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P00734 (THRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 197. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prothrombin

EC=3.4.21.5
Alternative name(s):
Coagulation factor II
Gene names
Name:F2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.14

Catalytic activity

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

Enzyme regulation

Inhibited by SERPINA5. Ref.12

Subunit structure

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

Subcellular location

Secretedextracellular 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.

N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). Ref.22 Ref.24

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.16

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.15

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 processAcute phase
Blood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Thrombophilia
   DomainKringle
Repeat
Signal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Inferred from direct assay PubMed 1672265. Source: BHF-UCL

cellular protein metabolic process

Traceable author statement. Source: Reactome

cytosolic calcium ion homeostasis

Inferred from direct assay PubMed 19052258. Source: BHF-UCL

fibrinolysis

Inferred from direct assay PubMed 12855810. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

multicellular organismal development

Traceable author statement PubMed 9639571. Source: ProtInc

negative regulation of astrocyte differentiation

Inferred from direct assay PubMed 1691280. Source: BHF-UCL

negative regulation of fibrinolysis

Traceable author statement PubMed 17379830. Source: BHF-UCL

negative regulation of platelet activation

Traceable author statement PubMed 17379830. Source: BHF-UCL

negative regulation of proteolysis

Inferred from direct assay PubMed 1695900. Source: BHF-UCL

peptidyl-glutamic acid carboxylation

Traceable author statement. Source: Reactome

platelet activation

Inferred from direct assay PubMed 9038223. Source: BHF-UCL

positive regulation of blood coagulation

Inferred from direct assay PubMed 9038223. Source: BHF-UCL

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of collagen biosynthetic process

Inferred from direct assay PubMed 9639571. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 20164183. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 7559487. Source: BHF-UCL

positive regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 17275676. Source: UniProtKB

positive regulation of release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 1672265PubMed 19052258. Source: BHF-UCL

post-translational protein modification

Traceable author statement. Source: Reactome

proteolysis

Traceable author statement. Source: Reactome

regulation of blood coagulation

Traceable author statement PubMed 12855810. Source: UniProtKB

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from direct assay PubMed 9639571. Source: BHF-UCL

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 9639571. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

growth factor activity

Traceable author statement PubMed 8626514. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 12855810. Source: UniProtKB

serine-type endopeptidase activity

Inferred from direct assay PubMed 12855810. Source: UniProtKB

thrombospondin receptor activity

Inferred from direct assay PubMed 2435757. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q846V45EBI-297094,EBI-989571From a different organism.
THBDP072044EBI-297094,EBI-941422

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 4319
PRO_0000028159
Chain44 – 622579Prothrombin
PRO_0000028160
Peptide44 – 198155Activation peptide fragment 1
PRO_0000028161
Peptide199 – 327129Activation peptide fragment 2
PRO_0000028162
Chain328 – 36336Thrombin light chain
PRO_0000028163
Chain364 – 622259Thrombin heavy chain
PRO_0000028164

Regions

Domain44 – 8946Gla
Domain108 – 18679Kringle 1
Domain213 – 29179Kringle 2
Domain364 – 618255Peptidase S1
Region551 – 57323High affinity receptor-binding region which is also known as the TP508 peptide

Sites

Active site4061Charge relay system
Active site4621Charge relay system
Active site5681Charge relay system
Site198 – 1992Cleavage; by thrombin
Site327 – 3282Cleavage; by factor Xa
Site363 – 3642Cleavage; by factor Xa

Amino acid modifications

Modified residue4914-carboxyglutamate
Modified residue5014-carboxyglutamate
Modified residue5714-carboxyglutamate
Modified residue5914-carboxyglutamate
Modified residue6214-carboxyglutamate
Modified residue6314-carboxyglutamate
Modified residue6814-carboxyglutamate
Modified residue6914-carboxyglutamate
Modified residue7214-carboxyglutamate
Modified residue7514-carboxyglutamate
Glycosylation1211N-linked (GlcNAc...) (complex) Ref.17 Ref.19 Ref.24
Glycosylation1431N-linked (GlcNAc...) (complex) Ref.17 Ref.19 Ref.24
Glycosylation4161N-linked (GlcNAc...) (complex) Ref.19 Ref.21 Ref.22 Ref.23
Disulfide bond60 ↔ 65
Disulfide bond90 ↔ 103
Disulfide bond108 ↔ 186
Disulfide bond129 ↔ 169
Disulfide bond157 ↔ 181
Disulfide bond213 ↔ 291
Disulfide bond234 ↔ 274
Disulfide bond262 ↔ 286
Disulfide bond336 ↔ 482Interchain (between light and heavy chains)
Disulfide bond391 ↔ 407
Disulfide bond536 ↔ 550 By similarity
Disulfide bond564 ↔ 594 By similarity

Natural variations

Natural variant721E → G in FA2D; Shanghai. Ref.2
VAR_055232
Natural variant1651T → M Polymorphism confirmed at protein level. Ref.3 Ref.5 Ref.48 Ref.50
Corresponds to variant rs5896 [ dbSNP | Ensembl ].
VAR_011781
Natural variant2001E → K in FA2D; prothrombin type 3; variant confirmed at protein level. Ref.37 Ref.50
Corresponds to variant rs62623459 [ dbSNP | Ensembl ].
VAR_006711
Natural variant3141R → C in FA2D; Barcelona/Madrid. Ref.38
VAR_006712
Natural variant3141R → H in FA2D; Padua-1. Ref.46
VAR_006713
Natural variant3801M → T in FA2D; Himi-1. Ref.44
VAR_006714
Natural variant3861P → T Polymorphism confirmed at protein level. Ref.48 Ref.50
Corresponds to variant rs5897 [ dbSNP | Ensembl ].
VAR_011782
Natural variant4251R → C in FA2D; Quick-1. Ref.41
VAR_006715
Natural variant4311R → H in FA2D; Himi-2. Ref.44
VAR_006716
Natural variant4611R → W in FA2D; Tokushima. Ref.39 Ref.40 Ref.45
VAR_006717
Natural variant5091E → A in FA2D; Salakta/Frankfurt. Ref.43 Ref.47
VAR_006718
Natural variant5321E → Q Polymorphism confirmed at protein level. Ref.10 Ref.50
VAR_068913
Natural variant6011G → V in FA2D; Quick-2. Ref.42
VAR_006719

Experimental info

Sequence conflict9 – 2517Missing in BAG64719. Ref.3
Sequence conflict661S → N in BAD96497. Ref.4
Sequence conflict1191H → N AA sequence Ref.9
Sequence conflict1211N → S AA sequence Ref.9
Sequence conflict1641T → I AA sequence Ref.9
Sequence conflict1641T → N in CAA23842. Ref.7
Sequence conflict1761V → A AA sequence Ref.9
Sequence conflict1831I → T AA sequence Ref.9
Sequence conflict194 – 1952AM → MV AA sequence Ref.9
Sequence conflict3081D → DEE AA sequence Ref.9
Sequence conflict3351D → N AA sequence Ref.10
Sequence conflict3371G → R in BAD96495. Ref.4
Sequence conflict3491D → N AA sequence Ref.10
Sequence conflict3691D → N AA sequence Ref.10
Sequence conflict3981D → N AA sequence Ref.10
Sequence conflict4141D → N AA sequence Ref.10
Sequence conflict4851D → N AA sequence Ref.10
Sequence conflict4941Q → G AA sequence Ref.10
Sequence conflict5041W → Y AA sequence Ref.10
Sequence conflict5091E → S AA sequence Ref.10
Sequence conflict5111W → V AA sequence Ref.10
Sequence conflict5141N → D AA sequence Ref.10
Sequence conflict529 – 5302PI → AL AA sequence Ref.10
Sequence conflict590 – 5923WGE → AGA in AAR08143. Ref.11

