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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]

 FA9_HUMAN               Reviewed;         461 AA.
P00740; A8K9N4; F2RM36; Q5FBE1; Q5JYJ8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
23-FEB-2022, entry version 268.
RecName: Full=Coagulation factor IX {ECO:0000303|PubMed:3857619};
EC=3.4.21.22 {ECO:0000269|PubMed:12444082, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373};
AltName: Full=Christmas factor;
AltName: Full=Plasma thromboplastin component;
Short=PTC;
Contains:
RecName: Full=Coagulation factor IXa light chain;
Contains:
RecName: Full=Coagulation factor IXa heavy chain;
Flags: Precursor;
Name=F9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=6959130; DOI=10.1073/pnas.79.21.6461;
Kurachi K., Davie E.W.;
"Isolation and characterization of a cDNA coding for human factor IX.";
Proc. Natl. Acad. Sci. U.S.A. 79:6461-6464(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=6687940; DOI=10.1093/nar/11.8.2325;
Jaye M., de la Salle H., Schamber F., Balland A., Kohli V., Findeli A.,
Tolstoshev P., Lecocq J.-P.;
"Isolation of a human anti-haemophilic factor IX cDNA clone using a unique
52-base synthetic oligonucleotide probe deduced from the amino acid
sequence of bovine factor IX.";
Nucleic Acids Res. 11:2325-2335(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-194.
PubMed=6329734; DOI=10.1002/j.1460-2075.1984.tb01926.x;
Anson D.S., Choo K.H., Rees D.J.G., Giannelli F., Gould K.G.,
Huddleston J.A., Brownlee G.G.;
"The gene structure of human anti-haemophilic factor IX.";
EMBO J. 3:1053-1060(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-194.
PubMed=2994716; DOI=10.1021/bi00335a049;
Yoshitake S., Schach B.G., Foster D.C., Davie E.W., Kurachi K.;
"Nucleotide sequence of the gene for human factor IX (antihemophilic factor
B).";
Biochemistry 24:3736-3750(1985).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-194, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3857619; DOI=10.1073/pnas.82.9.2847;
McGraw R.A., Davis L.M., Noyes C.M., Lundblad R.L., Roberts H.R.,
Graham J.B., Stafford D.W.;
"Evidence for a prevalent dimorphism in the activation peptide of human
coagulation factor IX.";
Proc. Natl. Acad. Sci. U.S.A. 82:2847-2851(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
TISSUE=Liver;
Sata S., Yonemitsu Y., Nakagawa K., Sueishi K.;
"Alternative splicing variant of Homo sapiens coagulation factor IX lacking
EGF like domain.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-461.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Nguyen D.T., Nguyen P.V., Nong H.V.;
"Homo sapiens coagulation factor IX (F9), mRNA.";
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-84, VARIANT HEMB GLN-43, FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
PubMed=8295821;
de la Salle C., Charmantier J.L., Ravanat C., Ohlmann P., Hartmann M.L.,
Schuhler S., Bischoff R., Ebel C., Roecklin D., Balland A.;
"The Arg-4 mutant factor IX Strasbourg 2 shows a delayed activation by
factor XIa.";
Nouv. Rev. Fr. Hematol. 35:473-480(1993).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-326 (ISOFORM 1).
TISSUE=Liver;
PubMed=6089357; DOI=10.1007/bf01534851;
Jagadeeswaran P., Lavelle D.E., Kaul R., Mohandas T., Warren S.T.;
"Isolation and characterization of human factor IX cDNA: identification of
Taq I polymorphism and regional assignment.";
Somat. Cell Mol. Genet. 10:465-473(1984).
[15]
PROTEIN SEQUENCE OF 47-461, VARIANT HEMB TRP-226, FUNCTION, CATALYTIC
ACTIVITY, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=2592373;
Suehiro K., Kawabata S., Miyata T., Takeya H., Takamatsu J., Ogata K.,
Kamiya T., Saito H., Niho Y., Iwanaga S.;
"Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by
tryptophan and its activation by alpha-chymotrypsin and rat mast cell
chymase.";
J. Biol. Chem. 264:21257-21265(1989).
[16]
PROTEIN SEQUENCE OF 47-52, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
CHARACTERIZATION OF VARIANTS HEMB GLN-43; LEU-43 AND TRP-43,
CALCIUM-BINDING, AND PROTEOLYTIC CLEAVAGE.
PubMed=9169594; DOI=10.1042/bj3230629;
Wojcik E.G., Van Den Berg M., Poort S.R., Bertina R.M.;
"Modification of the N-terminus of human factor IX by defective propeptide
cleavage or acetylation results in a destabilized calcium-induced
conformation: effects on phospholipid binding and activation by factor
XIa.";
Biochem. J. 323:629-636(1997).
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-359.
PubMed=3340835; DOI=10.1126/science.3340835;
Stoflet E.S., Koeberl D.D., Sarkar G., Sommer S.S.;
"Genomic amplification with transcript sequencing.";
Science 239:491-494(1988).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-461.
PubMed=8236150;
de la Salle C., Charmantier J.L., Baas M.-J., Schwartz A., Wiesel M.L.,
Grunebaum L., Cazenave J.-P.;
"A deletion located in the 3' non translated part of the factor IX gene
responsible for mild haemophilia B.";
Thromb. Haemost. 70:370-371(1993).
[19]
HYDROXYLATION AT ASP-110.
PubMed=6688526; DOI=10.1016/0006-291x(83)90961-0;
McMullen B.A., Fujikawa K., Kisiel W.;
"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent
blood coagulation zymogens.";
Biochem. Biophys. Res. Commun. 115:8-14(1983).
[20]
PROTEOLYTIC PROCESSING, AND ACTIVE SITE.
PubMed=659613; DOI=10.1172/jci109073;
di Scipio R.G., Kurachi K., Davie E.W.;
"Activation of human factor IX (Christmas factor).";
J. Clin. Invest. 61:1528-1538(1978).
[21]
CALCIUM-BINDING, AND DOMAIN.
PubMed=6425296;
Morita T., Isaacs B.S., Esmon C.T., Johnson A.E.;
"Derivatives of blood coagulation factor IX contain a high affinity Ca2+-
binding site that lacks gamma-carboxyglutamic acid.";
J. Biol. Chem. 259:5698-5704(1984).
[22]
ERRATUM OF PUBMED:6425296.
Morita T., Isaacs B.S., Esmon C.T., Johnson A.E.;
J. Biol. Chem. 260:2583-2583(1985).
[23]
GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
PubMed=2511201;
Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T.,
Shimonishi Y., Iwanaga S.;
"Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc)
O-glycosidically linked to a serine residue in the first epidermal growth
factor-like domain of human factors VII and IX and protein Z and bovine
protein Z.";
J. Biol. Chem. 264:20320-20325(1989).
[24]
GLYCOSYLATION AT SER-99, AND STRUCTURE OF CARBOHYDRATE ON SER-99.
PubMed=2129367; DOI=10.1007/978-1-4615-3806-6_12;
Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
"A new trisaccharide sugar chain linked to a serine residue in the first
EGF-like domain of clotting factors VII and IX and protein Z.";
Adv. Exp. Med. Biol. 281:121-131(1990).
[25]
FUNCTION, AND PROTEOLYTIC CLEAVAGE.
PubMed=1730085;
Rawala-Sheikh R., Ahmad S.S., Monroe D.M., Roberts H.R., Walsh P.N.;
"Role of gamma-carboxyglutamic acid residues in the binding of factor IXa
to platelets and in factor-X activation.";
Blood 79:398-405(1992).
[26]
GLYCOSYLATION AT SER-107, AND STRUCTURE OF CARBOHYDRATE ON SER-107.
PubMed=1517205;
Nishimura H., Takao T., Hase S., Shimonishi Y., Iwanaga S.;
"Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61
through the fucose residue.";
J. Biol. Chem. 267:17520-17525(1992).
[27]
GLYCOSYLATION AT THR-205 AND THR-215.
PubMed=8172892; DOI=10.1021/bi00183a021;
Agarwala K.L., Kawabata S., Takao T., Murata H., Shimonishi Y.,
Nishimura H., Iwanaga S.;
"Activation peptide of human factor IX has oligosaccharides O-
glycosidically linked to threonine residues at 159 and 169.";
Biochemistry 33:5167-5171(1994).
[28]
PHOSPHORYLATION AT SER-114.
Harris R.J., Papac D.I., Truong L., Smith K.J.;
"Partial phosphorylation of serine-68 in EGF-1 of human factor IX.";
(In) Proceedings of XIth international conference on methods in protein
structure analysis, pp.50-50, Annecy (1996).
[29]
SULFATION AT TYR-201, AND PHOSPHORYLATION AT SER-204.
PubMed=11133752; DOI=10.1182/blood.v97.1.130;
Arruda V.R., Hagstrom J.N., Deitch J., Heiman-Patterson T., Camire R.M.,
Chu K., Fields P.A., Herzog R.W., Couto L.B., Larson P.J., High K.A.;
"Posttranslational modifications of recombinant myotube-synthesized human
factor IX.";
Blood 97:130-138(2001).
[30]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-305; LYS-311; TYR-312 AND
TYR-391.
PubMed=12444082; DOI=10.1074/jbc.m210722200;
Sichler K., Kopetzki E., Huber R., Bode W., Hopfner K.P., Brandstetter H.;
"Physiological fIXa activation involves a cooperative conformational
rearrangement of the 99-loop.";
J. Biol. Chem. 278:4121-4126(2003).
[31]
GLYCOSYLATION AT THR-85; SER-99; SER-107; THR-205; THR-215 AND THR-225,
PHOSPHORYLATION AT SER-204 AND THR-205, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=25456591; DOI=10.1016/j.chroma.2014.10.046;
Huang L.J., Lin J.H., Tsai J.H., Chu Y.Y., Chen Y.W., Chen S.L., Chen S.H.;
"Identification of protein O-glycosylation site and corresponding glycans
using liquid chromatography-tandem mass spectrometry via mapping accurate
mass and retention time shift.";
J. Chromatogr. A 1371:136-145(2014).
[32]
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).
[33]
STRUCTURE BY NMR OF 47-93.
PubMed=7713897; DOI=10.1074/jbc.270.14.7980;
Freedman S.J., Furie B.C., Furie B., Baleja J.D.;
"Structure of the metal-free gamma-carboxyglutamic acid-rich membrane
binding region of factor IX by two-dimensional NMR spectroscopy.";
J. Biol. Chem. 270:7980-7987(1995).
[34]
STRUCTURE BY NMR OF 47-93.
PubMed=7547952; DOI=10.1021/bi00038a005;
Freedman S.J., Furie B.C., Furie B., Baleja J.D.;
"Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain
of factor IX.";
Biochemistry 34:12126-12137(1995).
[35]
STRUCTURE BY NMR OF 47-93.
PubMed=8663165; DOI=10.1074/jbc.271.27.16227;
Freedman S.J., Blostein M.D., Baleja J.D., Jacobs M., Furie B.C., Furie B.;
"Identification of the phospholipid binding site in the vitamin K-dependent
blood coagulation protein factor IX.";
J. Biol. Chem. 271:16227-16236(1996).
[36]
STRUCTURE BY NMR OF 47-93.
PubMed=9047312; DOI=10.1021/bi962250r;
Li L., Darden T.A., Freedman S.J., Furie B.C., Furie B., Baleja J.D.,
Smith H., Hiskey R.G., Pedersen L.G.;
"Refinement of the NMR solution structure of the gamma-carboxyglutamic acid
domain of coagulation factor IX using molecular dynamics simulation with
initial Ca2+ positions determined by a genetic algorithm.";
Biochemistry 36:2132-2138(1997).
[37]
STRUCTURE BY NMR OF 91-133.
PubMed=1854745; DOI=10.1021/bi00244a006;
Huang L.H., Cheng H., Pardi A., Tam J.P., Sweeney W.V.;
"Sequence-specific 1H NMR assignments, secondary structure, and location of
the calcium binding site in the first epidermal growth factor like domain
of blood coagulation factor IX.";
Biochemistry 30:7402-7409(1991).
[38]
STRUCTURE BY NMR OF 92-130, AND DISULFIDE BOND.
PubMed=1304885; DOI=10.1002/pro.5560010109;
Baron M., Norman D.G., Harvey T.S., Handford P.A., Mayhew M., Tse A.G.D.,
Brownlee G.G., Campbell I.D.C.;
"The three-dimensional structure of the first EGF-like module of human
factor IX: comparison with EGF and TGF-alpha.";
Protein Sci. 1:81-90(1992).
[39]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-130 IN COMPLEX WITH CALCIUM,
AND DISULFIDE BOND.
PubMed=7606779; DOI=10.1016/0092-8674(95)90059-4;
Rao Z., Handford P., Mayhew M., Knott V., Brownlee G.G., Stuart D.;
"The structure of a Ca(2+)-binding epidermal growth factor-like domain: its
role in protein-protein interactions.";
Cell 82:131-141(1995).
[40]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 133-461 IN COMPLEX WITH CALCIUM.
PubMed=10467148; DOI=10.1016/s0969-2126(99)80125-7;
Hopfner K.-P., Lang A., Karcher A., Sichler K., Kopetzki E.,
Brandstetter H., Huber R., Bode W., Engh R.A.;
"Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate
binding.";
Structure 7:989-996(1999).
[41]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 47-91 IN COMPLEX WITH CALCIUM.
PubMed=14722079; DOI=10.1074/jbc.m314011200;
Huang M., Furie B.C., Furie B.;
"Crystal structure of the calcium-stabilized human factor IX Gla domain
bound to a conformation-specific anti-factor IX antibody.";
J. Biol. Chem. 279:14338-14346(2004).
[42]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 133-191 AND 227-461 OF MUTANTS
PHE-305/THR-311/ALA-365/THR-391 IN COMPLEX WITH CALCIUM AND SYNTHETIC
INHIBITOR, ACTIVE SITE, DISULFIDE BOND, SUBUNIT, AND PROTEOLYTIC CLEAVAGE.
PubMed=20004170; DOI=10.1016/j.str.2009.10.011;
Zogg T., Brandstetter H.;
"Structural basis of the cofactor- and substrate-assisted activation of
human coagulation factor IXa.";
Structure 17:1669-1678(2009).
[43]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 133-461 IN COMPLEX WITH CALCIUM,
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISULFIDE BOND.
PubMed=20121198; DOI=10.1021/jm901475e;
Wang S., Beck R., Blench T., Burd A., Buxton S., Malic M., Ayele T.,
Shaikh S., Chahwala S., Chander C., Holland R., Merette S., Zhao L.,
Blackney M., Watts A.;
"Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors
in thrombosis.";
J. Med. Chem. 53:1465-1472(2010).
[44]
X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 133-188 AND 227-461 IN COMPLEX
WITH CALCIUM, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISULFIDE BOND.
PubMed=20121197; DOI=10.1021/jm901476x;
Wang S., Beck R., Burd A., Blench T., Marlin F., Ayele T., Buxton S.,
Dagostin C., Malic M., Joshi R., Barry J., Sajad M., Cheung C., Shaikh S.,
Chahwala S., Chander C., Baumgartner C., Holthoff H.P., Murray E.,
Blackney M., Giddings A.;
"Structure based drug design: development of potent and selective factor
IXa (FIXa) inhibitors.";
J. Med. Chem. 53:1473-1482(2010).
[45]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 131-188 AND 227-461 IN COMPLEX
WITH SERPINC1 AND CALCIUM, DISULFIDE BOND, PROTEOLYTIC CLEAVAGE, AND
SUBUNIT.
PubMed=20080729; DOI=10.1073/pnas.0910144107;
Johnson D.J., Langdown J., Huntington J.A.;
"Molecular basis of factor IXa recognition by heparin-activated
antithrombin revealed by a 1.7-A structure of the ternary complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:645-650(2010).
[46]
MOLECULAR PATHOLOGY OF HEMB B.
PubMed=2743975; DOI=10.1002/j.1460-2075.1989.tb03474.x;
Green P.M., Bentley D.R., Mibashan R.S., Nilsson I.M., Giannelli F.;
"Molecular pathology of haemophilia B.";
EMBO J. 8:1067-1072(1989).
[47]
REVIEW ON HEMB VARIANTS.
PubMed=1634040; DOI=10.1096/fasebj.6.10.1634040;
Sommer S.S.;
"Assessing the underlying pattern of human germline mutations: lessons from
the factor IX gene.";
FASEB J. 6:2767-2774(1992).
[48]
REVIEW ON HEMB VARIANTS.
PubMed=8392713; DOI=10.1093/nar/21.13.3075;
Giannelli F., Green P.M., High K.A., Sommer S., Poon M.-C., Ludwig M.,
Schwaab R., Reitsma P.H., Goossens M., Yoshioka A., Brownlee G.G.;
"Haemophilia B: database of point mutations and short additions and
deletions -- fourth edition, 1993.";
Nucleic Acids Res. 21:3075-3087(1993).
[49]
VARIANT HEMB HIS-191.
PubMed=6603618; DOI=10.1073/pnas.80.14.4200;
Noyes C.M., Griffith M.J., Roberts H.R., Lundblad R.L.;
"Identification of the molecular defect in factor IX Chapel Hill:
substitution of histidine for arginine at position 145.";
Proc. Natl. Acad. Sci. U.S.A. 80:4200-4202(1983).
[50]
VARIANT HEMB GLN-43, AND CHARACTERIZATION OF VARIANT HEMB GLN-43.
PubMed=3009023; DOI=10.1016/0092-8674(86)90319-3;
Bentley A.K., Rees D.J., Rizza C., Brownlee G.G.;
"Defective propeptide processing of blood clotting factor IX caused by
mutation of arginine to glutamine at position -4.";
Cell 45:343-348(1986).
[51]
VARIANT HEMB GLY-93.
PubMed=3790720;
Davis L.M., McGraw R.A., Ware J.L., Roberts H.R., Stafford D.W.;
"Factor IXAlabama: a point mutation in a clotting protein results in
hemophilia B.";
Blood 69:140-143(1987).
[52]
VARIANT HEMB THR-443.
PubMed=3401602;
Ware J., Davis L., Frazier D., Bajaj S.P., Stafford D.W.;
"Genetic defect responsible for the dysfunctional protein: factor IX (Long
Beach).";
Blood 72:820-822(1988).
[53]
VARIANT HEMB VAL-436.
PubMed=3243764; DOI=10.1093/oxfordjournals.jbchem.a122575;
Sugimoto M., Miyata T., Kawabata S., Yoshioka A., Fukui H., Takahashi H.,
Iwanaga S.;
"Blood clotting factor IX Niigata: substitution of alanine-390 by valine in
the catalytic domain.";
J. Biochem. 104:878-880(1988).
[54]
VARIANT HEMB GLN-226.
PubMed=2713493;
Monroe D.M., McCord D.M., Huang M.N., High K.A., Lundblad R.L.,
Kasper C.K., Roberts H.R.;
"Functional consequences of an arginine180 to glutamine mutation in factor
IX Hilo.";
Blood 73:1540-1544(1989).
[55]
VARIANT HEMB ARG-442.
PubMed=2714791; DOI=10.1016/0888-7543(89)90330-3;
Attree O., Vidaud D., Vidaud M., Amselem S., Lavergne J.-M., Goossens M.;
"Mutations in the catalytic domain of human coagulation factor IX: rapid
characterization by direct genomic sequencing of DNA fragments displaying
an altered melting behavior.";
Genomics 4:266-272(1989).
[56]
VARIANTS HEMB GLN-75; ASP-79; TRP-268; THR-279; SER-306; MET-342; ARG-357
AND ARG-453, AND VARIANT PHE-7.
PubMed=2773937;
Koeberl D.D., Bottema C.D., Buerstedde J.-M., Sommer S.S.;
"Functionally important regions of the factor IX gene have a low rate of
polymorphism and a high rate of mutation in the dinucleotide CpG.";
Am. J. Hum. Genet. 45:448-457(1989).
[57]
VARIANT HEMB CYS-191.
PubMed=2775660; DOI=10.1111/j.1365-2141.1989.tb04323.x;
Liddell M.B., Peake I.R., Taylor S.A., Lillicrap D.P., Giddings J.C.,
Bloom A.L.;
"Factor IX Cardiff: a variant factor IX protein that shows abnormal
activation is caused by an arginine to cysteine substitution at position
145.";
Br. J. Haematol. 72:556-560(1989).
[58]
VARIANT HEMB PHE-228.
PubMed=2753873; DOI=10.1093/oxfordjournals.jbchem.a122740;
Sakai T., Yoshioka A., Yamamoto K., Niinomi K., Fujimura Y., Fukui H.,
Miyata T., Iwanaga S.;
"Blood clotting factor IX Kashihara: amino acid substitution of valine-182
by phenylalanine.";
J. Biochem. 105:756-759(1989).
[59]
VARIANT HEMB GLN-43.
PubMed=2738071;
Ware J., Diuguid D.L., Liebman H.A., Rabiet M.J., Kasper C.K., Furie B.C.,
Furie B., Stafford D.W.;
"Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide
leads to incomplete gamma-carboxylation and altered phospholipid binding
properties.";
J. Biol. Chem. 264:11401-11406(1989).
[60]
VARIANTS HEMB LYS-73; SER-106 AND GLN-294.
PubMed=2472424; DOI=10.1172/jci114130;
Chen S.H., Thompson A.R., Zhang M., Scott C.R.;
"Three point mutations in the factor IX genes of five hemophilia B
patients. Identification strategy using localization by altered epitopes in
their hemophilic proteins.";
J. Clin. Invest. 84:113-118(1989).
[61]
VARIANT HEMB VAL-73.
PubMed=2339358;
Wang N.S., Zhang M., Thompson A.R., Chen S.H.;
"Factor IX Chongqing: a new mutation in the calcium-binding domain of
factor IX resulting in severe hemophilia B.";
Thromb. Haemost. 63:24-26(1990).
[62]
VARIANT HEMB LEU-228.
PubMed=2372509; DOI=10.1111/j.1365-2141.1990.tb02652.x;
Taylor S.A., Liddell M.B., Peake I.R., Bloom A.L., Lillicrap D.P.;
"A mutation adjacent to the beta cleavage site of factor IX (valine 182 to
leucine) results in mild haemophilia Bm.";
Br. J. Haematol. 75:217-221(1990).
[63]
VARIANTS HEMB GLN-226; TRP-226; PHE-227 AND THR-414.
PubMed=2162822;
Bertina R.M., van der Linden I.K., Mannucci P.M., Reinalda-Poot H.H.,
Cupers R., Poort S.R., Reitsma P.H.;
"Mutations in hemophilia Bm occur at the Arg180-Val activation site or in
the catalytic domain of factor IX.";
J. Biol. Chem. 265:10876-10883(1990).
[64]
VARIANT HEMB GLU-357.
PubMed=1958666; DOI=10.1021/bi00111a014;
Miyata T., Sakai T., Sugimoto M., Naka H., Yamamoto K., Yoshioka A.,
Fukui H., Mitsui K., Kamiya K., Umeyama H., Iwanaga S.;
"Factor IX Amagasaki: a new mutation in the catalytic domain resulting in
the loss of both coagulant and esterase activities.";
Biochemistry 30:11286-11291(1991).
[65]
VARIANT HEMB THR-443.
PubMed=1902289; DOI=10.1093/nar/19.5.1165;
Sarkar G., Cassady J.D., Pyeritz R.E., Gilchrist G.S., Sommer S.S.;
"Isoleucine-397 is changed to threonine in two females with hemophilia B.";
Nucleic Acids Res. 19:1165-1165(1991).
[66]
VARIANTS HEMB VAL-291; GLN-294; HIS-410; GLY-411 AND ILE-411.
PubMed=1346975;
Ludwig M., Sabharwal A.K., Brackmann H.H., Olek K., Smith K.J.,
Birktoft J.J., Bajaj S.P.;
"Hemophilia B caused by five different nondeletion mutations in the
protease domain of factor IX.";
Blood 79:1225-1232(1992).
[67]
VARIANT HEMB SER-252.
PubMed=1615485;
Taylor S.A., Duffin J., Cameron C., Teitel J., Garvey B., Lillicrap D.P.;
"Characterization of the original Christmas disease mutation (cysteine
206-->serine): from clinical recognition to molecular pathogenesis.";
Thromb. Haemost. 67:63-65(1992).
[68]
VARIANTS HEMB ARG-253; GLN-294; GLN-379; PRO-426 AND ILE-TYR-THR-445 INS.
PubMed=8257988; DOI=10.1002/humu.1380020506;
David D., Rosa H.A.V., Pemberton S., Diniz M.J., Campos M., Lavinha J.;
"Single-strand conformation polymorphism (SSCP) analysis of the molecular
pathology of hemophilia B.";
Hum. Mutat. 2:355-361(1993).
[69]
VARIANTS HEMB HIS-191; GLY-226; THR-279; GLN-379; GLU-419 AND GLN-449.
PubMed=8076946; DOI=10.1007/bf00208285;
Aguilar-Martinez P., Romey M.-C., Schved J.-F., Gris J.-C., Demaille J.,
Claustres M.;
"Factor IX gene mutations causing haemophilia B: comparison of SSC
screening versus systematic DNA sequencing and diagnostic applications.";
Hum. Genet. 94:287-290(1994).
[70]
VARIANT HEMB GLU-419.
PubMed=8199596; DOI=10.1002/humu.1380030211;
Aguilar-Martinez P., Romey M.-C., Gris J.-C., Schved J.-F., Demaille J.,
Claustres M.;
"A novel mutation (Val-373 to Glu) in the catalytic domain of factor IX,
resulting in moderately/severe hemophilia B in a southern French patient.";
Hum. Mutat. 3:156-158(1994).
[71]
VARIANTS HEMB GLN-294 AND ARG-413.
PubMed=7981722; DOI=10.1002/humu.1380040214;
Caglayan S.H., Vielhaber E., Guersel T., Aktuglu G., Sommer S.S.;
"Identification of mutations in four hemophilia B patients of Turkish
origin, including a novel deletion of base 6411.";
Hum. Mutat. 4:163-165(1994).
[72]
VARIANTS HEMB.
PubMed=8680410; DOI=10.1002/humu.1380060410;
Wulff K., Schroeder W., Wehnert M., Herrmann F.H.;
"Twenty-five novel mutations of the factor IX gene in haemophilia B.";
Hum. Mutat. 6:346-348(1995).
[73]
VARIANT WARFS THR-37, AND CHARACTERIZATION OF VARIANT WARFS THR-37.
PubMed=8833911; DOI=10.1172/jci118956;
Chu K., Wu S.M., Stanley T., Stafford D.W., High K.A.;
"A mutation in the propeptide of factor IX leads to warfarin sensitivity by
a novel mechanism.";
J. Clin. Invest. 98:1619-1625(1996).
[74]
VARIANTS WARFS THR-37 AND VAL-37.
PubMed=9233593; DOI=10.1046/j.1365-2141.1997.2213036.x;
Oldenburg J., Quenzel E.M., Harbrecht U., Fregin A., Kress W.,
Mueller C.R., Hertfelder H.J., Schwaab R., Brackmann H.H., Hanfland P.;
"Missense mutations at ALA-10 in the factor IX propeptide: an insignificant
variant in normal life but a decisive cause of bleeding during oral
anticoagulant therapy.";
Br. J. Haematol. 98:240-244(1997).
[75]
VARIANTS HEMB LYS-113; MET-342; ARG-413 AND VAL-424.
PubMed=9222764;
DOI=10.1002/(sici)1098-1004(1997)10:1<76::aid-humu11>3.0.co;2-x;
Caglayan S.H., Goekmen Y., Aktuglu G., Guergey A., Sommer S.S.;
"Mutations associated with hemophilia B in Turkish patients.";
Hum. Mutat. 10:76-79(1997).
[76]
VARIANT HEMB PRO-397.
PubMed=9590153;
DOI=10.1002/(sici)1096-8652(199805)58:1<72::aid-ajh13>3.0.co;2-7;
Chan V., Chan V.W.Y., Yip B., Chim C.S., Chan T.K.;
"Hemophilia B in a female carrier due to skewed inactivation of the normal
X-chromosome.";
Am. J. Hematol. 58:72-76(1998).
[77]
VARIANTS HEMB ARG-119 AND THR-454.
PubMed=9452115; DOI=10.1002/humu.1380110194;
David D., Moreira I., Morais S., de Deus G.;
"Five novel factor IX mutations in unrelated hemophilia B patients.";
Hum. Mutat. Suppl. 1:S301-S303(1998).
[78]
VARIANTS HEMB GLN-43; TRP-43; THR-46; SER-106; CYS-115; PHE-155; GLN-379;
GLU-387; VAL-432 AND CYS-450.
PubMed=9600455;
DOI=10.1002/(sici)1098-1004(1998)11:5<372::aid-humu4>3.0.co;2-m;
Heit J.A., Thorland E.C., Ketterling R.P., Lind T.J., Daniels T.M.,
Zapata R.E., Ordonez S.M., Kasper C.K., Sommer S.S.;
"Germline mutations in Peruvian patients with hemophilia B: pattern of
mutation in Amerindians is similar to the putative endogenous germline
pattern.";
Hum. Mutat. 11:372-376(1998).
[79]
VARIANTS HEMB.
PubMed=10698280;
Wulff K., Bykowska K., Lopaciuk S., Herrmann F.H.;
"Molecular analysis of hemophilia B in Poland: 12 novel mutations of the
factor IX gene.";
Acta Biochim. Pol. 46:721-726(1999).
[80]
VARIANTS HEMB.
PubMed=10094553;
DOI=10.1002/(sici)1098-1004(1999)13:2<160::aid-humu9>3.0.co;2-c;
Montejo J.M., Magallon M., Tizzano E., Solera J.;
"Identification of twenty-one new mutations in the factor IX gene by SSCP
analysis.";
Hum. Mutat. 13:160-165(1999).
[81]
VARIANT ALA-194.
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).
[82]
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).
[83]
VARIANTS HEMB CYS-169 AND THR-333.
PubMed=11122099; DOI=10.1046/j.1365-2141.2000.02389.x;
Vidal F., Farssac E., Altisent C., Puig L., Gallardo D.;
"Factor IX gene sequencing by a simple and sensitive 15-hour procedure for
haemophilia B diagnosis: identification of two novel mutations.";
Br. J. Haematol. 111:549-551(2000).
[84]
VARIANTS HEMB TYR-28; LEU-43; GLN-43; SER-52; ASP-106; LYS-124; TYR-134;
GLN-226; GLY-226; TRP-226; LYS-241; TYR-252; GLN-294; PHE-316; ARG-318;
GLY-379; ILE-383; PHE-383; ILE-395; PHE-396; ARG-407 AND GLU-412.
PubMed=12588353; DOI=10.1046/j.1365-2141.2003.04141.x;
Onay U.V., Kavakli K., Kilinc Y., Gurgey A., Aktuglu G., Kemahli S.,
Ozbek U., Caglayan S.H.;
"Molecular pathology of haemophilia B in Turkish patients: identification
of a large deletion and 33 independent point mutations.";
Br. J. Haematol. 120:656-659(2003).
[85]
VARIANTS HEMB TRP-43; ARG-84; ARG-125; VAL-125; PHE-170; ARG-302; MET-342;
LEU-344; LEU-395; THR-414; TYR-435; GLU-442 AND TRP-449.
PubMed=12604421;
Espinos C., Casana P., Haya S., Cid A.R., Aznar J.A.;
"Molecular analyses in hemophilia B families: identification of six new
mutations in the factor IX gene.";
Haematologica 88:235-236(2003).
[86]
VARIANT THPH8 LEU-384, CHARACTERIZATION OF VARIANT THPH8 LEU-384, FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19846852; DOI=10.1056/nejmoa0904377;
Simioni P., Tormene D., Tognin G., Gavasso S., Bulato C., Iacobelli N.P.,
Finn J.D., Spiezia L., Radu C., Arruda V.R.;
"X-linked thrombophilia with a mutant factor IX (factor IX Padua).";
N. Engl. J. Med. 361:1671-1675(2009).
[87]
VARIANTS HEMB ALA-194 AND HIS-241.
PubMed=25470321; DOI=10.1111/hae.12553;
Saini S., Hamasaki-Katagiri N., Pandey G.S., Yanover C., Guelcher C.,
Simhadri V.L., Dandekar S., Guerrera M.F., Kimchi-Sarfaty C., Sauna Z.E.;
"Genetic determinants of immunogenicity to factor IX during the treatment
of haemophilia B.";
Haemophilia 21:210-218(2015).
[88]
VARIANTS HEMB SER-20; TYR-28; SER-46; ASP-54; GLU-58; ARG-84; HIS-138;
GLN-226; ILE-284 DEL; MET-296; LYS-328; TYR-328; THR-414 AND
TYR-THR-LYS-VAL-447 INS, AND CHARACTERIZATION OF VARIANTS HEMB SER-20;
TYR-28; SER-46; ASP-54; GLU-58; ARG-84; HIS-138; GLN-226; ILE-284 DEL;
MET-296; LYS-328; TYR-328; THR-414 AND TYR-THR-LYS-VAL-447 INS.
PubMed=25251685; DOI=10.1111/hae.12534;
Guo Z.P., Yang L.H., Qin X.Y., Liu X.E., Chen J.F., Zhang Y.F.;
"Comprehensive analysis of phenotypes and genetics in 21 Chinese families
with haemophilia B: characterization of five novel mutations.";
Haemophilia 20:859-865(2014).
[89]
VARIANTS WARFS THR-37 AND VAL-37, AND CHARACTERIZATION OF VARIANTS WARFS
THR-37 AND VAL-37.
PubMed=29450643; DOI=10.1007/s00277-018-3264-2;
Pezeshkpoor B., Czogalla K.J., Caspers M., Berkemeier A.C., Liphardt K.,
Ghosh S., Kellner M., Ulrich S., Pavlova A., Oldenburg J.;
"Variants in FIX propeptide associated with vitamin K antagonist
hypersensitivity: functional analysis and additional data confirming the
common founder mutations.";
Ann. Hematol. 97:1061-1069(2018).
-!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
participates in the intrinsic pathway of blood coagulation by
converting factor X to its active form in the presence of Ca(2+) ions,
phospholipids, and factor VIIIa. {ECO:0000269|PubMed:1730085,
ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373,
ECO:0000269|PubMed:8295821}.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
factor Xa.; EC=3.4.21.22; Evidence={ECO:0000269|PubMed:12444082,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0000269|PubMed:2592373};
-!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-
linked (PubMed:20121198, PubMed:20121197, PubMed:20080729). Interacts
with SERPINC1. {ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373}.
-!- INTERACTION:
P00740; PRO_0000002968 [P00451]: F8; NbExp=2; IntAct=EBI-9640450, EBI-11621603;
P00740; Q3U4G3: Xxylt1; Xeno; NbExp=3; IntAct=EBI-9640450, EBI-16178491;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19846852,
ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:3857619,
ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00740-1; Sequence=Displayed;
Name=2;
IsoId=P00740-2; Sequence=VSP_047689;
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
(PubMed:3857619, PubMed:8295821, PubMed:2592373, PubMed:9169594,
PubMed:19846852). Synthesized primarily in the liver and secreted in
plasma. {ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:2592373,
ECO:0000269|PubMed:3857619}.
-!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla) residues
in the Gla domain. Calcium can also bind, with stronger affinity, to
another site beyond the Gla domain (PubMed:6425296). Under
physiological ion concentrations, Ca(2+) is displaced by Mg(2+) from
some of the gammaglutamate residues in the N-terminal Gla domain. This
leads to a subtle conformation change that may affect the interaction
with its binding protein (By similarity).
{ECO:0000250|UniProtKB:P00741, ECO:0000269|PubMed:14722079,
ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:6425296}.
-!- PTM: Activated by factor XIa, which excises the activation peptide
(PubMed:9169594, PubMed:1730085). The propeptide can also be removed by
snake venom protease (PubMed:20004170, PubMed:20080729).
{ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:2592373,
ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:6688526}.
-!- DISEASE: Hemophilia B (HEMB) [MIM:306900]: An X-linked blood
coagulation disorder characterized by a permanent tendency to
hemorrhage, due to factor IX deficiency. It is phenotypically similar
to hemophilia A, but patients present with fewer symptoms. Many
patients are asymptomatic until the hemostatic system is stressed by
surgery or trauma. {ECO:0000269|PubMed:10094553,
ECO:0000269|PubMed:10698280, ECO:0000269|PubMed:11122099,
ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:1346975, ECO:0000269|PubMed:1615485,
ECO:0000269|PubMed:1902289, ECO:0000269|PubMed:1958666,
ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:2339358,
ECO:0000269|PubMed:2372509, ECO:0000269|PubMed:2472424,
ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:25470321,
ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:2713493,
ECO:0000269|PubMed:2714791, ECO:0000269|PubMed:2738071,
ECO:0000269|PubMed:2753873, ECO:0000269|PubMed:2773937,
ECO:0000269|PubMed:2775660, ECO:0000269|PubMed:3009023,
ECO:0000269|PubMed:3243764, ECO:0000269|PubMed:3401602,
ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618,
ECO:0000269|PubMed:7981722, ECO:0000269|PubMed:8076946,
ECO:0000269|PubMed:8199596, ECO:0000269|PubMed:8257988,
ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:8680410,
ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9222764,
ECO:0000269|PubMed:9452115, ECO:0000269|PubMed:9590153,
ECO:0000269|PubMed:9600455}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- DISEASE: Note=Mutations in position 43 (Oxford-3, San Dimas) and 46
(Cambridge) prevents cleavage of the propeptide (PubMed:12588353,
PubMed:2738071, PubMed:3009023, PubMed:8295821, PubMed:9169594,
PubMed:9600455, PubMed:25251685). Mutation in position 93 (Alabama)
probably fails to bind to cell membranes (PubMed:3790720). Mutation in
position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent
cleavage of the activation peptide (PubMed:6603618, PubMed:8076946,
PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493).
{ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:2162822,
ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:2713493,
ECO:0000269|PubMed:2738071, ECO:0000269|PubMed:3009023,
ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618,
ECO:0000269|PubMed:8076946, ECO:0000269|PubMed:8295821,
ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9600455}.
-!- DISEASE: Thrombophilia, X-linked, due to factor IX defect (THPH8)
[MIM:300807]: A hemostatic disorder characterized by a tendency to
thrombosis. {ECO:0000269|PubMed:19846852}. Note=The disease is caused
by variants affecting the gene represented in this entry.
-!- DISEASE: Warfarin sensitivity, X-linked (WARFS) [MIM:301052]: A
condition characterized by sensitivity to warfarin, a drugs used as
anti-coagulants for the prevention of thromboembolic diseases in
subjects with deep vein thrombosis, atrial fibrillation, or mechanical
heart valve replacement. Warfarin sensitive individuals develop
bleeding complications when they are given warfarin within the
therapeutic ranges. {ECO:0000269|PubMed:29450643,
ECO:0000269|PubMed:8833911, ECO:0000269|PubMed:9233593}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- PHARMACEUTICAL: Available under the name BeneFix (Baxter and American
Home Products). Used to treat hemophilia B.
-!- MISCELLANEOUS: In 1952, one of the earliest researchers of the disease,
Dr. R.G. Macfarlane used the patient's surname, Christmas, to refer to
the disease and also to refer to the clotting factor which he called
the 'Christmas Factor' At the time Stephen Christmas was a 5-year-old
boy. He died in 1993 at the age of 46 from acquired immunodeficiency
syndrome contracted through treatment with blood products.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor IX entry;
URL="https://en.wikipedia.org/wiki/Factor_IX";
-!- WEB RESOURCE: Name=Factor IX Mutation Database;
URL="http://www.factorix.org/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f9/";
-!- WEB RESOURCE: Name=BeneFix; Note=Clinical information on BeneFix;
URL="https://www.pfizer.com/products/product-detail/benefix";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The Christmas Factor - Issue
41 of December 2003;
URL="https://web.expasy.org/spotlight/back_issues/041";
---------------------------------------------------------------------------
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EMBL; J00136; AAA98726.1; -; mRNA.
EMBL; J00137; AAA52763.1; -; mRNA.
EMBL; K02053; AAA56822.1; -; Genomic_DNA.
EMBL; K02048; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02049; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02051; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02052; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02402; AAB59620.1; -; Genomic_DNA.
EMBL; M11309; AAA52023.1; -; mRNA.
EMBL; AL033403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB186358; BAD89383.1; -; mRNA.
EMBL; AF536327; AAM96188.1; -; Genomic_DNA.
EMBL; FR846239; CCA61111.1; -; mRNA.
EMBL; AK292749; BAF85438.1; -; mRNA.
EMBL; CH471150; EAW88433.1; -; Genomic_DNA.
EMBL; BC109214; AAI09215.1; -; mRNA.
EMBL; BC109215; AAI09216.1; -; mRNA.
EMBL; S68634; AAB29758.1; -; Genomic_DNA.
EMBL; M35672; AAA51981.1; -; mRNA.
EMBL; M19063; AAA52456.1; -; Genomic_DNA.
EMBL; S66752; AAB28588.1; -; Genomic_DNA.
CCDS; CCDS14666.1; -. [P00740-1]
CCDS; CCDS83495.1; -. [P00740-2]
PIR; A00922; KFHU.
RefSeq; NP_000124.1; NM_000133.3. [P00740-1]
RefSeq; NP_001300842.1; NM_001313913.1. [P00740-2]
PDB; 1CFH; NMR; -; A=47-93.
PDB; 1CFI; NMR; -; A=47-93.
PDB; 1EDM; X-ray; 1.50 A; B/C=92-130.
PDB; 1IXA; NMR; -; A=92-130.
PDB; 1MGX; NMR; -; A=47-93.
PDB; 1NL0; X-ray; 2.20 A; G=47-91.
PDB; 1RFN; X-ray; 2.80 A; A=227-461, B=133-188.
PDB; 2WPH; X-ray; 1.50 A; E=133-191, S=227-461.
PDB; 2WPI; X-ray; 1.99 A; E=133-191, S=227-461.
PDB; 2WPJ; X-ray; 1.60 A; E=133-191, S=227-461.
PDB; 2WPK; X-ray; 2.21 A; E=133-191, S=227-461.
PDB; 2WPL; X-ray; 1.82 A; E=133-191, S=227-461.
PDB; 2WPM; X-ray; 2.00 A; E=133-191, S=227-461.
PDB; 3KCG; X-ray; 1.70 A; H=227-461, L=131-188.
PDB; 3LC3; X-ray; 1.90 A; A/C=227-461, B/D=133-188.
PDB; 3LC5; X-ray; 2.62 A; A=227-461, B=133-188.
PDB; 4WM0; X-ray; 2.37 A; D=92-130.
PDB; 4WMA; X-ray; 1.62 A; D=92-130.
PDB; 4WMB; X-ray; 2.05 A; D=92-130.
PDB; 4WMI; X-ray; 1.87 A; D=92-130.
PDB; 4WMK; X-ray; 2.08 A; D=92-130.
PDB; 4WN2; X-ray; 1.95 A; D=92-130.
PDB; 4WNH; X-ray; 1.95 A; D=92-130.
PDB; 4YZU; X-ray; 1.41 A; A=227-461, B=131-191.
PDB; 4Z0K; X-ray; 1.41 A; A=227-461, B=131-191.
PDB; 4ZAE; X-ray; 1.86 A; A=227-461, B=131-191.
PDB; 5EGM; X-ray; 1.84 A; A=227-461, B=131-191.
PDB; 5F84; X-ray; 2.50 A; B=92-130.
PDB; 5F85; X-ray; 2.15 A; B=92-130.
PDB; 5F86; X-ray; 1.90 A; B=92-130.
PDB; 5JB8; X-ray; 1.45 A; E=134-191, S=227-461.
PDB; 5JB9; X-ray; 1.30 A; E=134-191, S=227-461.
PDB; 5JBA; X-ray; 1.40 A; E=134-191, S=227-461.
PDB; 5JBB; X-ray; 1.56 A; E=134-191, S=227-461.
PDB; 5JBC; X-ray; 1.90 A; E=134-191, S=227-461.
PDB; 5TNO; X-ray; 1.54 A; A=227-461, B=130-191.
PDB; 5TNT; X-ray; 1.40 A; A=227-461, B=130-191.
PDB; 5VYG; X-ray; 2.20 A; A/B/C=92-130.
PDB; 6MV4; X-ray; 1.37 A; H=227-461, L=132-185.
PDB; 6RFK; X-ray; 1.60 A; E=130-191, S=227-461.
PDB; 6X5J; X-ray; 2.51 A; A=227-461, B=130-191.
PDB; 6X5L; X-ray; 2.25 A; A=227-460, B=130-191.
PDB; 6X5P; X-ray; 2.00 A; A=227-461, B=130-191.
PDB; 7AHV; X-ray; 3.11 A; H=227-461, L=130-188.
PDBsum; 1CFH; -.
PDBsum; 1CFI; -.
PDBsum; 1EDM; -.
PDBsum; 1IXA; -.
PDBsum; 1MGX; -.
PDBsum; 1NL0; -.
PDBsum; 1RFN; -.
PDBsum; 2WPH; -.
PDBsum; 2WPI; -.
PDBsum; 2WPJ; -.
PDBsum; 2WPK; -.
PDBsum; 2WPL; -.
PDBsum; 2WPM; -.
PDBsum; 3KCG; -.
PDBsum; 3LC3; -.
PDBsum; 3LC5; -.
PDBsum; 4WM0; -.
PDBsum; 4WMA; -.
PDBsum; 4WMB; -.
PDBsum; 4WMI; -.
PDBsum; 4WMK; -.
PDBsum; 4WN2; -.
PDBsum; 4WNH; -.
PDBsum; 4YZU; -.
PDBsum; 4Z0K; -.
PDBsum; 4ZAE; -.
PDBsum; 5EGM; -.
PDBsum; 5F84; -.
PDBsum; 5F85; -.
PDBsum; 5F86; -.
PDBsum; 5JB8; -.
PDBsum; 5JB9; -.
PDBsum; 5JBA; -.
PDBsum; 5JBB; -.
PDBsum; 5JBC; -.
PDBsum; 5TNO; -.
PDBsum; 5TNT; -.
PDBsum; 5VYG; -.
PDBsum; 6MV4; -.
PDBsum; 6RFK; -.
PDBsum; 6X5J; -.
PDBsum; 6X5L; -.
PDBsum; 6X5P; -.
PDBsum; 7AHV; -.
SMR; P00740; -.
BioGRID; 108456; 37.
ComplexPortal; CPX-4945; Coagulation factor IXa complex.
DIP; DIP-58520N; -.
ELM; P00740; -.
IntAct; P00740; 36.
MINT; P00740; -.
STRING; 9606.ENSP00000218099; -.
BindingDB; P00740; -.
ChEMBL; CHEMBL2016; -.
DrugBank; DB13151; Anti-inhibitor coagulant complex.
DrugBank; DB13192; Antihemophilic factor human.
DrugBank; DB00025; Antihemophilic factor, human recombinant.
DrugBank; DB13150; Coagulation factor VII human.
DrugBank; DB13923; Emicizumab.
DrugBank; DB09332; Kappadione.
DrugBank; DB13998; Lonoctocog alfa.
DrugBank; DB00170; Menadione.
DrugBank; DB13999; Moroctocog alfa.
DrugBank; DB05131; TTP889.
DrugBank; DB09109; Turoctocog alfa.
DrugBank; DB14738; Turoctocog alfa pegol.
GuidetoPHARMACOLOGY; 2364; -.
Allergome; 9616; Hom s Factor IX.
MEROPS; S01.214; -.
GlyConnect; 96; 13 N-Linked glycans, 12 O-Linked glycans (6 sites).
GlyGen; P00740; 10 sites, 23 N-linked glycans (1 site), 16 O-linked glycans (7 sites).
iPTMnet; P00740; -.
PhosphoSitePlus; P00740; -.
BioMuta; F9; -.
CPTAC; non-CPTAC-2647; -.
jPOST; P00740; -.
MassIVE; P00740; -.
PaxDb; P00740; -.
PeptideAtlas; P00740; -.
PRIDE; P00740; -.
ProteomicsDB; 51274; -. [P00740-1]
ABCD; P00740; 2 sequenced antibodies.
Antibodypedia; 367; 909 antibodies from 39 providers.
DNASU; 2158; -.
Ensembl; ENST00000218099; ENSP00000218099; ENSG00000101981.
Ensembl; ENST00000394090; ENSP00000377650; ENSG00000101981. [P00740-2]
GeneID; 2158; -.
KEGG; hsa:2158; -.
MANE-Select; ENST00000218099.7; ENSP00000218099.2; NM_000133.4; NP_000124.1.
UCSC; uc004fas.2; human. [P00740-1]
CTD; 2158; -.
DisGeNET; 2158; -.
GeneCards; F9; -.
GeneReviews; F9; -.
HGNC; HGNC:3551; F9.
HPA; ENSG00000101981; Tissue enriched (liver).
MalaCards; F9; -.
MIM; 300746; gene.
MIM; 300807; phenotype.
MIM; 301052; phenotype.
MIM; 306900; phenotype.
neXtProt; NX_P00740; -.
OpenTargets; ENSG00000101981; -.
Orphanet; 177929; Bleeding disorder in hemophilia B carriers without FIX deficiency.
Orphanet; 169799; Mild hemophilia B.
Orphanet; 169796; Moderate hemophilia B.
Orphanet; 169793; Severe hemophilia B.
PharmGKB; PA27954; -.
VEuPathDB; HostDB:ENSG00000101981; -.
eggNOG; ENOG502QUEV; Eukaryota.
GeneTree; ENSGT00940000159516; -.
HOGENOM; CLU_006842_19_5_1; -.
InParanoid; P00740; -.
OMA; SCTEGYQ; -.
OrthoDB; 1314811at2759; -.
PhylomeDB; P00740; -.
TreeFam; TF327329; -.
BRENDA; 3.4.21.22; 2681.
PathwayCommons; P00740; -.
Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140837; Intrinsic 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-9672383; Defective factor IX causes thrombophilia.
Reactome; R-HSA-9672396; Defective cofactor function of FVIIIa variant.
Reactome; R-HSA-9673202; Defective F9 variant does not activate FX.
Reactome; R-HSA-9673218; Defective F9 secretion.
Reactome; R-HSA-9673221; Defective F9 activation.
Reactome; R-HSA-9673240; Defective gamma-carboxylation of F9.
SABIO-RK; P00740; -.
SignaLink; P00740; -.
SIGNOR; P00740; -.
BioGRID-ORCS; 2158; 22 hits in 662 CRISPR screens.
EvolutionaryTrace; P00740; -.
GeneWiki; Factor_IX; -.
GenomeRNAi; 2158; -.
Pharos; P00740; Tchem.
PRO; PR:P00740; -.
Proteomes; UP000005640; Chromosome X.
RNAct; P00740; protein.
Bgee; ENSG00000101981; Expressed in liver and 43 other tissues.
Genevisible; P00740; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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:0016020; C:membrane; IDA:ComplexPortal.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032991; C:protein-containing complex; IPI:ComplexPortal.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; NAS:BHF-UCL.
GO; GO:0007596; P:blood coagulation; IDA:UniProtKB.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; IDA:ComplexPortal.
GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
GO; GO:0031638; P:zymogen activation; IDA:ComplexPortal.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR035694; Coagulation_factor_IX.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24278:SF31; PTHR24278:SF31; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Direct protein sequencing;
Disease variant; Disulfide bond; EGF-like domain;
Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia; Hemostasis;
Hydrolase; Hydroxylation; Magnesium; Metal-binding; Pharmaceutical;
Phosphoprotein; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Sulfation; Thrombophilia; Zymogen.
