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Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]

 FA5_HUMAN               Reviewed;        2224 AA.
P12259; A8K6E8; Q14285; Q2EHR5; Q5R346; Q5R347; Q6UPU6; Q8WWQ6;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
29-SEP-2021, entry version 240.
RecName: Full=Coagulation factor V;
AltName: Full=Activated protein C cofactor;
AltName: Full=Proaccelerin, labile factor;
Contains:
RecName: Full=Coagulation factor V heavy chain;
Contains:
RecName: Full=Coagulation factor V light chain;
Flags: Precursor;
Name=F5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC CLEAVAGE AT ARG-737; ARG-1046 AND
ARG-1573 BY THROMBIN, AND VARIANTS ARG-858; ARG-865; GLU-925; PHE-1397 AND
VAL-1764.
PubMed=3110773; DOI=10.1073/pnas.84.14.4846;
Jenny R.J., Pittman D.D., Toole J.J., Kriz R.W., Aldape R.A., Hewick R.M.,
Kaufman R.J., Mann K.G.;
"Complete cDNA and derived amino acid sequence of human factor V.";
Proc. Natl. Acad. Sci. U.S.A. 84:4846-4850(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1567832; DOI=10.1021/bi00130a007;
Cripe L.D., Moore K.D., Kane W.H.;
"Structure of the gene for human coagulation factor V.";
Biochemistry 31:3777-3785(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THPH2 GLN-534, AND VARIANTS
SER-15; HIS-107; THR-413; LYS-513; SER-809; THR-817; ARG-858; ARG-865;
SER-915; GLU-925; SER-969; LEU-980; GLN-1146; ILE-1285; SER-1404; ALA-1530
AND THR-2148.
SeattleSNPs variation discovery resource;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THPH2 GLN-534.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1030, AND VARIANT LYS-513.
TISSUE=Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1600, AND VARIANTS ARG-858; ARG-865;
GLU-925 AND ILE-1285.
PubMed=2827731; DOI=10.1021/bi00394a033;
Kane W.H., Ichinose A., Hagen F.S., Davie E.W.;
"Cloning of cDNAs coding for the heavy chain region and connecting region
of human factor V, a blood coagulation factor with four types of internal
repeats.";
Biochemistry 26:6508-6514(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 658-1598.
Kostka H.;
"Human coagulation factor V, exon 13, missense mutation Asn713Ser.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 660-1598, AND VARIANTS ARG-858; ARG-865;
GLU-925 AND PHE-1397.
PubMed=11758222;
Xie F., Cheng F., Zhu X.;
"Studies on hereditary deficiency of coagulation factor V.";
Zhonghua Xue Ye Xue Za Zhi 22:453-456(2001).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1188-1215 AND 1315-2224.
PubMed=3092220; DOI=10.1073/pnas.83.18.6800;
Kane W.H., Davie E.W.;
"Cloning of a cDNA coding for human factor V, a blood coagulation factor
homologous to factor VIII and ceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 83:6800-6804(1986).
[10]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=8454869;
Shen N.L.L., Fan S.-T., Pyati J., Graff R., Lapolla R.J., Edgington T.S.;
"The serine protease cofactor factor V is synthesized by lymphocytes.";
J. Immunol. 150:2992-3001(1993).
[11]
ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=6323392; DOI=10.1093/oxfordjournals.jbchem.a134583;
Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
"Mechanism of inhibition of activated protein C by protein C inhibitor.";
J. Biochem. 95:187-195(1984).
[12]
COPPER-BINDING.
PubMed=6490642;
Mann K.G., Lawler C.M., Vehar G.A., Church W.R.;
"Coagulation Factor V contains copper ion.";
J. Biol. Chem. 259:12949-12951(1984).
[13]
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).
[14]
SULFATION.
PubMed=8204629; DOI=10.1021/bi00188a026;
Pittman D.D., Tomkinson K.N., Michnick D., Selighsohn U., Kaufman R.J.;
"Posttranslational sulfation of factor V is required for efficient thrombin
cleavage and activation and for full procoagulant activity.";
Biochemistry 33:6952-6959(1994).
[15]
SULFATION.
PubMed=2168225;
Hortin G.L.;
"Sulfation of tyrosine residues in coagulation factor V.";
Blood 76:946-952(1990).
[16]
PROTEOLYTIC CLEAVAGE AT ARG-334; ARG-534; ARG-707 AND LYS-1022 BY ACTIVATED
PROTEIN C.
PubMed=7989361;
Kalafatis M., Rand M.D., Mann K.G.;
"The mechanism of inactivation of human factor V and human factor Va by
activated protein C.";
J. Biol. Chem. 269:31869-31880(1994).
[17]
HETERODIMER WITH SERPINA5.
PubMed=8665956; DOI=10.1111/j.1432-1033.1996.0088q.x;
Kise H., Nishioka J., Kawamura J., Suzuki K.;
"Characterization of semenogelin II and its molecular interaction with
prostate-specific antigen and protein C inhibitor.";
Eur. J. Biochem. 238:88-96(1996).
[18]
ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=9556620; DOI=10.1074/jbc.273.18.11281;
Nishioka J., Ning M., Hayashi T., Suzuki K.;
"Protein C inhibitor secreted from activated platelets efficiently inhibits
activated protein C on phosphatidylethanolamine of platelet membrane and
microvesicles.";
J. Biol. Chem. 273:11281-11287(1998).
[19]
INVOLVEMENT IN RPRGL1 SUSCEPTIBILITY.
PubMed=11018168; DOI=10.1056/nejm200010053431405;
Martinelli I., Taioli E., Cetin I., Marinoni A., Gerosa S., Villa M.V.,
Bozzo M., Mannucci P.M.;
"Mutations in coagulation factors in women with unexplained late fetal
loss.";
N. Engl. J. Med. 343:1015-1018(2000).
[20]
ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=15140131; DOI=10.1111/j.1538-7836.2004.00733.x;
Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H., Gabazza E.C.,
Ido M., Suzuki K.;
"Characterization of a novel human protein C inhibitor (PCI) gene
transgenic mouse useful for studying the role of PCI in physiological and
pathological conditions.";
J. Thromb. Haemost. 2:949-961(2004).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-460; ASN-821; ASN-977
AND ASN-1559.
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).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-640, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[25]
PHOSPHORYLATION AT SER-859.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted phosphoproteome.";
Cell 161:1619-1632(2015).
[26]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2065-2224.
PubMed=10586886; DOI=10.1038/46594;
Macedo-Ribeiro S., Bode W., Huber R., Quinn-Allen M.A., Kim S.W.,
Ortel T.L., Bourenkov G.P., Bartunik H.D., Stubbs M.T., Kane W.H.,
Fuentes-Prior P.;
"Crystal structures of the membrane-binding C2 domain of human coagulation
factor V.";
Nature 402:434-439(1999).
[27]
VARIANT VAL-1764.
PubMed=7874144;
Bayston T.A., Ireland H., Olds R.J., Thein S.L., Lane D.A.;
"A polymorphism in the human coagulation factor V gene.";
Hum. Mol. Genet. 3:2085-2085(1994).
[28]
VARIANT THPH2 GLN-534.
PubMed=8164741; DOI=10.1038/369064a0;
Bertina R.M., Koeleman B.P.C., Koster T., Rosendaal F.R., Dirven R.J.,
de Ronde H., van der Velden P.A., Reitsma P.H.;
"Mutation in blood coagulation factor V associated with resistance to
activated protein C.";
Nature 369:64-67(1994).
[29]
VARIANTS ILE-1285 AND ARG-1327.
PubMed=8713778;
Lunghi B., Iacoviello L., Gemmati D., Dilasio M.G., Castoldi E.,
Pinotti M., Castaman G., Redaelli R., Mariani G., Marchetti G.,
Bernardi F.;
"Detection of new polymorphic markers in the factor V gene: association
with factor V levels in plasma.";
Thromb. Haemost. 75:45-48(1996).
[30]
ASSOCIATION OF VARIANT LEIDEN GLN-534 WITH SUSCEPTIBILITY TO BUDD-CHIARI
SYNDROME.
PubMed=9245936; DOI=10.1136/gut.40.6.798;
Mahmoud A.E.A., Elias E., Beauchamp N., Wilde J.T.;
"Prevalence of the factor V Leiden mutation in hepatic and portal vein
thrombosis.";
Gut 40:798-800(1997).
[31]
VARIANT HONG KONG GLY-334, AND VARIANT LYS-513.
PubMed=9454741;
Chan W.P., Lee C.K., Kwong Y.L., Lam C.K., Liang R.;
"A novel mutation of Arg306 of factor V gene in Hong Kong Chinese.";
Blood 91:1135-1139(1998).
[32]
VARIANT THPH2 THR-334.
PubMed=9454742;
Williamson D., Brown K., Luddington R., Baglin C., Baglin T.;
"Factor V Cambridge: a new mutation (Arg306-to-Thr) associated with
resistance to activated protein C.";
Blood 91:1140-1144(1998).
[33]
VARIANT HONG KONG GLY-334.
PubMed=9746807;
Liang R., Lee C.K., Wat M.S., Kwong Y.L., Lam C.K., Liu H.W.;
"Clinical significance of Arg306 mutations of factor V gene.";
Blood 92:2599-2600(1998).
[34]
VARIANT THPH2 GLN-534, AND VARIANTS HIS-107; THR-413; LYS-513; SER-809;
THR-817; ARG-858; ARG-865; GLU-925; GLN-1146; ALA-1530; SER-1685; VAL-1749;
VAL-1764; ILE-1820 AND GLY-2222.
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).
[35]
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).
[36]
VARIANT FA5D CYS-1730, VARIANT THPH2 GLN-534, AND VARIANT ARG-1327.
PubMed=10942390;
Castoldi E., Simioni P., Kalafatis M., Lunghi B., Tormene D., Girelli D.,
Girolami A., Bernardi F.;
"Combinations of 4 mutations (FV R506Q, FV H1299R, FV Y1702C, PT 20210G/A)
affecting the prothrombinase complex in a thrombophilic family.";
Blood 96:1443-1448(2000).
[37]
VARIANTS THPH2 ARG-613 AND CYS-1730.
PubMed=11435304; DOI=10.1182/blood.v98.2.358;
van Wijk R., Nieuwenhuis K., van den Berg M., Huizinga E.G.,
van der Meijden B.B., Kraaijenhagen R.J., van Solinge W.W.;
"Five novel mutations in the gene for human blood coagulation factor V
associated with type I factor V deficiency.";
Blood 98:358-367(2001).
[38]
VARIANT THPH2 HIS-2102.
PubMed=11858490;
Schrijver I., Houissa-Kastally R., Jones C.D., Garcia K.C., Zehnder J.L.;
"Novel factor V C2-domain mutation (R2074H) in two families with factor V
deficiency and bleeding.";
Thromb. Haemost. 87:294-299(2002).
[39]
VARIANT FA5D CYS-2102, AND CHARACTERIZATION OF VARIANT FA5D CYS-2102.
PubMed=12393490; DOI=10.1182/blood-2002-06-1928;
Duga S., Montefusco M.C., Asselta R., Malcovati M., Peyvandi F.,
Santagostino E., Mannucci P.M., Tenchini M.L.;
"Arg2074Cys missense mutation in the C2 domain of factor V causing
moderately severe factor V deficiency: molecular characterization by
expression of the recombinant protein.";
Blood 101:173-177(2003).
[40]
VARIANT THPH2 THR-387.
PubMed=14617013; DOI=10.1046/j.1365-2141.2003.04624.x;
Mumford A.D., McVey J.H., Morse C.V., Gomez K., Steen M., Norstrom E.A.,
Tuddenham E.G.D., Dahlback B., Bolton-Maggs P.H.B.;
"Factor V I359T: a novel mutation associated with thrombosis and resistance
to activated protein C.";
Br. J. Haematol. 123:496-501(2003).
[41]
ASSOCIATION OF VARIANT GLN-534 WITH SUSCEPTIBILITY TO ISCHSTR.
PubMed=15534175; DOI=10.1001/archneur.61.11.1652;
Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes
involving approximately 18,000 cases and 58,000 controls.";
Arch. Neurol. 61:1652-1661(2004).
[42]
CHARACTERIZATION OF VARIANT THPH2 THR-387.
PubMed=14695241; DOI=10.1182/blood-2003-06-2092;
Steen M., Norstroem E.A., Tholander A.-L., Bolton-Maggs P.H.B., Mumford A.,
McVey J.H., Tuddenham E.G.D., Dahlbaeck B.;
"Functional characterization of factor V-Ile359Thr: a novel mutation
associated with thrombosis.";
Blood 103:3381-3387(2004).
[43]
VARIANT [LARGE SCALE ANALYSIS] ALA-775.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Central regulator of hemostasis. It serves as a critical
cofactor for the prothrombinase activity of factor Xa that results in
the activation of prothrombin to thrombin.
-!- ACTIVITY REGULATION: Inhibited by SERPINA5.
{ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:2844223,
ECO:0000269|PubMed:6323392, ECO:0000269|PubMed:9556620}.
-!- SUBUNIT: Factor Va, the activated form of factor V, is composed of a
heavy chain and a light chain, non-covalently bound. The interaction
between the two chains is calcium-dependent. Forms heterodimer with
SERPINA5.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Plasma.
-!- DOMAIN: Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA
repeats.
-!- PTM: Thrombin activates factor V proteolytically to the active
cofactor, factor Va (formation of a heavy chain at the N-terminus and a
light chain at the C-terminus).
-!- PTM: Sulfation is required for efficient thrombin cleavage and
activation and for full procoagulant activity.
{ECO:0000269|PubMed:2168225, ECO:0000269|PubMed:7989361,
ECO:0000269|PubMed:8204629}.
-!- PTM: Activated protein C inactivates factor V and factor Va by
proteolytic degradation. {ECO:0000269|PubMed:7989361}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- DISEASE: Factor V deficiency (FA5D) [MIM:227400]: A blood coagulation
disorder leading to a hemorrhagic diathesis known as parahemophilia.
{ECO:0000269|PubMed:10942390, ECO:0000269|PubMed:12393490}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- DISEASE: Thrombophilia due to activated protein C resistance (THPH2)
[MIM:188055]: A hemostatic disorder due to defective degradation of
factor V by activated protein C. It is characterized by a poor
anticoagulant response to activated protein C resulting in tendency to
thrombosis. {ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:11435304, ECO:0000269|PubMed:11858490,
ECO:0000269|PubMed:14617013, ECO:0000269|PubMed:14695241,
ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:8164741,
ECO:0000269|PubMed:9454742}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- DISEASE: Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused
by obstruction of hepatic venous outflow involving either the hepatic
veins or the terminal segment of the inferior vena cava. Obstructions
are generally caused by thrombosis and lead to hepatic congestion and
ischemic necrosis. Clinical manifestations observed in the majority of
patients include hepatomegaly, right upper quadrant pain and abdominal
ascites. Budd-Chiari syndrome is associated with a combination of
disease states including primary myeloproliferative syndromes and
thrombophilia due to factor V Leiden, protein C deficiency and
antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical
complication in patients with polycythemia vera.
{ECO:0000269|PubMed:9245936}. Note=Disease susceptibility is associated
with variants affecting the gene represented in this entry.
-!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute
neurologic event leading to death of neural tissue of the brain and
resulting in loss of motor, sensory and/or cognitive function. Ischemic
strokes, resulting from vascular occlusion, is considered to be a
highly complex disease consisting of a group of heterogeneous disorders
with multiple genetic and environmental risk factors.
{ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is
associated with variants affecting the gene represented in this entry.
-!- DISEASE: Pregnancy loss, recurrent, 1 (RPRGL1) [MIM:614389]: A common
complication of pregnancy, resulting in spontaneous abortion before the
fetus has reached viability. The term includes all miscarriages from
the time of conception until 24 weeks of gestation. Recurrent pregnancy
loss is defined as 3 or more consecutive spontaneous abortions.
{ECO:0000269|PubMed:11018168}. Note=Disease susceptibility is
associated with variants affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABD23003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor V entry;
URL="https://en.wikipedia.org/wiki/Factor_V";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f5/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F5";
---------------------------------------------------------------------------
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EMBL; M16967; AAA52424.1; -; mRNA.
EMBL; L32779; AAB59401.1; -; Genomic_DNA.
EMBL; L32755; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32756; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32757; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32758; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32759; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32760; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32761; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32762; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32763; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32764; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32765; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32766; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32767; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32768; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32769; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32770; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32771; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32772; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32773; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32774; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32775; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32776; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32777; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32778; AAB59401.1; JOINED; Genomic_DNA.
EMBL; AY364535; AAQ55063.1; -; Genomic_DNA.
EMBL; Z99572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK291613; BAF84302.1; -; mRNA.
EMBL; M14335; AAB59532.1; -; mRNA.
EMBL; DQ377944; ABD23003.1; ALT_SEQ; Genomic_DNA.
EMBL; AJ297255; CAC82573.1; -; mRNA.
CCDS; CCDS1281.1; -.
PIR; A56172; KFHU5.
RefSeq; NP_000121.2; NM_000130.4.
PDB; 1CZS; X-ray; 1.90 A; A=2065-2224.
PDB; 1CZT; X-ray; 1.87 A; A=2065-2224.
PDB; 1CZV; X-ray; 2.40 A; A/B=2065-2224.
PDB; 1FV4; Model; -; H=29-691, L=1574-2224.
PDB; 1Y61; Model; -; H=29-737, L=1574-2224.
PDB; 3P6Z; X-ray; 1.70 A; C/I=685-737.
PDB; 3P70; X-ray; 2.55 A; M/N/O/P=685-737.
PDB; 3S9C; X-ray; 1.80 A; B=1561-1574.
PDB; 7KVE; EM; 3.30 A; B=29-2224.
PDB; 7KVF; EM; 3.60 A; B=29-2224.
PDB; 7KXY; EM; 4.40 A; A=29-737, B=1574-2224.
PDBsum; 1CZS; -.
PDBsum; 1CZT; -.
PDBsum; 1CZV; -.
PDBsum; 1FV4; -.
PDBsum; 1Y61; -.
PDBsum; 3P6Z; -.
PDBsum; 3P70; -.
PDBsum; 3S9C; -.
PDBsum; 7KVE; -.
PDBsum; 7KVF; -.
PDBsum; 7KXY; -.
SMR; P12259; -.
BioGRID; 108452; 14.
ComplexPortal; CPX-6216; Coagulation factor Va complex.
DIP; DIP-47331N; -.
IntAct; P12259; 9.
MINT; P12259; -.
STRING; 9606.ENSP00000356771; -.
BindingDB; P12259; -.
ChEMBL; CHEMBL3618; -.
DrugBank; DB13151; Anti-inhibitor coagulant complex.
DrugBank; DB09130; Copper.
DrugBank; DB00055; Drotrecogin alfa.
DrugBank; DB11571; Human thrombin.
DrugBank; DB11312; Protein C.
DrugBank; DB13149; Protein S human.
DrugBank; DB11300; Thrombin.
DrugBank; DB11572; Thrombin alfa.
DrugBank; DB05777; Thrombomodulin Alfa.
CarbonylDB; P12259; -.
GlyConnect; 1120; 16 N-Linked glycans (9 sites).
GlyGen; P12259; 60 sites, 19 N-linked glycans (9 sites), 6 O-linked glycans (31 sites).
iPTMnet; P12259; -.
PhosphoSitePlus; P12259; -.
BioMuta; F5; -.
DMDM; 308153653; -.
CPTAC; non-CPTAC-2648; -.
jPOST; P12259; -.
MassIVE; P12259; -.
MaxQB; P12259; -.
PaxDb; P12259; -.
PeptideAtlas; P12259; -.
PRIDE; P12259; -.
ProteomicsDB; 52838; -.
Antibodypedia; 863; 398 antibodies.
DNASU; 2153; -.
Ensembl; ENST00000367797; ENSP00000356771; ENSG00000198734.
GeneID; 2153; -.
KEGG; hsa:2153; -.
UCSC; uc001ggg.2; human.
CTD; 2153; -.
DisGeNET; 2153; -.
GeneCards; F5; -.
GeneReviews; F5; -.
HGNC; HGNC:3542; F5.
HPA; ENSG00000198734; Tissue enhanced (brain, liver, placenta).
MalaCards; F5; -.
MIM; 188055; phenotype.
MIM; 227400; phenotype.
MIM; 600880; phenotype.
MIM; 601367; phenotype.
MIM; 612309; gene.
MIM; 614389; phenotype.
neXtProt; NX_P12259; -.
OpenTargets; ENSG00000198734; -.
Orphanet; 131; Budd-Chiari syndrome.
Orphanet; 329217; Cerebral sinovenous thrombosis.
Orphanet; 326; Congenital factor V deficiency.
Orphanet; 391320; East Texas bleeding disorder.
Orphanet; 64738; NON RARE IN EUROPE: Non rare thrombophilia.
PharmGKB; PA159; -.
VEuPathDB; HostDB:ENSG00000198734; -.
eggNOG; ENOG502QSUG; Eukaryota.
GeneTree; ENSGT00940000158556; -.
HOGENOM; CLU_000948_0_0_1; -.
InParanoid; P12259; -.
OMA; GDYWEPS; -.
OrthoDB; 454773at2759; -.
PhylomeDB; P12259; -.
TreeFam; TF329807; -.
PathwayCommons; P12259; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P12259; -.
BioGRID-ORCS; 2153; 1 hit in 1007 CRISPR screens.
ChiTaRS; F5; human.
EvolutionaryTrace; P12259; -.
GeneWiki; Factor_V; -.
GenomeRNAi; 2153; -.
Pharos; P12259; Tbio.
PRO; PR:P12259; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P12259; protein.
Bgee; ENSG00000198734; Expressed in liver and 181 other tissues.
ExpressionAtlas; P12259; baseline and differential.
Genevisible; P12259; HS.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031091; C:platelet alpha granule; IBA:GO_Central.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0008015; P:blood circulation; IBA:GO_Central.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
CDD; cd00057; FA58C; 2.
Gene3D; 2.60.40.420; -; 5.
InterPro; IPR009271; Coagulation_factor_V_LSPD.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR033138; Cu_oxidase_CS.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR000421; FA58C.
InterPro; IPR024715; Factor_5/8-like.
InterPro; IPR008979; Galactose-bd-like_sf.
Pfam; PF07732; Cu-oxidase_3; 2.
Pfam; PF00754; F5_F8_type_C; 2.
Pfam; PF06049; LSPR; 21.
PIRSF; PIRSF000354; Factors_V_VIII; 1.
SMART; SM00231; FA58C; 2.
SUPFAM; SSF49503; SSF49503; 6.
SUPFAM; SSF49785; SSF49785; 2.
PROSITE; PS01285; FA58C_1; 2.
PROSITE; PS01286; FA58C_2; 2.
PROSITE; PS50022; FA58C_3; 2.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
1: Evidence at protein level;
3D-structure; Blood coagulation; Calcium; Copper; Disease variant;
Disulfide bond; Glycoprotein; Hemostasis; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal; Sulfation; Thrombophilia;
Zymogen.
SIGNAL 1..28
CHAIN 29..2224
/note="Coagulation factor V"
/id="PRO_0000002978"
CHAIN 29..737
/note="Coagulation factor V heavy chain"
/id="PRO_0000002979"
PROPEP 738..1573
/note="Activation peptide (connecting region)"
/id="PRO_0000002980"
CHAIN 1574..2224
/note="Coagulation factor V light chain"
/id="PRO_0000002981"
DOMAIN 30..329
/note="F5/8 type A 1"
DOMAIN 30..193
/note="Plastocyanin-like 1"
DOMAIN 203..329
/note="Plastocyanin-like 2"
DOMAIN 348..684
/note="F5/8 type A 2"
DOMAIN 348..526
/note="Plastocyanin-like 3"
DOMAIN 536..684
/note="Plastocyanin-like 4"
REPEAT 895..911
/note="1-1"
REPEAT 912..928
/note="1-2"
REPEAT 1185..1193
/note="2-1"
REPEAT 1194..1202
/note="2-2"
REPEAT 1203..1211
/note="2-3"
REPEAT 1212..1220
/note="2-4"
REPEAT 1221..1229
/note="2-5"
REPEAT 1230..1238
/note="2-6"
REPEAT 1239..1247
/note="2-7"
REPEAT 1248..1256
/note="2-8"
REPEAT 1257..1265
/note="2-9"
REPEAT 1266..1274
/note="2-10"
REPEAT 1275..1283
/note="2-11"
REPEAT 1284..1292
/note="2-12"
REPEAT 1293..1301
/note="2-13"
REPEAT 1302..1310
/note="2-14"
REPEAT 1311..1319
/note="2-15"
REPEAT 1320..1328
/note="2-16"
REPEAT 1329..1337
/note="2-17"
REPEAT 1338..1346
/note="2-18"
REPEAT 1347..1355
/note="2-19"
REPEAT 1356..1364
/note="2-20"
REPEAT 1365..1373
/note="2-21"
REPEAT 1374..1382
/note="2-22"
REPEAT 1383..1391
/note="2-23"
REPEAT 1392..1400
/note="2-24"
REPEAT 1401..1409
/note="2-25"
REPEAT 1410..1418
/note="2-26"
REPEAT 1419..1427
/note="2-27"
REPEAT 1428..1436
/note="2-28"
REPEAT 1437..1445
/note="2-29"
REPEAT 1446..1454
/note="2-30"
REPEAT 1455..1463
/note="2-31"
REPEAT 1464..1472
/note="2-32"
REPEAT 1473..1481
/note="2-33"
REPEAT 1482..1490
/note="2-34"
REPEAT 1493..1501
/note="2-35"
DOMAIN 1578..1907
/note="F5/8 type A 3"
DOMAIN 1578..1751
/note="Plastocyanin-like 5"
DOMAIN 1761..1907
/note="Plastocyanin-like 6"
DOMAIN 1907..2061
/note="F5/8 type C 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
DOMAIN 2066..2221
/note="F5/8 type C 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
REGION 692..1573
/note="B"
REGION 822..842
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 894..927
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 895..928
/note="2 X 17 AA tandem repeats"
REGION 982..1001
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1029..1048
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1097..1157
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1185..1501
/note="35 X 9 AA approximate tandem repeats of [TNP]-L-S-P-
D-L-S-Q-T"
REGION 1341..1367
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1097..1115
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1133..1152
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
METAL 139
/note="Calcium"
/evidence="ECO:0000250"
METAL 140
/note="Calcium"
/evidence="ECO:0000250"
METAL 1843
/note="Copper"
/evidence="ECO:0000250"
METAL 1845
/note="Copper"
/evidence="ECO:0000250"
SITE 334..335
/note="Cleavage; by activated protein C"
/evidence="ECO:0000269|PubMed:7989361"
SITE 534..535
/note="Cleavage; by activated protein C"
/evidence="ECO:0000269|PubMed:7989361"
SITE 707..708
/note="Cleavage; by activated protein C"
/evidence="ECO:0000269|PubMed:7989361"
SITE 737..738
/note="Cleavage; by thrombin"
/evidence="ECO:0000269|PubMed:3110773"
SITE 1022..1023
/note="Cleavage; by activated protein C"
/evidence="ECO:0000269|PubMed:7989361"
SITE 1046..1047
/note="Cleavage; by thrombin"
/evidence="ECO:0000269|PubMed:3110773"
SITE 1573..1574
/note="Cleavage; by thrombin"
/evidence="ECO:0000269|PubMed:3110773"
MOD_RES 640
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:19690332"
MOD_RES 693
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 724
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 726
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 859
/note="Phosphoserine; by FAM20C"
/evidence="ECO:0000269|PubMed:26091039"
MOD_RES 1522
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 1538
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 1543
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 1593
/note="Sulfotyrosine"
/evidence="ECO:0000255"
CARBOHYD 51
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 55
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 239
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 297
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952"
CARBOHYD 382
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 460
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952"
CARBOHYD 468
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 554
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 741
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 752
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 760
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 776
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 782
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 821
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952"
CARBOHYD 938
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 977
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952"
CARBOHYD 1074
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1083
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1103
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1106
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1479
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1499
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1559