Secondary structure

........................................................................................... 622
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00734 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 8A25E1DA88208FCF

FASTA62270,037
        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 

« Hide

References

« Hide '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] [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. expand/collapse author list , 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.
[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, 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.
[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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-416.
[23]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, STRUCTURE OF CARBOHYDRATE.
Tissue: Cerebrospinal fluid.
[24]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-121 AND ASN-143, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[25]"The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment."
Bode W., Mayr I., Baumann U., Huber R., Stone S.R., Hofsteenge J.
EMBO J. 8:3467-3475(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[26]"Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition."
Gruetter M.G., Priestle J.P., Rahuel J., Grossenbacher H., Bode W., Hofsteenge J., Stone S.R.
EMBO J. 9:2361-2365(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
[27]"The structure of a complex of recombinant hirudin and human alpha-thrombin."
Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R., Roitsch C., Fenton J.W. II
Science 249:277-280(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
[28]"Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms."
Priestle J.P., Rahuel J., Rink H., Tones M., Gruetter M.G.
Protein Sci. 2:1630-1642(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH HIRUDIN AND SYNTHETIC INHIBITOR.
[29]"Crystallographic structure of human gamma-thrombin."
Rydel T.J., Yin M., Padmanabhan K.P., Blankenship D.T., Cardin A.D., Correa P.E., Fenton J.W. II, Tulinsky A.
J. Biol. Chem. 269:22000-22006(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[30]"The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin."
van de Locht A., Bode W., Huber R., le Bonniec B.F., Stone S.R., Esmon C.T., Stubbs M.T.
EMBO J. 16:2977-2984(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[31]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601.
[32]"Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate."
Skordalakes E., Dodson G.G., Green D.S., Goodwin C.A., Scully M.F., Hudson H.R., Kakkar V.V., Deadman J.J.
J. Mol. Biol. 311:549-555(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
[33]"Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors."
Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P., Obst-Sander U., Wagner B., Kansy M., Banner D.W., Diederich F.
Org. Biomol. Chem. 4:2364-2375(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH HIRUDIN AND SYNTHETIC INHIBITOR.
[34]"Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin."
Liu C.C., Brustad E., Liu W., Schultz P.G.
J. Am. Chem. Soc. 129:10648-10649(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH HIRUDIN.
[35]"Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles."
Isaacs R.C.A., Solinsky M.G., Cutrona K.J., Newton C.L., Naylor-Olsen A.M., McMasters D.R., Krueger J.A., Lewis S.D., Lucas B.J., Kuo L.C., Yan Y., Lynch J.J., Lyle E.A.
Bioorg. Med. Chem. Lett. 18:2062-2066(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
[36]"Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex."
Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.
Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH SERPINA5 AND HEPARIN.
[37]"Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site."
Board P.G., Shaw D.C.
Br. J. Haematol. 54:245-254(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D LYS-200, PARTIAL PROTEIN SEQUENCE.
[38]"Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273."
Rabiet M.-J., Furie B.C., Furie B.
J. Biol. Chem. 261:15045-15048(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D CYS-314, PROTEIN SEQUENCE OF 310-327.
[39]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D TRP-461, PARTIAL PROTEIN SEQUENCE.
[40]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D TRP-461.
[41]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D CYS-425, PARTIAL PROTEIN SEQUENCE.
[42]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D VAL-601, PARTIAL PROTEIN SEQUENCE.
[43]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D ALA-509, PARTIAL PROTEIN SEQUENCE.
