Reviewed, UniProtKB/Swiss-Prot P00734 (THRB_HUMAN)

Names and origin

Protein names

Recommended name:
    Prothrombin
    EC=3.4.21.5
Alternative name(s):
    Coagulation factor II
Cleaved into the following 4 chains:
    1- Recommended name:
            Activation peptide fragment 1
    2- Recommended name:
            Activation peptide fragment 2
    3- Recommended name:
            Thrombin light chain
    4- Recommended name:
            Thrombin heavy chain

Gene names

Name:

F2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	622 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.12
Catalytic activity	Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Expressed by the liver and secreted in plasma.
Post-translational modification	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.
Involvement in disease	Defects in F2 are the cause of various forms of dysprothrombinemia [MIM:176930]. Genetic variations in F2 may be a cause of susceptibility to ischemic stroke [MIM:601367]; also known as cerebrovascular accident or cerebral infarction. 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. Ref.42
Pharmaceutical use	The peptide TP508 also known as Chrysalin (Orthologic) could be used to accelerate repair of both soft and hard tissues.
Miscellaneous	Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin. It is not known whether 1 or 2 smaller activation peptides, with additional cleavage after Arg-314, are released in natural blood clotting. Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa. The cleavage after Arg-198, observed in vitro, does not occur in plasma.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 2 kringle domains. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Acute phase Blood coagulation
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Kringle Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Uncategorized	thrombin activity Inferred from direct assay. Source: UniProtKB
Biological process	STAT protein nuclear translocation Traceable author statement. Source: ProtInc activation of caspase activity Traceable author statement. Source: ProtInc acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW cell surface receptor linked signal transduction Inferred from direct assay. Source: UniProtKB fibrinolysis Inferred from direct assay. Source: UniProtKB multicellular organismal development Traceable author statement. Source: ProtInc platelet activation Traceable author statement. Source: UniProtKB positive regulation of blood coagulation Inferred from direct assay. Source: UniProtKB positive regulation of collagen biosynthetic process Inferred from direct assay. Source: UniProtKB positive regulation of protein amino acid phosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of release of sequestered calcium ion into cytosol Inferred from direct assay. Source: UniProtKB proteolysis Traceable author statement. Source: ProtInc release of sequestered calcium ion into cytosol Inferred from direct assay. Source: UniProtKB tyrosine phosphorylation of STAT protein Traceable author statement. Source: ProtInc
Cellular component	extracellular space Ref.33 Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from Experiment. Source: Reactome soluble fraction Ref.34 Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase activity Inferred from direct assay. Source: UniProtKB thrombospondin receptor activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q846V4	3	EBI-297094,EBI-989571	From a different organism.
THBD	P07204	1	EBI-297094,EBI-941422

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Propeptide

25 – 43

19

Ref.9

PRO_0000028159

Chain

44 – 622

579

Prothrombin

PRO_0000028160

Peptide

44 – 198

155

Activation peptide fragment 1

PRO_0000028161

Peptide

199 – 327

129

Activation peptide fragment 2

PRO_0000028162

Chain

328 – 363

36

Thrombin light chain

PRO_0000028163

Chain

364 – 622

259

Thrombin heavy chain

PRO_0000028164

Regions

Domain

44 – 89

46

Gla

Domain

108 – 186

79

Kringle 1

Domain

213 – 291

79

Kringle 2

Domain

364 – 618

255

Peptidase S1

Region

551 – 573

23

High affinity receptor-binding region which is also known as the TP508 peptide

Sites

Active site

406

1

Charge relay system

Active site

462

1

Charge relay system

Active site

568

1

Charge relay system

Site

198 – 199

2

Cleavage; by thrombin

Site

327 – 328

2

Cleavage; by factor Xa

Site

363 – 364

2

Cleavage; by factor Xa

Amino acid modifications

Modified residue

49

1

4-carboxyglutamate

Modified residue

50

1

4-carboxyglutamate

Modified residue

57

1

4-carboxyglutamate

Modified residue

59

1

4-carboxyglutamate

Modified residue

62

1

4-carboxyglutamate

Modified residue

63

1

4-carboxyglutamate

Modified residue

68

1

4-carboxyglutamate

Modified residue

69

1

4-carboxyglutamate

Modified residue

72

1

4-carboxyglutamate

Modified residue

75

1

4-carboxyglutamate

Glycosylation

121

1

N-linked (GlcNAc...) Ref.13 Ref.15

Glycosylation

143

1

N-linked (GlcNAc...) Ref.13 Ref.15

Glycosylation

416

1

N-linked (GlcNAc...) Ref.15

Disulfide bond

60 ↔ 65

Disulfide bond

90 ↔ 103

Disulfide bond

108 ↔ 186

Disulfide bond

129 ↔ 169

Disulfide bond

157 ↔ 181

Disulfide bond

213 ↔ 291

Disulfide bond

234 ↔ 274

Disulfide bond

262 ↔ 286

Disulfide bond

336 ↔ 482

Interchain (between light and heavy chains)

Disulfide bond

391 ↔ 407

Disulfide bond

536 ↔ 550

By similarity

Disulfide bond

564 ↔ 594

By similarity

Natural variations

Natural variant

72

1

E → G in dysprothrombinemia; Shanghai.

VAR_055232

Natural variant

165

1

T → M: dbSNP rs5896. Ref.3 Ref.40

VAR_011781

Natural variant

200

1

E → K in dysprothrombinemia; prothrombin type 3. Ref.39

VAR_006711

Natural variant

314

1

R → C in dysprothrombinemia; Barcelona/Madrid. Ref.29 Ref.32

VAR_006712

Natural variant

314

1

R → H in dysprothrombinemia; Padua-1. Ref.29 Ref.32

VAR_006713

Natural variant

380

1

M → T in dysprothrombinemia; Himi-1. Ref.31

VAR_006714

Natural variant

386

1

P → T: dbSNP rs5897. Ref.40

VAR_011782

Natural variant

425

1

R → C in dysprothrombinemia; Quick-1. Ref.33

VAR_006715

Natural variant

431

1

R → H in dysprothrombinemia; Himi-2. Ref.31

VAR_006716

Natural variant

461

1

R → W in dysprothrombinemia; Tokushima. Ref.36 Ref.37 Ref.38

VAR_006717

Natural variant

509

1

E → A in dysprothrombinemia; Salakta/Frankfurt. Ref.30 Ref.35

VAR_006718

Natural variant

601

1

G → V in dysprothrombinemia; Quick-2. Ref.34

VAR_006719

Experimental info

Sequence conflict

9 – 25

17

Missing in BAG64719. Ref.3

Sequence conflict

66

1

S → N in BAD96497. Ref.4

Sequence conflict

119

1

H → N AA sequence Ref.9

Sequence conflict

121

1

N → S AA sequence Ref.9

Sequence conflict

164

1

T → I AA sequence Ref.9

Sequence conflict

164

1

T → N in CAA23842. Ref.7

Sequence conflict

176

1

V → A AA sequence Ref.9

Sequence conflict

183

1

I → T AA sequence Ref.9

Sequence conflict

194 – 195

2

AM → MV AA sequence Ref.9

Sequence conflict

308

1

D → DEE AA sequence Ref.9

Sequence conflict

335

1

D → N AA sequence Ref.10

Sequence conflict

337

1

G → R in BAD96495. Ref.4

Sequence conflict

349

1

D → N AA sequence Ref.10

Sequence conflict

369

1

D → N AA sequence Ref.10

Sequence conflict

398

1

D → N AA sequence Ref.10

Sequence conflict

414

1

D → N AA sequence Ref.10

Sequence conflict

485

1

D → N AA sequence Ref.10

Sequence conflict

494

1

Q → G AA sequence Ref.10

Sequence conflict

504

1

W → Y AA sequence Ref.10

Sequence conflict

509

1

E → S AA sequence Ref.10

Sequence conflict

511

1

W → V AA sequence Ref.10

Sequence conflict

514

1

N → D AA sequence Ref.10

Sequence conflict

529 – 530

2

PI → AL AA sequence Ref.10

Sequence conflict

532

1

E → Q AA sequence Ref.10

Secondary structure

1

.

