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Reviewed, UniProtKB/Swiss-Prot P00734 (THRB_HUMAN)

Last modified January 19, 2010. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.

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Ontologies

Keywords
   Biological processAcute phase
Blood coagulation
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   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
Gene Ontology (GO)
   Biological processSTAT 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 componentextracellular 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 functioncalcium 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...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q846V43EBI-297094,EBI-989571From a different organism.
THBDP072041EBI-297094,EBI-941422

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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...) Ref.13 Ref.15
Glycosylation1431N-linked (GlcNAc...) Ref.13 Ref.15
Glycosylation4161N-linked (GlcNAc...) Ref.15 Ref.16
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 dysprothrombinemia; Shanghai. Ref.2
VAR_055232
Natural variant1651T → M: dbSNP rs5896. Ref.3 Ref.5 Ref.40
VAR_011781
Natural variant2001E → K in dysprothrombinemia; prothrombin type 3. Ref.39
VAR_006711
Natural variant3141R → C in dysprothrombinemia; Barcelona/Madrid. Ref.29
VAR_006712
Natural variant3141R → H in dysprothrombinemia; Padua-1. Ref.32
VAR_006713
Natural variant3801M → T in dysprothrombinemia; Himi-1. Ref.31
VAR_006714
Natural variant3861P → T: dbSNP rs5897. Ref.40
VAR_011782
Natural variant4251R → C in dysprothrombinemia; Quick-1. Ref.33
VAR_006715
Natural variant4311R → H in dysprothrombinemia; Himi-2. Ref.31
VAR_006716
Natural variant4611R → W in dysprothrombinemia; Tokushima. Ref.36 Ref.37 Ref.38
VAR_006717
Natural variant5091E → A in dysprothrombinemia; Salakta/Frankfurt. Ref.30 Ref.35
VAR_006718
Natural variant6011G → V in dysprothrombinemia; Quick-2. Ref.34
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 conflict5321E → Q AA sequence Ref.10

Secondary structure

1 .......................................................... 622
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00734-1 [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

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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: 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. 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: 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.

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Web resources

Wikipedia

Thrombin entry

GeneReviews
SeattleSNPs

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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.
IPIIPI00019568.
PIRTBHU. A29351.
RefSeqNP_000497.1.
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/F364-620[»]
1EB1X-ray1.80H364-620[»]
L337-360[»]
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-ray1.81A335-620[»]
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[»]
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[»]
4HTCX-ray2.30H364-622[»]
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[»]
SMRP00734. Positions 51-189, 78-198, 151-296.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6115N.
IntActP00734. 6 interactions.
STRINGP00734.

Protein family/group databases

MEROPSS01.217.

PTM databases

GlycoSuiteDBP00734.

2-D gel databases

SWISS-2DPAGEP00734.

Proteomic databases

PeptideAtlasP00734.
PRIDEP00734.

Genome annotation databases

EnsemblENST00000311907; ENSP00000308541; ENSG00000180210; Homo sapiens. [Genome view]
GeneID2147.
KEGGhsa:2147.
UCSCuc001ndf.2. human.

Organism-specific databases

CTD2147.
GeneCardsGC11P046697.
H-InvDBHIX0026188.
HGNCHGNC:3535. F2.
HPACAB016780.
CAB018650.
MIM176930. gene+phenotype.
601367. phenotype.
Orphanet325. Congenital factor II deficiency.
PharmGKBPA24406.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08832.
HOVERGENP00734.
InParanoidP00734.
OMAGIECQLW.
OrthoDBEOG90044C.

Enzyme and pathway databases

BRENDA3.4.21.5. 247.
Pathway_Interaction_DBangiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
ReactomeREACT_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

ArrayExpressP00734.
BgeeP00734.
CleanExHS_F2.
GenevestigatorP00734.
GermOnlineENSG00000180210. Homo sapiens.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla_dom.
IPR000294. GLA_domain.
IPR000001. Kringle.
IPR013806. Kringle-like.
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.
IPR009003. Ser/Cys_Pept_Trypsin-like.
IPR018992. Thrombin_light_chain.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 2 hits.
G3DSA:4.10.140.10. Thrombin_light_chain. 1 hit.
PANTHERPTHR19355:SF61. Peptidase_S1A_pr. 1 hit.
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.
PR00018. KRINGLE.
PR01505. PROTHROMBIN.
SMARTSM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
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 Resources

BindingDBP00734.
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.
NextBio8681.
PMAP-CutDBP00734.
SOURCESearch...

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Entry information

Entry nameTHRB_HUMAN
AccessionPrimary (citable) accession number: P00734
Secondary accession number(s): B2R7F7 expand/collapse secondary AC list , B4E1A7, Q4QZ40, Q53H04, Q53H06, Q7Z7P3, Q9UCA1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: January 19, 2010
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents