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P00734

- THRB_HUMAN

UniProt

P00734 - THRB_HUMAN

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Protein

Prothrombin

Gene

F2

Organism
Homo sapiens (Human)
Status
Reviewed - 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)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. receptor binding Source: UniProtKB
  4. serine-type endopeptidase activity Source: UniProtKB
  5. 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
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

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: UniProtKB
  6. Golgi lumen Source: Reactome
  7. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP00734.
CleanExiHS_F2.
ExpressionAtlasiP00734. baseline and differential.
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 44-622.
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.
GeneTreeiENSGT00760000118890.
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

        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)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 44-622.
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 CHEMBL2111379.
DrugBanki DB00025. Antihemophilic Factor.
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.
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.
GeneTreei ENSGT00760000118890.
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

Bgeei P00734.
CleanExi HS_F2.
ExpressionAtlasi P00734. baseline and differential.
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

« Hide 'large scale' publications
  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.
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    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]
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  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.
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    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
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    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 315-62