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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]

 FA11_HUMAN              Reviewed;         625 AA.
P03951; D3DP64; Q4W5C2; Q9Y495;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
23-OCT-1986, sequence version 1.
23-FEB-2022, entry version 239.
RecName: Full=Coagulation factor XI;
Short=FXI;
EC=3.4.21.27;
AltName: Full=Plasma thromboplastin antecedent;
Short=PTA;
Contains:
RecName: Full=Coagulation factor XIa heavy chain;
Contains:
RecName: Full=Coagulation factor XIa light chain;
Flags: Precursor;
Name=F11;
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).
PubMed=3636155; DOI=10.1021/bi00357a018;
Fujikawa K., Chung D.W., Hendrickson L.E., Davie E.W.;
"Amino acid sequence of human factor XI, a blood coagulation factor with
four tandem repeats that are highly homologous with plasma prekallikrein.";
Biochemistry 25:2417-2424(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=2827746; DOI=10.1021/bi00397a004;
Asakai R., Davie E.W., Chung D.W.;
"Organization of the gene for human factor XI.";
Biochemistry 26:7221-7228(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9593722; DOI=10.1074/jbc.273.22.13787;
Hsu T.-C., Shore S.K., Seshsmma T., Bagasra O., Walsh P.N.;
"Molecular cloning of platelet factor XI, an alternative splicing product
of the plasma factor XI gene.";
J. Biol. Chem. 273:13787-13793(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-339.
SeattleSNPs variation discovery resource;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[8]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=1998667; DOI=10.1021/bi00222a008;
McMullen B.A., Fujikawa K., Davie E.W.;
"Location of the disulfide bonds in human coagulation factor XI: the
presence of tandem apple domains.";
Biochemistry 30:2056-2060(1991).
[9]
ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=2844223; DOI=10.1021/bi00412a005;
Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M.,
Bouma B.N.;
"Inactivation of human plasma kallikrein and factor XIa by protein C
inhibitor.";
Biochemistry 27:4231-4237(1988).
[10]
HEPARIN-BINDING SITE.
PubMed=11412111; DOI=10.1021/bi0027433;
Badellino K.O., Walsh P.N.;
"Localization of a heparin binding site in the catalytic domain of factor
XIa.";
Biochemistry 40:7569-7580(2001).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-450 AND ASN-491.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-491.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple
enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
GLYCOSYLATION AT ASN-90; ASN-126; ASN-163; ASN-450 AND ASN-491, PARTIAL
PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND STRUCTURE OF
CARBOHYDRATES.
PubMed=25092234; DOI=10.1002/pmic.201400038;
Faid V., Denguir N., Chapuis V., Bihoreau N., Chevreux G.;
"Site-specific N-glycosylation analysis of human factor XI: Identification
of a noncanonical NXC glycosite.";
Proteomics 14:2460-2470(2014).
[14]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 388-625 IN COMPLEX WITH INHIBITOR,
AND DISULFIDE BONDS.
PubMed=18510371; DOI=10.1021/jm800314b;
Buchanan M.S., Carroll A.R., Wessling D., Jobling M., Avery V.M.,
Davis R.A., Feng Y., Xue Y., Oster L., Fex T., Deinum J., Hooper J.N.,
Quinn R.J.;
"Clavatadine A, a natural product with selective recognition and
irreversible inhibition of factor XIa.";
J. Med. Chem. 51:3583-3587(2008).
[15]
VARIANT FA11D LEU-301.
PubMed=2813350; DOI=10.1073/pnas.86.20.7667;
Asakai R., Chung D.W., Ratnoff O.D., Davie E.W.;
"Factor XI (plasma thromboplastin antecedent) deficiency in Ashkenazi Jews
is a bleeding disorder that can result from three types of point
mutations.";
Proc. Natl. Acad. Sci. U.S.A. 86:7667-7671(1989).
[16]
VARIANT FA11D LEU-301.
PubMed=1547342;
Meijers J.C., Davie E.W., Chung D.W.;
"Expression of human blood coagulation factor XI: characterization of the
defect in factor XI type III deficiency.";
Blood 79:1435-1440(1992).
[17]
VARIANTS FA11D HIS-34; PRO-320; ILE-322 AND LYS-341.
PubMed=7888672;
Pugh R.E., McVey J.H., Tuddenham E.G., Hancock J.F.;
"Six point mutations that cause factor XI deficiency.";
Blood 85:1509-1516(1995).
[18]
VARIANT FA11D VAL-460.
PubMed=7669672; DOI=10.1111/j.1365-2141.1995.tb05215.x;
Imanaka Y., Lal K., Nishimura T., Bolton-Maggs P.H., Tuddenham E.G.,
McVey J.H.;
"Identification of two novel mutations in non-Jewish factor XI
deficiency.";
Br. J. Haematol. 90:916-920(1995).
[19]
VARIANT FA11D ASN-404.
PubMed=9401068; DOI=10.1046/j.1365-2141.1997.4343244.x;
Wistinghausen B., Reischer A., Oddoux C., Ostrer H., Nardi M.,
Karpatkin M.;
"Severe factor XI deficiency in an Arab family associated with a novel
mutation in exon 11.";
Br. J. Haematol. 99:575-577(1997).
[20]
VARIANT FA11D ASN-266, AND VARIANT ARG-244.
PubMed=9787168;
Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A.,
Gailani D.;
"Identification of mutations and polymorphisms in the factor XI genes of an
African American family by dideoxyfingerprinting.";
Blood 92:3309-3317(1998).
[21]
ERRATUM OF PUBMED:9787168.
Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A.,
Gailani D.;
Blood 93:1786-1786(1999).
[22]
VARIANT FA11D CYS-246.
PubMed=10027710; DOI=10.1046/j.1365-2141.1999.01150.x;
Alhaq A., Mitchell M., Sethi M., Rahman S., Flynn G., Boulton P., Caeno G.,
Smith M., Savidge G.;
"Identification of a novel mutation in a non-Jewish factor XI deficient
kindred.";
Br. J. Haematol. 104:44-49(1999).
[23]
VARIANTS FA11D CYS-326; VAL-430 ILE-493 AND ARG-594.
PubMed=10606881; DOI=10.1046/j.1365-2141.1999.01769.x;
Mitchell M., Cutler J., Thompson S., Moore G., Jenkins Ap Rees E.,
Smith M., Savidge G., Alhaq A.;
"Heterozygous factor XI deficiency associated with three novel mutations.";
Br. J. Haematol. 107:763-765(1999).
[24]
VARIANTS LEU-66; ARG-244; PHE-308 AND PHE-339.
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).
[25]
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).
[26]
VARIANTS FA11D ARG-56; TYR-255 AND HIS-511, VARIANT PHE-339, AND
CHARACTERIZATION OF VARIANTS FA11D ARG-56; TYR-255 AND HIS-511.