[44]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS FA2D THR-380 AND HIS-431.
[45]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D TRP-461.
[46]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D HIS-314.
[47]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FA2D ALA-509.
[48]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-165 AND THR-386.
[49]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)
[50]"Quantitative detection of single amino acid polymorphisms by targeted proteomics."
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-165; LYS-200; THR-386 AND GLN-532, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRTBHU. A29351.
RefSeqNP_000497.1. NM_000506.3.
UniGeneHs.655207.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2CX-ray2.10H364-622[»]
L328-363[»]
1A3BX-ray1.80H364-622[»]
L328-363[»]
1A3EX-ray1.85H364-622[»]
L328-363[»]
1A46X-ray2.12H364-622[»]
L328-363[»]
1A4WX-ray1.80H364-622[»]
L328-363[»]
1A5GX-ray2.06H364-622[»]
L328-363[»]
1A61X-ray2.20H364-622[»]
L328-363[»]
1ABIX-ray2.30H364-622[»]
L328-363[»]
1ABJX-ray2.40H364-622[»]
L328-363[»]
1AD8X-ray2.00H364-622[»]
L328-363[»]
1AE8X-ray2.00H364-622[»]
L328-363[»]
1AFEX-ray2.00H364-622[»]
L328-363[»]
1AHTX-ray1.60H364-622[»]
L328-363[»]
1AI8X-ray1.85H364-622[»]
L328-363[»]
1AIXX-ray2.10H364-622[»]
L328-363[»]
1AWFX-ray2.20H364-622[»]
L328-363[»]
1AWHX-ray3.00A/C328-363[»]
B/D364-622[»]
1AY6X-ray1.80H364-622[»]
L328-363[»]
1B5GX-ray2.07H364-622[»]
L328-363[»]
1B7XX-ray2.10A328-363[»]
B364-622[»]
1BA8X-ray1.80A328-363[»]
B364-622[»]
1BB0X-ray2.10A328-363[»]
B364-622[»]
1BCUX-ray2.00H364-622[»]
L328-363[»]
1BHXX-ray2.30A331-360[»]
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/L328-363[»]
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-ray2.10A334-620[»]
1EOLX-ray2.10A334-620[»]
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-ray2.00E336-622[»]
1HAHX-ray2.30H364-622[»]
L328-363[»]
1HAIX-ray2.40H364-622[»]
L328-363[»]
1HAOX-ray2.80H364-622[»]
L328-363[»]
1HAPX-ray2.80H364-622[»]
L328-363[»]
1HBTX-ray2.00H364-622[»]
L328-363[»]
1HDTX-ray2.60H364-622[»]
L331-363[»]
1HGTX-ray2.20H364-622[»]
L328-363[»]
1HLTX-ray3.00H/K364-622[»]
J/L334-360[»]
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[»]
L328-363[»]
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[»]
L328-363[»]
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[»]
L328-363[»]
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-ray2.10A328-363[»]
B364-622[»]
1THRX-ray2.30H364-622[»]
L328-363[»]
1THSX-ray2.20H364-622[»]
L328-363[»]
1TMBX-ray2.30H364-622[»]
L328-363[»]
1TMTX-ray2.20H364-622[»]
L328-363[»]
1TMUX-ray2.50H364-622[»]
L333-360[»]
1TOMX-ray1.80H364-622[»]
L328-363[»]
1TQ0X-ray2.80A/C333-363[»]
B/D364-620[»]
1TQ7X-ray2.40A320-363[»]
B364-620[»]
1TWXX-ray2.40A334-361[»]
B364-622[»]
1UMAX-ray2.00H364-622[»]
L328-363[»]
1UVSX-ray2.80H364-622[»]
L328-363[»]
1VR1X-ray1.90H364-620[»]
L334-360[»]
1VZQX-ray1.54H364-620[»]
L334-360[»]
1W7GX-ray1.65H364-622[»]
L328-363[»]
1WAYX-ray2.02A328-363[»]
B364-622[»]
1WBGX-ray2.20A328-363[»]
B364-622[»]
1XM1X-ray2.30A328-622[»]
1XMNX-ray1.85A/C/E/G328-363[»]
B/D/F/H364-622[»]
1YPEX-ray1.81H364-620[»]
L334-360[»]
1YPGX-ray1.80H364-620[»]
L334-360[»]
1YPJX-ray1.78H364-620[»]
L334-360[»]
1YPKX-ray1.78H364-620[»]
L334-360[»]
1YPLX-ray1.85H364-620[»]
L334-360[»]
1YPMX-ray1.85H364-620[»]
L334-360[»]
1Z71X-ray1.80A336-621[»]
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/C334-363[»]
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-ray1.87A328-363[»]
B364-622[»]
2H9TX-ray2.40H364-622[»]
L328-363[»]
2HGTX-ray2.20H364-622[»]
L328-363[»]
2HNTX-ray2.50C364-433[»]
E437-517[»]
F518-622[»]
L328-363[»]
2HPPX-ray3.30H364-622[»]
L328-363[»]
2HPQX-ray3.30H364-622[»]
L328-363[»]
P213-291[»]
2HWLX-ray2.40A/C328-363[»]
B/D364-622[»]
2JH0X-ray1.70C328-363[»]
D364-622[»]
2JH5X-ray2.50C328-363[»]
D364-622[»]
2JH6X-ray2.21C328-363[»]
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/D318-363[»]
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-ray1.80B364-622[»]
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-ray1.86H364-622[»]
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[»]
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[»]
4THNX-ray2.50H364-622[»]
L328-363[»]
5GDSX-ray2.10H364-622[»]
L328-363[»]
7KMEX-ray2.10H364-622[»]
L328-363[»]
8KMEX-ray2.101328-363[»]
2364-620[»]
ProteinModelPortalP00734.
SMRP00734. Positions 51-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108447. 15 interactions.
DIPDIP-6115N.
IntActP00734. 8 interactions.
MINTMINT-147273.
STRING9606.ENSP00000308541.

Chemistry

BindingDBP00734.
ChEMBLCHEMBL2096988.
DrugBankDB00025. 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.
GuidetoPHARMACOLOGY2362.

Protein family/group databases

MEROPSS01.217.

PTM databases

PhosphoSiteP00734.
UniCarbKBP00734.

Polymorphism databases

DMDM135807.

2D gel databases

SWISS-2DPAGEP00734.

Proteomic databases

PaxDbP00734.
PeptideAtlasP00734.
PRIDEP00734.

Protocols and materials databases

DNASU2147.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311907; ENSP00000308541; ENSG00000180210.
GeneID2147.
KEGGhsa:2147.
UCSCuc001ndf.4. human.

Organism-specific databases

CTD2147.
GeneCardsGC11P046740.
H-InvDBHIX0026188.
HGNCHGNC:3535. F2.
HPACAB016780.
CAB018650.
HPA051476.
HPA054698.
MIM176930. gene.
188050. phenotype.
601367. phenotype.
613679. phenotype.
614390. phenotype.
neXtProtNX_P00734.
Orphanet325. Congenital factor II deficiency.
64738. Non rare thrombophilia.
PharmGKBPA157.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG108381.
InParanoidP00734.
KOK01313.
OMAGIECQLW.
PhylomeDBP00734.
TreeFamTF327329.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
SABIO-RKP00734.

Gene expression databases

ArrayExpressP00734.
BgeeP00734.
CleanExHS_F2.
GenevestigatorP00734.

Family and domain databases

Gene3D2.40.20.10. 2 hits.
4.10.140.10. 1 hit.
4.10.740.10. 1 hit.
InterProIPR017857. 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]
PfamPF00594. Gla. 1 hit.
PF00051. Kringle. 2 hits.
PF09396. Thrombin_light. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001149. Thrombin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
PR01505. PROTHROMBIN.
SMARTSM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEPS00011. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP00734.
GeneWikiThrombin.
GenomeRNAi2147.
NextBio8681.
PMAP-CutDBP00734.
PROP00734.
SOURCESearch...

Entry information

Entry nameTHRB_HUMAN
AccessionPrimary (citable) accession number: P00734
Secondary accession number(s): B2R7F7 expand/collapse secondary AC list , B4E1A7, Q4QZ40, Q53H04, Q53H06, Q69EZ7, Q7Z7P3, Q9UCA1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 197 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM