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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.
29-SEP-2021, entry version 268.
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]
ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=6323392; DOI=10.1093/oxfordjournals.jbchem.a134583;
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 11:1-17(2012).
[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; DOI=10.1002/j.1460-2075.1989.tb08511.x;
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; DOI=10.1002/j.1460-2075.1990.tb07410.x;
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; DOI=10.1097/00001721-199410000-00025;
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 OF PUBMED:10391209.
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:
Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form
fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
-!- ACTIVITY 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:
P00734; P05067: APP; NbExp=3; IntAct=EBI-297094, EBI-77613;
P00734; P07204: THBD; NbExp=4; IntAct=EBI-297094, EBI-941422;
P00734; Q846V4; Xeno; NbExp=5; IntAct=EBI-297094, EBI-989571;
-!- 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 variants
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 variants 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 variants 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 variants 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.
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; 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; 5MJT; X-ray; 1.40 A; H=364-622, L=328-363.
PDB; 5MLS; X-ray; 1.62 A; H=364-622, L=328-363.
PDB; 5MM6; X-ray; 1.29 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; 5Z5W; NMR; -; A=606-617.
PDB; 5Z5X; NMR; -; A=605-622.
PDB; 6BJR; X-ray; 6.00 A; A=44-622.
PDB; 6C2W; X-ray; 4.12 A; A/B=44-622.
PDB; 6EO6; X-ray; 1.69 A; H=364-622, L=328-363.
PDB; 6EO7; X-ray; 2.24 A; H=364-622, L=328-363.
PDB; 6EO8; X-ray; 1.94 A; H=364-622, L=328-363.
PDB; 6EO9; X-ray; 1.84 A; H=364-622, L=328-363.
PDB; 6V5T; X-ray; 2.10 A; E=333-622.
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; 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; 5MJT; -.
PDBsum; 5MLS; -.
PDBsum; 5MM6; -.
PDBsum; 5NHU; -.
PDBsum; 5TO3; -.
PDBsum; 5Z5W; -.
PDBsum; 5Z5X; -.
PDBsum; 6BJR; -.
PDBsum; 6C2W; -.
PDBsum; 6EO6; -.
PDBsum; 6EO7; -.
PDBsum; 6EO8; -.
PDBsum; 6EO9; -.
PDBsum; 6V5T; -.
PDBsum; 7KME; -.
PDBsum; 8KME; -.
BMRB; P00734; -.
SMR; P00734; -.
BioGRID; 108447; 24.
ComplexPortal; CPX-6222; alpha-thrombin complex.
DIP; DIP-6115N; -.
IntAct; P00734; 16.
MINT; P00734; -.
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; DB07796; (3ASR,4RS,8ASR,8BRS)-4-(2-(4-FLUOROBENZYL)-1,3-DIOXODEACAHYDROPYRROLO[3,4-A] PYRROLIZIN-4-YL)BENZAMIDINE.
DrugBank; DB07016; (3R)-8-(dioxidosulfanyl)-3-methyl-1,2,3,4-tetrahydroquinoline.
DrugBank; DB07521; (3Z,6S)-6-Chloro-1-(2-{[(5-chloro-1-benzothiophen-3-yl)methyl]amino}ethyl)-3-({2-[(2R)-2-piperidinyl]ethyl}imino)-2-piperazinol.
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; DB07515; 1-(2-{[(6-amino-2-methylpyridin-3-yl)methyl]amino}ethyl)-6-chloro-3-[(2,2-difluoro-2-pyridin-2-ylethyl)amino]-1,4-dihydropyrazin-2-ol.
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; DB08624; 1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine.
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; DB02287; 2-(2-hydroxy-phenyl)-3H-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; DB07550; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(1-OXIDO-2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUOROPHENYL)METHYL]ACETAMIDE.
DrugBank; DB07549; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUORO-3-METHYL-6-PYRIDINYL)METHYL]ACETAMIDE.
DrugBank; DB07548; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUORO-6-PYRIDINYL)METHYL]ACETAMIDE.
DrugBank; DB07105; 2-[2-(4-Chloro-Phenylsulfanyl)-Acetylamino]-3-(4-Guanidino-Phenyl)-Propionamide.
DrugBank; DB04722; 2-[3-chloro-6-[2,2-difluoro-2-(1-oxidopyridin-1-ium-2-yl)ethyl]imino-1-hydroxypyridin-2-yl]-N-[(1R)-1-(3-chlorophenyl)ethyl]acetamide.
DrugBank; DB07366; 2-[N'-(4-AMINO-BUTYL)-HYDRAZINOCARBONYL]-PYRROLIDINE-1-CARBOXYLIC ACID BENZYL ESTER.
DrugBank; DB08254; 2-Naphthalenesulfonic acid.
DrugBank; DB01725; 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide.
DrugBank; DB08062; 3-(4-CHLOROPHENYL)-5-(METHYLTHIO)-4H-1,2,4-TRIAZOLE.
DrugBank; DB07639; 3-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID ETHYL ESTER.
DrugBank; DB07461; 3-AMINO-3-BENZYL-9-CARBOXAMIDE[4.3.0]BICYCLO-1,6-DIAZANONAN-2-ONE.
DrugBank; DB07120; 3-Carbamimidamido-1,1-diphenylurea.
DrugBank; DB07190; 3-cyclohexyl-D-alanyl-N-(3-chlorobenzyl)-L-prolinamide.
DrugBank; DB07741; 4-(1R,3AS,4R,8AS,8BR)-[1-DIFLUOROMETHYL-2-(4-FLUOROBENZYL)-3-OXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZAMIDINE.
DrugBank; DB07353; 4-(2,5-DIAMINO-5-HYDROXY-PENTYL)-PHENOL.
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; DB08546; 4-[(3AS,4R,7R,8AS,8BR)-2-(1,3-BENZODIOXOL-5-YLMETHYL)-7-HYDROXY-1,3-DIOXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZENECARBOXIMIDAMIDE.
DrugBank; DB08061; 4-[3-(4-CHLOROPHENYL)-1H-PYRAZOL-5-YL]PIPERIDINE.
DrugBank; DB07718; 4-Hydroxyphenylpyruvic acid.
DrugBank; DB03136; 4-Iodobenzo[B]Thiophene-2-Carboxamidine.
DrugBank; DB02723; 4-Oxo-2-Phenylmethanesulfonyl-Octahydro-Pyrrolo[1,2-a]Pyrazine-6-Carboxylic Acid [1-(N-Hydroxycarbamimidoyl)-Piperidin-4-Ylmethyl]-Amide.
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; DB06841; [(2R)-1-[(2S)-2-[[(2S,3S)-1-Chloro-6-(diaminomethylideneamino)-2-hydroxyhexan-3-yl]carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-yl]azanium.
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; DB13151; Anti-inhibitor coagulant complex.
DrugBank; DB00025; Antihemophilic factor, human recombinant.
DrugBank; DB11166; Antithrombin Alfa.
DrugBank; DB00278; Argatroban.
DrugBank; DB01766; Beta-(2-Naphthyl)-Alanine.
DrugBank; DB07083; beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide.
DrugBank; DB12364; Betrixaban.
DrugBank; DB00006; Bivalirudin.
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB13152; Coagulation Factor IX Human.
DrugBank; DB09228; Conestat alfa.
DrugBank; DB09130; Copper.
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; 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; DB05714; Flovagatran.
DrugBank; DB12831; Gabexate.
DrugBank; DB03847; gamma-carboxy-L-glutamic acid.
DrugBank; DB07278; GW-813893.
DrugBank; DB01767; Hemi-Babim.
DrugBank; DB06404; Human C1-esterase inhibitor.
DrugBank; DB09332; Kappadione.
DrugBank; DB00001; Lepirudin.
DrugBank; DB13998; Lonoctocog alfa.
DrugBank; DB04136; Lysophosphotidylserine.
DrugBank; DB00170; Menadione.
DrugBank; DB06838; methyl L-phenylalaninate.
DrugBank; DB13999; Moroctocog alfa.
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; DB07527; N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]-4-METHOXY-2,3,6-TRIMETHYLBENZENESULFONAMIDE.
DrugBank; DB07522; N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]NAPHTHALENE-2-SULFONAMIDE.
DrugBank; DB07665; N-[2-(carbamimidamidooxy)ethyl]-2-{6-cyano-3-[(2,2-difluoro-2-pyridin-2-ylethyl)amino]-2-fluorophenyl}acetamide.
DrugBank; DB07946; N-[2-({[amino(imino)methyl]amino}oxy)ethyl]-2-{6-chloro-3-[(2,2-difluoro-2-phenylethyl)amino]-2-fluorophenyl}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; DB08187; N-Methylphenylalanyl-N-[(trans-4-aminocyclohexyl)methyl]-L-prolinamide.
DrugBank; DB04591; N-{2,2-DIFLUORO-2-[(2R)-PIPERIDIN-2-YL]ETHYL}-2-[2-(1H-1,2,4-TRIAZOL-1-YL)BENZYL][1,3]OXAZOLO[4,5-C]PYRIDIN-4-AMINE.
DrugBank; DB07944; N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDE.
DrugBank; DB07128; N7-BUTYL-N2-(5-CHLORO-2-METHYLPHENYL)-5-METHYL[1,2,4]TRIAZOLO[1,5-A]PYRIMIDINE-2,7-DIAMINE.
DrugBank; DB12598; Nafamostat.
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; DB09109; Turoctocog alfa.
DrugBank; DB14738; Turoctocog alfa pegol.
DrugBank; DB04898; Ximelagatran.
DrugBank; DB01593; Zinc.
DrugBank; DB14487; Zinc acetate.
DrugBank; DB08152; {(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetate.
DrugCentral; P00734; -.
GuidetoPHARMACOLOGY; 2362; -.
MEROPS; S01.217; -.
MoonDB; P00734; Curated.
GlyConnect; 518; 39 N-Linked glycans (4 sites).
GlyGen; P00734; 10 sites, 51 N-linked glycans (4 sites), 1 O-linked glycan (6 sites).
iPTMnet; P00734; -.
PhosphoSitePlus; P00734; -.
BioMuta; F2; -.
DMDM; 135807; -.
SWISS-2DPAGE; P00734; -.
EPD; P00734; -.
jPOST; P00734; -.
MassIVE; P00734; -.
MaxQB; P00734; -.
PaxDb; P00734; -.
PeptideAtlas; P00734; -.
PRIDE; P00734; -.
ProteomicsDB; 51269; -.
TopDownProteomics; P00734; -.
ABCD; P00734; 3 sequenced antibodies.
Antibodypedia; 857; 1158 antibodies.
DNASU; 2147; -.
Ensembl; ENST00000311907; ENSP00000308541; ENSG00000180210.
GeneID; 2147; -.
KEGG; hsa:2147; -.
UCSC; uc001ndf.5; human.
CTD; 2147; -.
DisGeNET; 2147; -.
GeneCards; F2; -.
GeneReviews; F2; -.
HGNC; HGNC:3535; F2.
HPA; ENSG00000180210; Tissue enriched (liver).
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 IN EUROPE: Non rare thrombophilia.
PharmGKB; PA157; -.
VEuPathDB; HostDB:ENSG00000180210; -.
eggNOG; ENOG502QTSX; Eukaryota.
GeneTree; ENSGT00940000154234; -.
HOGENOM; CLU_006842_19_4_1; -.
InParanoid; P00734; -.
OMA; VMIFRKS; -.
OrthoDB; 1314811at2759; -.
PhylomeDB; P00734; -.
TreeFam; TF327329; -.
BRENDA; 3.4.21.5; 2681.
PathwayCommons; P00734; -.
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-9657688; Defective factor XII causes hereditary angioedema.
Reactome; R-HSA-9672391; Defective F8 cleavage by thrombin.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SABIO-RK; P00734; -.
SIGNOR; P00734; -.
BioGRID-ORCS; 2147; 10 hits in 1004 CRISPR screens.
EvolutionaryTrace; P00734; -.
GeneWiki; Thrombin; -.
GenomeRNAi; 2147; -.
Pharos; P00734; Tclin.
PRO; PR:P00734; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; P00734; protein.
Bgee; ENSG00000180210; Expressed in right lobe of liver and 93 other tissues.
ExpressionAtlas; P00734; baseline and differential.
Genevisible; P00734; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA: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:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI: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:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
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: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 population 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:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; NAS:BHF-UCL.
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:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
CDD; cd00108; KR; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 2.40.20.10; -; 2.
Gene3D; 4.10.140.10; -; 1.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR003966; Prothrombin/thrombin.
InterPro; IPR018992; Thrombin_light_chain.
InterPro; IPR037111; Thrombin_light_chain_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24254:SF10; PTHR24254:SF10; 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; Direct protein sequencing;
Disease variant; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein;
Hemostasis; Hydrolase; Kringle; Pharmaceutical; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Thrombophilia; Zymogen.
SIGNAL 1..24
/evidence="ECO:0000255"
PROPEP 25..43
/evidence="ECO:0000269|PubMed:266717,
ECO:0000269|PubMed:8073540"
/id="PRO_0000028159"
CHAIN 44..622
/note="Prothrombin"
/id="PRO_0000028160"
PEPTIDE 44..198
/note="Activation peptide fragment 1"
/id="PRO_0000028161"
PEPTIDE 199..327
/note="Activation peptide fragment 2"
/id="PRO_0000028162"
CHAIN 328..363
/note="Thrombin light chain"
/id="PRO_0000028163"
CHAIN 364..622
/note="Thrombin heavy chain"
/id="PRO_0000028164"
DOMAIN 44..89
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 108..186
/note="Kringle 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
DOMAIN 213..291
/note="Kringle 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
DOMAIN 364..618
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
REGION 551..573
/note="High affinity receptor-binding region which is also
known as the TP508 peptide"
ACT_SITE 406
/note="Charge relay system"
ACT_SITE 462
/note="Charge relay system"
ACT_SITE 568
/note="Charge relay system"
SITE 198..199
/note="Cleavage; by thrombin"
SITE 327..328
/note="Cleavage; by factor Xa"
SITE 363..364
/note="Cleavage; by factor Xa"
MOD_RES 49
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407"
MOD_RES 50
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407"
MOD_RES 57
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
MOD_RES 59
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
MOD_RES 62
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
MOD_RES 63
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
MOD_RES 68
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
MOD_RES 69
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
MOD_RES 72
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
MOD_RES 75
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6305407"
CARBOHYD 121
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320"
CARBOHYD 143
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320"
CARBOHYD 416
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="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
/note="Interchain (between light and heavy chains)"
DISULFID 391..407
DISULFID 536..550
/evidence="ECO:0000250"
DISULFID 564..594
/evidence="ECO:0000250"
VARIANT 72
/note="E -> G (in FA2D; Shanghai)"
/evidence="ECO:0000269|PubMed:14962227"
/id="VAR_055232"
VARIANT 165
/note="T -> M (confirmed at protein level; dbSNP:rs5896)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:22028381,
ECO:0000269|Ref.5"
/id="VAR_011781"
VARIANT 200
/note="E -> K (in FA2D; prothrombin type 3; variant
confirmed at protein level; dbSNP:rs62623459)"
/evidence="ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:6405779"
/id="VAR_006711"
VARIANT 314
/note="R -> C (in FA2D; Barcelona/Madrid;
dbSNP:rs121918477)"
/evidence="ECO:0000269|PubMed:3771562"
/id="VAR_006712"
VARIANT 314
/note="R -> H (in FA2D; Padua-1; dbSNP:rs754231232)"
/evidence="ECO:0000269|PubMed:7865694"
/id="VAR_006713"
VARIANT 380
/note="M -> T (in FA2D; Himi-1; dbSNP:rs121918481)"
/evidence="ECO:0000269|PubMed:1421398"
/id="VAR_006714"
VARIANT 386
/note="P -> T (confirmed at protein level; dbSNP:rs5897)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:22028381"
/id="VAR_011782"
VARIANT 425
/note="R -> C (in FA2D; Quick-1; dbSNP:rs121918479)"
/evidence="ECO:0000269|PubMed:3242619"
/id="VAR_006715"
VARIANT 431
/note="R -> H (in FA2D; Himi-2; dbSNP:rs121918482)"
/evidence="ECO:0000269|PubMed:1421398"
/id="VAR_006716"
VARIANT 461
/note="R -> W (in FA2D; Tokushima; dbSNP:rs121918478)"
/evidence="ECO:0000269|PubMed:1349838,
ECO:0000269|PubMed:3567158, ECO:0000269|PubMed:3801671"
/id="VAR_006717"
VARIANT 509
/note="E -> A (in FA2D; Salakta/Frankfurt)"
/evidence="ECO:0000269|PubMed:1354985,
ECO:0000269|PubMed:7792730"
/id="VAR_006718"
VARIANT 532
/note="E -> Q"
/evidence="ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:873923"
/id="VAR_068913"
VARIANT 601
/note="G -> V (in FA2D; Quick-2; dbSNP:rs121918480)"
/evidence="ECO:0000269|PubMed:2719946"
/id="VAR_006719"
CONFLICT 9..25
/note="Missing (in Ref. 3; BAG64719)"
/evidence="ECO:0000305"
CONFLICT 66
/note="S -> N (in Ref. 4; BAD96497)"
/evidence="ECO:0000305"
CONFLICT 119
/note="H -> N (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 121
/note="N -> S (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 164
/note="T -> I (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 164
/note="T -> N (in Ref. 7; CAA23842)"
/evidence="ECO:0000305"
CONFLICT 176
/note="V -> A (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 183
/note="I -> T (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 194..195
/note="AM -> MV (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 308
/note="D -> DEE (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 335
/note="D -> N (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 337
/note="G -> R (in Ref. 4; BAD96495)"
/evidence="ECO:0000305"
CONFLICT 349
/note="D -> N (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 369
/note="D -> N (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 398
/note="D -> N (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 414
/note="D -> N (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 485
/note="D -> N (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 494
/note="Q -> G (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 504
/note="W -> Y (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 509
/note="E -> S (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 511
/note="W -> V (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 514
/note="N -> D (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 529..530
/note="PI -> AL (in Ref. 10; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 590..592
/note="WGE -> AGA (in Ref. 11; AAR08143)"
/evidence="ECO:0000305"
HELIX 47..60
/evidence="ECO:0007829|PDB:5EDM"
HELIX 67..74
/evidence="ECO:0007829|PDB:5EDM"
HELIX 77..89
/evidence="ECO:0007829|PDB:5EDM"
TURN 90..92
/evidence="ECO:0007829|PDB:5EDM"
HELIX 97..105
/evidence="ECO:0007829|PDB:5EDM"
STRAND 107..109
/evidence="ECO:0007829|PDB:5EDM"
TURN 112..115
/evidence="ECO:0007829|PDB:4HZH"
STRAND 124..126
/evidence="ECO:0007829|PDB:5EDK"
STRAND 128..130
/evidence="ECO:0007829|PDB:5EDK"
TURN 144..146
/evidence="ECO:0007829|PDB:5EDM"
STRAND 148..150
/evidence="ECO:0007829|PDB:4NZQ"
STRAND 167..173
/evidence="ECO:0007829|PDB:5EDM"
STRAND 177..180
/evidence="ECO:0007829|PDB:5EDM"
TURN 186..188
/evidence="ECO:0007829|PDB:4NZQ"
STRAND 191..193
/evidence="ECO:0007829|PDB:5EDM"
STRAND 211..214
/evidence="ECO:0007829|PDB:5EDM"
HELIX 216..218
/evidence="ECO:0007829|PDB:3K65"
STRAND 229..231
/evidence="ECO:0007829|PDB:4HZH"
STRAND 233..235
/evidence="ECO:0007829|PDB:4HZH"
STRAND 237..239
/evidence="ECO:0007829|PDB:4NZQ"
HELIX 240..246
/evidence="ECO:0007829|PDB:3K65"
STRAND 247..249
/evidence="ECO:0007829|PDB:5EDK"
STRAND 253..255
/evidence="ECO:0007829|PDB:5EDK"
STRAND 273..275
/evidence="ECO:0007829|PDB:3K65"
STRAND 277..279
/evidence="ECO:0007829|PDB:3K65"
STRAND 283..285
/evidence="ECO:0007829|PDB:3K65"
HELIX 295..297
/evidence="ECO:0007829|PDB:5EDM"
STRAND 322..324
/evidence="ECO:0007829|PDB:3BEI"
TURN 326..328
/evidence="ECO:0007829|PDB:4O03"
HELIX 329..333
/evidence="ECO:0007829|PDB:5NHU"
TURN 334..337
/evidence="ECO:0007829|PDB:5AFY"
TURN 340..342
/evidence="ECO:0007829|PDB:5AFY"
HELIX 343..345
/evidence="ECO:0007829|PDB:5AFY"
HELIX 352..358
/evidence="ECO:0007829|PDB:5AFY"
TURN 360..362
/evidence="ECO:0007829|PDB:1NO9"
STRAND 367..369
/evidence="ECO:0007829|PDB:3SQH"
STRAND 372..375
/evidence="ECO:0007829|PDB:3QDZ"
STRAND 378..383
/evidence="ECO:0007829|PDB:5AFY"
TURN 384..387
/evidence="ECO:0007829|PDB:5AFY"
STRAND 388..395
/evidence="ECO:0007829|PDB:5AFY"
STRAND 397..403
/evidence="ECO:0007829|PDB:5AFY"
HELIX 405..407
/evidence="ECO:0007829|PDB:5AFY"
STRAND 408..410
/evidence="ECO:0007829|PDB:4DY7"
HELIX 411..413
/evidence="ECO:0007829|PDB:5AFY"
HELIX 419..421
/evidence="ECO:0007829|PDB:5AFY"
STRAND 422..427
/evidence="ECO:0007829|PDB:5AFY"
STRAND 430..433
/evidence="ECO:0007829|PDB:5AFY"
TURN 436..438
/evidence="ECO:0007829|PDB:5AFY"
STRAND 440..449
/evidence="ECO:0007829|PDB:5AFY"
TURN 455..458
/evidence="ECO:0007829|PDB:5AFY"
STRAND 464..470
/evidence="ECO:0007829|PDB:5AFY"
STRAND 475..477
/evidence="ECO:0007829|PDB:4O03"
HELIX 486..492
/evidence="ECO:0007829|PDB:5AFY"
STRAND 495..497
/evidence="ECO:0007829|PDB:5EDM"
STRAND 498..504
/evidence="ECO:0007829|PDB:5AFY"
STRAND 507..510
/evidence="ECO:0007829|PDB:4UD9"
TURN 513..515
/evidence="ECO:0007829|PDB:4CH2"
STRAND 516..518
/evidence="ECO:0007829|PDB:4CH2"
STRAND 524..530
/evidence="ECO:0007829|PDB:5AFY"
HELIX 533..538
/evidence="ECO:0007829|PDB:5AFY"
STRAND 540..542
/evidence="ECO:0007829|PDB:1MH0"
STRAND 548..551
/evidence="ECO:0007829|PDB:5AFY"
HELIX 555..557
/evidence="ECO:0007829|PDB:5AFY"
TURN 565..569
/evidence="ECO:0007829|PDB:3U8O"
STRAND 571..575
/evidence="ECO:0007829|PDB:5AFY"
TURN 577..579
/evidence="ECO:0007829|PDB:5AFY"
STRAND 582..590
/evidence="ECO:0007829|PDB:5AFY"
STRAND 592..595
/evidence="ECO:0007829|PDB:5AFY"
STRAND 596..598
/evidence="ECO:0007829|PDB:3K65"
STRAND 601..605
/evidence="ECO:0007829|PDB:5AFY"
HELIX 607..609
/evidence="ECO:0007829|PDB:5AFY"
HELIX 610..619
/evidence="ECO:0007829|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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bs-10388R-Cy5 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, Cy5 Conjugated 100ul
bs-10388R-A488 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-10388R-A647 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-10387R-A488 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-10388R-A555 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-10387R-A555 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-10387R-A647 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-10388R-Biotin Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, Biotin Conjugated 100ul
