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Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]

 THRB_HUMAN              Reviewed;         622 AA.
P00734; B2R7F7; B4E1A7; Q4QZ40; Q53H04; Q53H06; Q69EZ7; Q7Z7P3;
Q9UCA1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
30-AUG-2017, entry version 232.
RecName: Full=Prothrombin;
EC=3.4.21.5;
AltName: Full=Coagulation factor II;
Contains:
RecName: Full=Activation peptide fragment 1;
Contains:
RecName: Full=Activation peptide fragment 2;
Contains:
RecName: Full=Thrombin light chain;
Contains:
RecName: Full=Thrombin heavy chain;
Flags: Precursor;
Name=F2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2825773; DOI=10.1021/bi00393a033;
Degen S.J.F., Davie E.W.;
"Nucleotide sequence of the gene for human prothrombin.";
Biochemistry 26:6165-6177(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT FA2D GLY-72.
TISSUE=Blood;
PubMed=14962227; DOI=10.1046/j.1365-2516.2003.00838.x;
Wang W., Fu Q., Zhou R., Wu W., Ding Q., Hu Y., Wang X., Wang H.,
Wang Z.;
"Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of
Gla29 by Gly.";
Haemophilia 10:94-97(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-165.
TISSUE=Liver, and Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-165.
SeattleSNPs variation discovery resource;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-622, AND GAMMA-CARBOXYGLUTAMATION AT
GLU-49; GLU-50; GLU-57; GLU-59; GLU-62; GLU-63; GLU-68; GLU-69; GLU-72
AND GLU-75.
PubMed=6305407; DOI=10.1021/bi00278a008;
Degen S.J.F., McGillivray R.T.A., Davie E.W.;
"Characterization of the complementary deoxyribonucleic acid and gene
coding for human prothrombin.";
Biochemistry 22:2087-2097(1983).
[8]
PROTEIN SEQUENCE OF 44-64.
TISSUE=Urine;
PubMed=8073540; DOI=10.1007/BF00431548;
Suzuki K., Moriyama M., Nakajima C., Kawamura K., Miyazawa K.,
Tsugawa R., Kikuchi N., Nagata K.;
"Isolation and partial characterization of crystal matrix protein as a
potent inhibitor of calcium oxalate crystal aggregation: evidence of
activation peptide of human prothrombin.";
Urol. Res. 22:45-50(1994).
[9]
PROTEIN SEQUENCE OF 44-314.
PubMed=266717; DOI=10.1073/pnas.74.5.1969;
Walz D.A., Hewett-Emmett D., Seegers W.H.;
"Amino acid sequence of human prothrombin fragments 1 and 2.";
Proc. Natl. Acad. Sci. U.S.A. 74:1969-1972(1977).
[10]
PROTEIN SEQUENCE OF 315-622, GLYCOSYLATION AT ASN-416, AND VARIANT
GLN-532.
PubMed=873923;
Butkowski R.J., Elion J., Downing M.R., Mann K.G.;
"Primary structure of human prethrombin 2 and alpha-thrombin.";
J. Biol. Chem. 252:4942-4957(1977).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 364-622.
Gruber A., Hanson S.R., DiCera E.;
"Antithrombotic thrombin variants.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[12]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=6323392;
Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
"Mechanism of inhibition of activated protein C by protein C
inhibitor.";
J. Biochem. 95:187-195(1984).
[13]
PROTEOLYTIC PROCESSING, AND GAMMA-CARBOXYGLUTAMATION AT GLU-49 AND
GLU-50.
PubMed=3759958;
Rabiet M.J., Blashill A., Furie B., Furie B.C.;
"Prothrombin fragment 1 X 2 X 3, a major product of prothrombin
activation in human plasma.";
J. Biol. Chem. 261:13210-13215(1986).
[14]
FUNCTION, AND CHARACTERIZATION.
PubMed=2856554;
Glenn K.C., Frost G.H., Bergmann J.S., Carney D.H.;
"Synthetic peptides bind to high-affinity thrombin receptors and
modulate thrombin mitogenesis.";
Pept. Res. 1:65-73(1988).
[15]
INVOLVEMENT IN RPRGL2 SUSCEPTIBILITY.
PubMed=11506076; DOI=10.1111/j.8755-8920.2001.460202.x;
Pihusch R., Buchholz T., Lohse P., Rubsamen H., Rogenhofer N.,
Hasbargen U., Hiller E., Thaler C.J.;
"Thrombophilic gene mutations and recurrent spontaneous abortion:
prothrombin mutation increases the risk in the first trimester.";
Am. J. Reprod. Immunol. 46:124-131(2001).
[16]
INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.
PubMed=15534175; DOI=10.1001/archneur.61.11.1652;
Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes
involving approximately 18,000 cases and 58,000 controls.";
Arch. Neurol. 61:1652-1661(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[18]
CHARACTERIZATION OF THE TP508 PEPTIDE.
PubMed=15885491; DOI=10.1016/j.orthres.2004.12.005;
Li G., Cui Y., McIlmurray L., Allen W.E., Wang H.;
"rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508
induce chemotaxis of human osteoblasts and microvascular endothelial
cells.";
J. Orthop. Res. 23:680-685(2005).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[20]
THERAPEUTIC USAGE OF THE TP508 PEPTIDE.
PubMed=17244316; DOI=10.1111/j.1524-475X.2006.00181.x;
Fife C., Mader J.T., Stone J., Brill L., Satterfield K., Norfleet A.,
Zwernemann A., Ryaby J.T., Carney D.H.;
"Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers
in a placebo-controlled phase I/II study.";
Wound Repair Regen. 15:23-34(2007).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[22]
GLYCOSYLATION AT ASN-416.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
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.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, AND STRUCTURE OF
CARBOHYDRATE.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[24]
GLYCOSYLATION AT ASN-121 AND ASN-143, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=2583108;
Bode W., Mayr I., Baumann U., Huber R., Stone S.R., Hofsteenge J.;
"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.";
EMBO J. 8:3467-3475(1989).
[27]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
PubMed=2369893;
Gruetter M.G., Priestle J.P., Rahuel J., Grossenbacher H., Bode W.,
Hofsteenge J., Stone S.R.;
"Crystal structure of the thrombin-hirudin complex: a novel mode of
serine protease inhibition.";
EMBO J. 9:2361-2365(1990).
[28]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
PubMed=2374926; DOI=10.1126/science.2374926;
Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R.,
Roitsch C., Fenton J.W. II;
"The structure of a complex of recombinant hirudin and human alpha-
thrombin.";
Science 249:277-280(1990).
[29]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH
HIRUDIN AND SYNTHETIC INHIBITOR.
PubMed=8251938; DOI=10.1002/pro.5560021009;
Priestle J.P., Rahuel J., Rink H., Tones M., Gruetter M.G.;
"Changes in interactions in complexes of hirudin derivatives and human
alpha-thrombin due to different crystal forms.";
Protein Sci. 2:1630-1642(1993).
[30]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8071320;
Rydel T.J., Yin M., Padmanabhan K.P., Blankenship D.T., Cardin A.D.,
Correa P.E., Fenton J.W. II, Tulinsky A.;
"Crystallographic structure of human gamma-thrombin.";
J. Biol. Chem. 269:22000-22006(1994).
[31]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=9214615; DOI=10.1093/emboj/16.11.2977;
van de Locht A., Bode W., Huber R., le Bonniec B.F., Stone S.R.,
Esmon C.T., Stubbs M.T.;
"The thrombin E192Q-BPTI complex reveals gross structural
rearrangements: implications for the interaction with antithrombin and
thrombomodulin.";
EMBO J. 16:2977-2984(1997).
[32]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601.
PubMed=10051558; DOI=10.1073/pnas.96.5.1852;
Guinto E.R., Caccia S., Rose T., Fuetterer K., Waksman G., di Cera E.;
"Unexpected crucial role of residue 225 in serine proteases.";
Proc. Natl. Acad. Sci. U.S.A. 96:1852-1857(1999).
[33]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH
SYNTHETIC INHIBITOR.
PubMed=11493008; DOI=10.1006/jmbi.2001.4872;
Skordalakes E., Dodson G.G., Green D.S., Goodwin C.A., Scully M.F.,
Hudson H.R., Kakkar V.V., Deadman J.J.;
"Inhibition of human alpha-thrombin by a phosphonate tripeptide
proceeds via a metastable pentacoordinated phosphorus intermediate.";
J. Mol. Biol. 311:549-555(2001).
[34]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH
HIRUDIN AND SYNTHETIC INHIBITOR.
PubMed=16763681; DOI=10.1039/b602585d;
Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P.,
Obst-Sander U., Wagner B., Kansy M., Banner D.W., Diederich F.;
"Multipolar interactions in the D pocket of thrombin: large
differences between tricyclic imide and lactam inhibitors.";
Org. Biomol. Chem. 4:2364-2375(2006).
[35]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH
HIRUDIN.
PubMed=17685615; DOI=10.1021/ja0735002;
Liu C.C., Brustad E., Liu W., Schultz P.G.;
"Crystal structure of a biosynthetic sulfo-hirudin complexed to
thrombin.";
J. Am. Chem. Soc. 129:10648-10649(2007).
[36]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH
SYNTHETIC INHIBITOR.
PubMed=18291642; DOI=10.1016/j.bmcl.2008.01.098;
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.;
"Structure-based design of novel groups for use in the P1 position of
thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles.";
Bioorg. Med. Chem. Lett. 18:2062-2066(2008).
[37]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH
SERPINA5 AND HEPARIN.
PubMed=18362344; DOI=10.1073/pnas.0711055105;
Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.;
"Molecular basis of thrombin recognition by protein C inhibitor
revealed by the 1.6-A structure of the heparin-bridged complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008).
[38]
VARIANT FA2D LYS-200, AND PARTIAL PROTEIN SEQUENCE.
PubMed=6405779; DOI=10.1111/j.1365-2141.1983.tb02092.x;
Board P.G., Shaw D.C.;
"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.";
Br. J. Haematol. 54:245-254(1983).
[39]
VARIANT FA2D CYS-314, AND PROTEIN SEQUENCE OF 310-327.
PubMed=3771562;
Rabiet M.-J., Furie B.C., Furie B.;
"Molecular defect of prothrombin Barcelona. Substitution of cysteine
for arginine at residue 273.";
J. Biol. Chem. 261:15045-15048(1986).
[40]
VARIANT FA2D TRP-461, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3567158; DOI=10.1021/bi00378a020;
Miyata T., Morita T., Inomoto T., Kawauchi S., Shirakami A.,
Iwanaga S.;
"Prothrombin Tokushima, a replacement of arginine-418 by tryptophan
that impairs the fibrinogen clotting activity of derived thrombin
Tokushima.";
Biochemistry 26:1117-1122(1987).
