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UniProtKB/Swiss-Prot entry P03951


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FA11_HUMAN
Primary accession number P03951
Secondary accession numbers Q4W5C2 Q9Y495
Integrated into Swiss-Prot on October 23, 1986
Sequence was last modified on October 23, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 121)
Name and origin of the protein
Protein name Coagulation factor XI [Precursor]
Synonyms FXI
EC 3.4.21.27
Plasma thromboplastin antecedent
PTA
Contains Coagulation factor XIa heavy chain
Coagulation factor XIa light chain
Gene name
Name: F11
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1021/bi00357a018; PubMed=3636155 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1021/bi00397a004; PubMed=2827746 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1074/jbc.273.22.13787; PubMed=9593722 [NCBI, ExPASy, EBI, Israel, Japan]
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 program for genomic applications;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
DOI=10.1021/bi00222a008; PubMed=1998667 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
HEPARIN-BINDING SITE.
PubMed=11412111 [NCBI, ExPASy, EBI, Israel, Japan]
Badellino K.O., Walsh P.N.;
"Localization of a heparin binding site in the catalytic domain of factor XIa.";
Biochemistry 40:7569-7580(2001).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-450 AND ASN-491, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND THR-22, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[11]
VARIANT F11 DEFICIENCY LEU-301.
PubMed=2813350 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
VARIANT F11 DEFICIENCY LEU-301.
PubMed=1547342 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
VARIANTS F11 DEFICIENCY HIS-34; PRO-320; ILE-322 AND LYS-341.
PubMed=7888672 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
VARIANT F11 DEFICIENCY VAL-460.
PubMed=7669672 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
VARIANT F11 DEFICIENCY ASN-404.
DOI=10.1046/j.1365-2141.1997.4343244.x; PubMed=9401068 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
VARIANTS F11 DEFICIENCY ARG-244 AND ASN-266.
PubMed=9787168 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
ERRATUM.
Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A., Gailani D.;
Blood 93:1786-1786(1999).
[18]
VARIANT F11 DEFICIENCY CYS-246.
DOI=10.1046/j.1365-2141.1999.01150.x; PubMed=10027710 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
VARIANTS F11 DEFICIENCY CYS-326; VAL-430 AND ARG-594.
DOI=10.1046/j.1365-2141.1999.01769.x; PubMed=10606881 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
VARIANTS LEU-66; ARG-244; PHE-308 AND PHE-339.
DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.;
Nat. Genet. 23:373-373(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M13142; AAA52487.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20218; AAA51985.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18296; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21184; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18298; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18299; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18300; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18301; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18302; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18303; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18304; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19417; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20217; AAA51985.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045649; AAC24506.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY191837; AAN85554.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC110771; AAY40901.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119014; AAI19015.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC122863; AAI22864.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A27431; KFHU1.
RefSeq NP_000119.1; -.
UniGene Hs.1430
3D structure databases
PDB
1XX9; X-ray; 2.20 A; A/B=388-625.[ExPASy / RCSB / EBI]
1XXD; X-ray; 2.91 A; A/B=388-625.[ExPASy / RCSB / EBI]
1XXF; X-ray; 2.60 A; A/B=388-625.[ExPASy / RCSB / EBI]
1ZHM; X-ray; 1.96 A; A=388-625.[ExPASy / RCSB / EBI]
1ZHP; X-ray; 2.70 A; A=388-625.[ExPASy / RCSB / EBI]
1ZHR; X-ray; 1.73 A; A=388-625.[ExPASy / RCSB / EBI]
1ZJD; X-ray; 2.60 A; A=388-624.[ExPASy / RCSB / EBI]
1ZLR; X-ray; 2.50 A; A=388-624.[ExPASy / RCSB / EBI]
1ZMJ; X-ray; 2.00 A; A=388-625.[ExPASy / RCSB / EBI]
1ZML; X-ray; 2.25 A; A=388-625.[ExPASy / RCSB / EBI]
1ZMN; X-ray; 2.05 A; A=388-625.[ExPASy / RCSB / EBI]
1ZOM; X-ray; 2.25 A; A=388-625.[ExPASy / RCSB / EBI]
1ZPB; X-ray; 2.10 A; A=388-625.[ExPASy / RCSB / EBI]
1ZPC; X-ray; 2.60 A; A=388-625.[ExPASy / RCSB / EBI]
1ZPZ; X-ray; 2.50 A; A=388-625.[ExPASy / RCSB / EBI]
1ZRK; X-ray; 2.30 A; A=388-625.[ExPASy / RCSB / EBI]
1ZSJ; X-ray; 1.90 A; A=388-625.[ExPASy / RCSB / EBI]
1ZSK; X-ray; 1.90 A; A=388-625.[ExPASy / RCSB / EBI]
1ZSL; X-ray; 2.05 A; A=388-625.[ExPASy / RCSB / EBI]
1ZTJ; X-ray; 2.05 A; A=388-625.[ExPASy / RCSB / EBI]
1ZTK; X-ray; 2.50 A; A=388-625.[ExPASy / RCSB / EBI]
1ZTL; X-ray; 2.60 A; A=388-625.[ExPASy / RCSB / EBI]
2F83; X-ray; 2.87 A; A=1-625.[ExPASy / RCSB / EBI]
2FDA; X-ray; 2.00 A; A=388-625.[ExPASy / RCSB / EBI]
2J8J; NMR; -; A/B=290-379.[ExPASy / RCSB / EBI]
2J8L; NMR; -; A/B=290-379.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XX9; -.