bs-10387R-Biotin Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, Biotin Conjugated 100ul
bs-10388R-FITC Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, FITC Conjugated 100ul
bs-10387R-FITC Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, FITC Conjugated 100ul
R1391T Rat IgG Fab Fragment (Heavy and Light chain) 1 mg
Pathways :
WP272: Blood Clotting Cascade
WP1614: 1- and 2-Methylnaphthalene degradation
WP545: Complement Activation, Classical Pathway
WP1001: Peptide GPCRs
WP977: Complement Activation, Classical Pathway
WP200: Complement Activation, Classical Pathway
WP1647: Fatty acid biosynthesis
WP59: Electron Transport Chain
WP1673: Naphthalene and anthracene degradation
WP772: Electron Transport Chain
WP1117: Peptide GPCRs
WP234: Peptide GPCRs
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1823: GP1b-IX-V activation signalling
WP1882: Platelet Activation
WP884: Electron Transport Chain
WP131: Peptide GPCRs
WP1502: Mitochondrial biogenesis
WP542: Electron Transport Chain
WP1929: Thrombin signalling through proteinase activated receptors (PARs)
WP1996: Linoleate Biosynthesis
WP1633: Bisphenol A degradation
WP1665: Limonene and pinene degradation
WP771: Peptide GPCRs
WP111: Electron Transport Chain

Related Genes :
[F2] 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]
[PROC] Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]
[] Venom prothrombin activator pseutarin-C catalytic subunit (PCCS) (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10 FX] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Virus-activating protease) (VAP) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[PLG] Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B]
[F7 Cf7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F2RL1 GPR11 PAR2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]
[F11] Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain]
[F12] Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)]
[F9] Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain]
[F8 F8C] Coagulation factor VIII (Antihemophilic factor) (AHF) (Procoagulant component) [Cleaved into: Factor VIIIa heavy chain, 200 kDa isoform; Factor VIIIa heavy chain, 92 kDa isoform; Factor VIII B chain; Factor VIIIa light chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B heavy chain]
[F2 ORTSPA_R05543] Activation peptide fragment 1 (EC 3.4.21.5) (Activation peptide fragment 2) (Coagulation factor II) (Prothrombin) (Thrombin heavy chain) (Thrombin light chain) (Fragment)
[F2 EULNIG_R03319] Activation peptide fragment 1 (EC 3.4.21.5) (Activation peptide fragment 2) (Coagulation factor II) (Prothrombin) (Thrombin heavy chain) (Thrombin light chain) (Fragment)
[F10 TrFX] Coagulation factor X (EC 3.4.21.6) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[HABP2 HGFAL PHBP] Hyaluronan-binding protein 2 (EC 3.4.21.-) (Factor VII-activating protease) (Factor seven-activating protease) (FSAP) (Hepatocyte growth factor activator-like protein) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form]
[F13A1 F13A] Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A chain)
[F2rl1 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (Thrombin receptor-like 1)
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F2rl1 Gpcr11 Gpr11 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1)
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc) (Neutrophil chemotactic factor-2) (ENCF-2); Complement C3 alpha chain; C3a anaphylatoxin (Neutrophil chemotactic factor-1) (ENCF-1); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]

Bibliography :
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