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622

Helix Strand Turn

Details...

Turn

334 – 337

4

Turn

340 – 342

3

Helix

343 – 345

3

Helix

352 – 358

7

Beta strand

378 – 383

6

Turn

384 – 387

4

Beta strand

388 – 395

8

Beta strand

397 – 403

7

Helix

405 – 407

3

Helix

411 – 413

3

Helix

419 – 421

3

Beta strand

422 – 427

6

Beta strand

430 – 433

4

Turn

436 – 438

3

Beta strand

440 – 442

3

Beta strand

444 – 449

6

Turn

455 – 458

4

Beta strand

464 – 470

7

Helix

486 – 492

7

Beta strand

498 – 504

7

Beta strand

524 – 530

7

Helix

533 – 538

6

Beta strand

548 – 551

4

Helix

555 – 557

3

Beta strand

571 – 575

5

Turn

577 – 579

3

Beta strand

582 – 590

9

Beta strand

592 – 595

4

Beta strand

601 – 605

5

Helix

607 – 609

3

Helix

610 – 620

11

Sequences

	Sequence		Length	Mass (Da)
	P00734-1 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: 8A25E1DA88208FCF	FASTA	622	70,037
	10 20 30 40 50 60 MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE VRKGNLEREC 70 80 90 100 110 120 VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL AACLEGNCAE GLGTNYRGHV 130 140 150 160 170 180 NITRSGIECQ LWRSRYPHKP EINSTTHPGA DLQENFCRNP DSSTTGPWCY TTDPTVRRQE 190 200 210 220 230 240 CSIPVCGQDQ VTVAMTPRSE GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA 250 260 270 280 290 300 QAKALSKHQD FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG 310 320 330 340 350 360 DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK TERELLESYI 370 380 390 400 410 420 DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW VLTAAHCLLY PPWDKNFTEN 430 440 450 460 470 480 DLLVRIGKHS RTRYERNIEK ISMLEKIYIH PRYNWRENLD RDIALMKLKK PVAFSDYIHP 490 500 510 520 530 540 VCLPDRETAA SLLQAGYKGR VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST 550 560 570 580 590 600 RIRITDNMFC AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY 610 620 GFYTHVFRLK KWIQKVIDQF GE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the gene for human prothrombin." Degen S.J.F., Davie E.W. Biochemistry 26:6165-6177(1987) [PubMed: 2825773] [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: 14962227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT DYSPROTHROMBINEMIA 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: 14702039] [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: 15489334] [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: 6305407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-622.
[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: 8073540] [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: 266717] [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: 873923] [Abstract] Cited for: PROTEIN SEQUENCE OF 315-622.
[11]	"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: 3759958] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[12]	"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: 2856554] [Abstract] Cited for: FUNCTION, CHARACTERIZATION.
[13]	"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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143, MASS SPECTROMETRY. Tissue: Plasma.
[14]	"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: 15885491] [Abstract] Cited for: CHARACTERIZATION OF THE TP508 PEPTIDE.
[15]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416, MASS SPECTROMETRY. Tissue: Plasma.
[16]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, MASS SPECTROMETRY. Tissue: Liver.
[17]	"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: 2583108] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[18]	"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: 2369893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
[19]	"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: 2374926] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
[20]	"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: 8251938] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH HIRUDIN AND SYNTHETIC INHIBITOR.
