BB0X-ray2.10A328-363[»]
B364-622[»]
1BCUX-ray2.00H364-622[»]
L328-363[»]
1BHXX-ray2.30A331-349[»]
B364-510[»]
F518-622[»]
1BMMX-ray2.60H364-622[»]
L328-363[»]
1BMNX-ray2.80H364-622[»]
L328-363[»]
1BTHX-ray2.30H/K364-622[»]
J/L328-363[»]
1C1UX-ray1.75H364-616[»]
L328-363[»]
1C1VX-ray1.98H364-616[»]
L328-363[»]
1C1WX-ray1.90H364-616[»]
L328-363[»]
1C4UX-ray2.101328-363[»]
2364-622[»]
1C4VX-ray2.101328-363[»]
2364-622[»]
1C4YX-ray2.701328-363[»]
2364-622[»]
1C5LX-ray1.47H364-622[»]
L328-363[»]
1C5NX-ray1.50H364-622[»]
L328-363[»]
1C5OX-ray1.90H364-622[»]
L328-363[»]
1CA8X-ray2.10A328-363[»]
B364-622[»]
1D3DX-ray2.04A333-360[»]
B364-620[»]
1D3PX-ray2.10A328-363[»]
B364-622[»]
1D3QX-ray2.90A328-363[»]
B364-622[»]
1D3TX-ray3.00A328-363[»]
B364-622[»]
1D4PX-ray2.07A328-363[»]
B364-622[»]
1D6WX-ray2.00A334-620[»]
1D9IX-ray2.30A334-621[»]
1DE7X-ray2.00H/K364-619[»]
J/L328-360[»]
1DITX-ray2.30H364-622[»]
L328-363[»]
1DM4X-ray2.50A328-362[»]
B363-622[»]
1DOJX-ray1.70A328-622[»]
1DWBX-ray3.16H364-622[»]
L328-363[»]
1DWCX-ray3.00H364-622[»]
L328-363[»]
1DWDX-ray3.00H364-622[»]
L328-363[»]
1DWEX-ray3.00H364-622[»]
L328-363[»]
1DX5X-ray2.30A/B/C/D328-363[»]
M/N/O/P364-622[»]
1E0FX-ray3.10A/B/C328-363[»]
D/E/F364-622[»]
1EB1X-ray1.80H364-620[»]
L334-360[»]
1EOJX-ray2.10A332-620[»]
1EOLX-ray2.10A332-620[»]
1FPCX-ray2.30H364-622[»]
L328-363[»]
1FPHX-ray2.50H364-622[»]
L328-363[»]
1G30X-ray2.00A328-363[»]
B364-622[»]
1G32X-ray1.90A328-363[»]
B364-622[»]
1G37X-ray2.00A334-620[»]
1GHVX-ray1.85H364-620[»]
L328-363[»]
1GHWX-ray1.75H364-620[»]
L328-363[»]
1GHXX-ray1.65H364-620[»]
L328-363[»]
1GHYX-ray1.85H364-620[»]
L328-363[»]
1GJ4X-ray1.81H364-621[»]
L328-363[»]
1GJ5X-ray1.73H364-621[»]
L328-363[»]
1H8DX-ray1.40H364-621[»]
L333-360[»]
1H8IX-ray1.75H364-622[»]
L334-360[»]
1HAGX-ray2.00E328-622[»]
1HAHX-ray2.30H364-622[»]
L328-363[»]
1HAIX-ray2.40H364-622[»]
L328-363[»]
1HAOX-ray2.80H364-622[»]
L328-363[»]
1HAPX-ray2.80H364-622[»]
L328-360[»]
1HBTX-ray2.00H364-622[»]
L328-363[»]
1HDTX-ray2.60H364-622[»]
L331-363[»]
1HGTX-ray2.20H364-622[»]
L328-363[»]
1HLTX-ray3.00H/K364-622[»]
J/L334-349[»]
1HUTX-ray2.90H364-622[»]
L328-363[»]
1HXEX-ray2.10H364-622[»]
L328-363[»]
1HXFX-ray2.10H364-622[»]
L328-363[»]
1IHSX-ray2.00H364-622[»]
L328-363[»]
1IHTX-ray2.10H364-622[»]
L328-363[»]
1JMOX-ray2.20H363-622[»]
L315-362[»]
1JOUX-ray1.80A/C/E315-363[»]
B/D/F364-622[»]
1JWTX-ray2.50A328-622[»]
1K21X-ray1.86H364-622[»]
L328-363[»]
1K22X-ray1.93H364-622[»]
L328-363[»]
1KTSX-ray2.40A328-363[»]
B364-622[»]
1KTTX-ray2.10A328-363[»]
B364-622[»]
1LHCX-ray1.95H364-622[»]
L328-363[»]
1LHDX-ray2.35H364-622[»]
L328-363[»]
1LHEX-ray2.25H364-622[»]
L328-363[»]
1LHFX-ray2.40H364-622[»]
L328-363[»]
1LHGX-ray2.25H364-622[»]
L328-363[»]
1MH0X-ray2.80A/B334-620[»]
1MU6X-ray1.99A328-363[»]
B364-622[»]
1MU8X-ray2.00A328-363[»]
B364-622[»]
1MUEX-ray2.00A328-363[»]
B364-622[»]
1NM6X-ray1.80A335-621[»]
1NO9X-ray1.90H364-622[»]
L328-363[»]
1NRNX-ray3.10H364-622[»]
L328-363[»]
1NROX-ray3.10H364-622[»]
L328-363[»]
1NRPX-ray3.00H364-622[»]
L328-363[»]
1NRQX-ray3.50H364-622[»]
L328-363[»]
1NRRX-ray2.40H364-622[»]
L328-363[»]
1NRSX-ray2.40H364-622[»]
L328-349[»]
1NT1X-ray2.00A335-621[»]
1NU7X-ray2.20A/E332-359[»]
B/F364-622[»]
1NU9X-ray2.20A/D332-622[»]
1NY2X-ray2.301328-363[»]
2364-622[»]
1NZQX-ray2.18H364-620[»]
L328-361[»]
1O0DX-ray2.44H364-622[»]
L328-363[»]
1O2GX-ray1.58H364-622[»]
L328-363[»]
1O5GX-ray1.75H364-622[»]
L328-363[»]
1OOKX-ray2.30A328-363[»]
B364-622[»]
1OYTX-ray1.67H364-622[»]
L328-363[»]
1P8VX-ray2.60B333-361[»]
C364-621[»]
1PPBX-ray1.92H364-622[»]
L328-363[»]
1QBVX-ray1.80H364-622[»]
L328-359[»]
1QHRX-ray2.20A328-363[»]
B364-622[»]
1QJ1X-ray2.00A328-363[»]
B364-622[»]
1QJ6X-ray2.20A328-363[»]
B364-622[»]
1QJ7X-ray2.20A328-363[»]
B364-622[»]
1QURX-ray2.00H364-620[»]
L334-360[»]
1RD3X-ray2.50A/C328-363[»]
B/D364-622[»]
1RIWX-ray2.04A328-363[»]
B364-510[»]
C518-622[»]
1SB1X-ray1.90H364-621[»]
L333-361[»]
1SFQX-ray1.91A/D328-363[»]
B/E364-622[»]
1SG8X-ray2.30A/D328-363[»]
B/E364-622[»]
1SGIX-ray2.30A/D328-363[»]
B/E364-622[»]
1SHHX-ray1.55A/D328-363[»]
B/E364-622[»]
1SL3X-ray1.81A335-621[»]
1SR5X-ray3.10B328-363[»]
C364-622[»]
1T4UX-ray2.00H364-622[»]
L334-359[»]
1T4VX-ray2.00H364-622[»]
L334-359[»]
1TA2X-ray2.30A335-621[»]
1TA6X-ray1.90A335-621[»]
1TB6X-ray2.50H364-622[»]
L315-363[»]
1TBZX-ray2.30H364-622[»]
L328-363[»]
1THPX-ray2.10A328-362[»]
B364-620[»]
1THRX-ray2.30H364-622[»]
L328-349[»]
1THSX-ray2.20H364-622[»]
L328-363[»]
1TMBX-ray2.30H364-622[»]
L328-363[»]
1TMTX-ray2.20H364-622[»]
L328-363[»]
1TMUX-ray2.50H364-620[»]
L333-349[»]
1TOMX-ray1.80H364-622[»]
L328-363[»]
1TQ0X-ray2.80A/C333-363[»]
B/D364-620[»]
1TQ7X-ray2.40A320-363[»]
B364-620[»]
1TWXX-ray2.40A334-349[»]
B364-622[»]
1UMAX-ray2.00H364-622[»]
L328-363[»]
1UVSX-ray2.80H364-622[»]
L328-363[»]
1VR1X-ray1.90H364-620[»]
L334-360[»]
1VZQX-ray1.54H364-620[»]
L334-360[»]
1W7GX-ray1.65H364-622[»]
L328-363[»]
1WAYX-ray2.02A328-363[»]
B364-622[»]
1WBGX-ray2.20A328-363[»]
B364-622[»]
1XM1X-ray2.30A328-622[»]
1XMNX-ray1.85A/C/E/G328-363[»]
B/D/F/H364-622[»]
1YPEX-ray1.81H364-620[»]
L334-360[»]
1YPGX-ray1.80H364-620[»]
L334-360[»]
1YPJX-ray1.78H364-620[»]
L334-360[»]
1YPKX-ray1.78H364-620[»]
L334-360[»]
1YPLX-ray1.85H364-620[»]
L334-360[»]
1YPMX-ray1.85H364-620[»]
L334-360[»]
1Z71X-ray1.80A335-621[»]
1Z8IX-ray2.00A324-361[»]
B364-622[»]
1Z8JX-ray2.00A322-361[»]
B364-622[»]
1ZGIX-ray2.20A335-621[»]
1ZGVX-ray2.20A335-621[»]
1ZRBX-ray1.90A335-621[»]
2A0QX-ray1.90A/C334-349[»]
B/D364-620[»]
2A2XX-ray2.44H364-622[»]
L330-363[»]
2A45X-ray3.65A/D328-363[»]
B/E364-622[»]
2AFQX-ray1.93A/C332-360[»]
B/D364-622[»]
2ANKX-ray2.46H364-622[»]
L330-363[»]
2ANMX-ray2.40H364-620[»]
L328-363[»]
2B5TX-ray2.10A/C315-363[»]
B/D364-622[»]
2BDYX-ray1.61A334-622[»]
2BVRX-ray1.25H364-622[»]
L328-363[»]
2BVSX-ray1.40H364-622[»]
L328-363[»]
2BVXX-ray3.20H364-622[»]
L328-363[»]
2BXTX-ray1.83H364-622[»]
L328-363[»]
2BXUX-ray2.80H364-622[»]
L328-363[»]
2C8WX-ray1.96A328-363[»]
B364-622[»]
2C8XX-ray2.17A328-363[»]
B364-622[»]
2C8YX-ray2.20A328-363[»]
B364-622[»]
2C8ZX-ray2.14A328-363[»]
B364-622[»]
2C90X-ray2.25A328-363[»]
B364-622[»]
2C93X-ray2.20A328-363[»]
B364-622[»]
2CF8X-ray1.30H364-620[»]
L334-361[»]
2CF9X-ray1.79H364-620[»]
L334-361[»]
2CN0X-ray1.30H364-620[»]
L334-361[»]
2FEQX-ray2.44H364-622[»]
L328-363[»]
2FESX-ray2.42H364-622[»]
L328-363[»]
2GDEX-ray2.00H364-622[»]
L328-363[»]
2GP9X-ray1.87A328-362[»]
B364-620[»]
2H9TX-ray2.40H364-622[»]
L328-363[»]
2HGTX-ray2.20H364-622[»]
L328-363[»]
2HNTX-ray2.50C364-433[»]
E437-517[»]
F518-622[»]
L328-363[»]
2HPPX-ray3.30H364-622[»]
L328-363[»]
2HPQX-ray3.30H364-622[»]
L328-363[»]
P213-291[»]
2HWLX-ray2.40A/C328-363[»]
B/D364-622[»]
2JH0X-ray1.70C328-361[»]
D364-622[»]
2JH5X-ray2.50C328-363[»]
D364-622[»]
2JH6X-ray2.21C328-361[»]
D364-622[»]
2OD3X-ray1.75A328-363[»]
B364-622[»]
2PGBX-ray1.54A328-363[»]
B364-622[»]
2PGQX-ray1.80A319-363[»]
B364-622[»]
2PKSX-ray2.50A334-360[»]
B364-510[»]
C518-619[»]
2PW8X-ray1.84H364-621[»]
L334-360[»]
2R2MX-ray2.10A334-359[»]
B364-622[»]
2THFX-ray2.10A328-363[»]
B364-622[»]
2UUFX-ray1.26A328-363[»]
B364-622[»]
2UUJX-ray1.32A328-363[»]
B364-622[»]
2UUKX-ray1.39A328-363[»]
B364-622[»]
2V3HX-ray1.79H364-620[»]
L334-361[»]
2V3OX-ray1.79H364-620[»]
L334-361[»]
2ZC9X-ray1.58H364-622[»]
L328-363[»]
2ZDAX-ray1.73H364-622[»]
L328-363[»]
2ZDVX-ray1.72H364-622[»]
L328-363[»]
2ZF0X-ray2.20H364-622[»]
L328-363[»]
2ZFFX-ray1.47H364-622[»]
L328-363[»]
2ZFPX-ray2.25H364-622[»]
L328-363[»]
2ZFQX-ray1.80H364-622[»]
L328-363[»]
2ZFRX-ray1.85H364-622[»]
L328-363[»]
2ZG0X-ray1.75H364-622[»]
L328-363[»]
2ZGBX-ray1.60H364-622[»]
L328-363[»]
2ZGXX-ray1.80H364-622[»]
L328-363[»]
2ZHEX-ray2.10H364-622[»]
L328-363[»]
2ZHFX-ray1.98H364-622[»]
L328-363[»]
2ZHQX-ray1.96H364-622[»]
L328-363[»]
2ZHWX-ray2.02H364-622[»]
L328-363[»]
2ZI2X-ray1.65H364-622[»]
L328-363[»]
2ZIQX-ray1.65H364-622[»]
L328-363[»]
2ZNKX-ray1.80H364-622[»]
L328-363[»]
2ZO3X-ray1.70H364-622[»]
L328-363[»]
3B23X-ray2.40A328-363[»]
B364-622[»]
3B9FX-ray1.60H364-622[»]
L315-363[»]
3BEFX-ray2.20A/D320-363[»]
B/E364-622[»]
3BEIX-ray1.55A320-363[»]
B364-622[»]
3BF6X-ray2.50H364-622[»]
L328-363[»]
3BIUX-ray2.30H364-620[»]
L333-361[»]
3BIVX-ray1.80H364-620[»]
L333-361[»]
3BV9X-ray1.80A333-363[»]
B364-622[»]
3C1KX-ray1.84A335-621[»]
3C27X-ray2.18A334-359[»]
B364-622[»]
3D49X-ray1.50H364-622[»]
L328-363[»]
3DA9X-ray1.80A328-363[»]
B364-622[»]
3DD2X-ray1.90H364-621[»]
L332-361[»]
3DHKX-ray1.73H364-622[»]
L328-363[»]
3DT0X-ray2.40H364-622[»]
L328-363[»]
3DUXX-ray1.60H364-622[»]
L328-363[»]
3E6PX-ray2.10H364-622[»]
L206-363[»]
3EE0X-ray2.75A328-363[»]
B364-622[»]
3EGKX-ray2.20H364-622[»]
L328-363[»]
3EQ0X-ray1.53H364-622[»]
L328-363[»]
3F68X-ray1.75H364-622[»]
L328-363[»]
3GICX-ray1.55A328-363[»]
B364-622[»]
3GISX-ray2.40A/C/E315-363[»]
B/D/F364-622[»]
3HATX-ray2.50H364-622[»]
L328-363[»]
3HKJX-ray2.60A/D333-363[»]
B/E364-622[»]
3HTCX-ray2.30H364-622[»]
L328-363[»]
3JZ1X-ray1.60A328-363[»]
B364-622[»]
3JZ2X-ray2.40A328-363[»]
B364-622[»]
3K65X-ray1.85A199-314[»]
B315-622[»]
3LDXX-ray2.25H364-622[»]
L328-363[»]
3LU9X-ray1.80A/D318-363[»]
B/E364-622[»]
3NXPX-ray2.20A199-622[»]
3P17X-ray1.43H364-622[»]
L328-363[»]
3P6ZX-ray1.70A/G328-363[»]
B/H364-622[»]
3P70X-ray2.55A/C/E/G328-363[»]
B/D/F/H364-622[»]
3PMHX-ray3.20A328-363[»]
B364-622[»]
3PO1X-ray1.65A334-360[»]
B364-510[»]
C518-619[»]
3QDZX-ray2.80A/C333-363[»]
B/D364-622[»]
3QGNX-ray2.10A333-363[»]
B364-622[»]
3QLPX-ray2.14H364-622[»]
L328-363[»]
3QTOX-ray1.52H364-622[»]
L328-363[»]
3QTVX-ray1.63H364-622[»]
L328-363[»]
3QWCX-ray1.75H364-622[»]
L328-363[»]
3QX5X-ray1.35H364-622[»]
L328-363[»]
3R3GX-ray1.75A333-363[»]
B364-622[»]
3RLWX-ray1.69H364-622[»]
L328-363[»]
3RLYX-ray1.51H364-622[»]
L328-363[»]
3RM0X-ray1.34H364-622[»]
L328-363[»]
3RM2X-ray1.23H364-622[»]
L328-363[»]
3RMLX-ray1.53H364-622[»]
L328-363[»]
3RMMX-ray1.58H364-622[»]
L328-363[»]
3RMNX-ray1.78H364-622[»]
L328-363[»]
3RMOX-ray1.40H364-622[»]
L328-363[»]
3S7HX-ray1.90A329-363[»]
B364-622[»]
3S7KX-ray1.90A/C329-363[»]
B/D364-622[»]
3SHAX-ray1.52H364-622[»]
L328-363[»]
3SHCX-ray1.90H364-622[»]
L328-363[»]
3SI3X-ray1.55H364-622[»]
L328-363[»]
3SI4X-ray1.27H364-622[»]
L328-363[»]
3SQEX-ray1.90E333-622[»]
3SQHX-ray2.20E333-622[»]
3SV2X-ray1.30H364-622[»]
L328-363[»]
3T5FX-ray1.45H364-622[»]
L328-363[»]
3TU7X-ray2.49H364-622[»]
L328-363[»]
3U69X-ray1.55H364-622[»]
L334-363[»]
3U8OX-ray1.28H364-622[»]
L334-363[»]
3U8RX-ray1.47H364-622[»]
L334-363[»]
3U8TX-ray1.86H364-620[»]
L334-360[»]
3U98X-ray1.45H364-622[»]
L328-363[»]
3U9AX-ray1.58H364-622[»]
L328-363[»]
3UTUX-ray1.55H364-622[»]
L328-363[»]
3UWJX-ray1.50H364-622[»]
L328-363[»]
3VXEX-ray1.25H364-622[»]
L328-363[»]
3VXFOther1.60H364-622[»]
L328-363[»]
4AX9X-ray1.90H364-620[»]
L334-361[»]
4AYVX-ray2.80A332-361[»]
B364-620[»]
4AYYX-ray2.60A332-361[»]
B364-620[»]
4AZ2X-ray2.60A332-361[»]
B364-620[»]
4BAHX-ray1.94A328-363[»]
B364-622[»]
4BAKX-ray1.94A328-363[»]
B364-622[»]
4BAMX-ray1.88A328-363[»]
B364-622[»]
4BANX-ray1.87A328-363[»]
B364-622[»]
4BAOX-ray1.87A328-363[»]
B364-622[»]
4BAQX-ray1.89A328-363[»]
B364-622[»]
4BOHX-ray2.60A/H364-622[»]
B/L328-363[»]
4CH2X-ray1.60A/C328-363[»]
B/D364-622[»]
4CH8X-ray1.75A/C/E/G328-363[»]
B/D/F/H364-622[»]
4DIHX-ray1.80H364-622[»]
L328-363[»]
4DIIX-ray2.05H364-622[»]
L328-363[»]
4DT7X-ray1.90A/C332-363[»]
B/D364-622[»]
4DY7X-ray2.80A/D315-363[»]
B/E364-622[»]
4E05X-ray2.30H364-622[»]
L328-363[»]
4E06X-ray3.20H364-622[»]
L328-363[»]
4E7RX-ray2.25G/H364-622[»]
L/M328-363[»]
4H6SX-ray2.19A333-363[»]
B364-622[»]
4H6TX-ray2.40A317-622[»]
4HFPX-ray2.40A/C333-363[»]
B/D364-622[»]
4HTCX-ray2.30H364-622[»]
L328-363[»]
4HZHX-ray3.30A/B90-622[»]
4I7YX-ray2.40H364-622[»]
L328-363[»]
4LOYX-ray1.77H364-620[»]
L334-360[»]
4LXBX-ray1.61H364-622[»]
L328-363[»]
4LZ1X-ray1.65H364-622[»]
L328-363[»]
4LZ4X-ray2.56A/C328-363[»]
B/D364-622[»]
4MLFX-ray2.20A331-363[»]
B364-622[»]
4N3LX-ray1.94H364-622[»]
L328-363[»]
4NZEX-ray1.98H364-622[»]
L328-363[»]
4NZQX-ray2.81A44-622[»]
4O03X-ray3.38A44-622[»]
4RKJX-ray1.70A330-363[»]
B364-622[»]
4RKOX-ray1.84A322-363[»]
B364-622[»]
4RN6X-ray3.00A/B333-622[»]
4THNX-ray2.50H364-622[»]
L328-363[»]
4UD9X-ray1.12H364-622[»]
L333-360[»]
4UDWX-ray1.16H364-621[»]
L333-360[»]
4UE7X-ray1.13H364-621[»]
L333-360[»]
4UEHX-ray1.16H364-621[»]
L333-361[»]
4UFDX-ray1.43H364-621[»]
L333-360[»]
4UFEX-ray1.59H364-621[»]
L333-361[»]
4UFFX-ray1.55H364-621[»]
L333-361[»]
4UFGX-ray1.65H364-621[»]
L333-361[»]
4YESX-ray1.50A328-363[»]
B364-622[»]
5A2MX-ray1.40H364-621[»]
L333-361[»]
5AF9X-ray1.18H364-621[»]
L333-361[»]
5AFYX-ray1.12H364-621[»]
L333-361[»]
5AFZX-ray1.53H364-621[»]
L333-361[»]
5AHGX-ray1.24H364-621[»]
L333-361[»]
5CMXX-ray2.98H364-622[»]
L328-363[»]
5DO4X-ray1.86H364-621[»]
L328-363[»]
5E8EX-ray1.90H364-622[»]
L328-363[»]
5EDKX-ray3.21A44-622[»]
5EDMX-ray2.20A44-622[»]
5GDSX-ray2.10H364-622[»]
L328-363[»]
5JDUX-ray1.70A/C331-363[»]
B/D364-622[»]
5LUWX-ray1.69H364-622[»]
L328-363[»]
5LUYX-ray2.24H364-622[»]
L328-363[»]
7KMEX-ray2.10H364-622[»]
L328-363[»]
8KMEX-ray2.101328-359[»]
2364-620[»]
ProteinModelPortaliP00734.
SMRiP00734.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00734.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 89GlaPROSITE-ProRule annotationAdd BLAST46
Domaini108 – 186Kringle 1PROSITE-ProRule annotationAdd BLAST79
Domaini213 – 291Kringle 2PROSITE-ProRule annotationAdd BLAST79
Domaini364 – 618Peptidase S1PROSITE-ProRule annotationAdd BLAST255

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni551 – 573High affinity receptor-binding region which is also known as the TP508 peptideAdd BLAST23

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 2 kringle domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IKPN. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOVERGENiHBG108381.
InParanoidiP00734.
KOiK01313.
OMAiGIECQLW.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00734.
TreeFamiTF327329.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.140.10. 1 hit.
4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000294. GLA_domain.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR003966. Prothrombin/thrombin.
IPR018992. Thrombin_light_chain.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PANTHERiPTHR24254:SF10. PTHR24254:SF10. 1 hit.
PfamiPF00594. Gla. 1 hit.
PF00051. Kringle. 2 hits.
PF09396. Thrombin_light. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001149. Thrombin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
PR01505. PROTHROMBIN.
SMARTiSM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS00021. KRINGLE_1. 2 hits.
PS50070. KRINGLE_2. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00734-1 [UniParc]FASTAAdd to basket

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        10         20         30         40         50
MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE
60 70 80 90 100
VRKGNLEREC VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL
110 120 130 140 150
AACLEGNCAE GLGTNYRGHV NITRSGIECQ LWRSRYPHKP EINSTTHPGA
160 170 180 190 200
DLQENFCRNP DSSTTGPWCY TTDPTVRRQE CSIPVCGQDQ VTVAMTPRSE
210 220 230 240 250
GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA QAKALSKHQD
260 270 280 290 300
FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG
310 320 330 340 350
DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK
360 370 380 390 400
TERELLESYI DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW
410 420 430 440 450
VLTAAHCLLY PPWDKNFTEN DLLVRIGKHS RTRYERNIEK ISMLEKIYIH
460 470 480 490 500
PRYNWRENLD RDIALMKLKK PVAFSDYIHP VCLPDRETAA SLLQAGYKGR
510 520 530 540 550
VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST RIRITDNMFC
560 570 580 590 600
AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY
610 620
GFYTHVFRLK KWIQKVIDQF GE
Length:622
Mass (Da):70,037
Last modified:January 1, 1990 - v2
Checksum:i8A25E1DA88208FCF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9 – 25Missing in BAG64719 (PubMed:14702039).CuratedAdd BLAST17
Sequence conflicti66S → N in BAD96497 (Ref. 4) Curated1
Sequence conflicti119H → N AA sequence (PubMed:266717).Curated1
Sequence conflicti121N → S AA sequence (PubMed:266717).Curated1
Sequence conflicti164T → I AA sequence (PubMed:266717).Curated1
Sequence conflicti164T → N in CAA23842 (PubMed:6305407).Curated1
Sequence conflicti176V → A AA sequence (PubMed:266717).Curated1
Sequence conflicti183I → T AA sequence (PubMed:266717).Curated1
Sequence conflicti194 – 195AM → MV AA sequence (PubMed:266717).Curated2
Sequence conflicti308D → DEE AA sequence (PubMed:266717).Curated1
Sequence conflicti335D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti337G → R in BAD96495 (Ref. 4) Curated1
Sequence conflicti349D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti369D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti398D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti414D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti485D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti494Q → G AA sequence (PubMed:873923).Curated1
Sequence conflicti504W → Y AA sequence (PubMed:873923).Curated1
Sequence conflicti509E → S AA sequence (PubMed:873923).Curated1
Sequence conflicti511W → V AA sequence (PubMed:873923).Curated1
Sequence conflicti514N → D AA sequence (PubMed:873923).Curated1
Sequence conflicti529 – 530PI → AL AA sequence (PubMed:873923).Curated2
Sequence conflicti590 – 592WGE → AGA in AAR08143 (Ref. 11) Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05523272E → G in FA2D; Shanghai. 1 Publication1
Natural variantiVAR_011781165T → M Polymorphism; confirmed at protein level. 4 PublicationsCorresponds to variant rs5896dbSNPEnsembl.1
Natural variantiVAR_006711200E → K in FA2D; prothrombin type 3; variant confirmed at protein level. 2 PublicationsCorresponds to variant rs62623459dbSNPEnsembl.1
Natural variantiVAR_006712314R → C in FA2D; Barcelona/Madrid. 1 PublicationCorresponds to variant rs121918477dbSNPEnsembl.1
Natural variantiVAR_006713314R → H in FA2D; Padua-1. 1 PublicationCorresponds to variant rs754231232dbSNPEnsembl.1
Natural variantiVAR_006714380M → T in FA2D; Himi-1. 1 PublicationCorresponds to variant rs121918481dbSNPEnsembl.1
Natural variantiVAR_011782386P → T Polymorphism; confirmed at protein level. 2 PublicationsCorresponds to variant rs5897dbSNPEnsembl.1
Natural variantiVAR_006715425R → C in FA2D; Quick-1. 1 PublicationCorresponds to variant rs121918479dbSNPEnsembl.1
Natural variantiVAR_006716431R → H in FA2D; Himi-2. 1 PublicationCorresponds to variant rs121918482dbSNPEnsembl.1
Natural variantiVAR_006717461R → W in FA2D; Tokushima. 3 PublicationsCorresponds to variant rs121918478dbSNPEnsembl.1
Natural variantiVAR_006718509E → A in FA2D; Salakta/Frankfurt. 2 Publications1
Natural variantiVAR_068913532E → Q Polymorphism; confirmed at protein level. 2 Publications1
Natural variantiVAR_006719601G → V in FA2D; Quick-2. 1 PublicationCorresponds to variant rs121918480dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17262 Genomic DNA. Translation: AAC63054.1.
AJ972449 mRNA. Translation: CAJ01369.1.
AK303747 mRNA. Translation: BAG64719.1.
AK312965 mRNA. Translation: BAG35804.1.
AK222775 mRNA. Translation: BAD96495.1.
AK222777 mRNA. Translation: BAD96497.1.
AF478696 Genomic DNA. Translation: AAL77436.1.
BC051332 mRNA. Translation: AAH51332.1.
V00595 mRNA. Translation: CAA23842.1.
AY344794 mRNA. Translation: AAR08143.1.
CCDSiCCDS31476.1.
PIRiA29351. TBHU.
RefSeqiNP_000497.1. NM_000506.4.
NP_001298186.1. NM_001311257.1.
UniGeneiHs.655207.

Genome annotation databases

EnsembliENST00000311907; ENSP00000308541; ENSG00000180210.
GeneIDi2147.
KEGGihsa:2147.
UCSCiuc001ndf.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Thrombin entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17262 Genomic DNA. Translation: AAC63054.1.
AJ972449 mRNA. Translation: CAJ01369.1.
AK303747 mRNA. Translation: BAG64719.1.
AK312965 mRNA. Translation: BAG35804.1.
AK222775 mRNA. Translation: BAD96495.1.
AK222777 mRNA. Translation: BAD96497.1.
AF478696 Genomic DNA. Translation: AAL77436.1.
BC051332 mRNA. Translation: AAH51332.1.
V00595 mRNA. Translation: CAA23842.1.
AY344794 mRNA. Translation: AAR08143.1.
CCDSiCCDS31476.1.
PIRiA29351. TBHU.
RefSeqiNP_000497.1. NM_000506.4.
NP_001298186.1. NM_001311257.1.
UniGeneiHs.655207.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2CX-ray2.10H364-622[»]
L328-363[»]
1A3BX-ray1.80H364-622[»]
L328-363[»]
1A3EX-ray1.85H364-622[»]
L328-363[»]
1A46X-ray2.12H364-622[»]
L328-363[»]
1A4WX-ray1.80H364-622[»]
L328-363[»]
1A5GX-ray2.06H364-622[»]
L328-363[»]
1A61X-ray2.20H364-622[»]
L328-363[»]
1ABIX-ray2.30H364-622[»]
L328-363[»]
1ABJX-ray2.40H364-622[»]
L328-363[»]
1AD8X-ray2.00H364-622[»]
L328-363[»]
1AE8X-ray2.00H364-622[»]
L328-363[»]
1AFEX-ray2.00H364-622[»]
L328-363[»]
1AHTX-ray1.60H364-622[»]
L328-363[»]
1AI8X-ray1.85H364-622[»]
L328-363[»]
1AIXX-ray2.10H364-622[»]
L328-363[»]
1AWFX-ray2.20H364-622[»]
L328-363[»]
1AWHX-ray3.00A/C328-363[»]
B/D364-622[»]
1AY6X-ray1.80H364-622[»]
L328-363[»]
1B5GX-ray2.07H364-622[»]
L328-363[»]
1B7XX-ray2.10A328-363[»]
B364-622[»]
1BA8X-ray1.80A328-363[»]
B364-622[»]
1BB0X-ray2.10A328-363[»]
B364-622[»]
1BCUX-ray2.00H364-622[»]
L328-363[»]
1BHXX-ray2.30A331-349[»]
B364-510[»]
F518-622[»]
1BMMX-ray2.60H364-622[»]
L328-363[»]
1BMNX-ray2.80H364-622[»]
L328-363[»]
1BTHX-ray2.30H/K364-622[»]
J/L328-363[»]
1C1UX-ray1.75H364-616[»]
L328-363[»]
1C1VX-ray1.98H364-616[»]
L328-363[»]
1C1WX-ray1.90H364-616[»]
L328-363[»]
1C4UX-ray2.101328-363[»]
2364-622[»]
1C4VX-ray2.101328-363[»]
2364-622[»]
1C4YX-ray2.701328-363[»]
2364-622[»]
1C5LX-ray1.47H364-622[»]
L328-363[»]
1C5NX-ray1.50H364-622[»]
L328-363[»]
1C5OX-ray1.90H364-622[»]
L328-363[»]
1CA8X-ray2.10A328-363[»]
B364-622[»]
1D3DX-ray2.04A333-360[»]
B364-620[»]
1D3PX-ray2.10A328-363[»]
B364-622[»]
1D3QX-ray2.90A328-363[»]
B364-622[»]
1D3TX-ray3.00A328-363[»]
B364-622[»]
1D4PX-ray2.07A328-363[»]
B364-622[»]
1D6WX-ray2.00A334-620[»]
1D9IX-ray2.30A334-621[»]
1DE7X-ray2.00H/K364-619[»]
J/L328-360[»]
1DITX-ray2.30H364-622[»]
L328-363[»]
1DM4X-ray2.50A328-362[»]
B363-622[»]
1DOJX-ray1.70A328-622[»]
1DWBX-ray3.16H364-622[»]
L328-363[»]
1DWCX-ray3.00H364-622[»]
L328-363[»]
1DWDX-ray3.00H364-622[»]
L328-363[»]
1DWEX-ray3.00H364-622[»]
L328-363[»]
1DX5X-ray2.30A/B/C/D328-363[»]
M/N/O/P364-622[»]
1E0FX-ray3.10A/B/C328-363[»]
D/E/F364-622[»]
1EB1X-ray1.80H364-620[»]
L334-360[»]
1EOJX-ray2.10A332-620[»]
1EOLX-ray2.10A332-620[»]
1FPCX-ray2.30H364-622[»]
L328-363[»]
1FPHX-ray2.50H364-622[»]
L328-363[»]
1G30X-ray2.00A328-363[»]
B364-622[»]
1G32X-ray1.90A328-363[»]
B364-622[»]
1G37X-ray2.00A334-620[»]
1GHVX-ray1.85H364-620[»]
L328-363[»]
1GHWX-ray1.75H364-620[»]
L328-363[»]
1GHXX-ray1.65H364-620[»]
L328-363[»]
1GHYX-ray1.85H364-620[»]
L328-363[»]
1GJ4X-ray1.81H364-621[»]
L328-363[»]
1GJ5X-ray1.73H364-621[»]
L328-363[»]
1H8DX-ray1.40H364-621[»]
L333-360[»]
1H8IX-ray1.75H364-622[»]
L334-360[»]
1HAGX-ray2.00E328-622[»]
1HAHX-ray2.30H364-622[»]
L328-363[»]
1HAIX-ray2.40H364-622[»]
L328-363[»]
1HAOX-ray2.80H364-622[»]
L328-363[»]
1HAPX-ray2.80H364-622[»]
L328-360[»]
1HBTX-ray2.00H364-622[»]
L328-363[»]
1HDTX-ray2.60H364-622[»]
L331-363[»]
1HGTX-ray2.20H364-622[»]
L328-363[»]
1HLTX-ray3.00H/K364-622[»]
J/L334-349[»]
1HUTX-ray2.90H364-622[»]
L328-363[»]
1HXEX-ray2.10H364-622[»]
L328-363[»]
1HXFX-ray2.10H364-622[»]
L328-363[»]
1IHSX-ray2.00H364-622[»]
L328-363[»]
1IHTX-ray2.10H364-622[»]
L328-363[»]
1JMOX-ray2.20H363-622[»]
L315-362[»]
1JOUX-ray1.80A/C/E315-363[»]
B/D/F364-622[»]
1JWTX-ray2.50A328-622[»]
1K21X-ray1.86H364-622[»]
L328-363[»]
1K22X-ray1.93H364-622[»]
L328-363[»]
1KTSX-ray2.40A328-363[»]
B364-622[»]
1KTTX-ray2.10A328-363[»]
B364-622[»]
1LHCX-ray1.95H364-622[»]
L328-363[»]
1LHDX-ray2.35H364-622[»]
L328-363[»]
1LHEX-ray2.25H364-622[»]
L328-363[»]
1LHFX-ray2.40H364-622[»]
L328-363[»]
1LHGX-ray2.25H364-622[»]
L