[41]
VARIANT FA2D TRP-461.
PubMed=3801671;
Inomoto T., Shirakami A., Kawauchi S., Shigekiyo T., Saito S.,
Miyoshi K., Morita T., Iwanaga S.;
"Prothrombin Tokushima: characterization of dysfunctional thrombin
derived from a variant of human prothrombin.";
Blood 69:565-569(1987).
[42]
VARIANT FA2D CYS-425, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3242619; DOI=10.1021/bi00426a013;
Henriksen R.A., Mann K.G.;
"Identification of the primary structural defect in the dysthrombin
thrombin Quick I: substitution of cysteine for arginine-382.";
Biochemistry 27:9160-9165(1988).
[43]
VARIANT FA2D VAL-601, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2719946; DOI=10.1021/bi00431a017;
Henriksen R.A., Mann K.G.;
"Substitution of valine for glycine-558 in the congenital dysthrombin
thrombin Quick II alters primary substrate specificity.";
Biochemistry 28:2078-2082(1989).
[44]
VARIANT FA2D ALA-509, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1354985; DOI=10.1021/bi00148a005;
Miyata T., Aruga R., Umeyama H., Bezeaud A., Guillin M.-C.,
Iwanaga S.;
"Prothrombin Salakta: substitution of glutamic acid-466 by alanine
reduces the fibrinogen clotting activity and the esterase activity.";
Biochemistry 31:7457-7462(1992).
[45]
VARIANTS FA2D THR-380 AND HIS-431.
PubMed=1421398;
Morishita E., Saito M., Kumabashiri I., Asakura H., Matsuda T.,
Yamaguchi K.;
"Prothrombin Himi: a compound heterozygote for two dysfunctional
prothrombin molecules (Met-337-->Thr and Arg-388-->His).";
Blood 80:2275-2280(1992).
[46]
VARIANT FA2D TRP-461.
PubMed=1349838;
Iwahana H., Yoshimoto K., Shigekiyo T., Shirakami A., Saito S.,
Itakura M.;
"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.";
Int. J. Hematol. 55:93-100(1992).
[47]
VARIANT FA2D HIS-314.
PubMed=7865694;
James H.L., Kim D.J., Zheng D.-Q., Girolami A.;
"Prothrombin Padua I: incomplete activation due to an amino acid
substitution at a factor Xa cleavage site.";
Blood Coagul. Fibrinolysis 5:841-844(1994).
[48]
VARIANT FA2D ALA-509.
PubMed=7792730;
Degen S.J.F., McDowell S.A., Sparks L.M., Scharrer I.;
"Prothrombin Frankfurt: a dysfunctional prothrombin characterized by
substitution of Glu-466 by Ala.";
Thromb. Haemost. 73:203-209(1995).
[49]
VARIANTS MET-165 AND THR-386.
PubMed=10391209; DOI=10.1038/10290;
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.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[50]
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).
[51]
VARIANTS MET-165; LYS-200; THR-386 AND GLN-532, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
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.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
-!- 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.
{ECO:0000269|PubMed:2856554}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in
fibrinogen to form fibrin and release fibrinopeptides A and B.
-!- ENZYME REGULATION: Inhibited by SERPINA5.
{ECO:0000269|PubMed:6323392}.
-!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy
chain; disulfide-linked. Forms a heterodimer with SERPINA5.
{ECO:0000269|PubMed:11493008, ECO:0000269|PubMed:16763681,
ECO:0000269|PubMed:17685615, ECO:0000269|PubMed:18291642,
ECO:0000269|PubMed:18362344, ECO:0000269|PubMed:2369893,
ECO:0000269|PubMed:2374926}.
-!- INTERACTION:
Q846V4:- (xeno); NbExp=5; IntAct=EBI-297094, EBI-989571;
P07204:THBD; NbExp=4; IntAct=EBI-297094, EBI-941422;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- PTM: 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.
{ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407}.
-!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-121:
Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).
At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).
{ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:873923}.
-!- 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. {ECO:0000269|PubMed:1349838,
ECO:0000269|PubMed:1354985, ECO:0000269|PubMed:1421398,
ECO:0000269|PubMed:14962227, ECO:0000269|PubMed:2719946,
ECO:0000269|PubMed:3242619, ECO:0000269|PubMed:3567158,
ECO:0000269|PubMed:3771562, ECO:0000269|PubMed:3801671,
ECO:0000269|PubMed:6405779, ECO:0000269|PubMed:7792730,
ECO:0000269|PubMed:7865694}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:15534175}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:2825773}. 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.
-!- DISEASE: 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. {ECO:0000269|PubMed:11506076}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- PHARMACEUTICAL: 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.
-!- MISCELLANEOUS: It is not known whether 1 or 2 smaller activation
peptides, with additional cleavage after Arg-314, are released in
natural blood clotting.
-!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment
(fragment 1) of the prothrombin, prior to its activation by factor
Xa.
-!- MISCELLANEOUS: The cleavage after Arg-198, observed in vitro, does
not occur in plasma.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Thrombin entry;
URL="https://en.wikipedia.org/wiki/Thrombin";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f2/";
-----------------------------------------------------------------------
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EMBL; M17262; AAC63054.1; -; Genomic_DNA.
EMBL; AJ972449; CAJ01369.1; -; mRNA.
EMBL; AK303747; BAG64719.1; -; mRNA.
EMBL; AK312965; BAG35804.1; -; mRNA.
EMBL; AK222775; BAD96495.1; -; mRNA.
EMBL; AK222777; BAD96497.1; -; mRNA.
EMBL; AF478696; AAL77436.1; -; Genomic_DNA.
EMBL; BC051332; AAH51332.1; -; mRNA.
EMBL; V00595; CAA23842.1; -; mRNA.
EMBL; AY344794; AAR08143.1; -; mRNA.
CCDS; CCDS31476.1; -.
PIR; A29351; TBHU.
RefSeq; NP_000497.1; NM_000506.4.
RefSeq; NP_001298186.1; NM_001311257.1.
UniGene; Hs.655207; -.
PDB; 1A2C; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 1A3B; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 1A3E; X-ray; 1.85 A; H=364-622, L=328-363.
PDB; 1A46; X-ray; 2.12 A; H=364-622, L=328-363.
PDB; 1A4W; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 1A5G; X-ray; 2.06 A; H=364-622, L=328-363.
PDB; 1A61; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 1ABI; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 1ABJ; X-ray; 2.40 A; H=364-622, L=328-363.
PDB; 1AD8; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 1AE8; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 1AFE; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 1AHT; X-ray; 1.60 A; H=364-622, L=328-363.
PDB; 1AI8; X-ray; 1.85 A; H=364-622, L=328-363.
PDB; 1AIX; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 1AWF; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 1AWH; X-ray; 3.00 A; A/C=328-363, B/D=364-622.
PDB; 1AY6; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 1B5G; X-ray; 2.07 A; H=364-622, L=328-363.
PDB; 1B7X; X-ray; 2.10 A; A=328-363, B=364-622.
PDB; 1BA8; X-ray; 1.80 A; A=328-363, B=364-622.
PDB; 1BB0; X-ray; 2.10 A; A=328-363, B=364-622.
PDB; 1BCU; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 1BHX; X-ray; 2.30 A; A=331-349, B=364-510, F=518-622.
PDB; 1BMM; X-ray; 2.60 A; H=364-622, L=328-363.
PDB; 1BMN; X-ray; 2.80 A; H=364-622, L=328-363.
PDB; 1BTH; X-ray; 2.30 A; H/K=364-622, J/L=328-363.
PDB; 1C1U; X-ray; 1.75 A; H=364-616, L=328-363.
PDB; 1C1V; X-ray; 1.98 A; H=364-616, L=328-363.
PDB; 1C1W; X-ray; 1.90 A; H=364-616, L=328-363.
PDB; 1C4U; X-ray; 2.10 A; 1=328-363, 2=364-622.
PDB; 1C4V; X-ray; 2.10 A; 1=328-363, 2=364-622.
PDB; 1C4Y; X-ray; 2.70 A; 1=328-363, 2=364-622.
PDB; 1C5L; X-ray; 1.47 A; H=364-622, L=328-363.
PDB; 1C5N; X-ray; 1.50 A; H=364-622, L=328-363.
PDB; 1C5O; X-ray; 1.90 A; H=364-622, L=328-363.
PDB; 1CA8; X-ray; 2.10 A; A=328-363, B=364-622.
PDB; 1D3D; X-ray; 2.04 A; A=333-360, B=364-620.
PDB; 1D3P; X-ray; 2.10 A; A=328-363, B=364-622.
PDB; 1D3Q; X-ray; 2.90 A; A=328-363, B=364-622.
PDB; 1D3T; X-ray; 3.00 A; A=328-363, B=364-622.
PDB; 1D4P; X-ray; 2.07 A; A=328-363, B=364-622.
PDB; 1D6W; X-ray; 2.00 A; A=334-620.
PDB; 1D9I; X-ray; 2.30 A; A=334-621.
PDB; 1DE7; X-ray; 2.00 A; H/K=364-619, J/L=328-360.
PDB; 1DIT; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 1DM4; X-ray; 2.50 A; A=328-362, B=363-622.
PDB; 1DOJ; X-ray; 1.70 A; A=328-622.
PDB; 1DWB; X-ray; 3.16 A; H=364-622, L=328-363.
PDB; 1DWC; X-ray; 3.00 A; H=364-622, L=328-363.
PDB; 1DWD; X-ray; 3.00 A; H=364-622, L=328-363.
PDB; 1DWE; X-ray; 3.00 A; H=364-622, L=328-363.
PDB; 1DX5; X-ray; 2.30 A; A/B/C/D=328-363, M/N/O/P=364-622.
PDB; 1E0F; X-ray; 3.10 A; A/B/C=328-363, D/E/F=364-622.
PDB; 1EB1; X-ray; 1.80 A; H=364-620, L=334-360.
PDB; 1EOJ; X-ray; 2.10 A; A=332-620.
PDB; 1EOL; X-ray; 2.10 A; A=332-620.
PDB; 1FPC; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 1FPH; X-ray; 2.50 A; H=364-622, L=328-363.
PDB; 1G30; X-ray; 2.00 A; A=328-363, B=364-622.
PDB; 1G32; X-ray; 1.90 A; A=328-363, B=364-622.
PDB; 1G37; X-ray; 2.00 A; A=334-620.
PDB; 1GHV; X-ray; 1.85 A; H=364-620, L=328-363.
PDB; 1GHW; X-ray; 1.75 A; H=364-620, L=328-363.
PDB; 1GHX; X-ray; 1.65 A; H=364-620, L=328-363.
PDB; 1GHY; X-ray; 1.85 A; H=364-620, L=328-363.
PDB; 1GJ4; X-ray; 1.81 A; H=364-621, L=328-363.
PDB; 1GJ5; X-ray; 1.73 A; H=364-621, L=328-363.
PDB; 1H8D; X-ray; 1.40 A; H=364-621, L=333-360.
PDB; 1H8I; X-ray; 1.75 A; H=364-622, L=334-360.
PDB; 1HAG; X-ray; 2.00 A; E=328-622.
PDB; 1HAH; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 1HAI; X-ray; 2.40 A; H=364-622, L=328-363.
PDB; 1HAO; X-ray; 2.80 A; H=364-622, L=328-363.
PDB; 1HAP; X-ray; 2.80 A; H=364-622, L=328-360.
PDB; 1HBT; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 1HDT; X-ray; 2.60 A; H=364-622, L=331-363.
PDB; 1HGT; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 1HLT; X-ray; 3.00 A; H/K=364-622, J/L=334-349.
PDB; 1HUT; X-ray; 2.90 A; H=364-622, L=328-363.
PDB; 1HXE; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 1HXF; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 1IHS; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 1IHT; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 1JMO; X-ray; 2.20 A; H=363-622, L=315-362.
PDB; 1JOU; X-ray; 1.80 A; A/C/E=315-363, B/D/F=364-622.
PDB; 1JWT; X-ray; 2.50 A; A=328-622.
PDB; 1K21; X-ray; 1.86 A; H=364-622, L=328-363.
PDB; 1K22; X-ray; 1.93 A; H=364-622, L=328-363.
PDB; 1KTS; X-ray; 2.40 A; A=328-363, B=364-622.
PDB; 1KTT; X-ray; 2.10 A; A=328-363, B=364-622.
PDB; 1LHC; X-ray; 1.95 A; H=364-622, L=328-363.
PDB; 1LHD; X-ray; 2.35 A; H=364-622, L=328-363.
PDB; 1LHE; X-ray; 2.25 A; H=364-622, L=328-363.
PDB; 1LHF; X-ray; 2.40 A; H=364-622, L=328-363.
PDB; 1LHG; X-ray; 2.25 A; H=364-622, L=328-363.
PDB; 1MH0; X-ray; 2.80 A; A/B=334-620.
PDB; 1MU6; X-ray; 1.99 A; A=328-363, B=364-622.
PDB; 1MU8; X-ray; 2.00 A; A=328-363, B=364-622.
PDB; 1MUE; X-ray; 2.00 A; A=328-363, B=364-622.
PDB; 1NM6; X-ray; 1.80 A; A=335-621.
PDB; 1NO9; X-ray; 1.90 A; H=364-622, L=328-363.
PDB; 1NRN; X-ray; 3.10 A; H=364-622, L=328-363.
PDB; 1NRO; X-ray; 3.10 A; H=364-622, L=328-363.
PDB; 1NRP; X-ray; 3.00 A; H=364-622, L=328-363.
PDB; 1NRQ; X-ray; 3.50 A; H=364-622, L=328-363.
PDB; 1NRR; X-ray; 2.40 A; H=364-622, L=328-363.
PDB; 1NRS; X-ray; 2.40 A; H=364-622, L=328-349.
PDB; 1NT1; X-ray; 2.00 A; A=335-621.
PDB; 1NU7; X-ray; 2.20 A; A/E=332-359, B/F=364-622.
PDB; 1NU9; X-ray; 2.20 A; A/D=332-622.
PDB; 1NY2; X-ray; 2.30 A; 1=328-363, 2=364-622.
PDB; 1NZQ; X-ray; 2.18 A; H=364-620, L=328-361.
PDB; 1O0D; X-ray; 2.44 A; H=364-622, L=328-363.
PDB; 1O2G; X-ray; 1.58 A; H=364-622, L=328-363.
PDB; 1O5G; X-ray; 1.75 A; H=364-622, L=328-363.
PDB; 1OOK; X-ray; 2.30 A; A=328-363, B=364-622.
PDB; 1OYT; X-ray; 1.67 A; H=364-622, L=328-363.
PDB; 1P8V; X-ray; 2.60 A; B=333-361, C=364-621.
PDB; 1PPB; X-ray; 1.92 A; H=364-622, L=328-363.
PDB; 1QBV; X-ray; 1.80 A; H=364-622, L=328-359.
PDB; 1QHR; X-ray; 2.20 A; A=328-363, B=364-622.
PDB; 1QJ1; X-ray; 2.00 A; A=328-363, B=364-622.
PDB; 1QJ6; X-ray; 2.20 A; A=328-363, B=364-622.
PDB; 1QJ7; X-ray; 2.20 A; A=328-363, B=364-622.
PDB; 1QUR; X-ray; 2.00 A; H=364-620, L=334-360.
PDB; 1RD3; X-ray; 2.50 A; A/C=328-363, B/D=364-622.
PDB; 1RIW; X-ray; 2.04 A; A=328-363, B=364-510, C=518-622.
PDB; 1SB1; X-ray; 1.90 A; H=364-621, L=333-361.
PDB; 1SFQ; X-ray; 1.91 A; A/D=328-363, B/E=364-622.
PDB; 1SG8; X-ray; 2.30 A; A/D=328-363, B/E=364-622.
PDB; 1SGI; X-ray; 2.30 A; A/D=328-363, B/E=364-622.
PDB; 1SHH; X-ray; 1.55 A; A/D=328-363, B/E=364-622.
PDB; 1SL3; X-ray; 1.81 A; A=335-621.
PDB; 1SR5; X-ray; 3.10 A; B=328-363, C=364-622.
PDB; 1T4U; X-ray; 2.00 A; H=364-622, L=334-359.
PDB; 1T4V; X-ray; 2.00 A; H=364-622, L=334-359.
PDB; 1TA2; X-ray; 2.30 A; A=335-621.
PDB; 1TA6; X-ray; 1.90 A; A=335-621.
PDB; 1TB6; X-ray; 2.50 A; H=364-622, L=315-363.
PDB; 1TBZ; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 1THP; X-ray; 2.10 A; A=328-362, B=364-620.
PDB; 1THR; X-ray; 2.30 A; H=364-622, L=328-349.
PDB; 1THS; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 1TMB; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 1TMT; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 1TMU; X-ray; 2.50 A; H=364-620, L=333-349.
PDB; 1TOM; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 1TQ0; X-ray; 2.80 A; A/C=333-363, B/D=364-620.
PDB; 1TQ7; X-ray; 2.40 A; A=320-363, B=364-620.
PDB; 1TWX; X-ray; 2.40 A; A=334-349, B=364-622.
PDB; 1UMA; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 1UVS; X-ray; 2.80 A; H=364-622, L=328-363.
PDB; 1VR1; X-ray; 1.90 A; H=364-620, L=334-360.
PDB; 1VZQ; X-ray; 1.54 A; H=364-620, L=334-360.
PDB; 1W7G; X-ray; 1.65 A; H=364-622, L=328-363.
PDB; 1WAY; X-ray; 2.02 A; A=328-363, B=364-622.
PDB; 1WBG; X-ray; 2.20 A; A=328-363, B=364-622.
PDB; 1XM1; X-ray; 2.30 A; A=328-622.
PDB; 1XMN; X-ray; 1.85 A; A/C/E/G=328-363, B/D/F/H=364-622.
PDB; 1YPE; X-ray; 1.81 A; H=364-620, L=334-360.
PDB; 1YPG; X-ray; 1.80 A; H=364-620, L=334-360.
PDB; 1YPJ; X-ray; 1.78 A; H=364-620, L=334-360.
PDB; 1YPK; X-ray; 1.78 A; H=364-620, L=334-360.
PDB; 1YPL; X-ray; 1.85 A; H=364-620, L=334-360.
PDB; 1YPM; X-ray; 1.85 A; H=364-620, L=334-360.
PDB; 1Z71; X-ray; 1.80 A; A=335-621.
PDB; 1Z8I; X-ray; 2.00 A; A=324-361, B=364-622.
PDB; 1Z8J; X-ray; 2.00 A; A=322-361, B=364-622.
PDB; 1ZGI; X-ray; 2.20 A; A=335-621.
PDB; 1ZGV; X-ray; 2.20 A; A=335-621.
PDB; 1ZRB; X-ray; 1.90 A; A=335-621.
PDB; 2A0Q; X-ray; 1.90 A; A/C=334-349, B/D=364-620.
PDB; 2A2X; X-ray; 2.44 A; H=364-622, L=330-363.
PDB; 2A45; X-ray; 3.65 A; A/D=328-363, B/E=364-622.
PDB; 2AFQ; X-ray; 1.93 A; A/C=332-360, B/D=364-622.
PDB; 2ANK; X-ray; 2.46 A; H=364-622, L=330-363.
PDB; 2ANM; X-ray; 2.40 A; H=364-620, L=328-363.
PDB; 2B5T; X-ray; 2.10 A; A/C=315-363, B/D=364-622.
PDB; 2BDY; X-ray; 1.61 A; A=334-622.
PDB; 2BVR; X-ray; 1.25 A; H=364-622, L=328-363.
PDB; 2BVS; X-ray; 1.40 A; H=364-622, L=328-363.
PDB; 2BVX; X-ray; 3.20 A; H=364-622, L=328-363.
PDB; 2BXT; X-ray; 1.83 A; H=364-622, L=328-363.
PDB; 2BXU; X-ray; 2.80 A; H=364-622, L=328-363.
PDB; 2C8W; X-ray; 1.96 A; A=328-363, B=364-622.
PDB; 2C8X; X-ray; 2.17 A; A=328-363, B=364-622.
PDB; 2C8Y; X-ray; 2.20 A; A=328-363, B=364-622.
PDB; 2C8Z; X-ray; 2.14 A; A=328-363, B=364-622.
PDB; 2C90; X-ray; 2.25 A; A=328-363, B=364-622.
PDB; 2C93; X-ray; 2.20 A; A=328-363, B=364-622.
PDB; 2CF8; X-ray; 1.30 A; H=364-620, L=334-361.
PDB; 2CF9; X-ray; 1.79 A; H=364-620, L=334-361.
PDB; 2CN0; X-ray; 1.30 A; H=364-620, L=334-361.
PDB; 2FEQ; X-ray; 2.44 A; H=364-622, L=328-363.
PDB; 2FES; X-ray; 2.42 A; H=364-622, L=328-363.
PDB; 2GDE; X-ray; 2.00 A; H=364-622, L=328-363.
PDB; 2GP9; X-ray; 1.87 A; A=328-362, B=364-620.
PDB; 2H9T; X-ray; 2.40 A; H=364-622, L=328-363.
PDB; 2HGT; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 2HNT; X-ray; 2.50 A; C=364-433, E=437-517, F=518-622, L=328-363.
PDB; 2HPP; X-ray; 3.30 A; H=364-622, L=328-363.
PDB; 2HPQ; X-ray; 3.30 A; H=364-622, L=328-363, P=213-291.
PDB; 2HWL; X-ray; 2.40 A; A/C=328-363, B/D=364-622.
PDB; 2JH0; X-ray; 1.70 A; C=328-361, D=364-622.
PDB; 2JH5; X-ray; 2.50 A; C=328-363, D=364-622.
PDB; 2JH6; X-ray; 2.21 A; C=328-361, D=364-622.
PDB; 2OD3; X-ray; 1.75 A; A=328-363, B=364-622.
PDB; 2PGB; X-ray; 1.54 A; A=328-363, B=364-622.
PDB; 2PGQ; X-ray; 1.80 A; A=319-363, B=364-622.
PDB; 2PKS; X-ray; 2.50 A; A=334-360, B=364-510, C=518-619.
PDB; 2PW8; X-ray; 1.84 A; H=364-621, L=334-360.
PDB; 2R2M; X-ray; 2.10 A; A=334-359, B=364-622.
PDB; 2THF; X-ray; 2.10 A; A=328-363, B=364-622.
PDB; 2UUF; X-ray; 1.26 A; A=328-363, B=364-622.
PDB; 2UUJ; X-ray; 1.32 A; A=328-363, B=364-622.
PDB; 2UUK; X-ray; 1.39 A; A=328-363, B=364-622.
PDB; 2V3H; X-ray; 1.79 A; H=364-620, L=334-361.
PDB; 2V3O; X-ray; 1.79 A; H=364-620, L=334-361.
PDB; 2ZC9; X-ray; 1.58 A; H=364-622, L=328-363.
PDB; 2ZDA; X-ray; 1.73 A; H=364-622, L=328-363.
PDB; 2ZDV; X-ray; 1.72 A; H=364-622, L=328-363.
PDB; 2ZF0; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 2ZFF; X-ray; 1.47 A; H=364-622, L=328-363.
PDB; 2ZFP; X-ray; 2.25 A; H=364-622, L=328-363.
PDB; 2ZFQ; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 2ZFR; X-ray; 1.85 A; H=364-622, L=328-363.
PDB; 2ZG0; X-ray; 1.75 A; H=364-622, L=328-363.
PDB; 2ZGB; X-ray; 1.60 A; H=364-622, L=328-363.
PDB; 2ZGX; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 2ZHE; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 2ZHF; X-ray; 1.98 A; H=364-622, L=328-363.
PDB; 2ZHQ; X-ray; 1.96 A; H=364-622, L=328-363.
PDB; 2ZHW; X-ray; 2.02 A; H=364-622, L=328-363.
PDB; 2ZI2; X-ray; 1.65 A; H=364-622, L=328-363.
PDB; 2ZIQ; X-ray; 1.65 A; H=364-622, L=328-363.
PDB; 2ZNK; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 2ZO3; X-ray; 1.70 A; H=364-622, L=328-363.
PDB; 3B23; X-ray; 2.40 A; A=328-363, B=364-622.
PDB; 3B9F; X-ray; 1.60 A; H=364-622, L=315-363.
PDB; 3BEF; X-ray; 2.20 A; A/D=320-363, B/E=364-622.
PDB; 3BEI; X-ray; 1.55 A; A=320-363, B=364-622.
PDB; 3BF6; X-ray; 2.50 A; H=364-622, L=328-363.
PDB; 3BIU; X-ray; 2.30 A; H=364-620, L=333-361.
PDB; 3BIV; X-ray; 1.80 A; H=364-620, L=333-361.
PDB; 3BV9; X-ray; 1.80 A; A=333-363, B=364-622.
PDB; 3C1K; X-ray; 1.84 A; A=335-621.
PDB; 3C27; X-ray; 2.18 A; A=334-359, B=364-622.
PDB; 3D49; X-ray; 1.50 A; H=364-622, L=328-363.
PDB; 3DA9; X-ray; 1.80 A; A=328-363, B=364-622.
PDB; 3DD2; X-ray; 1.90 A; H=364-621, L=332-361.
PDB; 3DHK; X-ray; 1.73 A; H=364-622, L=328-363.
PDB; 3DT0; X-ray; 2.40 A; H=364-622, L=328-363.
PDB; 3DUX; X-ray; 1.60 A; H=364-622, L=328-363.
PDB; 3E6P; X-ray; 2.10 A; H=364-622, L=206-363.
PDB; 3EE0; X-ray; 2.75 A; A=328-363, B=364-622.
PDB; 3EGK; X-ray; 2.20 A; H=364-622, L=328-363.
PDB; 3EQ0; X-ray; 1.53 A; H=364-622, L=328-363.
PDB; 3F68; X-ray; 1.75 A; H=364-622, L=328-363.
PDB; 3GIC; X-ray; 1.55 A; A=328-363, B=364-622.
PDB; 3GIS; X-ray; 2.40 A; A/C/E=315-363, B/D/F=364-622.
PDB; 3HAT; X-ray; 2.50 A; H=364-622, L=328-363.
PDB; 3HKJ; X-ray; 2.60 A; A/D=333-363, B/E=364-622.
PDB; 3HTC; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 3JZ1; X-ray; 1.60 A; A=328-363, B=364-622.
PDB; 3JZ2; X-ray; 2.40 A; A=328-363, B=364-622.
PDB; 3K65; X-ray; 1.85 A; A=199-314, B=315-622.
PDB; 3LDX; X-ray; 2.25 A; H=364-622, L=328-363.
PDB; 3LU9; X-ray; 1.80 A; A/D=318-363, B/E=364-622.
PDB; 3NXP; X-ray; 2.20 A; A=199-622.
PDB; 3P17; X-ray; 1.43 A; H=364-622, L=328-363.
PDB; 3P6Z; X-ray; 1.70 A; A/G=328-363, B/H=364-622.
PDB; 3P70; X-ray; 2.55 A; A/C/E/G=328-363, B/D/F/H=364-622.
PDB; 3PMH; X-ray; 3.20 A; A=328-363, B=364-622.
PDB; 3PO1; X-ray; 1.65 A; A=334-360, B=364-510, C=518-619.
PDB; 3QDZ; X-ray; 2.80 A; A/C=333-363, B/D=364-622.
PDB; 3QGN; X-ray; 2.10 A; A=333-363, B=364-622.
PDB; 3QLP; X-ray; 2.14 A; H=364-622, L=328-363.
PDB; 3QTO; X-ray; 1.52 A; H=364-622, L=328-363.
PDB; 3QTV; X-ray; 1.63 A; H=364-622, L=328-363.
PDB; 3QWC; X-ray; 1.75 A; H=364-622, L=328-363.
PDB; 3QX5; X-ray; 1.35 A; H=364-622, L=328-363.
PDB; 3R3G; X-ray; 1.75 A; A=333-363, B=364-622.
PDB; 3RLW; X-ray; 1.69 A; H=364-622, L=328-363.
PDB; 3RLY; X-ray; 1.51 A; H=364-622, L=328-363.
PDB; 3RM0; X-ray; 1.34 A; H=364-622, L=328-363.
PDB; 3RM2; X-ray; 1.23 A; H=364-622, L=328-363.
PDB; 3RML; X-ray; 1.53 A; H=364-622, L=328-363.
PDB; 3RMM; X-ray; 1.58 A; H=364-622, L=328-363.
PDB; 3RMN; X-ray; 1.78 A; H=364-622, L=328-363.
PDB; 3RMO; X-ray; 1.40 A; H=364-622, L=328-363.
PDB; 3S7H; X-ray; 1.90 A; A=329-363, B=364-622.
PDB; 3S7K; X-ray; 1.90 A; A/C=329-363, B/D=364-622.
PDB; 3SHA; X-ray; 1.52 A; H=364-622, L=328-363.
PDB; 3SHC; X-ray; 1.90 A; H=364-622, L=328-363.
PDB; 3SI3; X-ray; 1.55 A; H=364-622, L=328-363.
PDB; 3SI4; X-ray; 1.27 A; H=364-622, L=328-363.
PDB; 3SQE; X-ray; 1.90 A; E=333-622.
PDB; 3SQH; X-ray; 2.20 A; E=333-622.
PDB; 3SV2; X-ray; 1.30 A; H=364-622, L=328-363.
PDB; 3T5F; X-ray; 1.45 A; H=364-622, L=328-363.
PDB; 3TU7; X-ray; 2.49 A; H=364-622, L=328-363.
PDB; 3U69; X-ray; 1.55 A; H=364-622, L=334-363.
PDB; 3U8O; X-ray; 1.28 A; H=364-622, L=334-363.
PDB; 3U8R; X-ray; 1.47 A; H=364-622, L=334-363.
PDB; 3U8T; X-ray; 1.86 A; H=364-620, L=334-360.
PDB; 3U98; X-ray; 1.45 A; H=364-622, L=328-363.
PDB; 3U9A; X-ray; 1.58 A; H=364-622, L=328-363.
PDB; 3UTU; X-ray; 1.55 A; H=364-622, L=328-363.
PDB; 3UWJ; X-ray; 1.50 A; H=364-622, L=328-363.
PDB; 3VXE; X-ray; 1.25 A; H=364-622, L=328-363.
PDB; 3VXF; Other; 1.60 A; H=364-622, L=328-363.
PDB; 4AX9; X-ray; 1.90 A; H=364-620, L=334-361.
PDB; 4AYV; X-ray; 2.80 A; A=332-361, B=364-620.
PDB; 4AYY; X-ray; 2.60 A; A=332-361, B=364-620.
PDB; 4AZ2; X-ray; 2.60 A; A=332-361, B=364-620.
PDB; 4BAH; X-ray; 1.94 A; A=328-363, B=364-622.
PDB; 4BAK; X-ray; 1.94 A; A=328-363, B=364-622.
PDB; 4BAM; X-ray; 1.88 A; A=328-363, B=364-622.
PDB; 4BAN; X-ray; 1.87 A; A=328-363, B=364-622.
PDB; 4BAO; X-ray; 1.87 A; A=328-363, B=364-622.
PDB; 4BAQ; X-ray; 1.89 A; A=328-363, B=364-622.
PDB; 4BOH; X-ray; 2.60 A; A/H=364-622, B/L=328-363.
PDB; 4CH2; X-ray; 1.60 A; A/C=328-363, B/D=364-622.
PDB; 4CH8; X-ray; 1.75 A; A/C/E/G=328-363, B/D/F/H=364-622.
PDB; 4DIH; X-ray; 1.80 A; H=364-622, L=328-363.
PDB; 4DII; X-ray; 2.05 A; H=364-622, L=328-363.
PDB; 4DT7; X-ray; 1.90 A; A/C=332-363, B/D=364-622.
PDB; 4DY7; X-ray; 2.80 A; A/D=315-363, B/E=364-622.
PDB; 4E05; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 4E06; X-ray; 3.20 A; H=364-622, L=328-363.
PDB; 4E7R; X-ray; 2.25 A; G/H=364-622, L/M=328-363.
PDB; 4H6S; X-ray; 2.19 A; A=333-363, B=364-622.
PDB; 4H6T; X-ray; 2.40 A; A=317-622.
PDB; 4HFP; X-ray; 2.40 A; A/C=333-363, B/D=364-622.
PDB; 4HTC; X-ray; 2.30 A; H=364-622, L=328-363.
PDB; 4HZH; X-ray; 3.30 A; A/B=90-622.
PDB; 4I7Y; X-ray; 2.40 A; H=364-622, L=328-363.
PDB; 4LOY; X-ray; 1.77 A; H=364-620, L=334-360.
PDB; 4LXB; X-ray; 1.61 A; H=364-622, L=328-363.
PDB; 4LZ1; X-ray; 1.65 A; H=364-622, L=328-363.
PDB; 4LZ4; X-ray; 2.56 A; A/C=328-363, B/D=364-622.
PDB; 4MLF; X-ray; 2.20 A; A=331-363, B=364-622.
PDB; 4N3L; X-ray; 1.94 A; H=364-622, L=328-363.
PDB; 4NZE; X-ray; 1.98 A; H=364-622, L=328-363.
PDB; 4NZQ; X-ray; 2.81 A; A=44-622.
PDB; 4O03; X-ray; 3.38 A; A=44-622.
PDB; 4RKJ; X-ray; 1.70 A; A=330-363, B=364-622.
PDB; 4RKO; X-ray; 1.84 A; A=322-363, B=364-622.
PDB; 4RN6; X-ray; 3.00 A; A/B=333-622.
PDB; 4THN; X-ray; 2.50 A; H=364-622, L=328-363.
PDB; 4UD9; X-ray; 1.12 A; H=364-622, L=333-360.
PDB; 4UDW; X-ray; 1.16 A; H=364-621, L=333-360.
PDB; 4UE7; X-ray; 1.13 A; H=364-621, L=333-360.
PDB; 4UEH; X-ray; 1.16 A; H=364-621, L=333-361.
PDB; 4UFD; X-ray; 1.43 A; H=364-621, L=333-360.
PDB; 4UFE; X-ray; 1.59 A; H=364-621, L=333-361.
PDB; 4UFF; X-ray; 1.55 A; H=364-621, L=333-361.
PDB; 4UFG; X-ray; 1.65 A; H=364-621, L=333-361.
PDB; 4YES; X-ray; 1.50 A; A=328-363, B=364-622.
PDB; 5A2M; X-ray; 1.40 A; H=364-621, L=333-361.
PDB; 5AF9; X-ray; 1.18 A; H=364-621, L=333-361.
PDB; 5AFY; X-ray; 1.12 A; H=364-621, L=333-361.
PDB; 5AFZ; X-ray; 1.53 A; H=364-621, L=333-361.
PDB; 5AHG; X-ray; 1.24 A; H=364-621, L=333-361.
PDB; 5CMX; X-ray; 2.98 A; H=364-622, L=328-363.
PDB; 5DO4; X-ray; 1.86 A; H=364-621, L=328-363.
PDB; 5E8E; X-ray; 1.90 A; H=364-622, L=328-363.
PDB; 5EDK; X-ray; 3.21 A; A=44-622.
PDB; 5EDM; X-ray; 2.20 A; A=44-622.
PDB; 5EW1; X-ray; 2.95 A; H=364-622, L=328-363.
PDB; 5EW2; X-ray; 3.59 A; H=364-622, L=328-363.
PDB; 5GDS; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 5GIM; X-ray; 2.09 A; A=328-363.
PDB; 5JDU; X-ray; 1.70 A; A/C=331-363, B/D=364-622.
PDB; 5JFD; X-ray; 1.46 A; H=364-622, L=328-363.
PDB; 5JZY; X-ray; 1.27 A; H=364-622, L=328-363.
PDB; 5L6N; X-ray; 1.63 A; H=364-622, L=328-363.
PDB; 5LUW; X-ray; 1.69 A; H=364-622, L=328-363.
PDB; 5LUY; X-ray; 2.24 A; H=364-622, L=328-363.
PDB; 5NHU; X-ray; 1.45 A; A/C/H=364-622, B/D/L=328-363.
PDB; 5TO3; X-ray; 2.34 A; A=318-363, B=364-621.
PDB; 7KME; X-ray; 2.10 A; H=364-622, L=328-363.
PDB; 8KME; X-ray; 2.10 A; 1=328-359, 2=364-620.
PDBsum; 1A2C; -.
PDBsum; 1A3B; -.
PDBsum; 1A3E; -.
PDBsum; 1A46; -.
PDBsum; 1A4W; -.
PDBsum; 1A5G; -.
PDBsum; 1A61; -.
PDBsum; 1ABI; -.
PDBsum; 1ABJ; -.
PDBsum; 1AD8; -.
PDBsum; 1AE8; -.
PDBsum; 1AFE; -.
PDBsum; 1AHT; -.
PDBsum; 1AI8; -.
PDBsum; 1AIX; -.
PDBsum; 1AWF; -.
PDBsum; 1AWH; -.
PDBsum; 1AY6; -.
PDBsum; 1B5G; -.
PDBsum; 1B7X; -.
PDBsum; 1BA8; -.
PDBsum; 1BB0; -.
PDBsum; 1BCU; -.
PDBsum; 1BHX; -.
PDBsum; 1BMM; -.
PDBsum; 1BMN; -.
PDBsum; 1BTH; -.
PDBsum; 1C1U; -.
PDBsum; 1C1V; -.
PDBsum; 1C1W; -.
PDBsum; 1C4U; -.
PDBsum; 1C4V; -.
PDBsum; 1C4Y; -.
PDBsum; 1C5L; -.
PDBsum; 1C5N; -.
PDBsum; 1C5O; -.
PDBsum; 1CA8; -.
PDBsum; 1D3D; -.
PDBsum; 1D3P; -.
PDBsum; 1D3Q; -.
PDBsum; 1D3T; -.
PDBsum; 1D4P; -.
PDBsum; 1D6W; -.
PDBsum; 1D9I; -.
PDBsum; 1DE7; -.
PDBsum; 1DIT; -.
PDBsum; 1DM4; -.
PDBsum; 1DOJ; -.
PDBsum; 1DWB; -.
PDBsum; 1DWC; -.
PDBsum; 1DWD; -.
PDBsum; 1DWE; -.
PDBsum; 1DX5; -.
PDBsum; 1E0F; -.
PDBsum; 1EB1; -.
PDBsum; 1EOJ; -.
PDBsum; 1EOL; -.
PDBsum; 1FPC; -.
PDBsum; 1FPH; -.
PDBsum; 1G30; -.
PDBsum; 1G32; -.
PDBsum; 1G37; -.
PDBsum; 1GHV; -.
PDBsum; 1GHW; -.
PDBsum; 1GHX; -.
PDBsum; 1GHY; -.
PDBsum; 1GJ4; -.
PDBsum; 1GJ5; -.
PDBsum; 1H8D; -.
PDBsum; 1H8I; -.
PDBsum; 1HAG; -.
PDBsum; 1HAH; -.
PDBsum; 1HAI; -.
PDBsum; 1HAO; -.
PDBsum; 1HAP; -.
PDBsum; 1HBT; -.
PDBsum; 1HDT; -.
PDBsum; 1HGT; -.
PDBsum; 1HLT; -.
PDBsum; 1HUT; -.
PDBsum; 1HXE; -.
PDBsum; 1HXF; -.
PDBsum; 1IHS; -.
PDBsum; 1IHT; -.
PDBsum; 1JMO; -.
PDBsum; 1JOU; -.
PDBsum; 1JWT; -.
PDBsum; 1K21; -.
PDBsum; 1K22; -.
PDBsum; 1KTS; -.
PDBsum; 1KTT; -.
PDBsum; 1LHC; -.
PDBsum; 1LHD; -.
PDBsum; 1LHE; -.
PDBsum; 1LHF; -.
PDBsum; 1LHG; -.
PDBsum; 1MH0; -.
PDBsum; 1MU6; -.
PDBsum; 1MU8; -.
PDBsum; 1MUE; -.
PDBsum; 1NM6; -.
PDBsum; 1NO9; -.
PDBsum; 1NRN; -.
PDBsum; 1NRO; -.
PDBsum; 1NRP; -.
PDBsum; 1NRQ; -.
PDBsum; 1NRR; -.
PDBsum; 1NRS; -.
PDBsum; 1NT1; -.
PDBsum; 1NU7; -.
PDBsum; 1NU9; -.
PDBsum; 1NY2; -.
PDBsum; 1NZQ; -.
PDBsum; 1O0D; -.
PDBsum; 1O2G; -.
PDBsum; 1O5G; -.
PDBsum; 1OOK; -.
PDBsum; 1OYT; -.
PDBsum; 1P8V; -.
PDBsum; 1PPB; -.
PDBsum; 1QBV; -.
PDBsum; 1QHR; -.
PDBsum; 1QJ1; -.
PDBsum; 1QJ6; -.
PDBsum; 1QJ7; -.
PDBsum; 1QUR; -.
PDBsum; 1RD3; -.
PDBsum; 1RIW; -.
PDBsum; 1SB1; -.
PDBsum; 1SFQ; -.
PDBsum; 1SG8; -.
PDBsum; 1SGI; -.
PDBsum; 1SHH; -.
PDBsum; 1SL3; -.
PDBsum; 1SR5; -.
PDBsum; 1T4U; -.
PDBsum; 1T4V; -.
PDBsum; 1TA2; -.
PDBsum; 1TA6; -.
PDBsum; 1TB6; -.
PDBsum; 1TBZ; -.
PDBsum; 1THP; -.
PDBsum; 1THR; -.
PDBsum; 1THS; -.
PDBsum; 1TMB; -.
PDBsum; 1TMT; -.
PDBsum; 1TMU; -.
PDBsum; 1TOM; -.
PDBsum; 1TQ0; -.
PDBsum; 1TQ7; -.
PDBsum; 1TWX; -.
PDBsum; 1UMA; -.