SIGNAL 1..28
/evidence="ECO:0000255"
PROPEP 29..46
/evidence="ECO:0000269|PubMed:2592373"
/id="PRO_0000027755"
CHAIN 47..461
/note="Coagulation factor IX"
/id="PRO_0000027756"
CHAIN 47..191
/note="Coagulation factor IXa light chain"
/id="PRO_0000027757"
PROPEP 192..226
/note="Activation peptide"
/id="PRO_0000027758"
CHAIN 227..461
/note="Coagulation factor IXa heavy chain"
/id="PRO_0000027759"
DOMAIN 47..92
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 93..129
/note="EGF-like 1; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 130..171
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 227..459
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
ACT_SITE 267
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:659613"
ACT_SITE 315
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:659613"
ACT_SITE 411
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:659613"
METAL 47
/note="Calcium 1; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 48
/note="Calcium 2"
/evidence="ECO:0000269|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 53
/note="Calcium 1; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 53
/note="Calcium 2; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 54
/note="Calcium 2; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 54
/note="Calcium 3; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 61
/note="Calcium 4; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 61
/note="Magnesium 1; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 63
/note="Calcium 1; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 63
/note="Calcium 2; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 63
/note="Calcium 3; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 66
/note="Calcium 4; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 66
/note="Magnesium 1; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 67
/note="Calcium 1; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 72
/note="Calcium 5; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 72
/note="Magnesium 2; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 73
/note="Calcium 2; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 73
/note="Calcium 3; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 76
/note="Calcium 3; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 76
/note="Calcium 5; via 4-carboxyglutamate"
/evidence="ECO:0000305|PubMed:14722079,
ECO:0007744|PDB:1NL0"
METAL 76
/note="Magnesium 2; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 82
/note="Calcium 6; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 82
/note="Magnesium 3; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 86
/note="Calcium 6; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 86
/note="Magnesium 3; via 4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741"
METAL 93
/note="Calcium 7"
/evidence="ECO:0000269|PubMed:7606779,
ECO:0007744|PDB:1EDM"
METAL 94
/note="Calcium 7; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:7606779,
ECO:0007744|PDB:1EDM"
METAL 96
/note="Calcium 7"
/evidence="ECO:0000269|PubMed:7606779,
ECO:0007744|PDB:1EDM"
METAL 110
/note="Calcium 7"
/evidence="ECO:0000269|PubMed:7606779,
ECO:0007744|PDB:1EDM"
METAL 111
/note="Calcium 7; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:7606779,
ECO:0007744|PDB:1EDM"
METAL 281
/note="Calcium 8"
/evidence="ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH,
ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ,
ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
METAL 283
/note="Calcium 8; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH,
ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ,
ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
METAL 286
/note="Calcium 8; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH,
ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ,
ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
METAL 288
/note="Calcium 8"
/evidence="ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH,
ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ,
ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
METAL 291
/note="Calcium 8"
/evidence="ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG,
ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5"
SITE 191..192
/note="Cleavage; by factor XIa"
SITE 226..227
/note="Cleavage; by factor XIa"
MOD_RES 53
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 54
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 61
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 63
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 66
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 67
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 72
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 73
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 76
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 79
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 82
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 86
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 110
/note="(3R)-3-hydroxyaspartate"
/evidence="ECO:0000269|PubMed:6688526"
MOD_RES 114
/note="Phosphoserine"
/evidence="ECO:0000269|Ref.28"
MOD_RES 201
/note="Sulfotyrosine"
/evidence="ECO:0000269|PubMed:11133752"
MOD_RES 204
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:11133752,
ECO:0000269|PubMed:25456591"
MOD_RES 205
/note="Phosphothreonine; alternate"
/evidence="ECO:0000269|PubMed:25456591"
CARBOHYD 85
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:25456591"
CARBOHYD 99
/note="O-linked (Glc...) serine"
/evidence="ECO:0000269|PubMed:2129367,
ECO:0000269|PubMed:2511201, ECO:0000269|PubMed:25456591"
/id="CAR_000009"
CARBOHYD 107
/note="O-linked (Fuc...) serine"
/evidence="ECO:0000269|PubMed:1517205,
ECO:0000269|PubMed:25456591"
/id="CAR_000010"
CARBOHYD 203
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 205
/note="O-linked (GalNAc...) threonine; alternate"
/evidence="ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:8172892"
CARBOHYD 213
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 215
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:8172892"
CARBOHYD 225
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:25456591"
DISULFID 64..69
/evidence="ECO:0000250|UniProtKB:P00741"
DISULFID 97..108
/evidence="ECO:0000269|PubMed:1304885,
ECO:0000269|PubMed:7606779, ECO:0007744|PDB:1EDM,
ECO:0007744|PDB:1IXA"
DISULFID 102..117
/evidence="ECO:0000269|PubMed:1304885,
ECO:0000269|PubMed:7606779, ECO:0007744|PDB:1EDM,
ECO:0007744|PDB:1IXA"
DISULFID 119..128
/evidence="ECO:0000269|PubMed:1304885,
ECO:0000269|PubMed:7606779, ECO:0007744|PDB:1EDM,
ECO:0007744|PDB:1IXA"
DISULFID 134..145
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPL, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
DISULFID 141..155
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPL, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
DISULFID 157..170
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPL, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
DISULFID 178..335
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPL, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
DISULFID 252..268
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPL, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
DISULFID 382..396
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPL, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
DISULFID 407..435
/evidence="ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN,
ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI,
ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK,
ECO:0007744|PDB:2WPL, ECO:0007744|PDB:2WPM,
ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3,
ECO:0007744|PDB:3LC5"
VAR_SEQ 93..130
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.6"
/id="VSP_047689"
VARIANT 7
/note="I -> F (in dbSNP:rs150190385)"
/evidence="ECO:0000269|PubMed:2773937"
/id="VAR_006520"
VARIANT 17
/note="I -> N (in HEMB; severe; UK 22)"
/id="VAR_006521"
VARIANT 20
/note="L -> S (in HEMB; unknown pathological significance;
decreased protein abundance; decreased function in blood
coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073975"
VARIANT 28
/note="C -> R (in HEMB; moderate; HB130;
dbSNP:rs387906481)"
/id="VAR_006522"
VARIANT 28
/note="C -> Y (in HEMB; decreased protein abundance;
decreased function in blood coagulation)"
/evidence="ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:25251685"
/id="VAR_017343"
VARIANT 30
/note="V -> I (in HEMB)"
/id="VAR_006523"
VARIANT 37
/note="A -> T (in WARFS; reduced affinity of the glutamate
carboxylase for the factor IX precursor; 4.4-fold decreased
in the EC(50) for warfarin; dbSNP:rs367569299)"
/evidence="ECO:0000269|PubMed:29450643,
ECO:0000269|PubMed:8833911, ECO:0000269|PubMed:9233593"
/id="VAR_017307"
VARIANT 37
/note="A -> V (in WARFS; 2.5-fold decreased in the EC(50)
for warfarin; dbSNP:rs1327097914)"
/evidence="ECO:0000269|PubMed:29450643,
ECO:0000269|PubMed:9233593"
/id="VAR_083981"
VARIANT 43
/note="R -> L (in HEMB; severe; Bendorf, Beuten, Gleiwitz;
impairs removal of propeptide; dbSNP:rs1275708479)"
/evidence="ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:9169594"
/id="VAR_006525"
VARIANT 43
/note="R -> Q (in HEMB; severe; San Dimas, Oxford-3,
Strasbourg-2; impairs removal of propeptide;
dbSNP:rs1275708479)"
/evidence="ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:2738071, ECO:0000269|PubMed:3009023,
ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594,
ECO:0000269|PubMed:9600455"
/id="VAR_006524"
VARIANT 43
/note="R -> W (in HEMB; severe; Boxtel, Heiden, Lienen;
impairs removal of propeptide; dbSNP:rs1603264205)"
/evidence="ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9600455"
/id="VAR_006526"
VARIANT 45
/note="K -> N (in HEMB; severe; Seattle E)"
/id="VAR_006527"
VARIANT 46
/note="R -> S (in HEMB; severe; Cambridge; impaired
processing of the propeptide; impaired gamma-carboxylation;
decreased protein abundance; loss of function in blood
coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_006528"
VARIANT 46
/note="R -> T (in HEMB; severe)"
/evidence="ECO:0000269|PubMed:9600455"
/id="VAR_006529"
VARIANT 48
/note="N -> I (in HEMB; severe; Calgary-16)"
/id="VAR_006530"
VARIANT 49
/note="S -> P (in HEMB)"
/id="VAR_006531"
VARIANT 52
/note="L -> S (in HEMB; severe; Gla mutant)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017344"
VARIANT 53
/note="E -> A (in HEMB; severe; Oxford-B2; Gla mutant)"
/id="VAR_006532"
VARIANT 54
/note="E -> D (in HEMB; unknown pathological significance;
no effect on protein abundance; loss of function in blood
coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073976"
VARIANT 54
/note="E -> G (in HEMB; severe; HB151; Gla mutant)"
/id="VAR_006533"
VARIANT 55
/note="F -> C (in HEMB)"
/id="VAR_006534"
VARIANT 58
/note="G -> A (in HEMB; severe; Hong Kong-1)"
/id="VAR_006535"
VARIANT 58
/note="G -> E (in HEMB; unknown pathological significance;
no effect on protein abundance; loss of function in blood
coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073977"
VARIANT 58
/note="G -> R (in HEMB; severe; Los Angeles-4)"
/id="VAR_006536"
VARIANT 62..63
/note="Missing (in HEMB; severe)"
/id="VAR_006537"
VARIANT 66
/note="E -> V (in HEMB; moderate)"
/id="VAR_006538"
VARIANT 67
/note="E -> K (in HEMB; severe; Nagoya-4; Gla mutant;
dbSNP:rs1410080079)"
/id="VAR_006539"
VARIANT 71
/note="F -> S (in HEMB; severe)"
/id="VAR_006540"
VARIANT 73
/note="E -> K (in HEMB; severe; Seattle-3; Gla mutant;
dbSNP:rs137852225)"
/evidence="ECO:0000269|PubMed:2472424"
/id="VAR_006541"
VARIANT 73
/note="E -> V (in HEMB; severe; Chongqing; Gla mutant;
dbSNP:rs137852226)"
/evidence="ECO:0000269|PubMed:2339358"
/id="VAR_006542"
VARIANT 75
/note="R -> Q (in HEMB; mild; dbSNP:rs137852228)"
/evidence="ECO:0000269|PubMed:2773937"
/id="VAR_017308"
VARIANT 79
/note="E -> D (in HEMB; dbSNP:rs137852229)"
/evidence="ECO:0000269|PubMed:2773937"
/id="VAR_017309"
VARIANT 84
/note="T -> R (in HEMB; decreased protein abundance; loss
of function in blood coagulation)"
/evidence="ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:25251685"
/id="VAR_017345"
VARIANT 91
/note="Y -> C (in HEMB; moderate)"
/id="VAR_006543"
VARIANT 93
/note="D -> G (in HEMB; moderate; Alabama;
dbSNP:rs137852230)"
/evidence="ECO:0000269|PubMed:3790720"
/id="VAR_006544"
VARIANT 96
/note="Q -> P (in HEMB; severe; New London;
dbSNP:rs137852231)"
/id="VAR_006545"
VARIANT 97
/note="C -> S (in HEMB)"
/id="VAR_006546"
VARIANT 101
/note="P -> R (in HEMB)"
/id="VAR_006547"
VARIANT 102
/note="C -> R (in HEMB; severe; Basel; dbSNP:rs1603264719)"
/id="VAR_006548"
VARIANT 106
/note="G -> D (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017346"
VARIANT 106
/note="G -> S (in HEMB; mild; Durham; dbSNP:rs137852233)"
/evidence="ECO:0000269|PubMed:2472424,
ECO:0000269|PubMed:9600455"
/id="VAR_006549"
VARIANT 108
/note="C -> S (in HEMB)"
/id="VAR_006550"
VARIANT 110
/note="D -> N (in HEMB; severe; Oxford-D1;
dbSNP:rs137852274)"
/id="VAR_006551"
VARIANT 112
/note="I -> S (in HEMB)"
/id="VAR_006552"
VARIANT 113
/note="N -> K (in HEMB; mild)"
/evidence="ECO:0000269|PubMed:9222764"
/id="VAR_006553"
VARIANT 115
/note="Y -> C (in HEMB; severe; dbSNP:rs1603264727)"
/evidence="ECO:0000269|PubMed:9600455"
/id="VAR_006554"
VARIANT 119
/note="C -> F (in HEMB; severe)"
/id="VAR_006555"
VARIANT 119
/note="C -> R (in HEMB; Iran)"
/evidence="ECO:0000269|PubMed:9452115"
/id="VAR_006556"
VARIANT 124
/note="E -> K (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017347"
VARIANT 125
/note="G -> E (in HEMB)"
/id="VAR_006557"
VARIANT 125
/note="G -> R (in HEMB)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_017348"
VARIANT 125
/note="G -> V (in HEMB)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_006558"
VARIANT 129..130
/note="Missing (in HEMB)"
/id="VAR_006559"
VARIANT 134
/note="C -> Y (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017349"
VARIANT 136
/note="I -> T (in HEMB; mild; dbSNP:rs1603265481)"
/id="VAR_006560"
VARIANT 138
/note="N -> H (in HEMB; unknown pathological significance;
decreased protein abundance; decreased function in blood
coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073978"
VARIANT 139
/note="G -> D (in HEMB; severe; dbSNP:rs1216516070)"
/id="VAR_006561"
VARIANT 139
/note="G -> S (in HEMB)"
/id="VAR_006562"
VARIANT 155
/note="C -> F (in HEMB; severe; dbSNP:rs1330705989)"
/evidence="ECO:0000269|PubMed:9600455"
/id="VAR_006563"
VARIANT 160
/note="G -> E (in HEMB; mild)"
/id="VAR_006564"
VARIANT 167
/note="Q -> H (in HEMB; mild)"
/id="VAR_006565"
VARIANT 169
/note="S -> C (in HEMB)"
/evidence="ECO:0000269|PubMed:11122099"
/id="VAR_017350"
VARIANT 170
/note="C -> F (in HEMB)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_017351"
VARIANT 178
/note="C -> R (in HEMB)"
/id="VAR_006566"
VARIANT 178
/note="C -> W (in HEMB; severe)"
/id="VAR_006567"
VARIANT 191
/note="R -> C (in HEMB; moderate; Albuquerque, Cardiff-1;
dbSNP:rs137852237)"
/evidence="ECO:0000269|PubMed:2775660"
/id="VAR_006569"
VARIANT 191
/note="R -> H (in HEMB; moderate; Chapel-Hill, Chicago-2;
dbSNP:rs137852238)"
/evidence="ECO:0000269|PubMed:6603618,
ECO:0000269|PubMed:8076946"
/id="VAR_006568"
VARIANT 194
/note="T -> A (in dbSNP:rs6048)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:25470321, ECO:0000269|PubMed:2994716,
ECO:0000269|PubMed:3857619, ECO:0000269|PubMed:6329734"
/id="VAR_011773"
VARIANT 226
/note="R -> G (in HEMB; severe; Madrid)"
/evidence="ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:8076946"
/id="VAR_006571"
VARIANT 226
/note="R -> Q (in HEMB; severe; Hilo and Novara; no effect
on protein abundance; loss of function in blood
coagulation; dbSNP:rs137852241)"
/evidence="ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:25251685,
ECO:0000269|PubMed:2713493"
/id="VAR_006572"
VARIANT 226
/note="R -> W (in HEMB; severe; Nagoya-1, Dernbach,
Deventer, Idaho; dbSNP:rs137852240)"
/evidence="ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:2592373"
/id="VAR_006570"
VARIANT 227
/note="V -> D (in HEMB; mild)"
/id="VAR_006573"
VARIANT 227
/note="V -> F (in HEMB; Milano; dbSNP:rs137852242)"
/evidence="ECO:0000269|PubMed:2162822"
/id="VAR_017310"
VARIANT 228
/note="V -> F (in HEMB; severe; Kashihara;
dbSNP:rs137852243)"
/evidence="ECO:0000269|PubMed:2753873"
/id="VAR_017311"
VARIANT 228
/note="V -> L (in HEMB; mild; Cardiff-2;
dbSNP:rs137852243)"
/evidence="ECO:0000269|PubMed:2372509"
/id="VAR_006574"
VARIANT 241
/note="Q -> H (in HEMB; dbSNP:rs1182648920)"
/evidence="ECO:0000269|PubMed:25470321"
/id="VAR_006575"
VARIANT 241
/note="Q -> K (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017352"
VARIANT 252
/note="C -> S (in HEMB; severe; dbSNP:rs267606792)"
/evidence="ECO:0000269|PubMed:1615485"
/id="VAR_017312"
VARIANT 252
/note="C -> Y (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017353"
VARIANT 253
/note="G -> E (in HEMB; severe)"
/id="VAR_006576"
VARIANT 253
/note="G -> R (in HEMB; severe; Luanda;
dbSNP:rs1603267181)"
/evidence="ECO:0000269|PubMed:8257988"
/id="VAR_006577"
VARIANT 265
/note="A -> T (in HEMB; mild)"
/id="VAR_006578"
VARIANT 268
/note="C -> W (in HEMB; moderate; dbSNP:rs137852246)"
/evidence="ECO:0000269|PubMed:2773937"
/id="VAR_017313"
VARIANT 279
/note="A -> T (in HEMB; mild; dbSNP:rs137852247)"
/evidence="ECO:0000269|PubMed:2773937,
ECO:0000269|PubMed:8076946"
/id="VAR_006579"
VARIANT 283
/note="N -> D (in HEMB; severe)"
/id="VAR_006580"
VARIANT 284
/note="Missing (in HEMB; severe; decreased protein
abundance; loss of function in blood coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073979"
VARIANT 286
/note="Missing (in HEMB; severe)"
/id="VAR_006581"
VARIANT 291
/note="E -> V (in HEMB; Monschau; dbSNP:rs137852279)"
/evidence="ECO:0000269|PubMed:1346975"
/id="VAR_017314"
VARIANT 294
/note="R -> G (in HEMB; severe)"
/id="VAR_006582"
VARIANT 294
/note="R -> Q (in HEMB; mild to moderate; Dreihacken,
Penafiel and Seattle-4; dbSNP:rs137852249)"
/evidence="ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:1346975, ECO:0000269|PubMed:2472424,
ECO:0000269|PubMed:7981722, ECO:0000269|PubMed:8257988"
/id="VAR_006583"
VARIANT 296
/note="V -> M (in HEMB; unknown pathological significance;
decreased protein abundance; decreased function in blood
coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073980"
VARIANT 302
/note="H -> R (in HEMB)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_006584"
VARIANT 306
/note="N -> S (in HEMB; mild; dbSNP:rs137852251)"
/evidence="ECO:0000269|PubMed:2773937"
/id="VAR_017315"
VARIANT 316
/note="I -> F (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_006585"
VARIANT 318
/note="L -> R (in HEMB; dbSNP:rs1222227572)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017354"
VARIANT 321
/note="L -> Q (in HEMB; severe)"
/id="VAR_006586"
VARIANT 328
/note="N -> K (in HEMB; unknown pathological significance;
decreased protein abundance; decreased function in blood
coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073981"
VARIANT 328
/note="N -> Y (in HEMB; moderate; decreased protein
abundance; decreased function in blood coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073982"
VARIANT 333
/note="P -> H (in HEMB; severe)"
/id="VAR_006587"
VARIANT 333
/note="P -> T (in HEMB)"
/evidence="ECO:0000269|PubMed:11122099"
/id="VAR_017355"
VARIANT 342
/note="T -> K (in HEMB; mild)"
/id="VAR_006588"
VARIANT 342
/note="T -> M (in HEMB; moderate; dbSNP:rs137852254)"
/evidence="ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:2773937, ECO:0000269|PubMed:9222764"
/id="VAR_006589"
VARIANT 344
/note="I -> L (in HEMB)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_017356"
VARIANT 351
/note="G -> D (in HEMB)"
/id="VAR_006590"
VARIANT 356
/note="W -> C (in HEMB; severe)"
/id="VAR_006591"
VARIANT 357
/note="G -> E (in HEMB; severe; Amagasaki;
dbSNP:rs137852275)"
/evidence="ECO:0000269|PubMed:1958666"
/id="VAR_006592"
VARIANT 357
/note="G -> R (in HEMB; dbSNP:rs137852257)"
/evidence="ECO:0000269|PubMed:2773937"
/id="VAR_017316"
VARIANT 362
/note="K -> E (in HEMB; moderate)"
/id="VAR_006593"
VARIANT 363
/note="G -> W (in HEMB)"
/id="VAR_006594"
VARIANT 366
/note="A -> D (in HEMB)"
/id="VAR_006595"
VARIANT 379
/note="R -> G (in HEMB; moderate; dbSNP:rs137852258)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_006596"
VARIANT 379
/note="R -> Q (in HEMB; severe; Iceland-1, London and
Sesimbra; dbSNP:rs137852259)"
/evidence="ECO:0000269|PubMed:8076946,
ECO:0000269|PubMed:8257988, ECO:0000269|PubMed:9600455"
/id="VAR_006597"
VARIANT 382
/note="C -> Y (in HEMB; dbSNP:rs1303221289)"
/id="VAR_006598"
VARIANT 383
/note="L -> F (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017358"
VARIANT 383
/note="L -> I (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017357"
VARIANT 384
/note="R -> L (in THPH8; factor IX Padua; higher specific
activity than wild-type; dbSNP:rs137852283)"
/evidence="ECO:0000269|PubMed:19846852"
/id="VAR_062999"
VARIANT 387
/note="K -> E (in HEMB; mild)"
/evidence="ECO:0000269|PubMed:9600455"
/id="VAR_006599"
VARIANT 390
/note="I -> F (in HEMB; severe)"
/id="VAR_006600"
VARIANT 394
/note="M -> K (in HEMB)"
/id="VAR_006601"
VARIANT 395
/note="F -> I (in HEMB; dbSNP:rs1175050951)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017359"
VARIANT 395
/note="F -> L (in HEMB; dbSNP:rs1175050951)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_017360"
VARIANT 396
/note="C -> F (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017361"
VARIANT 396
/note="C -> S (in HEMB; severe; dbSNP:rs137852273)"
/id="VAR_006602"
VARIANT 397
/note="A -> P (in HEMB; mild; Hong Kong-11;
dbSNP:rs137852281)"
/evidence="ECO:0000269|PubMed:9590153"
/id="VAR_017317"
VARIANT 404
/note="R -> T (in HEMB)"
/id="VAR_006603"
VARIANT 407
/note="C -> R (in HEMB)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017362"
VARIANT 407
/note="C -> S (in HEMB; severe)"
/id="VAR_006604"
VARIANT 410
/note="D -> H (in HEMB; Mechtal; dbSNP:rs137852278)"
/evidence="ECO:0000269|PubMed:1346975"
/id="VAR_017318"
VARIANT 411
/note="S -> G (in HEMB; Varel; dbSNP:rs137852277)"
/evidence="ECO:0000269|PubMed:1346975"
/id="VAR_017320"
VARIANT 411
/note="S -> I (in HEMB; Schmallenberg; dbSNP:rs137852276)"
/evidence="ECO:0000269|PubMed:1346975"
/id="VAR_017319"
VARIANT 412
/note="G -> E (in HEMB; dbSNP:rs1233706534)"
/evidence="ECO:0000269|PubMed:12588353"
/id="VAR_017363"
VARIANT 413
/note="G -> R (in HEMB; moderate to severe;
dbSNP:rs1306658513)"
/evidence="ECO:0000269|PubMed:7981722,
ECO:0000269|PubMed:9222764"
/id="VAR_006605"
VARIANT 414
/note="P -> T (in HEMB; Bergamo; increased protein
abundance; loss of function in blood coagulation;
dbSNP:rs137852265)"
/evidence="ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:25251685"
/id="VAR_017321"
VARIANT 419
/note="V -> E (in HEMB; moderately severe;
dbSNP:rs137852280)"
/evidence="ECO:0000269|PubMed:8076946,
ECO:0000269|PubMed:8199596"
/id="VAR_006606"
VARIANT 424
/note="F -> V (in HEMB)"
/evidence="ECO:0000269|PubMed:9222764"
/id="VAR_006607"
VARIANT 426
/note="T -> P (in HEMB; severe; Barcelos)"
/evidence="ECO:0000269|PubMed:8257988"
/id="VAR_006608"
VARIANT 430
/note="S -> T (in HEMB)"
/id="VAR_006609"
VARIANT 431
/note="W -> G (in HEMB)"
/id="VAR_006610"
VARIANT 431
/note="W -> R (in HEMB; moderate)"
/id="VAR_006611"
VARIANT 432
/note="G -> S (in HEMB; severe; dbSNP:rs1170838100)"
/id="VAR_006612"
VARIANT 432
/note="G -> V (in HEMB; severe)"
/evidence="ECO:0000269|PubMed:9600455"
/id="VAR_006613"
VARIANT 433
/note="E -> A (in HEMB)"
/id="VAR_006614"
VARIANT 433
/note="E -> K (in HEMB; dbSNP:rs767828752)"
/id="VAR_006615"
VARIANT 435
/note="C -> Y (in HEMB; dbSNP:rs1385141619)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_017364"
VARIANT 436
/note="A -> V (in HEMB; moderately severe; Niigata;
dbSNP:rs137852266)"
/evidence="ECO:0000269|PubMed:3243764"
/id="VAR_006616"
VARIANT 442
/note="G -> E (in HEMB; dbSNP:rs1603267474)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_017365"
VARIANT 442
/note="G -> R (in HEMB; severe; Angers; dbSNP:rs137852267)"
/evidence="ECO:0000269|PubMed:2714791"
/id="VAR_017322"
VARIANT 443
/note="I -> T (in HEMB; moderately severe; Long Beach, Los
Angeles and Vancouver; dbSNP:rs137852268)"
/evidence="ECO:0000269|PubMed:1902289,
ECO:0000269|PubMed:3401602"
/id="VAR_017323"
VARIANT 445
/note="T -> TIYT (in HEMB; severe; Lousada)"
/id="VAR_006617"
VARIANT 447
/note="V -> VYTKV (in HEMB; reduced protein abundance; loss
of function in blood coagulation)"
/evidence="ECO:0000269|PubMed:25251685"
/id="VAR_073983"
VARIANT 449
/note="R -> Q (in HEMB; mild; dbSNP:rs143018900)"
/evidence="ECO:0000269|PubMed:8076946"
/id="VAR_006618"
VARIANT 449
/note="R -> W (in HEMB; mild; dbSNP:rs757996262)"
/evidence="ECO:0000269|PubMed:12604421"
/id="VAR_006619"
VARIANT 450
/note="Y -> C (in HEMB; severe; dbSNP:rs1243180674)"
/evidence="ECO:0000269|PubMed:9600455"
/id="VAR_006620"
VARIANT 453
/note="W -> R (in HEMB; dbSNP:rs137852269)"
/evidence="ECO:0000269|PubMed:2773937"
/id="VAR_017324"
VARIANT 454
/note="I -> T (in HEMB; Italy; dbSNP:rs1603267486)"
/evidence="ECO:0000269|PubMed:9452115"
/id="VAR_006621"
VARIANT 461
/note="T -> P (in dbSNP:rs4149751)"
/evidence="ECO:0000269|Ref.7"
/id="VAR_014308"
MUTAGEN 305
/note="Y->F: Strongly increases enzyme activity with a
synthetic peptide substrate; when associated with T-311; A-
365 and T-391."
/evidence="ECO:0000269|PubMed:12444082"
MUTAGEN 311
/note="K->T: Strongly increases enzyme activity with a
synthetic peptide substrate; when associated with F-305; A-
365 and T-391."
/evidence="ECO:0000269|PubMed:12444082"
MUTAGEN 312
/note="Y->A: Strongly decreases enzyme activity with a
synthetic peptide substrate."
/evidence="ECO:0000269|PubMed:12444082"
MUTAGEN 391
/note="Y->T: Strongly increases enzyme activity with a
synthetic peptide substrate; when associated with F-305; T-
311 and A-365."
/evidence="ECO:0000269|PubMed:12444082"
STRAND 50..52
/evidence="ECO:0007829|PDB:1NL0"
HELIX 60..64
/evidence="ECO:0007829|PDB:1NL0"
STRAND 65..67
/evidence="ECO:0007829|PDB:1CFH"
HELIX 71..75
/evidence="ECO:0007829|PDB:1NL0"
STRAND 78..80
/evidence="ECO:0007829|PDB:1NL0"
HELIX 81..90
/evidence="ECO:0007829|PDB:1NL0"
TURN 96..99
/evidence="ECO:0007829|PDB:1EDM"
STRAND 102..105
/evidence="ECO:0007829|PDB:4WMA"
STRAND 107..111
/evidence="ECO:0007829|PDB:1EDM"
STRAND 114..118
/evidence="ECO:0007829|PDB:1EDM"
TURN 125..128
/evidence="ECO:0007829|PDB:4WMA"
TURN 134..136
/evidence="ECO:0007829|PDB:6MV4"
HELIX 137..140
/evidence="ECO:0007829|PDB:5JB9"
STRAND 142..148
/evidence="ECO:0007829|PDB:5JB9"
TURN 149..151
/evidence="ECO:0007829|PDB:5JB9"
STRAND 152..156
/evidence="ECO:0007829|PDB:5JB9"
STRAND 161..163
/evidence="ECO:0007829|PDB:5JB9"
STRAND 165..168
/evidence="ECO:0007829|PDB:2WPI"
STRAND 170..172
/evidence="ECO:0007829|PDB:5JB9"
STRAND 174..176
/evidence="ECO:0007829|PDB:5JB9"
STRAND 187..189
/evidence="ECO:0007829|PDB:2WPJ"
STRAND 241..248
/evidence="ECO:0007829|PDB:5JB9"
STRAND 252..258
/evidence="ECO:0007829|PDB:5JB9"
STRAND 261..264
/evidence="ECO:0007829|PDB:5JB9"
HELIX 266..268
/evidence="ECO:0007829|PDB:5JB9"
STRAND 269..271
/evidence="ECO:0007829|PDB:5JB9"
STRAND 276..280
/evidence="ECO:0007829|PDB:5JB9"
STRAND 282..286
/evidence="ECO:0007829|PDB:6MV4"
STRAND 292..301
/evidence="ECO:0007829|PDB:5JB9"
TURN 303..306
/evidence="ECO:0007829|PDB:5JB9"
STRAND 307..310
/evidence="ECO:0007829|PDB:5JB9"
TURN 311..314
/evidence="ECO:0007829|PDB:5TNT"
STRAND 317..323
/evidence="ECO:0007829|PDB:5JB9"
HELIX 339..347
/evidence="ECO:0007829|PDB:5JB9"
STRAND 350..360
/evidence="ECO:0007829|PDB:5JB9"
STRAND 370..377
/evidence="ECO:0007829|PDB:5JB9"
HELIX 379..384
/evidence="ECO:0007829|PDB:5JB9"
STRAND 394..398
/evidence="ECO:0007829|PDB:5JB9"
STRAND 400..403
/evidence="ECO:0007829|PDB:6MV4"
STRAND 414..419
/evidence="ECO:0007829|PDB:5JB9"
STRAND 422..431
/evidence="ECO:0007829|PDB:5JB9"
STRAND 433..436
/evidence="ECO:0007829|PDB:5JB9"
STRAND 442..446
/evidence="ECO:0007829|PDB:5JB9"
HELIX 447..450
/evidence="ECO:0007829|PDB:5JB9"
HELIX 451..457
/evidence="ECO:0007829|PDB:5JB9"
SEQUENCE 461 AA; 51778 MW; C4720C1234477EF5 CRC64;
MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL
ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP
FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR
VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW
QVVLNGKVDA FCGGSIVNEK WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRII
PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF
HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE
GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T


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WP1983: Splicing factor NOVA regulated synpatic proteins
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP2148: Brain derived neurotrophic factor
WP938: Complement and Coagulation Cascades
WP1172: Complement and Coagulation Cascades
WP449: Complement and Coagulation Cascades
WP558: Complement and Coagulation Cascades
WP2328: Allograft rejection
WP1056: Complement and Coagulation Cascades
WP547: Complement and Coagulation Cascades
WP820: Complement and Coagulation Cascades
WP1647: Fatty acid biosynthesis
WP1002: Electron Transport Chain

Related Genes :
[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]
[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]
[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]
[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]
[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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII 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]
[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)]
[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]
[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]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light 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]
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B heavy chain]
[] 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]
[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]
[] Coagulation factor X-activating enzyme heavy chain (EC 3.4.24.58) (Coagulation factor X-activating enzyme chain alpha) (Snake venom metalloproteinase) (SVMP) (VL factor X activator) (VLFXA heavy chain) [Cleaved into: Coagulation factor X-activating enzyme heavy chain alternate form]
[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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[KLKB1 KLK3] Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) (PKK) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light 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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F3] Tissue factor (TF) (Coagulation factor III) (Thromboplastin) (CD antigen CD142)
[F13A1 F13A] Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A chain)

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