PubMed=11895778; DOI=10.1182/blood.v99.7.2448;
Zivelin A., Bauduer F., Ducout L., Peretz H., Rosenberg N., Yatuv R.,
Seligsohn U.;
"Factor XI deficiency in French Basques is caused predominantly by an
ancestral Cys38Arg mutation in the factor XI gene.";
Blood 99:2448-2454(2002).
[27]
VARIANTS FA11D VAL-418 AND SER-587, AND CHARACTERIZATION OF VARIANTS FA11D
VAL-418 AND SER-587.
PubMed=15026311; DOI=10.1182/blood-2003-10-3530;
Kravtsov D.V., Wu W., Meijers J.C.M., Sun M.-F., Blinder M.A., Dang T.P.,
Wang H., Gailani D.;
"Dominant factor XI deficiency caused by mutations in the factor XI
catalytic domain.";
Blood 104:128-134(2004).
[28]
VARIANT FA11D ILE-270, AND CHARACTERIZATION OF VARIANT F11 DEFICIENCY
ILE-270.
PubMed=15180874; DOI=10.1111/j.1365-2141.2004.04979.x;
Dai L., Mitchell M., Carson P., Creagh D., Cutler J., Savidge G., Alhaq A.;
"Severe factor XI deficiency caused by compound heterozygosity.";
Br. J. Haematol. 125:817-818(2004).
[29]
VARIANTS FA11D PHE-46; ARG-101; CYS-151; GLU-263; VAL-430; LEU-538; LYS-565
AND SER-618.
PubMed=15953011; DOI=10.1111/j.1365-2141.2005.05536.x;
Hill M., McLeod F., Franks H., Gordon B., Dolan G.;
"Genetic analysis in FXI deficiency: six novel mutations and the use of a
polymerase chain reaction-based test to define a whole gene deletion.";
Br. J. Haematol. 129:825-829(2005).
[30]
VARIANTS FA11D TYR-140; LYS-315 AND LYS-597.
PubMed=16607084; DOI=10.1097/01.mbc.0000198054.50257.96;
Quelin F., Mathonnet F., Potentini-Esnault C., Trigui N., Peynet J.,
Bastenaire B., Guillon L., Bigel M.L., Sauger A., Mazurier C.,
de Mazancourt P.;
"Identification of five novel mutations in the factor XI gene (F11) of
patients with factor XI deficiency.";
Blood Coagul. Fibrinolysis 17:69-73(2006).
[31]
VARIANTS FA11D ILE-51; PRO-51; ILE-331; PRO-360; PRO-503 AND HIS-608.
PubMed=18005151; DOI=10.1111/j.1365-2516.2007.01593.x;
Fard-Esfahani P., Lari G.R., Ravanbod S., Mirkhani F., Allahyari M.,
Rassoulzadegan M., Ala F.;
"Seven novel point mutations in the F11 gene in Iranian FXI-deficient
patients.";
Haemophilia 14:91-95(2008).
[32]
VARIANTS FA11D ARG-32; GLN-53; THR-252; ARG-401 AND GLU-526.
PubMed=21668437; DOI=10.1111/j.1399-0004.2011.01732.x;
Kim J., Song J., Lyu C., Kim Y., Oh S., Choi Y., Yoo J., Choi J., Kim H.,
Lee K.A.;
"Population-specific spectrum of the F11 mutations in Koreans: evidence for
a founder effect.";
Clin. Genet. 82:180-186(2012).
[33]
VARIANTS FA11D THR-43; LEU-241 AND MET-403, AND CHARACTERIZATION OF
VARIANTS FA11D THR-43; LEU-241 AND MET-403.
PubMed=21457405; DOI=10.1111/j.1365-2516.2011.02519.x;
Dai L., Rangarajan S., Mitchell M.;
"Three dominant-negative mutations in factor XI-deficient patients.";
Haemophilia 17:E919-E922(2011).
[34]
VARIANT FA11D GLY-506.
PubMed=22016685; DOI=10.3343/kjlm.2011.31.4.290;
Lee J.H., Cho H.S., Hyun M.S., Kim H.Y., Kim H.J.;
"A novel missense mutation Asp506Gly in exon 13 of the F11 gene in an
asymptomatic Korean woman with mild factor XI deficiency.";
Korean J. Lab. Med. 31:290-293(2011).
[35]
VARIANT FA11D SER-481.
PubMed=22322133; DOI=10.1097/mbc.0b013e32834ea02a;
Tirefort Y., Uhr M.R., Neerman-Arbez M., de Moerloose P.;
"Identification of a novel F11 missense mutation (Ile463Ser) in a family
with congenital factor XI deficiency.";
Blood Coagul. Fibrinolysis 23:251-252(2012).
[36]
VARIANT FA11D LYS-454.
PubMed=21999818; DOI=10.1111/j.1600-0609.2011.01723.x;
Girolami A., Scarparo P., Bonamigo E., Santarossa L., Cristiani A.,
Moro S., Lombardi A.M.;
"A cluster of factor XI-deficient patients due to a new mutation (Ile 436
Lys) in northeastern Italy.";
Eur. J. Haematol. 88:229-236(2012).
[37]
VARIANTS FA11D PRO-51; ARG-56; VAL-63; TYR-222; GLN-228; CYS-276; ASP-277;
PHE-514; LEU-575 AND LYS-597.
PubMed=22159456; DOI=10.1160/th11-06-0415;
Gueguen P., Chauvin A., Quemener-Redon S., Pan-Petesch B., Ferec C.,
Abgrall J.F., Le Marechal C.;
"Revisiting the molecular epidemiology of factor XI deficiency: nine new
mutations and an original large 4qTer deletion in western Brittany
(France).";
Thromb. Haemost. 107:44-50(2012).
[38]
VARIANTS FA11D SER-30; THR-109; ASN-216; LYS-315; LYS-543 AND ARG-552.
PubMed=25158988; DOI=10.1097/mbc.0000000000000185;
Keskin E.Y., Guersel T., Kaya Z., Dai L., Kocak U., Yenicesu I.,
Belen F.B., Mitchell M.;
"Molecular basis and bleeding manifestations of factor XI deficiency in 11
Turkish families.";
Blood Coagul. Fibrinolysis 26:63-68(2015).
-!- FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway
of blood coagulation by activating factor IX.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor
IX to form factor IXa.; EC=3.4.21.27;
-!- ACTIVITY REGULATION: Inhibited by SERPINA5.
{ECO:0000269|PubMed:2844223}.
-!- SUBUNIT: Homodimer; disulfide-linked. Forms a heterodimer with
SERPINA5. After activation the heavy and light chains are also linked
by a disulfide bond. {ECO:0000269|PubMed:18510371,
ECO:0000269|PubMed:1998667}.
-!- INTERACTION:
P03951; P23827: eco; Xeno; NbExp=3; IntAct=EBI-1041019, EBI-1029159;
P03951-1; P03951-1: F11; NbExp=5; IntAct=EBI-15583061, EBI-15583061;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P03951-1; Sequence=Displayed;
Name=2; Synonyms=Platelet;
IsoId=P03951-2; Sequence=VSP_005388;
-!- TISSUE SPECIFICITY: Isoform 2 is produced by platelets and
megakaryocytes but absent from other blood cells.
-!- PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist
of nonfucosylated sialylated biantennary (in high abundance) and/or
triantennary (in low abundance) complex structures. Glycosylation at
Asn-163 uses a rare non-canonical Asn-X-Cys glycosite.
{ECO:0000269|PubMed:25092234}.
-!- PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide
after Arg-387 into the light chain, which contains the active site, and
the heavy chain, which associates with high molecular weight (HMW)
kininogen.
-!- DISEASE: Factor XI deficiency (FA11D) [MIM:612416]: A hemorrhagic
disease characterized by reduced levels and activity of factor XI
resulting in moderate bleeding symptoms, usually occurring after trauma
or surgery. Patients usually do not present spontaneous bleeding but
women can present with menorrhagia. Hemorrhages are usually moderate.
{ECO:0000269|PubMed:10027710, ECO:0000269|PubMed:10606881,
ECO:0000269|PubMed:11895778, ECO:0000269|PubMed:15026311,
ECO:0000269|PubMed:15180874, ECO:0000269|PubMed:1547342,
ECO:0000269|PubMed:15953011, ECO:0000269|PubMed:16607084,
ECO:0000269|PubMed:18005151, ECO:0000269|PubMed:21457405,
ECO:0000269|PubMed:21668437, ECO:0000269|PubMed:21999818,
ECO:0000269|PubMed:22016685, ECO:0000269|PubMed:22159456,
ECO:0000269|PubMed:22322133, ECO:0000269|PubMed:25158988,
ECO:0000269|PubMed:2813350, ECO:0000269|PubMed:7669672,
ECO:0000269|PubMed:7888672, ECO:0000269|PubMed:9401068,
ECO:0000269|PubMed:9787168}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor XI entry;
URL="https://en.wikipedia.org/wiki/Factor_XI";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f11/";
-!- WEB RESOURCE: Name=Mendelian genes Coagulation factor XI (F11);
Note=Leiden Open Variation Database (LOVD);
URL="https://databases.lovd.nl/shared/genes/F11";
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EMBL; M13142; AAA52487.1; -; mRNA.
EMBL; M20218; AAA51985.1; -; Genomic_DNA.
EMBL; M18296; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M21184; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M18298; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M18299; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M18300; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M18301; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M18302; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M18303; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M18304; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M19417; AAA51985.1; JOINED; Genomic_DNA.
EMBL; M20217; AAA51985.1; JOINED; Genomic_DNA.
EMBL; AF045649; AAC24506.1; -; mRNA.
EMBL; AY191837; AAN85554.1; -; Genomic_DNA.
EMBL; AC110771; AAY40901.1; -; Genomic_DNA.
EMBL; CH471056; EAX04621.1; -; Genomic_DNA.
EMBL; BC119014; AAI19015.1; -; mRNA.
EMBL; BC122863; AAI22864.1; -; mRNA.
CCDS; CCDS3847.1; -. [P03951-1]
PIR; A27431; KFHU1.
RefSeq; NP_000119.1; NM_000128.3. [P03951-1]
PDB; 1XX9; X-ray; 2.20 A; A/B=388-625.
PDB; 1XXD; X-ray; 2.91 A; A/B=388-625.
PDB; 1XXF; X-ray; 2.60 A; A/B=388-625.
PDB; 1ZHM; X-ray; 1.96 A; A=388-624.
PDB; 1ZHP; X-ray; 2.70 A; A=388-625.
PDB; 1ZHR; X-ray; 1.73 A; A=388-625.
PDB; 1ZJD; X-ray; 2.60 A; A=388-624.
PDB; 1ZLR; X-ray; 2.50 A; A=388-624.
PDB; 1ZMJ; X-ray; 2.00 A; A=388-624.
PDB; 1ZML; X-ray; 2.25 A; A=388-625.
PDB; 1ZMN; X-ray; 2.05 A; A=388-625.
PDB; 1ZOM; X-ray; 2.25 A; A=388-624.
PDB; 1ZPB; X-ray; 2.10 A; A=388-624.
PDB; 1ZPC; X-ray; 2.60 A; A=388-624.
PDB; 1ZPZ; X-ray; 2.50 A; A=388-625.
PDB; 1ZRK; X-ray; 2.30 A; A=388-625.
PDB; 1ZSJ; X-ray; 1.90 A; A=388-625.
PDB; 1ZSK; X-ray; 1.90 A; A=388-625.
PDB; 1ZSL; X-ray; 2.05 A; A=388-625.
PDB; 1ZTJ; X-ray; 2.05 A; A=388-624.
PDB; 1ZTK; X-ray; 2.50 A; A=388-624.
PDB; 1ZTL; X-ray; 2.60 A; A=388-624.
PDB; 2F83; X-ray; 2.87 A; A=1-625.
PDB; 2FDA; X-ray; 2.00 A; A=388-625.
PDB; 2J8J; NMR; -; A/B=290-379.
PDB; 2J8L; NMR; -; A/B=290-379.
PDB; 3BG8; X-ray; 1.60 A; A=388-625.
PDB; 3SOR; X-ray; 1.80 A; A=388-625.
PDB; 3SOS; X-ray; 2.58 A; A=388-625.
PDB; 4CR5; X-ray; 2.00 A; A=388-625.
PDB; 4CR9; X-ray; 1.70 A; A=388-625.
PDB; 4CRA; X-ray; 1.80 A; A=388-625.
PDB; 4CRB; X-ray; 1.85 A; A=388-625.
PDB; 4CRC; X-ray; 1.60 A; A=388-625.
PDB; 4CRD; X-ray; 2.10 A; A=388-625.
PDB; 4CRE; X-ray; 1.73 A; A=388-625.
PDB; 4CRF; X-ray; 2.30 A; A=388-625.
PDB; 4CRG; X-ray; 1.25 A; A=388-625.
PDB; 4D76; X-ray; 1.77 A; A=388-625.
PDB; 4D7F; X-ray; 1.62 A; A=388-625.
PDB; 4D7G; X-ray; 2.33 A; A=388-625.
PDB; 4NA7; X-ray; 2.80 A; A=388-625.
PDB; 4NA8; X-ray; 2.30 A; A=388-625.
PDB; 4TY6; X-ray; 1.85 A; A=388-625, H=375-387.
PDB; 4TY7; X-ray; 2.09 A; A=388-625.
PDB; 4WXI; X-ray; 2.60 A; A=388-625.
PDB; 4X6M; X-ray; 2.40 A; A=388-625.
PDB; 4X6N; X-ray; 2.10 A; A=388-625, H=375-387.
PDB; 4X6O; X-ray; 2.10 A; A=388-625.
PDB; 4X6P; X-ray; 1.93 A; A/B=388-625.
PDB; 4Y8X; X-ray; 1.90 A; A=388-625.
PDB; 4Y8Y; X-ray; 2.60 A; A=388-625.
PDB; 4Y8Z; X-ray; 2.20 A; A=388-625.
PDB; 5E2O; X-ray; 2.08 A; A=388-625.
PDB; 5E2P; X-ray; 2.11 A; A=388-625.
PDB; 5EOD; X-ray; 3.10 A; A=20-625.
PDB; 5EOK; X-ray; 2.80 A; A=20-625.
PDB; 5EXL; X-ray; 2.30 A; A=388-625.
PDB; 5EXM; X-ray; 2.09 A; A=388-625.
PDB; 5EXN; X-ray; 1.49 A; A=388-625.
PDB; 5I25; X-ray; 2.85 A; A=19-625.
PDB; 5Q0D; X-ray; 2.12 A; A=388-625.
PDB; 5Q0E; X-ray; 2.12 A; A=388-625.
PDB; 5Q0F; X-ray; 2.12 A; A=388-625.
PDB; 5Q0G; X-ray; 2.60 A; A=388-625.
PDB; 5Q0H; X-ray; 2.50 A; A=388-625.
PDB; 5QCK; X-ray; 2.64 A; A=388-625.
PDB; 5QCL; X-ray; 2.11 A; A=388-625.
PDB; 5QCM; X-ray; 2.20 A; A=388-625.
PDB; 5QCN; X-ray; 2.30 A; A=388-625.
PDB; 5QQO; X-ray; 2.00 A; A=388-625.
PDB; 5QQP; X-ray; 2.08 A; A=388-625.
PDB; 5QTT; X-ray; 2.23 A; A=388-625.
PDB; 5QTV; X-ray; 2.20 A; A=388-625.
PDB; 5QTW; X-ray; 2.12 A; A=388-625.
PDB; 5QTY; X-ray; 1.89 A; A=388-625.
PDB; 5TKS; X-ray; 1.55 A; A=388-625.
PDB; 5TKT; X-ray; 2.12 A; A=388-625.
PDB; 5TKU; X-ray; 2.12 A; A=388-625.
PDB; 5WB6; X-ray; 2.35 A; A=388-625.
PDB; 6AOD; X-ray; 1.80 A; C=388-624.
PDB; 6C0S; X-ray; 2.35 A; A=388-625.
PDB; 6HHC; X-ray; 2.70 A; A=388-625.
PDB; 6I58; X-ray; 2.60 A; A=19-625.
PDB; 6R8X; X-ray; 2.04 A; A=388-625.
PDB; 6TS4; X-ray; 1.17 A; A=388-625.
PDB; 6TS5; X-ray; 1.29 A; A=388-625.
PDB; 6TS6; X-ray; 1.33 A; A=388-625.
PDB; 6TS7; X-ray; 2.63 A; A=388-625.
PDB; 6TWB; X-ray; 2.91 A; A/H=375-625.
PDB; 6USY; X-ray; 1.26 A; A=388-625.
PDB; 6VLU; X-ray; 1.60 A; A=388-625.
PDB; 6VLV; X-ray; 1.72 A; A=388-625.
PDB; 6W50; X-ray; 1.95 A; A=388-625.
PDB; 7MBO; X-ray; 0.92 A; A=388-625.
PDBsum; 1XX9; -.
PDBsum; 1XXD; -.
PDBsum; 1XXF; -.
PDBsum; 1ZHM; -.
PDBsum; 1ZHP; -.
PDBsum; 1ZHR; -.
PDBsum; 1ZJD; -.
PDBsum; 1ZLR; -.
PDBsum; 1ZMJ; -.
PDBsum; 1ZML; -.
PDBsum; 1ZMN; -.
PDBsum; 1ZOM; -.
PDBsum; 1ZPB; -.
PDBsum; 1ZPC; -.
PDBsum; 1ZPZ; -.
PDBsum; 1ZRK; -.
PDBsum; 1ZSJ; -.
PDBsum; 1ZSK; -.
PDBsum; 1ZSL; -.
PDBsum; 1ZTJ; -.
PDBsum; 1ZTK; -.
PDBsum; 1ZTL; -.
PDBsum; 2F83; -.
PDBsum; 2FDA; -.
PDBsum; 2J8J; -.
PDBsum; 2J8L; -.
PDBsum; 3BG8; -.
PDBsum; 3SOR; -.
PDBsum; 3SOS; -.
PDBsum; 4CR5; -.
PDBsum; 4CR9; -.
PDBsum; 4CRA; -.
PDBsum; 4CRB; -.
PDBsum; 4CRC; -.
PDBsum; 4CRD; -.
PDBsum; 4CRE; -.
PDBsum; 4CRF; -.
PDBsum; 4CRG; -.
PDBsum; 4D76; -.
PDBsum; 4D7F; -.
PDBsum; 4D7G; -.
PDBsum; 4NA7; -.
PDBsum; 4NA8; -.
PDBsum; 4TY6; -.
PDBsum; 4TY7; -.
PDBsum; 4WXI; -.
PDBsum; 4X6M; -.
PDBsum; 4X6N; -.
PDBsum; 4X6O; -.
PDBsum; 4X6P; -.
PDBsum; 4Y8X; -.
PDBsum; 4Y8Y; -.
PDBsum; 4Y8Z; -.
PDBsum; 5E2O; -.
PDBsum; 5E2P; -.
PDBsum; 5EOD; -.
PDBsum; 5EOK; -.
PDBsum; 5EXL; -.
PDBsum; 5EXM; -.
PDBsum; 5EXN; -.
PDBsum; 5I25; -.
PDBsum; 5Q0D; -.
PDBsum; 5Q0E; -.
PDBsum; 5Q0F; -.
PDBsum; 5Q0G; -.
PDBsum; 5Q0H; -.
PDBsum; 5QCK; -.
PDBsum; 5QCL; -.
PDBsum; 5QCM; -.
PDBsum; 5QCN; -.
PDBsum; 5QQO; -.
PDBsum; 5QQP; -.
PDBsum; 5QTT; -.
PDBsum; 5QTV; -.
PDBsum; 5QTW; -.
PDBsum; 5QTY; -.
PDBsum; 5TKS; -.
PDBsum; 5TKT; -.
PDBsum; 5TKU; -.
PDBsum; 5WB6; -.
PDBsum; 6AOD; -.
PDBsum; 6C0S; -.
PDBsum; 6HHC; -.
PDBsum; 6I58; -.
PDBsum; 6R8X; -.
PDBsum; 6TS4; -.
PDBsum; 6TS5; -.
PDBsum; 6TS6; -.
PDBsum; 6TS7; -.
PDBsum; 6TWB; -.
PDBsum; 6USY; -.
PDBsum; 6VLU; -.
PDBsum; 6VLV; -.
PDBsum; 6W50; -.
PDBsum; 7MBO; -.
SMR; P03951; -.
BioGRID; 108458; 9.
ComplexPortal; CPX-6205; Coagulation factor XIa complex.
DIP; DIP-29085N; -.
IntAct; P03951; 7.
STRING; 9606.ENSP00000384957; -.
BindingDB; P03951; -.
ChEMBL; CHEMBL2820; -.
DrugBank; DB07023; (1R)-2-[(Diaminomethylene)amino]-1-{4-[(4R)-4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl]phenyl}ethyl nicotinate.
DrugBank; DB07887; (R)-1-(4-(4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl)benzyl)guanidine.
DrugBank; DB07071; (R)-1-(4-(4-(Hydroxymethyl)-1,3,2-dioxaborolan-2-YL)phenethyl)guanidine.
DrugBank; DB07077; (R)-1-(4-(4-(Hydroxymethyl)-1,3,2-dioxaborolan-2-YL)phenyl)guanidine.
DrugBank; DB07022; 3-Hydroxypropyl 3-[(7-carbamimidoyl-1-naphthyl)carbamoyl]benzenesulfonate.
DrugBank; DB07299; 4-METHYL-PENTANOIC ACID {1-[4-GUANIDINO-1-(THIAZOLE-2-CARBONYL)-BUTYLCARBAMOYL]-2-METHYL-PROPYL}-AMIDE.
DrugBank; DB07074; 6-CARBAMIMIDOYL-4-(3-HYDROXY-2-METHYL-BENZOYLAMINO)-NAPHTHALENE-2-CARBOXYLIC ACID METHYL ESTER.
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB13152; Coagulation Factor IX Human.
DrugBank; DB09228; Conestat alfa.
DrugBank; DB06404; Human C1-esterase inhibitor.
DrugBank; DB11571; Human thrombin.
DrugBank; DB07212; N-(7-CARBAMIMIDOYL-NAPHTHALEN-1-YL)-3-HYDROXY-2-METHYL-BENZAMIDE.
DrugBank; DB11300; Thrombin.
DrugBank; DB14533; Zinc chloride.
DrugBank; DB14548; Zinc sulfate, unspecified form.
DrugCentral; P03951; -.
GuidetoPHARMACOLOGY; 2360; -.
MEROPS; S01.213; -.
GlyConnect; 818; 21 N-Linked glycans (5 sites).
GlyGen; P03951; 5 sites, 23 N-linked glycans (5 sites).
iPTMnet; P03951; -.
PhosphoSitePlus; P03951; -.
BioMuta; F11; -.
DMDM; 119762; -.
jPOST; P03951; -.
MassIVE; P03951; -.
PaxDb; P03951; -.
PeptideAtlas; P03951; -.
PRIDE; P03951; -.
ProteomicsDB; 51620; -. [P03951-1]
ProteomicsDB; 51621; -. [P03951-2]
ABCD; P03951; 53 sequenced antibodies.
Antibodypedia; 17547; 571 antibodies from 31 providers.
DNASU; 2160; -.
Ensembl; ENST00000264692; ENSP00000264692; ENSG00000088926. [P03951-2]
Ensembl; ENST00000403665; ENSP00000384957; ENSG00000088926.
GeneID; 2160; -.
KEGG; hsa:2160; -.
MANE-Select; ENST00000403665.7; ENSP00000384957.2; NM_000128.4; NP_000119.1.
UCSC; uc003iza.2; human. [P03951-1]
CTD; 2160; -.
DisGeNET; 2160; -.
GeneCards; F11; -.
HGNC; HGNC:3529; F11.
HPA; ENSG00000088926; Tissue enriched (liver).
MalaCards; F11; -.
MIM; 264900; gene.
MIM; 612416; phenotype.
neXtProt; NX_P03951; -.
OpenTargets; ENSG00000088926; -.
Orphanet; 329; Congenital factor XI deficiency.
PharmGKB; PA27941; -.
VEuPathDB; HostDB:ENSG00000088926; -.
eggNOG; KOG3627; Eukaryota.
GeneTree; ENSGT00940000158569; -.
HOGENOM; CLU_031604_0_0_1; -.
InParanoid; P03951; -.
OMA; TTMNYTD; -.
OrthoDB; 1314811at2759; -.
PhylomeDB; P03951; -.
TreeFam; TF343687; -.
BRENDA; 3.4.21.27; 2681.
PathwayCommons; P03951; -.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-9673221; Defective F9 activation.
SABIO-RK; P03951; -.
SignaLink; P03951; -.
SIGNOR; P03951; -.
BioGRID-ORCS; 2160; 4 hits in 1040 CRISPR screens.
ChiTaRS; F11; human.
EvolutionaryTrace; P03951; -.
GeneWiki; Factor_XI; -.
GenomeRNAi; 2160; -.
Pharos; P03951; Tchem.
PRO; PR:P03951; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; P03951; protein.
Bgee; ENSG00000088926; Expressed in right lobe of liver and 122 other tissues.
ExpressionAtlas; P03951; baseline and differential.
Genevisible; P03951; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0007596; P:blood coagulation; IDA:BHF-UCL.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; IDA:ComplexPortal.
GO; GO:0031639; P:plasminogen activation; IDA:BHF-UCL.
GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:BHF-UCL.
CDD; cd01100; APPLE_Factor_XI_like; 4.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
InterPro; IPR000177; Apple.
InterPro; IPR003609; Pan_app.
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.
Pfam; PF00024; PAN_1; 4.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00005; APPLEDOMAIN.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00223; APPLE; 4.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS00495; APPLE; 4.
PROSITE; PS50948; PAN; 4.
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;
Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
Hemostasis; Heparin-binding; Hydrolase; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal.
SIGNAL 1..18
CHAIN 19..387
/note="Coagulation factor XIa heavy chain"
/id="PRO_0000027825"
CHAIN 388..625
/note="Coagulation factor XIa light chain"
/id="PRO_0000027826"
DOMAIN 20..103
/note="Apple 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
DOMAIN 110..193
/note="Apple 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
DOMAIN 200..283
/note="Apple 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
DOMAIN 291..374
/note="Apple 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
DOMAIN 388..623
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
REGION 547..550
/note="Heparin-binding"
ACT_SITE 431
/note="Charge relay system"
ACT_SITE 480
/note="Charge relay system"
ACT_SITE 575
/note="Charge relay system"
CARBOHYD 90
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:25092234"
CARBOHYD 126
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:25092234"
CARBOHYD 163
/note="N-linked (GlcNAc...) (complex) asparagine; atypical"
/evidence="ECO:0000269|PubMed:25092234"
CARBOHYD 450
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234"
CARBOHYD 491
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667,
ECO:0000269|PubMed:25092234"
DISULFID 20..103
/evidence="ECO:0000255"
DISULFID 29
/note="Interchain"
DISULFID 46..76
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 50..56
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 110..193
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 136..165
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 140..146
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 200..283
DISULFID 226..255
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 230..236
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 291..374
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 317..346
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 321..327
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 339
/note="Interchain"
/evidence="ECO:0000255"
DISULFID 380..500
/note="Interchain (between heavy and light chains)"
DISULFID 416..432
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 514..581
DISULFID 545..560
/evidence="ECO:0000269|PubMed:1998667"
DISULFID 571..599
VAR_SEQ 109..162
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:9593722"
/id="VSP_005388"
VARIANT 30
/note="F -> S (in FA11D)"
/evidence="ECO:0000269|PubMed:25158988"
/id="VAR_076515"
VARIANT 32
/note="G -> R (in FA11D; dbSNP:rs281875259)"
/evidence="ECO:0000269|PubMed:21668437"
/id="VAR_067929"
VARIANT 34
/note="D -> H (in FA11D; dbSNP:rs281875267)"
/evidence="ECO:0000269|PubMed:7888672"
/id="VAR_012085"
VARIANT 43
/note="A -> T (in FA11D; dominant-negative mutation that
results in severely decreased protein secretion;
dbSNP:rs281875264)"
/evidence="ECO:0000269|PubMed:21457405"
/id="VAR_067930"
VARIANT 46
/note="C -> F (in FA11D; dbSNP:rs281875271)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_054894"
VARIANT 51
/note="T -> I (in FA11D; dbSNP:rs281875252)"
/evidence="ECO:0000269|PubMed:18005151"
/id="VAR_067931"
VARIANT 51
/note="T -> P (in FA11D; dbSNP:rs281875243)"
/evidence="ECO:0000269|PubMed:18005151,
ECO:0000269|PubMed:22159456"
/id="VAR_067932"
VARIANT 53
/note="H -> Q (in FA11D; dbSNP:rs281875261)"
/evidence="ECO:0000269|PubMed:21668437"
/id="VAR_067933"
VARIANT 56
/note="C -> R (in FA11D; secretion of the mutant protein is
impaired; dbSNP:rs121965069)"
/evidence="ECO:0000269|PubMed:11895778,
ECO:0000269|PubMed:22159456"
/id="VAR_054895"
VARIANT 63
/note="A -> V (in FA11D; dbSNP:rs281875244)"
/evidence="ECO:0000269|PubMed:22159456"
/id="VAR_067934"
VARIANT 66
/note="P -> L (in dbSNP:rs5968)"
/evidence="ECO:0000269|PubMed:10391209"
/id="VAR_011774"
VARIANT 101
/note="K -> R (in FA11D; dbSNP:rs281875272)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_054896"
VARIANT 109
/note="A -> T (in FA11D; dbSNP:rs768474112)"
/evidence="ECO:0000269|PubMed:25158988"
/id="VAR_076516"
VARIANT 140
/note="C -> Y (in FA11D; dbSNP:rs281875256)"
/evidence="ECO:0000269|PubMed:16607084"
/id="VAR_067935"
VARIANT 151
/note="Y -> C (in FA11D; dbSNP:rs281875273)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_054897"
VARIANT 216
/note="D -> N (in FA11D)"
/evidence="ECO:0000269|PubMed:25158988"
/id="VAR_076517"
VARIANT 222
/note="D -> Y (in FA11D; dbSNP:rs281875245)"
/evidence="ECO:0000269|PubMed:22159456"
/id="VAR_067936"
VARIANT 228
/note="R -> Q (in FA11D; dbSNP:rs281875246)"
/evidence="ECO:0000269|PubMed:22159456"
/id="VAR_067937"
VARIANT 241
/note="F -> L (in FA11D; dominant-negative mutation that
results in severely decreased protein secretion;
dbSNP:rs281875265)"
/evidence="ECO:0000269|PubMed:21457405"
/id="VAR_067938"
VARIANT 244
/note="Q -> R (found in a patient with factor XI deficiency
that also carries mutation N-266; dbSNP:rs5969)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:9787168"
/id="VAR_011775"
VARIANT 246
/note="W -> C (in FA11D; dbSNP:rs281875279)"
/evidence="ECO:0000269|PubMed:10027710"
/id="VAR_012086"
VARIANT 252
/note="R -> T (in FA11D; dbSNP:rs281875260)"
/evidence="ECO:0000269|PubMed:21668437"
/id="VAR_067939"
VARIANT 255
/note="C -> Y (in FA11D; secretion of the mutant protein is
impaired; dbSNP:rs281875277)"
/evidence="ECO:0000269|PubMed:11895778"
/id="VAR_054898"
VARIANT 263
/note="G -> E (in FA11D; dbSNP:rs281875274)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_054899"
VARIANT 266
/note="S -> N (in FA11D; dbSNP:rs145168351)"
/evidence="ECO:0000269|PubMed:9787168"
/id="VAR_012087"
VARIANT 270
/note="K -> I (in FA11D; although the mutant protein is
synthesized the secretion is reduced; dbSNP:rs121965070)"
/evidence="ECO:0000269|PubMed:15180874"
/id="VAR_054900"
VARIANT 276
/note="S -> C (in FA11D; dbSNP:rs281875247)"
/evidence="ECO:0000269|PubMed:22159456"
/id="VAR_067940"
VARIANT 277
/note="G -> D (in FA11D; dbSNP:rs281875248)"
/evidence="ECO:0000269|PubMed:22159456"
/id="VAR_067941"
VARIANT 301
/note="F -> L (in FA11D; dbSNP:rs121965064)"
/evidence="ECO:0000269|PubMed:1547342,
ECO:0000269|PubMed:2813350"
/id="VAR_006622"
VARIANT 308
/note="I -> F (in dbSNP:rs5972)"
/evidence="ECO:0000269|PubMed:10391209"
/id="VAR_011776"
VARIANT 315
/note="E -> K (in FA11D; dbSNP:rs281875257)"
/evidence="ECO:0000269|PubMed:16607084,
ECO:0000269|PubMed:25158988"
/id="VAR_067942"
VARIANT 320
/note="L -> P (in FA11D; dbSNP:rs281875268)"
/evidence="ECO:0000269|PubMed:7888672"
/id="VAR_012088"
VARIANT 322
/note="T -> I (in FA11D; dbSNP:rs281875269)"
/evidence="ECO:0000269|PubMed:7888672"
/id="VAR_012089"
VARIANT 326
/note="R -> C (in FA11D; dbSNP:rs28934608)"
/evidence="ECO:0000269|PubMed:10606881"
/id="VAR_012090"
VARIANT 331
/note="T -> I (in FA11D; dbSNP:rs281875253)"
/evidence="ECO:0000269|PubMed:18005151"
/id="VAR_067943"
VARIANT 339
/note="C -> F (in dbSNP:rs5967)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11895778, ECO:0000269|Ref.4"
/id="VAR_011777"
VARIANT 341
/note="E -> K (in FA11D; dbSNP:rs281875270)"
/evidence="ECO:0000269|PubMed:7888672"
/id="VAR_012091"
VARIANT 360
/note="L -> P (in FA11D; dbSNP:rs281875254)"
/evidence="ECO:0000269|PubMed:18005151"
/id="VAR_067944"
VARIANT 399
/note="W -> R (in dbSNP:rs1800439)"
/id="VAR_011778"
VARIANT 401
/note="W -> R (in FA11D; dbSNP:rs281875262)"
/evidence="ECO:0000269|PubMed:21668437"
/id="VAR_067945"
VARIANT 403
/note="V -> M (in FA11D; dominant-negative mutation that
results in severely decreased protein secretion;
dbSNP:rs281875266)"
/evidence="ECO:0000269|PubMed:21457405"
/id="VAR_067946"
VARIANT 404
/note="T -> N (in FA11D; dbSNP:rs121965067)"
/evidence="ECO:0000269|PubMed:9401068"
/id="VAR_012092"
VARIANT 418
/note="G -> V (in FA11D; mutant is not secreted by
transfected fibroblasts; dominant-negative effect;
dbSNP:rs121965071)"
/evidence="ECO:0000269|PubMed:15026311"
/id="VAR_054901"
VARIANT 430
/note="A -> V (in FA11D; dbSNP:rs121965068)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_012093"
VARIANT 454
/note="I -> K (in FA11D; dbSNP:rs281875241)"
/evidence="ECO:0000269|PubMed:21999818"
/id="VAR_067947"
VARIANT 460
/note="F -> V (in FA11D; dbSNP:rs121965065)"
/evidence="ECO:0000269|PubMed:7669672"
/id="VAR_012094"
VARIANT 481
/note="I -> S (in FA11D; dbSNP:rs281875242)"
/evidence="ECO:0000269|PubMed:22322133"
/id="VAR_067948"
VARIANT 493
/note="T -> I (in FA11D; dbSNP:rs1554083754)"
/evidence="ECO:0000269|PubMed:10606881"
/id="VAR_012095"
VARIANT 503
/note="S -> P (in FA11D; dbSNP:rs140068026)"
/evidence="ECO:0000269|PubMed:18005151"
/id="VAR_067949"
VARIANT 506
/note="D -> G (in FA11D; mild phenotype;
dbSNP:rs281875258)"
/evidence="ECO:0000269|PubMed:22016685"
/id="VAR_067950"
VARIANT 511
/note="Y -> H (in FA11D; transfected cells contain reduced
amount of mutant protein and display decreased secretion;
dbSNP:rs281875278)"
/evidence="ECO:0000269|PubMed:11895778"
/id="VAR_054902"
VARIANT 514
/note="C -> F (in FA11D; dbSNP:rs281875249)"
/evidence="ECO:0000269|PubMed:22159456"
/id="VAR_067951"
VARIANT 526
/note="D -> E (in FA11D; dbSNP:rs281875263)"
/evidence="ECO:0000269|PubMed:21668437"
/id="VAR_067952"
VARIANT 538
/note="P -> L (in FA11D; dbSNP:rs139695003)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_054903"
VARIANT 543
/note="E -> K (in FA11D; dbSNP:rs142952627)"
/evidence="ECO:0000269|PubMed:25158988"
/id="VAR_076518"
VARIANT 552
/note="H -> R (in FA11D; dbSNP:rs369935706)"
/evidence="ECO:0000269|PubMed:25158988"
/id="VAR_076519"
VARIANT 565
/note="E -> K (in FA11D; dbSNP:rs281875275)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_054904"
VARIANT 575
/note="S -> L (in FA11D; dbSNP:rs281875250)"
/evidence="ECO:0000269|PubMed:22159456"
/id="VAR_067953"
VARIANT 587
/note="W -> S (in FA11D; mutant is not secreted by
transfected fibroblasts; dominant-negative effect;
dbSNP:rs121965072)"
/evidence="ECO:0000269|PubMed:15026311"
/id="VAR_054905"
VARIANT 594
/note="S -> R (in FA11D; dbSNP:rs28934609)"
/evidence="ECO:0000269|PubMed:10606881"
/id="VAR_012096"
VARIANT 597
/note="E -> K (in FA11D; dbSNP:rs281875251)"
/evidence="ECO:0000269|PubMed:16607084,
ECO:0000269|PubMed:22159456"
/id="VAR_067954"
VARIANT 608
/note="Y -> H (in FA11D; dbSNP:rs281875255)"
/evidence="ECO:0000269|PubMed:18005151"
/id="VAR_067955"
VARIANT 618
/note="I -> S (in FA11D; dbSNP:rs281875276)"
/evidence="ECO:0000269|PubMed:15953011"
/id="VAR_054906"
CONFLICT 226
/note="C -> S (in Ref. 2; AAA51985)"
/evidence="ECO:0000305"
STRAND 28..30
/evidence="ECO:0007829|PDB:6I58"
STRAND 34..39
/evidence="ECO:0007829|PDB:6I58"
HELIX 43..52
/evidence="ECO:0007829|PDB:6I58"
STRAND 53..55
/evidence="ECO:0007829|PDB:6I58"
STRAND 58..62
/evidence="ECO:0007829|PDB:6I58"
HELIX 70..72
/evidence="ECO:0007829|PDB:5EOK"
STRAND 75..79