[21]	"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: 8071320] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[22]	"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: 9214615] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[23]	"Unexpected crucial role of residue 225 in serine proteases." Guinto E.R., Caccia S., Rose T., Fuetterer K., Waksman G., di Cera E. Proc. Natl. Acad. Sci. U.S.A. 96:1852-1857(1999) [PubMed: 10051558] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601.
[24]	"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: 11493008] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
[25]	"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: 16763681] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH HIRUDIN AND SYNTHETIC INHIBITOR.
[26]	"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: 17685615] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH HIRUDIN.
[27]	"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: 18291642] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
[28]	"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: 18362344] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH SERPINA5 AND HEPARIN.
[29]	"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: 3771562] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA CYS-314.
[30]	"Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala." Degen S.J.F., McDowell S.A., Sparks L.M., Scharrer I. Thromb. Haemost. 73:203-209(1995) [PubMed: 7792730] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA ALA-509.
[31]	"Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337-->Thr and Arg-388-->His)." Morishita E., Saito M., Kumabashiri I., Asakura H., Matsuda T., Yamaguchi K. Blood 80:2275-2280(1992) [PubMed: 1421398] [Abstract] Cited for: VARIANTS DYSPROTHROMBINEMIA THR-380 AND HIS-431.
[32]	"Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site." James H.L., Kim D.J., Zheng D.-Q., Girolami A. Blood Coagul. Fibrinolysis 5:841-844(1994) [PubMed: 7865694] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA HIS-314.
[33]	"Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382." Henriksen R.A., Mann K.G. Biochemistry 27:9160-9165(1988) [PubMed: 3242619] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA CYS-425.
[34]	"Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity." Henriksen R.A., Mann K.G. Biochemistry 28:2078-2082(1989) [PubMed: 2719946] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA VAL-601.
[35]	"Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity." Miyata T., Aruga R., Umeyama H., Bezeaud A., Guillin M.-C., Iwanaga S. Biochemistry 31:7457-7462(1992) [PubMed: 1354985] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA ALA-509.
[36]	"Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima." Miyata T., Morita T., Inomoto T., Kawauchi S., Shirakami A., Iwanaga S. Biochemistry 26:1117-1122(1987) [PubMed: 3567158] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA TRP-461.
[37]	"Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin." Inomoto T., Shirakami A., Kawauchi S., Shigekiyo T., Saito S., Miyoshi K., Morita T., Iwanaga S. Blood 69:565-569(1987) [PubMed: 3801671] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA TRP-461.
[38]	"Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia." Iwahana H., Yoshimoto K., Shigekiyo T., Shirakami A., Saito S., Itakura M. Int. J. Hematol. 55:93-100(1992) [PubMed: 1349838] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA TRP-461.
[39]	"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: 6405779] [Abstract] Cited for: VARIANT DYSPROTHROMBINEMIA LYS-200.
[40]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANTS MET-165 AND THR-386.
[41]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[42]	"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: 15534175] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ISCHEMIC STROKE.
[43]	"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: 17244316] [Abstract] Cited for: THERAPEUTIC USAGE OF THE TP508 PEPTIDE.
+	Additional computationally mapped references.

Web resources

Wikipedia

Thrombin entry

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00019568.

PIR

TBHU. A29351.

RefSeq

NP_000497.1.

UniGene

Hs.655207

3D structure databases

PDBPDBe

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	328-363	[»]
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	331-360	[»]
			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	328-363	[»]
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	364-620	[»]
1EB1	X-ray	1.80	H	364-620	[»]
			L	337-360	[»]
1EOJ	X-ray	2.10	A	334-620	[»]
1EOL	X-ray	2.10	A	334-620	[»]
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	336-622	[»]
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	328-363	[»]
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	334-360	[»]
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	328-363	[»]
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	328-363	[»]
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	328-363	[»]
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	335-620	[»]
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	328-363	[»]
			B	364-622	[»]
1THR	X-ray	2.30	H	364-622	[»]
			L	328-363	[»]
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	364-622	[»]
			L	333-360	[»]
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	334-361	[»]
			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	[»]
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	A	328-363	[»]
			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	336-621	[»]
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	334-363	[»]
			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	328-363	[»]
			B	364-622	[»]
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	[»]
			L	328-363	[»]
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	328-363	[»]
			D	364-622	[»]
2JH5	X-ray	2.50	C	328-363	[»]
			D	364-622	[»]
2JH6	X-ray	2.21	C	328-363	[»]
			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	L	328-363	[»]
			H	364-622	[»]
2ZO3	X-ray	1.70	L	328-363	[»]
			H	364-622	[»]
3B9F	X-ray	1.60	H	364-622	[»]
			L	315-363	[»]
3BEF	X-ray	2.20	A/D	318-363	[»]
			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	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	L	328-363	[»]
			H	364-622	[»]
3DD2	X-ray	1.90	H	364-621	[»]
			L	332-361	[»]
3E6P	X-ray	2.10	H	364-622	[»]
			L	206-363	[»]
3EGK	X-ray	2.20	H	364-622	[»]
			L	328-363	[»]
3HAT	X-ray	2.50	H	364-622	[»]
			L	328-363	[»]
3HTC	X-ray	2.30	H	364-622	[»]
			L	328-363	[»]
4HTC	X-ray	2.30	H	364-622	[»]
			L	328-363	[»]
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	328-363	[»]
			2	364-620	[»]

SMR

P00734. Positions 207-363.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6115N.

IntAct

P00734. 6 interactions.

Protein family/group databases

MEROPS

S01.217.

PTM databases

GlycoSuiteDB

P00734.

2-D gel databases

SWISS-2DPAGE

P00734.

Proteomic databases

PeptideAtlas

P00734.

PRIDE

P00734.

Genome annotation databases

Ensembl

ENSG00000180210. Homo sapiens. [Contig view]

GeneID

2147.

KEGG

hsa:2147.

UCSC

uc001ndf.2. human.

Organism-specific databases

GeneCards

GC11P046697.

H-InvDB

HIX0026188.

HGNC

HGNC:3535. F2.

HPA

CAB016780.
CAB018650.

MIM

176930. gene+phenotype.
601367. phenotype.

Orphanet

325. Congenital factor II deficiency.

PharmGKB

PA24406.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P00734.

HOVERGEN

P00734.

OMA

P00734. EGNCAEG.

Enzyme and pathway databases

BRENDA

3.4.21.5. 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_14797. Signaling by GPCR.
REACT_15380. Diabetes pathways.
REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

P00734.

Bgee

P00734.

CleanEx

HS_F2.

GermOnline

ENSG00000180210. Homo sapiens.

Family and domain databases

InterPro

IPR002383. Coagulation_factor_Gla.
IPR000294. GLA_domain.
IPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR012051. Peptidase_S1A_pr.
IPR003966. Peptidase_S1A_prothrombin.
IPR018992. Thrombin_light_chain.
[Graphical view]

Gene3D

G3DSA:2.40.20.10. Kringle. 2 hits.
G3DSA:4.10.140.10. Thrombin_light_chain. 1 hit.

PANTHER

PTHR19355:SF61. Peptidase_S1A_pr. 1 hit.

Pfam

PF00594. Gla. 1 hit.
PF00051. Kringle. 2 hits.
PF09396. Thrombin_light. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001149. Thrombin. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
PR00018. KRINGLE.
PR01505. PROTHROMBIN.

ProDom

PD000395. Kringle. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other Resources

BindingDB

P00734.

DrugBank

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.

NextBio

8681.

PMAP-CutDB

P00734.

SOURCE

Search...

Entry information

Entry name

THRB_HUMAN

Accession

Primary (citable) accession number: P00734
Secondary accession number(s): B2R7F7 , B4E1A7, Q4QZ40, Q53H04, Q53H06, Q7Z7P3, Q9UCA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1990
Last modified:	July 7, 2009
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)