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952"
CARBOHYD 1703
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2010
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2209
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 167..193
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
DISULFID 248..329
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
DISULFID 500..526
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
DISULFID 603..684
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
DISULFID 1725..1751
/evidence="ECO:0000305"
DISULFID 1907..2061
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
DISULFID 2066..2221
/evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
VARIANT 15
/note="G -> S (in dbSNP:rs9332485)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021297"
VARIANT 107
/note="D -> H (in dbSNP:rs6019)"
/evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3"
/id="VAR_013886"
VARIANT 334
/note="R -> G (in Hong Kong; does not predispose to
clinical thrombosis; dbSNP:rs118203905)"
/evidence="ECO:0000269|PubMed:9454741,
ECO:0000269|PubMed:9746807"
/id="VAR_013620"
VARIANT 334
/note="R -> T (in THPH2; Cambridge; dbSNP:rs118203906)"
/evidence="ECO:0000269|PubMed:9454742"
/id="VAR_013621"
VARIANT 387
/note="I -> T (in THPH2; Liverpool; mutant protein is
expressed with an additional carbohydrate chain;
dbSNP:rs118203911)"
/evidence="ECO:0000269|PubMed:14617013,
ECO:0000269|PubMed:14695241"
/id="VAR_032698"
VARIANT 413
/note="M -> T (in dbSNP:rs6033)"
/evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3"
/id="VAR_013887"
VARIANT 513
/note="R -> K (in dbSNP:rs6020)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9454741,
ECO:0000269|Ref.3"
/id="VAR_013622"
VARIANT 534
/note="R -> Q (in THPH2; factor V Leiden; associated with
susceptibility to Budd-Chiari syndrome; associated with
susceptibility to ischemic stroke; dbSNP:rs6025)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10942390, ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:8164741, ECO:0000269|Ref.3"
/id="VAR_001213"
VARIANT 613
/note="C -> R (in THPH2; Nijkerk; dbSNP:rs1453479152)"
/evidence="ECO:0000269|PubMed:11435304"
/id="VAR_032699"
VARIANT 775
/note="S -> A (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035817"
VARIANT 781
/note="S -> R (in dbSNP:rs13306350)"
/id="VAR_047740"
VARIANT 809
/note="P -> S (in dbSNP:rs6031)"
/evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3"
/id="VAR_013888"
VARIANT 817
/note="N -> T (in dbSNP:rs6018)"
/evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3"
/id="VAR_013889"
VARIANT 858
/note="K -> R (in dbSNP:rs4524)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11758222, ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:3110773, ECO:0000269|Ref.3"
/id="VAR_001214"
VARIANT 865
/note="H -> R (in dbSNP:rs4525)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11758222, ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:3110773, ECO:0000269|Ref.3"
/id="VAR_001215"
VARIANT 915
/note="T -> S (in dbSNP:rs9332695)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021298"
VARIANT 925
/note="K -> E (in dbSNP:rs6032)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11758222, ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:3110773, ECO:0000269|Ref.3"
/id="VAR_013890"
VARIANT 969
/note="N -> S (in dbSNP:rs9332604)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021299"
VARIANT 980
/note="R -> L (in dbSNP:rs9332605)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021300"
VARIANT 1146
/note="H -> Q (in dbSNP:rs6005)"
/evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3"
/id="VAR_013891"
VARIANT 1285
/note="L -> I (in dbSNP:rs1046712)"
/evidence="ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:8713778, ECO:0000269|Ref.3"
/id="VAR_013892"
VARIANT 1327
/note="H -> R (in dbSNP:rs1800595)"
/evidence="ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:8713778"
/id="VAR_013893"
VARIANT 1397
/note="L -> F (in dbSNP:rs13306334)"
/evidence="ECO:0000269|PubMed:11758222,
ECO:0000269|PubMed:3110773"
/id="VAR_047741"
VARIANT 1404
/note="P -> S (in dbSNP:rs9332608)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021301"
VARIANT 1530
/note="E -> A (in dbSNP:rs6007)"
/evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.3"
/id="VAR_013894"
VARIANT 1685
/note="T -> S (in dbSNP:rs6011)"
/evidence="ECO:0000269|PubMed:10391209"
/id="VAR_013895"
VARIANT 1730
/note="Y -> C (in FA5D; Seoul 2; dbSNP:rs118203907)"
/evidence="ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:11435304"
/id="VAR_032700"
VARIANT 1749
/note="L -> V (in dbSNP:rs6034)"
/evidence="ECO:0000269|PubMed:10391209"
/id="VAR_013896"
VARIANT 1764
/note="M -> V (in dbSNP:rs6030)"
/evidence="ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:3110773, ECO:0000269|PubMed:7874144"
/id="VAR_013897"
VARIANT 1820
/note="M -> I (in dbSNP:rs6026)"
/evidence="ECO:0000269|PubMed:10391209"
/id="VAR_013898"
VARIANT 2102
/note="R -> C (in FA5D; impairs both factor V secretion and
activity; dbSNP:rs118203910)"
/evidence="ECO:0000269|PubMed:12393490"
/id="VAR_032701"
VARIANT 2102
/note="R -> H (in THPH2)"
/evidence="ECO:0000269|PubMed:11858490"
/id="VAR_017329"
VARIANT 2148
/note="M -> T (in dbSNP:rs9332701)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021302"
VARIANT 2185
/note="K -> R (in dbSNP:rs6679078)"
/id="VAR_034603"
VARIANT 2222
/note="D -> G (in dbSNP:rs6027)"
/evidence="ECO:0000269|PubMed:10391209"