/evidence="ECO:0007829|PDB:6I58"
STRAND 82..84
/evidence="ECO:0007829|PDB:5I25"
STRAND 88..90
/evidence="ECO:0007829|PDB:6I58"
STRAND 94..98
/evidence="ECO:0007829|PDB:6I58"
HELIX 100..102
/evidence="ECO:0007829|PDB:5EOD"
STRAND 114..129
/evidence="ECO:0007829|PDB:6I58"
HELIX 133..141
/evidence="ECO:0007829|PDB:6I58"
STRAND 143..145
/evidence="ECO:0007829|PDB:6I58"
STRAND 147..152
/evidence="ECO:0007829|PDB:6I58"
TURN 159..163
/evidence="ECO:0007829|PDB:6I58"
STRAND 164..169
/evidence="ECO:0007829|PDB:6I58"
STRAND 171..174
/evidence="ECO:0007829|PDB:5EOK"
STRAND 176..188
/evidence="ECO:0007829|PDB:6I58"
HELIX 191..193
/evidence="ECO:0007829|PDB:6I58"
STRAND 205..209
/evidence="ECO:0007829|PDB:6I58"
STRAND 212..219
/evidence="ECO:0007829|PDB:6I58"
HELIX 223..232
/evidence="ECO:0007829|PDB:6I58"
STRAND 237..242
/evidence="ECO:0007829|PDB:6I58"
HELIX 249..251
/evidence="ECO:0007829|PDB:6I58"
STRAND 254..259
/evidence="ECO:0007829|PDB:6I58"
STRAND 261..264
/evidence="ECO:0007829|PDB:6I58"
STRAND 269..278
/evidence="ECO:0007829|PDB:6I58"
HELIX 281..283
/evidence="ECO:0007829|PDB:5EOK"
HELIX 284..286
/evidence="ECO:0007829|PDB:6I58"
STRAND 296..302
/evidence="ECO:0007829|PDB:6I58"
STRAND 304..312
/evidence="ECO:0007829|PDB:6I58"
HELIX 314..322
/evidence="ECO:0007829|PDB:6I58"
STRAND 329..333
/evidence="ECO:0007829|PDB:6I58"
TURN 337..339
/evidence="ECO:0007829|PDB:5EOK"
STRAND 344..350
/evidence="ECO:0007829|PDB:6I58"
STRAND 352..355
/evidence="ECO:0007829|PDB:6I58"
STRAND 357..369
/evidence="ECO:0007829|PDB:6I58"
HELIX 374..376
/evidence="ECO:0007829|PDB:6I58"
HELIX 379..381
/evidence="ECO:0007829|PDB:6I58"
STRAND 391..393
/evidence="ECO:0007829|PDB:6I58"
STRAND 402..407
/evidence="ECO:0007829|PDB:4CRG"
STRAND 409..411
/evidence="ECO:0007829|PDB:4CRG"
STRAND 413..422
/evidence="ECO:0007829|PDB:4CRG"
STRAND 425..428
/evidence="ECO:0007829|PDB:4CRG"
HELIX 430..433
/evidence="ECO:0007829|PDB:4CRG"
HELIX 439..441
/evidence="ECO:0007829|PDB:4CRG"
STRAND 442..445
/evidence="ECO:0007829|PDB:4CRG"
HELIX 451..453
/evidence="ECO:0007829|PDB:4CRG"
STRAND 456..458
/evidence="ECO:0007829|PDB:1ZTJ"
STRAND 461..468
/evidence="ECO:0007829|PDB:4CRG"
HELIX 475..477
/evidence="ECO:0007829|PDB:4CRG"
STRAND 482..488
/evidence="ECO:0007829|PDB:4CRG"
STRAND 494..496
/evidence="ECO:0007829|PDB:4X6P"
HELIX 504..506
/evidence="ECO:0007829|PDB:4CRG"
HELIX 508..510
/evidence="ECO:0007829|PDB:6AOD"
STRAND 514..519
/evidence="ECO:0007829|PDB:4CRG"
STRAND 522..525
/evidence="ECO:0007829|PDB:4CRG"
STRAND 533..536
/evidence="ECO:0007829|PDB:4CRG"
HELIX 542..548
/evidence="ECO:0007829|PDB:4CRG"
TURN 549..551
/evidence="ECO:0007829|PDB:4X6P"
STRAND 558..561
/evidence="ECO:0007829|PDB:4CRG"
TURN 572..576
/evidence="ECO:0007829|PDB:6HHC"
STRAND 578..583
/evidence="ECO:0007829|PDB:4CRG"
STRAND 586..595
/evidence="ECO:0007829|PDB:4CRG"
STRAND 597..600
/evidence="ECO:0007829|PDB:4CRG"
STRAND 606..610
/evidence="ECO:0007829|PDB:4CRG"
HELIX 611..614
/evidence="ECO:0007829|PDB:4CRG"
HELIX 615..622
/evidence="ECO:0007829|PDB:4CRG"
SEQUENCE 625 AA; 70109 MW; 147AFA94B7709E8F CRC64;
MIFLYQVVHF ILFTSVSGEC VTQLLKDTCF EGGDITTVFT PSAKYCQVVC TYHPRCLLFT
FTAESPSEDP TRWFTCVLKD SVTETLPRVN RTAAISGYSF KQCSHQISAC NKDIYVDLDM
KGINYNSSVA KSAQECQERC TDDVHCHFFT YATRQFPSLE HRNICLLKHT QTGTPTRITK
LDKVVSGFSL KSCALSNLAC IRDIFPNTVF ADSNIDSVMA PDAFVCGRIC THHPGCLFFT
FFSQEWPKES QRNLCLLKTS ESGLPSTRIK KSKALSGFSL QSCRHSIPVF CHSSFYHDTD
FLGEELDIVA AKSHEACQKL CTNAVRCQFF TYTPAQASCN EGKGKCYLKL SSNGSPTKIL
HGRGGISGYT LRLCKMDNEC TTKIKPRIVG GTASVRGEWP WQVTLHTTSP TQRHLCGGSI
IGNQWILTAA HCFYGVESPK ILRVYSGILN QSEIKEDTSF FGVQEIIIHD QYKMAESGYD
IALLKLETTV NYTDSQRPIC LPSKGDRNVI YTDCWVTGWG YRKLRDKIQN TLQKAKIPLV
TNEECQKRYR GHKITHKMIC AGYREGGKDA CKGDSGGPLS CKHNEVWHLV GITSWGEGCA
QRERPGVYTN VVEYVDWILE KTQAV


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Related Genes :
[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]
[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]
[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]
[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]
[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)]
[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]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[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]
[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]
[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]
[F7] 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]
[PROC] Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]
[] Venom prothrombin activator pseutarin-C catalytic subunit (PCCS) (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain]
[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]
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B heavy 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]
[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]
[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]
[Klkb1 Klk3 Pk] Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light chain]
[F3] Tissue factor (TF) (Coagulation factor III) (Thromboplastin) (CD antigen CD142)
[Klkb1 Klk3 Pk] Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light 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]
[F13A1 F13A] Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A chain)

Bibliography :