PDBsum; 1UVS; -.
PDBsum; 1VR1; -.
PDBsum; 1VZQ; -.
PDBsum; 1W7G; -.
PDBsum; 1WAY; -.
PDBsum; 1WBG; -.
PDBsum; 1XM1; -.
PDBsum; 1XMN; -.
PDBsum; 1YPE; -.
PDBsum; 1YPG; -.
PDBsum; 1YPJ; -.
PDBsum; 1YPK; -.
PDBsum; 1YPL; -.
PDBsum; 1YPM; -.
PDBsum; 1Z71; -.
PDBsum; 1Z8I; -.
PDBsum; 1Z8J; -.
PDBsum; 1ZGI; -.
PDBsum; 1ZGV; -.
PDBsum; 1ZRB; -.
PDBsum; 2A0Q; -.
PDBsum; 2A2X; -.
PDBsum; 2A45; -.
PDBsum; 2AFQ; -.
PDBsum; 2ANK; -.
PDBsum; 2ANM; -.
PDBsum; 2B5T; -.
PDBsum; 2BDY; -.
PDBsum; 2BVR; -.
PDBsum; 2BVS; -.
PDBsum; 2BVX; -.
PDBsum; 2BXT; -.
PDBsum; 2BXU; -.
PDBsum; 2C8W; -.
PDBsum; 2C8X; -.
PDBsum; 2C8Y; -.
PDBsum; 2C8Z; -.
PDBsum; 2C90; -.
PDBsum; 2C93; -.
PDBsum; 2CF8; -.
PDBsum; 2CF9; -.
PDBsum; 2CN0; -.
PDBsum; 2FEQ; -.
PDBsum; 2FES; -.
PDBsum; 2GDE; -.
PDBsum; 2GP9; -.
PDBsum; 2H9T; -.
PDBsum; 2HGT; -.
PDBsum; 2HNT; -.
PDBsum; 2HPP; -.
PDBsum; 2HPQ; -.
PDBsum; 2HWL; -.
PDBsum; 2JH0; -.
PDBsum; 2JH5; -.
PDBsum; 2JH6; -.
PDBsum; 2OD3; -.
PDBsum; 2PGB; -.
PDBsum; 2PGQ; -.
PDBsum; 2PKS; -.
PDBsum; 2PW8; -.
PDBsum; 2R2M; -.
PDBsum; 2THF; -.
PDBsum; 2UUF; -.
PDBsum; 2UUJ; -.
PDBsum; 2UUK; -.
PDBsum; 2V3H; -.
PDBsum; 2V3O; -.
PDBsum; 2ZC9; -.
PDBsum; 2ZDA; -.
PDBsum; 2ZDV; -.
PDBsum; 2ZF0; -.
PDBsum; 2ZFF; -.
PDBsum; 2ZFP; -.
PDBsum; 2ZFQ; -.
PDBsum; 2ZFR; -.
PDBsum; 2ZG0; -.
PDBsum; 2ZGB; -.
PDBsum; 2ZGX; -.
PDBsum; 2ZHE; -.
PDBsum; 2ZHF; -.
PDBsum; 2ZHQ; -.
PDBsum; 2ZHW; -.
PDBsum; 2ZI2; -.
PDBsum; 2ZIQ; -.
PDBsum; 2ZNK; -.
PDBsum; 2ZO3; -.
PDBsum; 3B23; -.
PDBsum; 3B9F; -.
PDBsum; 3BEF; -.
PDBsum; 3BEI; -.
PDBsum; 3BF6; -.
PDBsum; 3BIU; -.
PDBsum; 3BIV; -.
PDBsum; 3BV9; -.
PDBsum; 3C1K; -.
PDBsum; 3C27; -.
PDBsum; 3D49; -.
PDBsum; 3DA9; -.
PDBsum; 3DD2; -.
PDBsum; 3DHK; -.
PDBsum; 3DT0; -.
PDBsum; 3DUX; -.
PDBsum; 3E6P; -.
PDBsum; 3EE0; -.
PDBsum; 3EGK; -.
PDBsum; 3EQ0; -.
PDBsum; 3F68; -.
PDBsum; 3GIC; -.
PDBsum; 3GIS; -.
PDBsum; 3HAT; -.
PDBsum; 3HKJ; -.
PDBsum; 3HTC; -.
PDBsum; 3JZ1; -.
PDBsum; 3JZ2; -.
PDBsum; 3K65; -.
PDBsum; 3LDX; -.
PDBsum; 3LU9; -.
PDBsum; 3NXP; -.
PDBsum; 3P17; -.
PDBsum; 3P6Z; -.
PDBsum; 3P70; -.
PDBsum; 3PMH; -.
PDBsum; 3PO1; -.
PDBsum; 3QDZ; -.
PDBsum; 3QGN; -.
PDBsum; 3QLP; -.
PDBsum; 3QTO; -.
PDBsum; 3QTV; -.
PDBsum; 3QWC; -.
PDBsum; 3QX5; -.
PDBsum; 3R3G; -.
PDBsum; 3RLW; -.
PDBsum; 3RLY; -.
PDBsum; 3RM0; -.
PDBsum; 3RM2; -.
PDBsum; 3RML; -.
PDBsum; 3RMM; -.
PDBsum; 3RMN; -.
PDBsum; 3RMO; -.
PDBsum; 3S7H; -.
PDBsum; 3S7K; -.
PDBsum; 3SHA; -.
PDBsum; 3SHC; -.
PDBsum; 3SI3; -.
PDBsum; 3SI4; -.
PDBsum; 3SQE; -.
PDBsum; 3SQH; -.
PDBsum; 3SV2; -.
PDBsum; 3T5F; -.
PDBsum; 3TU7; -.
PDBsum; 3U69; -.
PDBsum; 3U8O; -.
PDBsum; 3U8R; -.
PDBsum; 3U8T; -.
PDBsum; 3U98; -.
PDBsum; 3U9A; -.
PDBsum; 3UTU; -.
PDBsum; 3UWJ; -.
PDBsum; 3VXE; -.
PDBsum; 3VXF; -.
PDBsum; 4AX9; -.
PDBsum; 4AYV; -.
PDBsum; 4AYY; -.
PDBsum; 4AZ2; -.
PDBsum; 4BAH; -.
PDBsum; 4BAK; -.
PDBsum; 4BAM; -.
PDBsum; 4BAN; -.
PDBsum; 4BAO; -.
PDBsum; 4BAQ; -.
PDBsum; 4BOH; -.
PDBsum; 4CH2; -.
PDBsum; 4CH8; -.
PDBsum; 4DIH; -.
PDBsum; 4DII; -.
PDBsum; 4DT7; -.
PDBsum; 4DY7; -.
PDBsum; 4E05; -.
PDBsum; 4E06; -.
PDBsum; 4E7R; -.
PDBsum; 4H6S; -.
PDBsum; 4H6T; -.
PDBsum; 4HFP; -.
PDBsum; 4HTC; -.
PDBsum; 4HZH; -.
PDBsum; 4I7Y; -.
PDBsum; 4LOY; -.
PDBsum; 4LXB; -.
PDBsum; 4LZ1; -.
PDBsum; 4LZ4; -.
PDBsum; 4MLF; -.
PDBsum; 4N3L; -.
PDBsum; 4NZE; -.
PDBsum; 4NZQ; -.
PDBsum; 4O03; -.
PDBsum; 4RKJ; -.
PDBsum; 4RKO; -.
PDBsum; 4RN6; -.
PDBsum; 4THN; -.
PDBsum; 4UD9; -.
PDBsum; 4UDW; -.
PDBsum; 4UE7; -.
PDBsum; 4UEH; -.
PDBsum; 4UFD; -.
PDBsum; 4UFE; -.
PDBsum; 4UFF; -.
PDBsum; 4UFG; -.
PDBsum; 4YES; -.
PDBsum; 5A2M; -.
PDBsum; 5AF9; -.
PDBsum; 5AFY; -.
PDBsum; 5AFZ; -.
PDBsum; 5AHG; -.
PDBsum; 5CMX; -.
PDBsum; 5DO4; -.
PDBsum; 5E8E; -.
PDBsum; 5EDK; -.
PDBsum; 5EDM; -.
PDBsum; 5EW1; -.
PDBsum; 5EW2; -.
PDBsum; 5GDS; -.
PDBsum; 5GIM; -.
PDBsum; 5JDU; -.
PDBsum; 5JFD; -.
PDBsum; 5JZY; -.
PDBsum; 5L6N; -.
PDBsum; 5LUW; -.
PDBsum; 5LUY; -.
PDBsum; 5NHU; -.
PDBsum; 5TO3; -.
PDBsum; 7KME; -.
PDBsum; 8KME; -.
ProteinModelPortal; P00734; -.
SMR; P00734; -.
BioGrid; 108447; 16.
DIP; DIP-6115N; -.
IntAct; P00734; 10.
MINT; MINT-147273; -.
STRING; 9606.ENSP00000308541; -.
BindingDB; P00734; -.
ChEMBL; CHEMBL204; -.
DrugBank; DB07211; (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE.
DrugBank; DB06850; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide.
DrugBank; DB07091; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide.
DrugBank; DB06845; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide.
DrugBank; DB07088; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide.
DrugBank; DB07131; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide.
DrugBank; DB07095; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide.
DrugBank; DB07897; 1-(HYDROXYMETHYLENEAMINO)-8-HYDROXY-OCTANE.
DrugBank; DB06878; 1-[(2R)-2-aminobutanoyl]-N-(3-chlorobenzyl)-L-prolinamide.
DrugBank; DB06947; 1-[(2R)-2-aminobutanoyl]-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DrugBank; DB06869; 1-[2-AMINO-2-CYCLOHEXYL-ACETYL]-PYRROLIDINE-3-CARBOXYLIC ACID 5-CHLORO-2-(2-ETHYLCARBAMOYL-ETHOXY)-BENZYLAMIDE.
DrugBank; DB06929; 1-butanoyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DrugBank; DB07400; 1-ETHOXYCARBONYL-D-PHE-PRO-2(4-AMINOBUTYL)HYDRAZINE.
DrugBank; DB04771; 1-GUANIDINO-4-(N-NITRO-BENZOYLAMINO-L-LEUCYL-L-PROLYLAMINO)BUTANE.
DrugBank; DB04772; 1-GUANIDINO-4-(N-PHENYLMETHANESULFONYL-L-LEUCYL-L-PROLYLAMINO)BUTANE.
DrugBank; DB06854; 2-(2-HYDROXY-BIPHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE.
DrugBank; DB02193; 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine.
DrugBank; DB07277; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE.
DrugBank; DB07278; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE.
DrugBank; DB07105; 2-[2-(4-CHLORO-PHENYLSULFANYL)-ACETYLAMINO]-3-(4-GUANIDINO-PHENYL)-PROPIONAMIDE.
DrugBank; DB07366; 2-[N'-(4-AMINO-BUTYL)-HYDRAZINOCARBONYL]-PYRROLIDINE-1-CARBOXYLIC ACID BENZYL ESTER.
DrugBank; DB08254; 2-NAPHTHALENESULFONIC ACID.
DrugBank; DB07718; 3-(4-HYDROXY-PHENYL)PYRUVIC ACID.
DrugBank; DB07639; 3-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID ETHYL ESTER.
DrugBank; DB07190; 3-cyclohexyl-D-alanyl-N-(3-chlorobenzyl)-L-prolinamide.
DrugBank; DB07508; 4-(5-BENZENESULFONYLAMINO-1-METHYL-1H-BENZOIMIDAZOL-2-YLMETHYL)-BENZAMIDINE.
DrugBank; DB07809; 4-({[4-(3-METHYLBENZOYL)PYRIDIN-2-YL]AMINO}METHYL)BENZENECARBOXIMIDAMIDE.
DrugBank; DB08061; 4-[3-(4-CHLOROPHENYL)-1H-PYRAZOL-5-YL]PIPERIDINE.
DrugBank; DB03136; 4-Iodobenzo[B]Thiophene-2-Carboxamidine.
DrugBank; DB07440; 4-TERT-BUTYLBENZENESULFONIC ACID.
DrugBank; DB07376; 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID).
DrugBank; DB06861; 6-(2-HYDROXY-CYCLOPENTYL)-7-OXO-HEPTANAMIDINE.
DrugBank; DB06866; 6-CARBAMIMIDOYL-2-[2-HYDROXY-5-(3-METHOXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID.
DrugBank; DB06865; 6-CARBAMIMIDOYL-2-[2-HYDROXY-6-(4-HYDROXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID.
DrugBank; DB03865; 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine.
DrugBank; DB07934; [[CYCLOHEXANESULFONYL-GLYCYL]-3[PYRIDIN-4-YL-AMINOMETHYL]ALANYL]PIPERIDINE.
DrugBank; DB08422; [PHENYLALANINYL-PROLINYL]-[2-(PYRIDIN-4-YLAMINO)-ETHYL]-AMINE.
DrugBank; DB07659; AC-(D)PHE-PRO-BOROHOMOLYS-OH.
DrugBank; DB07660; AC-(D)PHE-PRO-BOROHOMOORNITHINE-OH.
DrugBank; DB07658; AC-(D)PHE-PRO-BOROLYS-OH.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
DrugBank; DB00278; Argatroban.
DrugBank; DB08624; BENZOTHIAZOLE.
DrugBank; DB01766; Beta-(2-Naphthyl)-Alanine.
DrugBank; DB07083; beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide.
DrugBank; DB00006; Bivalirudin.
DrugBank; DB06404; C1 Esterase Inhibitor (Human).
DrugBank; DB09228; C1 Esterase Inhibitor (Recombinant).
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB03159; CRA_8696.
DrugBank; DB06911; D-leucyl-N-(3-chlorobenzyl)-L-prolinamide.
DrugBank; DB06996; D-leucyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DrugBank; DB06919; D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide.
DrugBank; DB07027; D-phenylalanyl-N-(3-fluorobenzyl)-L-prolinamide.
DrugBank; DB07133; D-phenylalanyl-N-(3-methylbenzyl)-L-prolinamide.
DrugBank; DB06841; D-phenylalanyl-N-[(1S)-4-{[amino(iminio)methyl]amino}-1-(chloroacetyl)butyl]-L-prolinamide.
DrugBank; DB07143; D-phenylalanyl-N-benzyl-L-prolinamide.
DrugBank; DB07005; D-phenylalanyl-N-{4-[amino(iminio)methyl]benzyl}-L-prolinamide.
DrugBank; DB06695; Dabigatran etexilate.
DrugBank; DB00055; Drotrecogin alfa.
DrugBank; DB03847; Gamma-Carboxy-Glutamic Acid.
DrugBank; DB01767; Hemi-Babim.
DrugBank; DB00001; Lepirudin.
DrugBank; DB04136; Lysophosphotidylserine.
DrugBank; DB00170; Menadione.
DrugBank; DB06838; methyl L-phenylalaninate.
DrugBank; DB08187; METHYL-PHE-PRO-AMINO-CYCLOHEXYLGLYCINE.
DrugBank; DB06868; N-(3-chlorobenzyl)-1-(4-methylpentanoyl)-L-prolinamide.
DrugBank; DB06942; N-(4-carbamimidoylbenzyl)-1-(3-phenylpropanoyl)-L-prolinamide.
DrugBank; DB06936; N-(4-carbamimidoylbenzyl)-1-(4-methylpentanoyl)-L-prolinamide.
DrugBank; DB07165; N-(5-CHLORO-BENZO[B]THIOPHEN-3-YLMETHYL)-2-[6-CHLORO-OXO-3-(2-PYRIDIN-2-YL-ETHYLAMINO)-2H-PYRAZIN-1-YL]-ACETAMIDE.
DrugBank; DB06859; N-ALLYL-5-AMIDINOAMINOOXY-PROPYLOXY-3-CHLORO-N-CYCLOPENTYLBENZAMIDE.
DrugBank; DB06853; N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DrugBank; DB06858; N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DrugBank; DB07279; N-ETHYL-N-ISOPROPYL-3-METHYL-5-{[(2S)-2-(PYRIDIN-4-YLAMINO)PROPYL]OXY}BENZAMIDE.
DrugBank; DB07944; N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDE.
DrugBank; DB01123; Proflavine.
DrugBank; DB04786; Suramin.
DrugBank; DB05777; Thrombomodulin Alfa.
DrugBank; DB04697; TRANS-4-(GUANIDINOMETHYL)-CYCLOHEXANE-L-YL-D-3-CYCLOHEXYLALANYL-L-AZETIDINE-2-YL-D-TYROSINYL-L-HOMOARGININAMIDE.
DrugBank; DB04898; Ximelagatran.
DrugBank; DB08152; {(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetate.
GuidetoPHARMACOLOGY; 2362; -.
MEROPS; S01.217; -.
iPTMnet; P00734; -.
PhosphoSitePlus; P00734; -.
UniCarbKB; P00734; -.
BioMuta; F2; -.
DMDM; 135807; -.
SWISS-2DPAGE; P00734; -.
MaxQB; P00734; -.
PaxDb; P00734; -.
PeptideAtlas; P00734; -.
PRIDE; P00734; -.
TopDownProteomics; P00734; -.
DNASU; 2147; -.
Ensembl; ENST00000311907; ENSP00000308541; ENSG00000180210.
GeneID; 2147; -.
KEGG; hsa:2147; -.
UCSC; uc001ndf.5; human.
CTD; 2147; -.
DisGeNET; 2147; -.
GeneCards; F2; -.
GeneReviews; F2; -.
H-InvDB; HIX0026188; -.
HGNC; HGNC:3535; F2.
HPA; CAB016780; -.
HPA; CAB018650; -.
HPA; HPA051476; -.
HPA; HPA054698; -.
MalaCards; F2; -.
MIM; 176930; gene.
MIM; 188050; phenotype.
MIM; 601367; phenotype.
MIM; 613679; phenotype.
MIM; 614390; phenotype.
neXtProt; NX_P00734; -.
OpenTargets; ENSG00000180210; -.
Orphanet; 329217; Cerebral sinovenous thrombosis.
Orphanet; 325; Congenital factor II deficiency.
Orphanet; 64738; Non rare thrombophilia.
PharmGKB; PA157; -.
eggNOG; ENOG410IKPN; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOVERGEN; HBG108381; -.
InParanoid; P00734; -.
KO; K01313; -.
OMA; GIECQLW; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P00734; -.
TreeFam; TF327329; -.
BRENDA; 3.4.21.5; 2681.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
Reactome; R-HSA-977606; Regulation of Complement cascade.
SABIO-RK; P00734; -.
SIGNOR; P00734; -.
EvolutionaryTrace; P00734; -.
GeneWiki; Thrombin; -.
GenomeRNAi; 2147; -.
PMAP-CutDB; P00734; -.
PRO; PR:P00734; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000180210; -.
CleanEx; HS_F2; -.
ExpressionAtlas; P00734; baseline and differential.
Genevisible; P00734; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008083; F:growth factor activity; TAS:BHF-UCL.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0070053; F:thrombospondin receptor activity; IDA:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; IDA:BHF-UCL.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
GO; GO:0051918; P:negative regulation of fibrinolysis; TAS:BHF-UCL.
GO; GO:0010544; P:negative regulation of platelet activation; TAS:BHF-UCL.
GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL.
GO; GO:0070945; P:neutrophil mediated killing of gram-negative bacterium; IDA:UniProtKB.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
GO; GO:0030168; P:platelet activation; IDA:BHF-UCL.
GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0090218; P:positive regulation of lipid kinase activity; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:1900738; P:positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0030193; P:regulation of blood coagulation; TAS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
GO; GO:0006465; P:signal peptide processing; TAS:Reactome.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.140.10; -; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR000294; GLA_domain.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR003966; Prothrombin/thrombin.
InterPro; IPR018992; Thrombin_light_chain.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24254:SF13; PTHR24254:SF13; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00051; Kringle; 2.
Pfam; PF09396; Thrombin_light; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001149; Thrombin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
PRINTS; PR01505; PROTHROMBIN.
SMART; SM00069; GLA; 1.
SMART; SM00130; KR; 2.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 2.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS00021; KRINGLE_1; 2.
PROSITE; PS50070; KRINGLE_2; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
Kringle; Pharmaceutical; Polymorphism; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal; Thrombophilia; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 43 {ECO:0000269|PubMed:266717,
ECO:0000269|PubMed:8073540}.
/FTId=PRO_0000028159.
CHAIN 44 622 Prothrombin.
/FTId=PRO_0000028160.
PEPTIDE 44 198 Activation peptide fragment 1.
/FTId=PRO_0000028161.
PEPTIDE 199 327 Activation peptide fragment 2.
/FTId=PRO_0000028162.
CHAIN 328 363 Thrombin light chain.
/FTId=PRO_0000028163.
CHAIN 364 622 Thrombin heavy chain.
/FTId=PRO_0000028164.
DOMAIN 44 89 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 108 186 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 213 291 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 364 618 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 551 573 High affinity receptor-binding region
which is also known as the TP508 peptide.
ACT_SITE 406 406 Charge relay system.
ACT_SITE 462 462 Charge relay system.
ACT_SITE 568 568 Charge relay system.
SITE 198 199 Cleavage; by thrombin.
SITE 327 328 Cleavage; by factor Xa.
SITE 363 364 Cleavage; by factor Xa.
MOD_RES 49 49 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3759958,
ECO:0000269|PubMed:6305407}.
MOD_RES 50 50 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:3759958,
ECO:0000269|PubMed:6305407}.
MOD_RES 57 57 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
MOD_RES 59 59 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
MOD_RES 62 62 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
MOD_RES 63 63 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
MOD_RES 68 68 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
MOD_RES 69 69 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
MOD_RES 72 72 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
MOD_RES 75 75 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6305407}.
CARBOHYD 121 121 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:22171320}.
CARBOHYD 143 143 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:22171320}.
CARBOHYD 416 416 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:873923}.
DISULFID 60 65
DISULFID 90 103
DISULFID 108 186
DISULFID 129 169
DISULFID 157 181
DISULFID 213 291
DISULFID 234 274
DISULFID 262 286
DISULFID 336 482 Interchain (between light and heavy
chains).
DISULFID 391 407
DISULFID 536 550 {ECO:0000250}.
DISULFID 564 594 {ECO:0000250}.
VARIANT 72 72 E -> G (in FA2D; Shanghai).
{ECO:0000269|PubMed:14962227}.
/FTId=VAR_055232.
VARIANT 165 165 T -> M (polymorphism; confirmed at
protein level; dbSNP:rs5896).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:22028381,
ECO:0000269|Ref.5}.
/FTId=VAR_011781.
VARIANT 200 200 E -> K (in FA2D; prothrombin type 3;
variant confirmed at protein level;
dbSNP:rs62623459).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:6405779}.
/FTId=VAR_006711.
VARIANT 314 314 R -> C (in FA2D; Barcelona/Madrid;
dbSNP:rs121918477).
{ECO:0000269|PubMed:3771562}.
/FTId=VAR_006712.
VARIANT 314 314 R -> H (in FA2D; Padua-1;
dbSNP:rs754231232).
{ECO:0000269|PubMed:7865694}.
/FTId=VAR_006713.
VARIANT 380 380 M -> T (in FA2D; Himi-1;
dbSNP:rs121918481).
{ECO:0000269|PubMed:1421398}.
/FTId=VAR_006714.
VARIANT 386 386 P -> T (polymorphism; confirmed at
protein level; dbSNP:rs5897).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:22028381}.
/FTId=VAR_011782.
VARIANT 425 425 R -> C (in FA2D; Quick-1;
dbSNP:rs121918479).
{ECO:0000269|PubMed:3242619}.
/FTId=VAR_006715.
VARIANT 431 431 R -> H (in FA2D; Himi-2;
dbSNP:rs121918482).
{ECO:0000269|PubMed:1421398}.
/FTId=VAR_006716.
VARIANT 461 461 R -> W (in FA2D; Tokushima;
dbSNP:rs121918478).
{ECO:0000269|PubMed:1349838,
ECO:0000269|PubMed:3567158,
ECO:0000269|PubMed:3801671}.
/FTId=VAR_006717.
VARIANT 509 509 E -> A (in FA2D; Salakta/Frankfurt).
{ECO:0000269|PubMed:1354985,
ECO:0000269|PubMed:7792730}.
/FTId=VAR_006718.
VARIANT 532 532 E -> Q (polymorphism; confirmed at
protein level).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:873923}.
/FTId=VAR_068913.
VARIANT 601 601 G -> V (in FA2D; Quick-2;
dbSNP:rs121918480).
{ECO:0000269|PubMed:2719946}.
/FTId=VAR_006719.
CONFLICT 9 25 Missing (in Ref. 3; BAG64719).
{ECO:0000305}.
CONFLICT 66 66 S -> N (in Ref. 4; BAD96497).
{ECO:0000305}.
CONFLICT 119 119 H -> N (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 121 121 N -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 164 164 T -> I (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 164 164 T -> N (in Ref. 7; CAA23842).
{ECO:0000305}.
CONFLICT 176 176 V -> A (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 183 183 I -> T (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 194 195 AM -> MV (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 308 308 D -> DEE (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 335 335 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 337 337 G -> R (in Ref. 4; BAD96495).
{ECO:0000305}.
CONFLICT 349 349 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 369 369 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 398 398 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 414 414 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 485 485 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 494 494 Q -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 504 504 W -> Y (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 509 509 E -> S (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 511 511 W -> V (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 514 514 N -> D (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 529 530 PI -> AL (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 590 592 WGE -> AGA (in Ref. 11; AAR08143).
{ECO:0000305}.
HELIX 47 60 {ECO:0000244|PDB:5EDM}.
HELIX 67 74 {ECO:0000244|PDB:5EDM}.
HELIX 77 89 {ECO:0000244|PDB:5EDM}.
TURN 90 92 {ECO:0000244|PDB:5EDM}.
HELIX 97 105 {ECO:0000244|PDB:5EDM}.
STRAND 107 109 {ECO:0000244|PDB:5EDM}.
TURN 112 115 {ECO:0000244|PDB:4HZH}.
STRAND 124 126 {ECO:0000244|PDB:5EDK}.
STRAND 128 130 {ECO:0000244|PDB:5EDK}.
TURN 144 146 {ECO:0000244|PDB:5EDM}.
STRAND 148 150 {ECO:0000244|PDB:4NZQ}.
STRAND 167 173 {ECO:0000244|PDB:5EDM}.
STRAND 177 180 {ECO:0000244|PDB:5EDM}.
TURN 186 188 {ECO:0000244|PDB:4NZQ}.
STRAND 191 193 {ECO:0000244|PDB:5EDM}.
STRAND 211 214 {ECO:0000244|PDB:5EDM}.
HELIX 216 218 {ECO:0000244|PDB:3K65}.
STRAND 229 231 {ECO:0000244|PDB:4HZH}.
STRAND 233 235 {ECO:0000244|PDB:4HZH}.
STRAND 237 239 {ECO:0000244|PDB:4NZQ}.
HELIX 240 246 {ECO:0000244|PDB:3K65}.
STRAND 247 249 {ECO:0000244|PDB:5EDK}.
STRAND 253 255 {ECO:0000244|PDB:5EDK}.
STRAND 273 275 {ECO:0000244|PDB:3K65}.
STRAND 277 279 {ECO:0000244|PDB:3K65}.
STRAND 283 285 {ECO:0000244|PDB:3K65}.
HELIX 295 297 {ECO:0000244|PDB:5EDM}.
STRAND 322 324 {ECO:0000244|PDB:3BEI}.
HELIX 326 329 {ECO:0000244|PDB:3BEI}.
STRAND 330 332 {ECO:0000244|PDB:1QJ1}.
TURN 334 337 {ECO:0000244|PDB:5AFY}.
TURN 340 342 {ECO:0000244|PDB:5AFY}.
HELIX 343 345 {ECO:0000244|PDB:5AFY}.
HELIX 352 358 {ECO:0000244|PDB:5AFY}.
STRAND 361 367 {ECO:0000244|PDB:2BVR}.
HELIX 369 371 {ECO:0000244|PDB:2BVR}.
STRAND 372 374 {ECO:0000244|PDB:2HPP}.
HELIX 375 377 {ECO:0000244|PDB:2BVR}.
STRAND 378 383 {ECO:0000244|PDB:5AFY}.
TURN 384 387 {ECO:0000244|PDB:5AFY}.
STRAND 388 395 {ECO:0000244|PDB:5AFY}.
STRAND 397 403 {ECO:0000244|PDB:5AFY}.
HELIX 405 407 {ECO:0000244|PDB:5AFY}.
STRAND 408 410 {ECO:0000244|PDB:4DY7}.
HELIX 411 413 {ECO:0000244|PDB:5AFY}.
TURN 415 417 {ECO:0000244|PDB:2BVR}.
HELIX 419 421 {ECO:0000244|PDB:5AFY}.
STRAND 422 427 {ECO:0000244|PDB:5AFY}.
STRAND 430 433 {ECO:0000244|PDB:5AFY}.
TURN 436 438 {ECO:0000244|PDB:5AFY}.
STRAND 440 449 {ECO:0000244|PDB:5AFY}.
TURN 455 458 {ECO:0000244|PDB:5AFY}.
STRAND 464 470 {ECO:0000244|PDB:5AFY}.
STRAND 475 477 {ECO:0000244|PDB:4O03}.
HELIX 486 492 {ECO:0000244|PDB:5AFY}.
STRAND 495 497 {ECO:0000244|PDB:5EDM}.
STRAND 498 504 {ECO:0000244|PDB:5AFY}.
STRAND 507 510 {ECO:0000244|PDB:4UD9}.
TURN 513 515 {ECO:0000244|PDB:4CH2}.
STRAND 516 518 {ECO:0000244|PDB:4CH2}.
STRAND 524 530 {ECO:0000244|PDB:5AFY}.
HELIX 533 538 {ECO:0000244|PDB:5AFY}.
STRAND 540 542 {ECO:0000244|PDB:1MH0}.
STRAND 548 551 {ECO:0000244|PDB:5AFY}.
HELIX 555 557 {ECO:0000244|PDB:5AFY}.
TURN 565 569 {ECO:0000244|PDB:3U8O}.
STRAND 571 575 {ECO:0000244|PDB:5AFY}.
TURN 577 579 {ECO:0000244|PDB:5AFY}.
STRAND 582 590 {ECO:0000244|PDB:5AFY}.
STRAND 592 595 {ECO:0000244|PDB:5AFY}.
STRAND 596 598 {ECO:0000244|PDB:3K65}.
STRAND 601 605 {ECO:0000244|PDB:5AFY}.
HELIX 607 609 {ECO:0000244|PDB:5AFY}.
HELIX 610 619 {ECO:0000244|PDB:5AFY}.
SEQUENCE 622 AA; 70037 MW; 8A25E1DA88208FCF CRC64;
MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE VRKGNLEREC
VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL AACLEGNCAE GLGTNYRGHV
NITRSGIECQ LWRSRYPHKP EINSTTHPGA DLQENFCRNP DSSTTGPWCY TTDPTVRRQE
CSIPVCGQDQ VTVAMTPRSE GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA
QAKALSKHQD FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG
DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK TERELLESYI
DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW VLTAAHCLLY PPWDKNFTEN
DLLVRIGKHS RTRYERNIEK ISMLEKIYIH PRYNWRENLD RDIALMKLKK PVAFSDYIHP
VCLPDRETAA SLLQAGYKGR VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST
RIRITDNMFC AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY
GFYTHVFRLK KWIQKVIDQF GE


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