/id="VAR_013899"
CONFLICT 741
/note="N -> S (in Ref. 7; ABD23003)"
/evidence="ECO:0000305"
CONFLICT 908
/note="E -> K (in Ref. 1; AAA52424 and 8; CAC82573)"
/evidence="ECO:0000305"
CONFLICT 991
/note="K -> E (in Ref. 5; BAF84302)"
/evidence="ECO:0000305"
CONFLICT 2213
/note="A -> T (in Ref. 1; AAA52424)"
/evidence="ECO:0000305"
TURN 1569..1571
/evidence="ECO:0007829|PDB:3S9C"
TURN 2072..2074
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2075..2077
/evidence="ECO:0007829|PDB:1CZV"
HELIX 2079..2081
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2082..2085
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2093..2095
/evidence="ECO:0007829|PDB:1CZV"
HELIX 2098..2100
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2107..2109
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2111..2113
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2123..2139
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2141..2143
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2146..2163
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2182..2185
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2188..2211
/evidence="ECO:0007829|PDB:1CZT"
STRAND 2213..2222
/evidence="ECO:0007829|PDB:1CZT"
SEQUENCE 2224 AA; 251703 MW; 24AEF3FEA7332E37 CRC64;
MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT NSSLNLSVTS
FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV HFKNKADKPL SIHPQGIRYS
KLSEGASYLD HTFPAEKMDD AVAPGREYTY EWSISEDSGP THDDPPCLTH IYYSHENLIE
DFNSGLIGPL LICKKGTLTE GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG
TMPDITVCAH DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV
GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW EYFIAAEEVI
WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE DESFTKHTVN PNMKEDGILG
PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV TFSPYEDEVN SSFTSGRNNT MIRAVQPGET
YTYKWNILEF DEPTENDAQC LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA
DIEQQAVFAV FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL
GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES VTVTMDNVGT
WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE STVMATRKMH DRLEPEDEES
DADYDYQNRL AAALGIRSFR NSSLNQEEEE FNLTALALEN GTEFVSSNTD IIVGSNYSSP
SNISKFTVNN LAEPQKAPSH QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL
QPDVTGIRLL SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS
PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA SEKGSYEIIQ
DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK FPRVRHKSLQ VRQDGGKSRL
KKSQFLIKTR KKKKEKHTHH APLSPRTFHP LRSEAYNTFS ERRLKHSLVL HKSNETSLPT
DLNQTLPSMD FGWIASLPDH NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS
TSDPSHRSSS PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS
QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS LDLSQTNLSP
ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH MTLSPELSQT NLSPALGQMP
ISPDLSHTTL SLDFSQTNLS PELSQTNLSP ALGQMPLSPD PSHTTLSLDL SQTNLSPELS
QTNLSPDLSE MPLFADLSQI PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP
DISDTTLLPD LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND
TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY KTDVRTNINS
SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE TDIEDSDDIP EDTTYKKVVF
RKYLDSTFTK RDPRGEYEEH LGILGPIIRA EVDDVIQVRF KNLASRPYSL HAHGLSYEKS
SEGKTYEDDS PEWFKEDNAV QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI
HSGLIGPLLI CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK
KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL ENGNKQHQLG
VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF LIMDRDCRMP MGLSTGIISD
SQIKASEFLG YWEPRLARLN NGGSYNAWSV EKLAAEFASK PWIQVDMQKE VIITGIQTQG
AKHYLKSCYT TEFYVAYSSN QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY
IRISPTRAYN RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR
ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV KSYTIHYSEQ
GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF IRVIPKTWNQ SIALRLELFG
CDIY


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[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) [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) (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]
[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]
[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)]
[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]
[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]
[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]
[] 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]
[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]
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B 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]
[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]
[F2RL1 GPR11 PAR2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]
[F11] Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain]
[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]
[F13A1 F13A] Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A 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)
[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 isoform 2 (PFX2) (EC 3.4.21.6) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F2rl1 Gpcr11 Gpr11 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1)
[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]
[F2rl1 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (Thrombin receptor-like 1)

Bibliography :
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