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P00734

- THRB_HUMAN

UniProt

P00734 - THRB_HUMAN

Protein

Prothrombin

Gene

F2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 202 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei198 – 1992Cleavage; by thrombin
    Sitei327 – 3282Cleavage; by factor Xa
    Sitei363 – 3642Cleavage; by factor Xa
    Active sitei406 – 4061Charge relay system
    Active sitei462 – 4621Charge relay system
    Active sitei568 – 5681Charge relay system

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. growth factor activity Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. receptor binding Source: UniProtKB
    5. serine-type endopeptidase activity Source: UniProtKB
    6. thrombospondin receptor activity Source: BHF-UCL

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. blood coagulation, intrinsic pathway Source: Reactome
    4. cell surface receptor signaling pathway Source: BHF-UCL
    5. cellular protein metabolic process Source: Reactome
    6. cytosolic calcium ion homeostasis Source: BHF-UCL
    7. fibrinolysis Source: UniProtKB
    8. leukocyte migration Source: Reactome
    9. multicellular organismal development Source: ProtInc
    10. negative regulation of astrocyte differentiation Source: BHF-UCL
    11. negative regulation of fibrinolysis Source: BHF-UCL
    12. negative regulation of platelet activation Source: BHF-UCL
    13. negative regulation of proteolysis Source: BHF-UCL
    14. peptidyl-glutamic acid carboxylation Source: Reactome
    15. platelet activation Source: BHF-UCL
    16. positive regulation of blood coagulation Source: BHF-UCL
    17. positive regulation of cell growth Source: Ensembl
    18. positive regulation of cell proliferation Source: Ensembl
    19. positive regulation of collagen biosynthetic process Source: BHF-UCL
    20. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    21. positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
    22. positive regulation of protein phosphorylation Source: BHF-UCL
    23. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    24. positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
    25. post-translational protein modification Source: Reactome
    26. proteolysis Source: Reactome
    27. regulation of blood coagulation Source: UniProtKB
    28. regulation of cell shape Source: Ensembl
    29. response to wounding Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Acute phase, Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1439. Common Pathway.
    REACT_14819. Peptide ligand-binding receptors.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_18283. G alpha (q) signalling events.
    REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_278. Platelet Aggregation (Plug Formation).
    REACT_326. Intrinsic Pathway.
    REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
    SABIO-RKP00734.

    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
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3535. F2.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi lumen Source: Reactome
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Factor II deficiency (FA2D) [MIM:613679]: A very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721E → G in FA2D; Shanghai. 1 Publication
    VAR_055232
    Natural varianti200 – 2001E → K in FA2D; prothrombin type 3; variant confirmed at protein level. 2 Publications
    Corresponds to variant rs62623459 [ dbSNP | Ensembl ].
    VAR_006711
    Natural varianti314 – 3141R → C in FA2D; Barcelona/Madrid. 1 Publication
    VAR_006712
    Natural varianti314 – 3141R → H in FA2D; Padua-1. 1 Publication
    VAR_006713
    Natural varianti380 – 3801M → T in FA2D; Himi-1. 1 Publication
    VAR_006714
    Natural varianti425 – 4251R → C in FA2D; Quick-1. 1 Publication
    VAR_006715
    Natural varianti431 – 4311R → H in FA2D; Himi-2. 1 Publication
    VAR_006716
    Natural varianti461 – 4611R → W in FA2D; Tokushima. 3 Publications
    VAR_006717
    Natural varianti509 – 5091E → A in FA2D; Salakta/Frankfurt. 2 Publications
    VAR_006718
    Natural varianti601 – 6011G → V in FA2D; Quick-2. 1 Publication
    VAR_006719
    Ischemic stroke (ISCHSTR) [MIM:601367]: A 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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Thrombophilia due to thrombin defect (THPH1) [MIM:188050]: A multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
    Note: 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.
    Pregnancy loss, recurrent, 2 (RPRGL2) [MIM:614390]: A 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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    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

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 43192 PublicationsPRO_0000028159Add
    BLAST
    Chaini44 – 622579ProthrombinPRO_0000028160Add
    BLAST
    Peptidei44 – 198155Activation peptide fragment 1PRO_0000028161Add
    BLAST
    Peptidei199 – 327129Activation peptide fragment 2PRO_0000028162Add
    BLAST
    Chaini328 – 36336Thrombin light chainPRO_0000028163Add
    BLAST
    Chaini364 – 622259Thrombin heavy chainPRO_0000028164Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 4914-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
    Modified residuei50 – 5014-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
    Modified residuei57 – 5714-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei59 – 5914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Disulfide bondi60 ↔ 65
    Modified residuei62 – 6214-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei63 – 6314-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei68 – 6814-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei69 – 6914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei72 – 7214-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei75 – 7514-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Disulfide bondi90 ↔ 103
    Disulfide bondi108 ↔ 186
    Glycosylationi121 – 1211N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi129 ↔ 169
    Glycosylationi143 – 1431N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi157 ↔ 181
    Disulfide bondi213 ↔ 291
    Disulfide bondi234 ↔ 274
    Disulfide bondi262 ↔ 286
    Disulfide bondi336 ↔ 482Interchain (between light and heavy chains)
    Disulfide bondi391 ↔ 407
    Glycosylationi416 – 4161N-linked (GlcNAc...) (complex)5 Publications
    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

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP00734.
    PaxDbiP00734.
    PeptideAtlasiP00734.
    PRIDEiP00734.

    2D gel databases

    SWISS-2DPAGEP00734.

    PTM databases

    PhosphoSiteiP00734.
    UniCarbKBiP00734.

    Miscellaneous databases

    PMAP-CutDBP00734.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Gene expression databases

    ArrayExpressiP00734.
    BgeeiP00734.
    CleanExiHS_F2.
    GenevestigatoriP00734.

    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

    Protein-protein interaction databases

    BioGridi108447. 15 interactions.
    DIPiDIP-6115N.
    IntActiP00734. 10 interactions.
    MINTiMINT-147273.
    STRINGi9606.ENSP00000308541.

    Structurei

    Secondary structure

    1
    622
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 605
    Helixi67 – 737
    Beta strandi74 – 763
    Helixi78 – 8912
    Turni90 – 923
    Helixi97 – 1048
    Beta strandi107 – 1093
    Turni144 – 1463
    Beta strandi148 – 1503
    Beta strandi167 – 1737
    Beta strandi177 – 1804
    Turni186 – 1883
    Helixi216 – 2183
    Beta strandi229 – 2313
    Beta strandi233 – 2353
    Beta strandi237 – 2393
    Helixi240 – 2467
    Beta strandi273 – 2753
    Beta strandi277 – 2793
    Beta strandi283 – 2853
    Helixi295 – 2973
    Beta strandi322 – 3243
    Helixi326 – 3294
    Beta strandi330 – 3323
    Turni334 – 3374
    Turni340 – 3423
    Helixi343 – 3453
    Helixi352 – 3587
    Turni360 – 3623
    Beta strandi367 – 3693
    Beta strandi372 – 3754
    Beta strandi378 – 3836
    Turni384 – 3874
    Beta strandi388 – 3958
    Beta strandi397 – 4037
    Helixi405 – 4073
    Beta strandi408 – 4103
    Helixi411 – 4133
    Helixi419 – 4213
    Beta strandi422 – 4276
    Beta strandi430 – 4334
    Turni436 – 4383
    Beta strandi440 – 44910
    Turni455 – 4584
    Beta strandi464 – 4707
    Beta strandi475 – 4773
    Helixi486 – 4927
    Beta strandi498 – 5047
    Beta strandi507 – 5093
    Turni513 – 5153
    Beta strandi516 – 5183
    Beta strandi524 – 5307
    Helixi533 – 5386
    Beta strandi540 – 5423
    Beta strandi548 – 5514
    Helixi555 – 5573
    Turni565 – 5695
    Beta strandi571 – 5755
    Turni577 – 5793
    Beta strandi582 – 5909
    Beta strandi592 – 5954
    Beta strandi596 – 5983
    Beta strandi601 – 6055
    Helixi607 – 6093
    Helixi610 – 62011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    L328-341[»]
    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-ray2.20B364-622[»]
    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[»]
    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[»]
    4HFYX-ray3.00A/B333-622[»]
    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[»]
    4THNX-ray2.50H364-622[»]
    L328-363[»]
    5GDSX-ray2.10H364-622[»]
    L328-363[»]
    7KMEX-ray2.10H364-622[»]
    L328-363[»]
    8KMEX-ray2.101328-359[»]
    2364-620[»]
    ProteinModelPortaliP00734.
    SMRiP00734. Positions 51-622.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00734.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 8946GlaPROSITE-ProRule annotationAdd
    BLAST
    Domaini108 – 18679Kringle 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini213 – 29179Kringle 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 618255Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni551 – 57323High affinity receptor-binding region which is also known as the TP508 peptideAdd
    BLAST

    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

    eggNOGiCOG5640.
    HOVERGENiHBG108381.
    InParanoidiP00734.
    KOiK01313.
    OMAiGIECQLW.
    PhylomeDBiP00734.
    TreeFamiTF327329.

    Family and domain databases

    Gene3Di2.40.20.10. 2 hits.
    4.10.140.10. 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.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR003966. Prothrombin/thrombin.
    IPR018992. Thrombin_light_chain.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    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

    « Hide

    MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE    50
    VRKGNLEREC VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL 100
    AACLEGNCAE GLGTNYRGHV NITRSGIECQ LWRSRYPHKP EINSTTHPGA 150
    DLQENFCRNP DSSTTGPWCY TTDPTVRRQE CSIPVCGQDQ VTVAMTPRSE 200
    GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA QAKALSKHQD 250
    FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG 300
    DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK 350
    TERELLESYI DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW 400
    VLTAAHCLLY PPWDKNFTEN DLLVRIGKHS RTRYERNIEK ISMLEKIYIH 450
    PRYNWRENLD RDIALMKLKK PVAFSDYIHP VCLPDRETAA SLLQAGYKGR 500
    VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST RIRITDNMFC 550
    AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY 600
    GFYTHVFRLK KWIQKVIDQF GE 622
    Length:622
    Mass (Da):70,037
    Last modified:January 1, 1990 - v2
    Checksum:i8A25E1DA88208FCF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 2517Missing in BAG64719. (PubMed:14702039)CuratedAdd
    BLAST
    Sequence conflicti66 – 661S → N in BAD96497. 1 PublicationCurated
    Sequence conflicti119 – 1191H → N AA sequence (PubMed:266717)Curated
    Sequence conflicti121 – 1211N → S AA sequence (PubMed:266717)Curated
    Sequence conflicti164 – 1641T → I AA sequence (PubMed:266717)Curated
    Sequence conflicti164 – 1641T → N in CAA23842. (PubMed:6305407)Curated
    Sequence conflicti176 – 1761V → A AA sequence (PubMed:266717)Curated
    Sequence conflicti183 – 1831I → T AA sequence (PubMed:266717)Curated
    Sequence conflicti194 – 1952AM → MV AA sequence (PubMed:266717)Curated
    Sequence conflicti308 – 3081D → DEE AA sequence (PubMed:266717)Curated
    Sequence conflicti335 – 3351D → N AA sequence (PubMed:873923)Curated
    Sequence conflicti337 – 3371G → R in BAD96495. 1 PublicationCurated
    Sequence conflicti349 – 3491D → N AA sequence (PubMed:873923)Curated
    Sequence conflicti369 – 3691D → N AA sequence (PubMed:873923)Curated
    Sequence conflicti398 – 3981D → N AA sequence (PubMed:873923)Curated
    Sequence conflicti414 – 4141D → N AA sequence (PubMed:873923)Curated
    Sequence conflicti485 – 4851D → N AA sequence (PubMed:873923)Curated
    Sequence conflicti494 – 4941Q → G AA sequence (PubMed:873923)Curated
    Sequence conflicti504 – 5041W → Y AA sequence (PubMed:873923)Curated
    Sequence conflicti509 – 5091E → S AA sequence (PubMed:873923)Curated
    Sequence conflicti511 – 5111W → V AA sequence (PubMed:873923)Curated
    Sequence conflicti514 – 5141N → D AA sequence (PubMed:873923)Curated
    Sequence conflicti529 – 5302PI → AL AA sequence (PubMed:873923)Curated
    Sequence conflicti590 – 5923WGE → AGA in AAR08143. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721E → G in FA2D; Shanghai. 1 Publication
    VAR_055232
    Natural varianti165 – 1651T → M Polymorphism confirmed at protein level. 4 Publications
    Corresponds to variant rs5896 [ dbSNP | Ensembl ].
    VAR_011781
    Natural varianti200 – 2001E → K in FA2D; prothrombin type 3; variant confirmed at protein level. 2 Publications
    Corresponds to variant rs62623459 [ dbSNP | Ensembl ].
    VAR_006711
    Natural varianti314 – 3141R → C in FA2D; Barcelona/Madrid. 1 Publication
    VAR_006712
    Natural varianti314 – 3141R → H in FA2D; Padua-1. 1 Publication
    VAR_006713
    Natural varianti380 – 3801M → T in FA2D; Himi-1. 1 Publication
    VAR_006714
    Natural varianti386 – 3861P → T Polymorphism confirmed at protein level. 2 Publications
    Corresponds to variant rs5897 [ dbSNP | Ensembl ].
    VAR_011782
    Natural varianti425 – 4251R → C in FA2D; Quick-1. 1 Publication
    VAR_006715
    Natural varianti431 – 4311R → H in FA2D; Himi-2. 1 Publication
    VAR_006716
    Natural varianti461 – 4611R → W in FA2D; Tokushima. 3 Publications
    VAR_006717
    Natural varianti509 – 5091E → A in FA2D; Salakta/Frankfurt. 2 Publications
    VAR_006718
    Natural varianti532 – 5321E → Q Polymorphism confirmed at protein level. 2 Publications
    VAR_068913
    Natural varianti601 – 6011G → V in FA2D; Quick-2. 1 Publication
    VAR_006719

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_000506.3.
    UniGeneiHs.655207.

    Genome annotation databases

    EnsembliENST00000311907; ENSP00000308541; ENSG00000180210.
    GeneIDi2147.
    KEGGihsa:2147.
    UCSCiuc001ndf.4. human.

    Polymorphism databases

    DMDMi135807.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Thrombin entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31476.1.
    PIRi A29351. TBHU.
    RefSeqi NP_000497.1. NM_000506.3.
    UniGenei Hs.655207.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A2C X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    1A3B X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    1A3E X-ray 1.85 H 364-622 [» ]
    L 328-363 [» ]
    1A46 X-ray 2.12 H 364-622 [» ]
    L 328-363 [» ]
    1A4W X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    1A5G X-ray 2.06 H 364-622 [» ]
    L 328-363 [» ]
    1A61 X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    1ABI X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    1ABJ X-ray 2.40 H 364-622 [» ]
    L 328-363 [» ]
    1AD8 X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    1AE8 X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    1AFE X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    1AHT X-ray 1.60 H 364-622 [» ]
    L 328-363 [» ]
    1AI8 X-ray 1.85 H 364-622 [» ]
    L 328-363 [» ]
    1AIX X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    1AWF X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    1AWH X-ray 3.00 A/C 328-363 [» ]
    B/D 364-622 [» ]
    1AY6 X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    1B5G X-ray 2.07 H 364-622 [» ]
    L 328-341 [» ]
    1B7X X-ray 2.10 A 328-363 [» ]
    B 364-622 [» ]
    1BA8 X-ray 1.80 A 328-363 [» ]
    B 364-622 [» ]
    1BB0 X-ray 2.10 A 328-363 [» ]
    B 364-622 [» ]
    1BCU X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    1BHX X-ray 2.30 A 331-349 [» ]
    B 364-510 [» ]
    F 518-622 [» ]
    1BMM X-ray 2.60 H 364-622 [» ]
    L 328-363 [» ]
    1BMN X-ray 2.80 H 364-622 [» ]
    L 328-363 [» ]
    1BTH X-ray 2.30 H/K 364-622 [» ]
    J/L 328-363 [» ]
    1C1U X-ray 1.75 H 364-616 [» ]
    L 328-363 [» ]
    1C1V X-ray 1.98 H 364-616 [» ]
    L 328-363 [» ]
    1C1W X-ray 1.90 H 364-616 [» ]
    L 328-363 [» ]
    1C4U X-ray 2.10 1 328-363 [» ]
    2 364-622 [» ]
    1C4V X-ray 2.10 1 328-363 [» ]
    2 364-622 [» ]
    1C4Y X-ray 2.70 1 328-363 [» ]
    2 364-622 [» ]
    1C5L X-ray 1.47 H 364-622 [» ]
    L 328-363 [» ]
    1C5N X-ray 1.50 H 364-622 [» ]
    L 328-363 [» ]
    1C5O X-ray 1.90 H 364-622 [» ]
    L 328-363 [» ]
    1CA8 X-ray 2.10 A 328-363 [» ]
    B 364-622 [» ]
    1D3D X-ray 2.04 A 333-360 [» ]
    B 364-620 [» ]
    1D3P X-ray 2.10 A 328-363 [» ]
    B 364-622 [» ]
    1D3Q X-ray 2.90 A 328-363 [» ]
    B 364-622 [» ]
    1D3T X-ray 3.00 A 328-363 [» ]
    B 364-622 [» ]
    1D4P X-ray 2.07 A 328-363 [» ]
    B 364-622 [» ]
    1D6W X-ray 2.00 A 334-620 [» ]
    1D9I X-ray 2.30 A 334-621 [» ]
    1DE7 X-ray 2.00 H/K 364-619 [» ]
    J/L 328-360 [» ]
    1DIT X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    1DM4 X-ray 2.50 A 328-362 [» ]
    B 363-622 [» ]
    1DOJ X-ray 1.70 A 328-622 [» ]
    1DWB X-ray 3.16 H 364-622 [» ]
    L 328-363 [» ]
    1DWC X-ray 3.00 H 364-622 [» ]
    L 328-363 [» ]
    1DWD X-ray 3.00 H 364-622 [» ]
    L 328-363 [» ]
    1DWE X-ray 3.00 H 364-622 [» ]
    L 328-363 [» ]
    1DX5 X-ray 2.30 A/B/C/D 328-363 [» ]
    M/N/O/P 364-622 [» ]
    1E0F X-ray 3.10 A/B/C 328-363 [» ]
    D/E/F 364-622 [» ]
    1EB1 X-ray 1.80 H 364-620 [» ]
    L 334-360 [» ]
    1EOJ X-ray 2.10 A 332-620 [» ]
    1EOL X-ray 2.10 A 332-620 [» ]
    1FPC X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    1FPH X-ray 2.50 H 364-622 [» ]
    L 328-363 [» ]
    1G30 X-ray 2.00 A 328-363 [» ]
    B 364-622 [» ]
    1G32 X-ray 1.90 A 328-363 [» ]
    B 364-622 [» ]
    1G37 X-ray 2.00 A 334-620 [» ]
    1GHV X-ray 1.85 H 364-620 [» ]
    L 328-363 [» ]
    1GHW X-ray 1.75 H 364-620 [» ]
    L 328-363 [» ]
    1GHX X-ray 1.65 H 364-620 [» ]
    L 328-363 [» ]
    1GHY X-ray 1.85 H 364-620 [» ]
    L 328-363 [» ]
    1GJ4 X-ray 1.81 H 364-621 [» ]
    L 328-363 [» ]
    1GJ5 X-ray 1.73 H 364-621 [» ]
    L 328-363 [» ]
    1H8D X-ray 1.40 H 364-621 [» ]
    L 333-360 [» ]
    1H8I X-ray 1.75 H 364-622 [» ]
    L 334-360 [» ]
    1HAG X-ray 2.00 E 328-622 [» ]
    1HAH X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    1HAI X-ray 2.40 H 364-622 [» ]
    L 328-363 [» ]
    1HAO X-ray 2.80 H 364-622 [» ]
    L 328-363 [» ]
    1HAP X-ray 2.80 H 364-622 [» ]
    L 328-360 [» ]
    1HBT X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    1HDT X-ray 2.60 H 364-622 [» ]
    L 331-363 [» ]
    1HGT X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    1HLT X-ray 3.00 H/K 364-622 [» ]
    J/L 334-349 [» ]
    1HUT X-ray 2.90 H 364-622 [» ]
    L 328-363 [» ]
    1HXE X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    1HXF X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    1IHS X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    1IHT X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    1JMO X-ray 2.20 H 363-622 [» ]
    L 315-362 [» ]
    1JOU X-ray 1.80 A/C/E 315-363 [» ]
    B/D/F 364-622 [» ]
    1JWT X-ray 2.50 A 328-622 [» ]
    1K21 X-ray 1.86 H 364-622 [» ]
    L 328-363 [» ]
    1K22 X-ray 1.93 H 364-622 [» ]
    L 328-363 [» ]
    1KTS X-ray 2.40 A 328-363 [» ]
    B 364-622 [» ]
    1KTT X-ray 2.10 A 328-363 [» ]
    B 364-622 [» ]
    1LHC X-ray 1.95 H 364-622 [» ]
    L 328-363 [» ]
    1LHD X-ray 2.35 H 364-622 [» ]
    L 328-363 [» ]
    1LHE X-ray 2.25 H 364-622 [» ]
    L 328-363 [» ]
    1LHF X-ray 2.40 H 364-622 [» ]
    L 328-363 [» ]
    1LHG X-ray 2.25 H 364-622 [» ]
    L 328-363 [» ]
    1MH0 X-ray 2.80 A/B 334-620 [» ]
    1MU6 X-ray 1.99 A 328-363 [» ]
    B 364-622 [» ]
    1MU8 X-ray 2.00 A 328-363 [» ]
    B 364-622 [» ]
    1MUE X-ray 2.00 A 328-363 [» ]
    B 364-622 [» ]
    1NM6 X-ray 1.80 A 335-621 [» ]
    1NO9 X-ray 1.90 H 364-622 [» ]
    L 328-363 [» ]
    1NRN X-ray 3.10 H 364-622 [» ]
    L 328-363 [» ]
    1NRO X-ray 3.10 H 364-622 [» ]
    L 328-363 [» ]
    1NRP X-ray 3.00 H 364-622 [» ]
    L 328-363 [» ]
    1NRQ X-ray 3.50 H 364-622 [» ]
    L 328-363 [» ]
    1NRR X-ray 2.40 H 364-622 [» ]
    L 328-363 [» ]
    1NRS X-ray 2.40 H 364-622 [» ]
    L 328-349 [» ]
    1NT1 X-ray 2.00 A 335-621 [» ]
    1NU7 X-ray 2.20 A/E 332-359 [» ]
    B/F 364-622 [» ]
    1NU9 X-ray 2.20 A/D 332-622 [» ]
    1NY2 X-ray 2.30 1 328-363 [» ]
    2 364-622 [» ]
    1NZQ X-ray 2.18 H 364-620 [» ]
    L 328-361 [» ]
    1O0D X-ray 2.44 H 364-622 [» ]
    L 328-363 [» ]
    1O2G X-ray 1.58 H 364-622 [» ]
    L 328-363 [» ]
    1O5G X-ray 1.75 H 364-622 [» ]
    L 328-363 [» ]
    1OOK X-ray 2.30 A 328-363 [» ]
    B 364-622 [» ]
    1OYT X-ray 1.67 H 364-622 [» ]
    L 328-363 [» ]
    1P8V X-ray 2.60 B 333-361 [» ]
    C 364-621 [» ]
    1PPB X-ray 1.92 H 364-622 [» ]
    L 328-363 [» ]
    1QBV X-ray 1.80 H 364-622 [» ]
    L 328-359 [» ]
    1QHR X-ray 2.20 A 328-363 [» ]
    B 364-622 [» ]
    1QJ1 X-ray 2.00 A 328-363 [» ]
    B 364-622 [» ]
    1QJ6 X-ray 2.20 A 328-363 [» ]
    B 364-622 [» ]
    1QJ7 X-ray 2.20 A 328-363 [» ]
    B 364-622 [» ]
    1QUR X-ray 2.00 H 364-620 [» ]
    L 334-360 [» ]
    1RD3 X-ray 2.50 A/C 328-363 [» ]
    B/D 364-622 [» ]
    1RIW X-ray 2.04 A 328-363 [» ]
    B 364-510 [» ]
    C 518-622 [» ]
    1SB1 X-ray 1.90 H 364-621 [» ]
    L 333-361 [» ]
    1SFQ X-ray 1.91 A/D 328-363 [» ]
    B/E 364-622 [» ]
    1SG8 X-ray 2.30 A/D 328-363 [» ]
    B/E 364-622 [» ]
    1SGI X-ray 2.30 A/D 328-363 [» ]
    B/E 364-622 [» ]
    1SHH X-ray 1.55 A/D 328-363 [» ]
    B/E 364-622 [» ]
    1SL3 X-ray 1.81 A 335-621 [» ]
    1SR5 X-ray 3.10 B 328-363 [» ]
    C 364-622 [» ]
    1T4U X-ray 2.00 H 364-622 [» ]
    L 334-359 [» ]
    1T4V X-ray 2.00 H 364-622 [» ]
    L 334-359 [» ]
    1TA2 X-ray 2.30 A 335-621 [» ]
    1TA6 X-ray 1.90 A 335-621 [» ]
    1TB6 X-ray 2.50 H 364-622 [» ]
    L 315-363 [» ]
    1TBZ X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    1THP X-ray 2.10 A 328-362 [» ]
    B 364-620 [» ]
    1THR X-ray 2.30 H 364-622 [» ]
    L 328-349 [» ]
    1THS X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    1TMB X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    1TMT X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    1TMU X-ray 2.50 H 364-620 [» ]
    L 333-349 [» ]
    1TOM X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    1TQ0 X-ray 2.80 A/C 333-363 [» ]
    B/D 364-620 [» ]
    1TQ7 X-ray 2.40 A 320-363 [» ]
    B 364-620 [» ]
    1TWX X-ray 2.40 A 334-349 [» ]
    B 364-622 [» ]
    1UMA X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    1UVS X-ray 2.80 H 364-622 [» ]
    L 328-363 [» ]
    1VR1 X-ray 1.90 H 364-620 [» ]
    L 334-360 [» ]
    1VZQ X-ray 1.54 H 364-620 [» ]
    L 334-360 [» ]
    1W7G X-ray 1.65 H 364-622 [» ]
    L 328-363 [» ]
    1WAY X-ray 2.02 A 328-363 [» ]
    B 364-622 [» ]
    1WBG X-ray 2.20 B 364-622 [» ]
    1XM1 X-ray 2.30 A 328-622 [» ]
    1XMN X-ray 1.85 A/C/E/G 328-363 [» ]
    B/D/F/H 364-622 [» ]
    1YPE X-ray 1.81 H 364-620 [» ]
    L 334-360 [» ]
    1YPG X-ray 1.80 H 364-620 [» ]
    L 334-360 [» ]
    1YPJ X-ray 1.78 H 364-620 [» ]
    L 334-360 [» ]
    1YPK X-ray 1.78 H 364-620 [» ]
    L 334-360 [» ]
    1YPL X-ray 1.85 H 364-620 [» ]
    L 334-360 [» ]
    1YPM X-ray 1.85 H 364-620 [» ]
    L 334-360 [» ]
    1Z71 X-ray 1.80 A 335-621 [» ]
    1Z8I X-ray 2.00 A 324-361 [» ]
    B 364-622 [» ]
    1Z8J X-ray 2.00 A 322-361 [» ]
    B 364-622 [» ]
    1ZGI X-ray 2.20 A 335-621 [» ]
    1ZGV X-ray 2.20 A 335-621 [» ]
    1ZRB X-ray 1.90 A 335-621 [» ]
    2A0Q X-ray 1.90 A/C 334-349 [» ]
    B/D 364-620 [» ]
    2A2X X-ray 2.44 H 364-622 [» ]
    L 330-363 [» ]
    2A45 X-ray 3.65 A/D 328-363 [» ]
    B/E 364-622 [» ]
    2AFQ X-ray 1.93 A/C 332-360 [» ]
    B/D 364-622 [» ]
    2ANK X-ray 2.46 H 364-622 [» ]
    L 330-363 [» ]
    2ANM X-ray 2.40 H 364-620 [» ]
    L 328-363 [» ]
    2B5T X-ray 2.10 A/C 315-363 [» ]
    B/D 364-622 [» ]
    2BDY X-ray 1.61 A 334-622 [» ]
    2BVR X-ray 1.25 H 364-622 [» ]
    L 328-363 [» ]
    2BVS X-ray 1.40 H 364-622 [» ]
    L 328-363 [» ]
    2BVX X-ray 3.20 H 364-622 [» ]
    L 328-363 [» ]
    2BXT X-ray 1.83 H 364-622 [» ]
    L 328-363 [» ]
    2BXU X-ray 2.80 H 364-622 [» ]
    L 328-363 [» ]
    2C8W X-ray 1.96 A 328-363 [» ]
    B 364-622 [» ]
    2C8X X-ray 2.17 A 328-363 [» ]
    B 364-622 [» ]
    2C8Y X-ray 2.20 A 328-363 [» ]
    B 364-622 [» ]
    2C8Z X-ray 2.14 A 328-363 [» ]
    B 364-622 [» ]
    2C90 X-ray 2.25 A 328-363 [» ]
    B 364-622 [» ]
    2C93 X-ray 2.20 A 328-363 [» ]
    B 364-622 [» ]
    2CF8 X-ray 1.30 H 364-620 [» ]
    L 334-361 [» ]
    2CF9 X-ray 1.79 H 364-620 [» ]
    L 334-361 [» ]
    2CN0 X-ray 1.30 H 364-620 [» ]
    L 334-361 [» ]
    2FEQ X-ray 2.44 H 364-622 [» ]
    L 328-363 [» ]
    2FES X-ray 2.42 H 364-622 [» ]
    L 328-363 [» ]
    2GDE X-ray 2.00 H 364-622 [» ]
    L 328-363 [» ]
    2GP9 X-ray 1.87 A 328-362 [» ]
    B 364-620 [» ]
    2H9T X-ray 2.40 H 364-622 [» ]
    L 328-363 [» ]
    2HGT X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    2HNT X-ray 2.50 C 364-433 [» ]
    E 437-517 [» ]
    F 518-622 [» ]
    L 328-363 [» ]
    2HPP X-ray 3.30 H 364-622 [» ]
    2HPQ X-ray 3.30 H 364-622 [» ]
    L 328-363 [» ]
    P 213-291 [» ]
    2HWL X-ray 2.40 A/C 328-363 [» ]
    B/D 364-622 [» ]
    2JH0 X-ray 1.70 C 328-361 [» ]
    D 364-622 [» ]
    2JH5 X-ray 2.50 C 328-363 [» ]
    D 364-622 [» ]
    2JH6 X-ray 2.21 C 328-361 [» ]
    D 364-622 [» ]
    2OD3 X-ray 1.75 A 328-363 [» ]
    B 364-622 [» ]
    2PGB X-ray 1.54 A 328-363 [» ]
    B 364-622 [» ]
    2PGQ X-ray 1.80 A 319-363 [» ]
    B 364-622 [» ]
    2PKS X-ray 2.50 A 334-360 [» ]
    B 364-510 [» ]
    C 518-619 [» ]
    2PW8 X-ray 1.84 H 364-621 [» ]
    L 334-360 [» ]
    2R2M X-ray 2.10 A 334-359 [» ]
    B 364-622 [» ]
    2THF X-ray 2.10 A 328-363 [» ]
    B 364-622 [» ]
    2UUF X-ray 1.26 A 328-363 [» ]
    B 364-622 [» ]
    2UUJ X-ray 1.32 A 328-363 [» ]
    B 364-622 [» ]
    2UUK X-ray 1.39 A 328-363 [» ]
    B 364-622 [» ]
    2V3H X-ray 1.79 H 364-620 [» ]
    L 334-361 [» ]
    2V3O X-ray 1.79 H 364-620 [» ]
    L 334-361 [» ]
    2ZC9 X-ray 1.58 H 364-622 [» ]
    L 328-363 [» ]
    2ZDA X-ray 1.73 H 364-622 [» ]
    L 328-363 [» ]
    2ZDV X-ray 1.72 H 364-622 [» ]
    L 328-363 [» ]
    2ZF0 X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    2ZFF X-ray 1.47 H 364-622 [» ]
    L 328-363 [» ]
    2ZFP X-ray 2.25 H 364-622 [» ]
    L 328-363 [» ]
    2ZFQ X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    2ZFR X-ray 1.85 H 364-622 [» ]
    L 328-363 [» ]
    2ZG0 X-ray 1.75 H 364-622 [» ]
    L 328-363 [» ]
    2ZGB X-ray 1.60 H 364-622 [» ]
    L 328-363 [» ]
    2ZGX X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    2ZHE X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    2ZHF X-ray 1.98 H 364-622 [» ]
    L 328-363 [» ]
    2ZHQ X-ray 1.96 H 364-622 [» ]
    L 328-363 [» ]
    2ZHW X-ray 2.02 H 364-622 [» ]
    L 328-363 [» ]
    2ZI2 X-ray 1.65 H 364-622 [» ]
    L 328-363 [» ]
    2ZIQ X-ray 1.65 H 364-622 [» ]
    L 328-363 [» ]
    2ZNK X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    2ZO3 X-ray 1.70 H 364-622 [» ]
    L 328-363 [» ]
    3B23 X-ray 2.40 A 328-363 [» ]
    B 364-622 [» ]
    3B9F X-ray 1.60 H 364-622 [» ]
    L 315-363 [» ]
    3BEF X-ray 2.20 A/D 320-363 [» ]
    B/E 364-622 [» ]
    3BEI X-ray 1.55 A 320-363 [» ]
    B 364-622 [» ]
    3BF6 X-ray 2.50 H 364-622 [» ]
    L 328-363 [» ]
    3BIU X-ray 2.30 H 364-620 [» ]
    L 333-361 [» ]
    3BIV X-ray 1.80 H 364-620 [» ]
    L 333-361 [» ]
    3BV9 X-ray 1.80 A 333-363 [» ]
    B 364-622 [» ]
    3C1K X-ray 1.84 A 335-621 [» ]
    3C27 X-ray 2.18 A 334-359 [» ]
    B 364-622 [» ]
    3D49 X-ray 1.50 H 364-622 [» ]
    L 328-363 [» ]
    3DA9 X-ray 1.80 A 328-363 [» ]
    B 364-622 [» ]
    3DD2 X-ray 1.90 H 364-621 [» ]
    L 332-361 [» ]
    3DHK X-ray 1.73 H 364-622 [» ]
    L 328-363 [» ]
    3DT0 X-ray 2.40 H 364-622 [» ]
    L 328-363 [» ]
    3DUX X-ray 1.60 H 364-622 [» ]
    L 328-363 [» ]
    3E6P X-ray 2.10 H 364-622 [» ]
    L 206-363 [» ]
    3EE0 X-ray 2.75 A 328-363 [» ]
    B 364-622 [» ]
    3EGK X-ray 2.20 H 364-622 [» ]
    L 328-363 [» ]
    3EQ0 X-ray 1.53 H 364-622 [» ]
    L 328-363 [» ]
    3F68 X-ray 1.75 H 364-622 [» ]
    L 328-363 [» ]
    3GIC X-ray 1.55 A 328-363 [» ]
    B 364-622 [» ]
    3GIS X-ray 2.40 A/C/E 315-363 [» ]
    B/D/F 364-622 [» ]
    3HAT X-ray 2.50 H 364-622 [» ]
    L 328-363 [» ]
    3HKJ X-ray 2.60 A/D 333-363 [» ]
    B/E 364-622 [» ]
    3HTC X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    3JZ1 X-ray 1.60 A 328-363 [» ]
    B 364-622 [» ]
    3JZ2 X-ray 2.40 A 328-363 [» ]
    B 364-622 [» ]
    3K65 X-ray 1.85 A 199-314 [» ]
    B 315-622 [» ]
    3LDX X-ray 2.25 H 364-622 [» ]
    L 328-363 [» ]
    3LU9 X-ray 1.80 A/D 318-363 [» ]
    B/E 364-622 [» ]
    3NXP X-ray 2.20 A 199-622 [» ]
    3P17 X-ray 1.43 H 364-622 [» ]
    L 328-363 [» ]
    3P6Z X-ray 1.70 A/G 328-363 [» ]
    B/H 364-622 [» ]
    3P70 X-ray 2.55 A/C/E/G 328-363 [» ]
    B/D/F/H 364-622 [» ]
    3PMH X-ray 3.20 A 328-363 [» ]
    B 364-622 [» ]
    3PO1 X-ray 1.65 A 334-360 [» ]
    B 364-510 [» ]
    C 518-619 [» ]
    3QDZ X-ray 2.80 A/C 333-363 [» ]
    B/D 364-622 [» ]
    3QGN X-ray 2.10 A 333-363 [» ]
    B 364-622 [» ]
    3QLP X-ray 2.14 H 364-622 [» ]
    L 328-363 [» ]
    3QTO X-ray 1.52 H 364-622 [» ]
    L 328-363 [» ]
    3QTV X-ray 1.63 H 364-622 [» ]
    L 328-363 [» ]
    3QWC X-ray 1.75 H 364-622 [» ]
    L 328-363 [» ]
    3QX5 X-ray 1.35 H 364-622 [» ]
    L 328-363 [» ]
    3R3G X-ray 1.75 A 333-363 [» ]
    B 364-622 [» ]
    3RLW X-ray 1.69 H 364-622 [» ]
    L 328-363 [» ]
    3RLY X-ray 1.51 H 364-622 [» ]
    L 328-363 [» ]
    3RM0 X-ray 1.34 H 364-622 [» ]
    L 328-363 [» ]
    3RM2 X-ray 1.23 H 364-622 [» ]
    L 328-363 [» ]
    3RML X-ray 1.53 H 364-622 [» ]
    L 328-363 [» ]
    3RMM X-ray 1.58 H 364-622 [» ]
    L 328-363 [» ]
    3RMN X-ray 1.78 H 364-622 [» ]
    L 328-363 [» ]
    3RMO X-ray 1.40 H 364-622 [» ]
    L 328-363 [» ]
    3S7H X-ray 1.90 A 329-363 [» ]
    B 364-622 [» ]
    3S7K X-ray 1.90 A/C 329-363 [» ]
    B/D 364-622 [» ]
    3SHA X-ray 1.52 H 364-622 [» ]
    L 328-363 [» ]
    3SHC X-ray 1.90 H 364-622 [» ]
    L 328-363 [» ]
    3SI3 X-ray 1.55 H 364-622 [» ]
    L 328-363 [» ]
    3SI4 X-ray 1.27 H 364-622 [» ]
    L 328-363 [» ]
    3SQE X-ray 1.90 E 333-622 [» ]
    3SQH X-ray 2.20 E 333-622 [» ]
    3SV2 X-ray 1.30 H 364-622 [» ]
    L 328-363 [» ]
    3T5F X-ray 1.45 H 364-622 [» ]
    L 328-363 [» ]
    3TU7 X-ray 2.49 H 364-622 [» ]
    L 328-363 [» ]
    3U69 X-ray 1.55 H 364-622 [» ]
    L 334-363 [» ]
    3U8O X-ray 1.28 H 364-622 [» ]
    L 334-363 [» ]
    3U8R X-ray 1.47 H 364-622 [» ]
    L 334-363 [» ]
    3U8T X-ray 1.86 H 364-620 [» ]
    L 334-360 [» ]
    3U98 X-ray 1.45 H 364-622 [» ]
    L 328-363 [» ]
    3U9A X-ray 1.58 H 364-622 [» ]
    L 328-363 [» ]
    3UTU X-ray 1.55 H 364-622 [» ]
    L 328-363 [» ]
    3UWJ X-ray 1.50 H 364-622 [» ]
    L 328-363 [» ]
    3VXE X-ray 1.25 H 364-622 [» ]
    L 328-363 [» ]
    3VXF Other 1.60 H 364-622 [» ]
    L 328-363 [» ]
    4AX9 X-ray 1.90 H 364-620 [» ]
    L 334-361 [» ]
    4AYV X-ray 2.80 A 332-361 [» ]
    B 364-620 [» ]
    4AYY X-ray 2.60 A 332-361 [» ]
    B 364-620 [» ]
    4AZ2 X-ray 2.60 A 332-361 [» ]
    B 364-620 [» ]
    4BAH X-ray 1.94 A 328-363 [» ]
    B 364-622 [» ]
    4BAK X-ray 1.94 A 328-363 [» ]
    B 364-622 [» ]
    4BAM X-ray 1.88 A 328-363 [» ]
    B 364-622 [» ]
    4BAN X-ray 1.87 A 328-363 [» ]
    B 364-622 [» ]
    4BAO X-ray 1.87 A 328-363 [» ]
    B 364-622 [» ]
    4BAQ X-ray 1.89 A 328-363 [» ]
    B 364-622 [» ]
    4BOH X-ray 2.60 A/H 364-622 [» ]
    B/L 328-363 [» ]
    4CH2 X-ray 1.60 A/C 328-363 [» ]
    B/D 364-622 [» ]
    4CH8 X-ray 1.75 A/C/E/G 328-363 [» ]
    B/D/F/H 364-622 [» ]
    4DIH X-ray 1.80 H 364-622 [» ]
    L 328-363 [» ]
    4DII X-ray 2.05 H 364-622 [» ]
    L 328-363 [» ]
    4DT7 X-ray 1.90 A/C 332-363 [» ]
    B/D 364-622 [» ]
    4DY7 X-ray 2.80 A/D 315-363 [» ]
    B/E 364-622 [» ]
    4E05 X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    4E06 X-ray 3.20 H 364-622 [» ]
    L 328-363 [» ]
    4E7R X-ray 2.25 G/H 364-622 [» ]
    L/M 328-363 [» ]
    4H6S X-ray 2.19 A 333-363 [» ]
    B 364-622 [» ]
    4H6T X-ray 2.40 A 317-622 [» ]
    4HFP X-ray 2.40 A/C 333-363 [» ]
    B/D 364-622 [» ]
    4HFY X-ray 3.00 A/B 333-622 [» ]
    4HTC X-ray 2.30 H 364-622 [» ]
    L 328-363 [» ]
    4HZH X-ray 3.30 A/B 90-622 [» ]
    4I7Y X-ray 2.40 H 364-622 [» ]
    L 328-363 [» ]
    4LOY X-ray 1.77 H 364-620 [» ]
    L 334-360 [» ]
    4LXB X-ray 1.61 H 364-622 [» ]
    L 328-363 [» ]
    4LZ1 X-ray 1.65 H 364-622 [» ]
    L 328-363 [» ]
    4LZ4 X-ray 2.56 A/C 328-363 [» ]
    B/D 364-622 [» ]
    4MLF X-ray 2.20 A 331-363 [» ]
    B 364-622 [» ]
    4N3L X-ray 1.94 H 364-622 [» ]
    L 328-363 [» ]
    4NZE X-ray 1.98 H 364-622 [» ]
    L 328-363 [» ]
    4NZQ X-ray 2.81 A 44-622 [» ]
    4O03 X-ray 3.38 A 44-622 [» ]
    4THN X-ray 2.50 H 364-622 [» ]
    L 328-363 [» ]
    5GDS X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    7KME X-ray 2.10 H 364-622 [» ]
    L 328-363 [» ]
    8KME X-ray 2.10 1 328-359 [» ]
    2 364-620 [» ]
    ProteinModelPortali P00734.
    SMRi P00734. Positions 51-622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108447. 15 interactions.
    DIPi DIP-6115N.
    IntActi P00734. 10 interactions.
    MINTi MINT-147273.
    STRINGi 9606.ENSP00000308541.

    Chemistry

    BindingDBi P00734.
    ChEMBLi CHEMBL2096988.
    DrugBanki DB00025. Antihemophilic Factor.
    DB00278. Argatroban.
    DB00006. Bivalirudin.
    DB00100. Coagulation Factor IX.
    DB00055. Drotrecogin alfa.
    DB01225. Enoxaparin.
    DB01109. Heparin.
    DB00001. Lepirudin.
    DB00170. Menadione.
    DB01123. Proflavine.
    DB00641. Simvastatin.
    DB04786. Suramin.
    DB00682. Warfarin.
    DB04898. Ximelagatran.
    GuidetoPHARMACOLOGYi 2362.

    Protein family/group databases

    MEROPSi S01.217.

    PTM databases

    PhosphoSitei P00734.
    UniCarbKBi P00734.

    Polymorphism databases

    DMDMi 135807.

    2D gel databases

    SWISS-2DPAGE P00734.

    Proteomic databases

    MaxQBi P00734.
    PaxDbi P00734.
    PeptideAtlasi P00734.
    PRIDEi P00734.

    Protocols and materials databases

    DNASUi 2147.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311907 ; ENSP00000308541 ; ENSG00000180210 .
    GeneIDi 2147.
    KEGGi hsa:2147.
    UCSCi uc001ndf.4. human.

    Organism-specific databases

    CTDi 2147.
    GeneCardsi GC11P046740.
    GeneReviewsi F2.
    H-InvDB HIX0026188.
    HGNCi HGNC:3535. F2.
    HPAi CAB016780.
    CAB018650.
    HPA051476.
    HPA054698.
    MIMi 176930. gene.
    188050. phenotype.
    601367. phenotype.
    613679. phenotype.
    614390. phenotype.
    neXtProti NX_P00734.
    Orphaneti 329217. Cerebral sinovenous thrombosis.
    325. Congenital factor II deficiency.
    64738. Non rare thrombophilia.
    PharmGKBi PA157.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG108381.
    InParanoidi P00734.
    KOi K01313.
    OMAi GIECQLW.
    PhylomeDBi P00734.
    TreeFami TF327329.

    Enzyme and pathway databases

    Reactomei REACT_1050. Gamma-carboxylation of protein precursors.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1439. Common Pathway.
    REACT_14819. Peptide ligand-binding receptors.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_18283. G alpha (q) signalling events.
    REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_278. Platelet Aggregation (Plug Formation).
    REACT_326. Intrinsic Pathway.
    REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
    SABIO-RK P00734.

    Miscellaneous databases

    EvolutionaryTracei P00734.
    GeneWikii Thrombin.
    GenomeRNAii 2147.
    NextBioi 8681.
    PMAP-CutDB P00734.
    PROi P00734.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00734.
    Bgeei P00734.
    CleanExi HS_F2.
    Genevestigatori P00734.

    Family and domain databases

    Gene3Di 2.40.20.10. 2 hits.
    4.10.140.10. 1 hit.
    4.10.740.10. 1 hit.
    InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR000294. GLA_domain.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR003966. Prothrombin/thrombin.
    IPR018992. Thrombin_light_chain.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00594. Gla. 1 hit.
    PF00051. Kringle. 2 hits.
    PF09396. Thrombin_light. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001149. Thrombin. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    PR00001. GLABLOOD.
    PR01505. PROTHROMBIN.
    SMARTi SM00069. GLA. 1 hit.
    SM00130. KR. 2 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 2 hits.
    SSF57630. SSF57630. 1 hit.
    PROSITEi PS00011. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the gene for human prothrombin."
      Degen S.J.F., Davie E.W.
      Biochemistry 26:6165-6177(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 by Gly."
      Wang W., Fu Q., Zhou R., Wu W., Ding Q., Hu Y., Wang X., Wang H., Wang Z.
      Haemophilia 10:94-97(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT FA2D GLY-72.
      Tissue: Blood.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-165.
      Tissue: Liver and Mammary gland.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    5. SeattleSNPs variation discovery resource
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-165.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    7. "Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin."
      Degen S.J.F., McGillivray R.T.A., Davie E.W.
      Biochemistry 22:2087-2097(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-622, GAMMA-CARBOXYGLUTAMATION AT GLU-49; GLU-50; GLU-57; GLU-59; GLU-62; GLU-63; GLU-68; GLU-69; GLU-72 AND GLU-75.
    8. "Isolation and partial characterization of crystal matrix protein as a potent inhibitor of calcium oxalate crystal aggregation: evidence of activation peptide of human prothrombin."
      Suzuki K., Moriyama M., Nakajima C., Kawamura K., Miyazawa K., Tsugawa R., Kikuchi N., Nagata K.
      Urol. Res. 22:45-50(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-64.
      Tissue: Urine.
    9. "Amino acid sequence of human prothrombin fragments 1 and 2."
      Walz D.A., Hewett-Emmett D., Seegers W.H.
      Proc. Natl. Acad. Sci. U.S.A. 74:1969-1972(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-314.
    10. "Primary structure of human prethrombin 2 and alpha-thrombin."
      Butkowski R.J., Elion J., Downing M.R., Mann K.G.
      J. Biol. Chem. 252:4942-4957(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 315-622, GLYCOSYLATION AT ASN-416, VARIANT GLN-532.
    11. "Antithrombotic thrombin variants."
      Gruber A., Hanson S.R., DiCera E.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-622.
    12. "Mechanism of inhibition of activated protein C by protein C inhibitor."
      Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.
      J. Biochem. 95:187-195(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
    13. "Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma."
      Rabiet M.J., Blashill A., Furie B., Furie B.C.
      J. Biol. Chem. 261:13210-13215(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, GAMMA-CARBOXYGLUTAMATION AT GLU-49 AND GLU-50.
    14. "Synthetic peptides bind to high-affinity thrombin receptors and modulate thrombin mitogenesis."
      Glenn K.C., Frost G.H., Bergmann J.S., Carney D.H.
      Pept. Res. 1:65-73(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION.
    15. "Thrombophilic gene mutations and recurrent spontaneous abortion: prothrombin mutation increases the risk in the first trimester."
      Pihusch R., Buchholz T., Lohse P., Rubsamen H., Rogenhofer N., Hasbargen U., Hiller E., Thaler C.J.
      Am. J. Reprod. Immunol. 46:124-131(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RPRGL2 SUSCEPTIBILITY.
    16. "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls."
      Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.
      Arch. Neurol. 61:1652-1661(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.
    17. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143.
      Tissue: Plasma.
    18. "rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce chemotaxis of human osteoblasts and microvascular endothelial cells."
      Li G., Cui Y., McIlmurray L., Allen W.E., Wang H.
      J. Orthop. Res. 23:680-685(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE TP508 PEPTIDE.
    19. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416.
      Tissue: Plasma.
    20. "Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a placebo-controlled phase I/II study."
      Fife C., Mader J.T., Stone J., Brill L., Satterfield K., Norfleet A., Zwernemann A., Ryaby J.T., Carney D.H.
      Wound Repair Regen. 15:23-34(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: THERAPEUTIC USAGE OF THE TP508 PEPTIDE.
    21. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416.
      Tissue: Liver.
    22. Cited for: GLYCOSYLATION AT ASN-416.
    23. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, STRUCTURE OF CARBOHYDRATE.
      Tissue: Cerebrospinal fluid.
    24. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-121 AND ASN-143, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    25. "The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment."
      Bode W., Mayr I., Baumann U., Huber R., Stone S.R., Hofsteenge J.
      EMBO J. 8:3467-3475(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    26. "Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition."
      Gruetter M.G., Priestle J.P., Rahuel J., Grossenbacher H., Bode W., Hofsteenge J., Stone S.R.
      EMBO J. 9:2361-2365(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
    27. "The structure of a complex of recombinant hirudin and human alpha-thrombin."
      Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R., Roitsch C., Fenton J.W. II
      Science 249:277-280(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
    28. "Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms."
      Priestle J.P., Rahuel J., Rink H., Tones M., Gruetter M.G.
      Protein Sci. 2:1630-1642(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH HIRUDIN AND SYNTHETIC INHIBITOR.
    29. "Crystallographic structure of human gamma-thrombin."
      Rydel T.J., Yin M., Padmanabhan K.P., Blankenship D.T., Cardin A.D., Correa P.E., Fenton J.W. II, Tulinsky A.
      J. Biol. Chem. 269:22000-22006(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    30. "The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin."
      van de Locht A., Bode W., Huber R., le Bonniec B.F., Stone S.R., Esmon C.T., Stubbs M.T.
      EMBO J. 16:2977-2984(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    31. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601.
    32. "Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate."
      Skordalakes E., Dodson G.G., Green D.S., Goodwin C.A., Scully M.F., Hudson H.R., Kakkar V.V., Deadman J.J.
      J. Mol. Biol. 311:549-555(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    33. "Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors."
      Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P., Obst-Sander U., Wagner B., Kansy M., Banner D.W., Diederich F.
      Org. Biomol. Chem. 4:2364-2375(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH HIRUDIN AND SYNTHETIC INHIBITOR.
    34. "Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin."
      Liu C.C., Brustad E., Liu W., Schultz P.G.
      J. Am. Chem. Soc. 129:10648-10649(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH HIRUDIN.
    35. "Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles."
      Isaacs R.C.A., Solinsky M.G., Cutrona K.J., Newton C.L., Naylor-Olsen A.M., McMasters D.R., Krueger J.A., Lewis S.D., Lucas B.J., Kuo L.C., Yan Y., Lynch J.J., Lyle E.A.
      Bioorg. Med. Chem. Lett. 18:2062-2066(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    36. "Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex."
      Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.
      Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH SERPINA5 AND HEPARIN.
    37. "Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site."
      Board P.G., Shaw D.C.
      Br. J. Haematol. 54:245-254(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA2D LYS-200, PARTIAL PROTEIN SEQUENCE.
    38. "Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273."
      Rabiet M.-J., Furie B.C., Furie B.
      J. Biol. Chem. 261:15045-15048(1986) [PubMed] [