1XXD; -.
1XXF; -.
1ZHM; -.
1ZHP; -.
1ZHR; -.
1ZJD; -.
1ZLR; -.
1ZMJ; -.
1ZML; -.
1ZMN; -.
1ZOM; -.
1ZPB; -.
1ZPC; -.
1ZPZ; -.
1ZRK; -.
1ZSJ; -.
1ZSK; -.
1ZSL; -.
1ZTJ; -.
1ZTK; -.
1ZTL; -.
2F83; -.
2FDA; -.
2J8J; -.
2J8L; -.
ModBase P03951.
Protein-protein interaction databases
DIP DIP:29085N; -.
Protein family/group databases
MEROPS S01.213; -.
PTM databases
PhosphoSite P03951; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
Organism-specific databases
H-InvDB HIX0031358; -.
HGNC HGNC:3529; F11.
GenAtlas F11.
MIM 264900; gene+phenotype. [NCBI / EBI]
Orphanet 329; Factor XI deficiency, congenital.
PharmGKB PA24968; -.
GeneCards P03951.
Gene expression databases
ArrayExpress P03951; -.
CleanEx HS_F11; -.
GermOnline ENSG00000088926; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0016020; Cellular component: membrane (non-traceable author statement from UniProtKB).
GO:0004252; Molecular function: serine-type endopeptidase activity (non-traceable author statement from UniProtKB).
GO:0007596; Biological process: blood coagulation (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000177; Apple.
IPR003014; PAN.
IPR003609; Pan_app.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Pfam PF00024; PAN_1; 4.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00005; APPLEDOMAIN.
PR00722; CHYMOTRYPSIN.
SMART SM00223; APPLE; 4.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS00495; APPLE; 4.
PS50948; PAN; 4.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P03951.
ProtoNet P03951.
Proteomic databases
PeptideAtlas P03951; -.
Genome annotation databases
Ensembl ENSG00000088926; Homo sapiens. [Contig view]
GeneID 2160; -.
KEGG hsa:2160; -.
NMPDR fig|9606.3.peg.24953; -.
Phylogenomic databases
HOGENOM P03951; -.
HOVERGEN P03951; -.
Other
BindingDB P03951; -.
DrugBank DB00100; Coagulation Factor IX.
NextBio 8727; -.
SOURCE F11; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Blood coagulation; Direct protein sequencing; Disease mutation; Glycoprotein; Heparin-binding; Hydrolase; Phosphoprotein; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   387  369     Coagulation factor XIa heavy chain. PRO_0000027825
CHAIN   388   625  238     Coagulation factor XIa light chain. PRO_0000027826
DOMAIN   20   103  84     Apple 1. 
DOMAIN   110   193  84     Apple 2. 
DOMAIN   200   283  84     Apple 3. 
DOMAIN   291   374  84     Apple 4. 
DOMAIN   388   623  236     Peptidase S1. 
REGION   547   550  4     Heparin-binding. 
ACT_SITE   431   431        Charge relay system. 
ACT_SITE   480   480        Charge relay system. 
ACT_SITE   575   575        Charge relay system. 
MOD_RES   17    17        Phosphoserine. 
MOD_RES   22    22        Phosphothreonine. 
CARBOHYD   90    90        N-linked (GlcNAc...). 
CARBOHYD   126   126        N-linked (GlcNAc...). 
CARBOHYD   353   353        N-linked (GlcNAc...). 
CARBOHYD   450   450        N-linked (GlcNAc...). 
CARBOHYD   491   491        N-linked (GlcNAc...). 
DISULFID   20   103        Potential. 
DISULFID   29    29        Interchain. 
DISULFID   46    76         
DISULFID   50    56         
DISULFID   110   193         
DISULFID   136   165         
DISULFID   140   146         
DISULFID   200   283         
DISULFID   226   255         
DISULFID   230   236         
DISULFID   291   374         
DISULFID   317   346         
DISULFID   321   327         
DISULFID   339   339        Interchain (Potential). 
DISULFID   380   500        Interchain (between heavy and light chains). 
DISULFID   416   432         
DISULFID   514   581        Potential. 
DISULFID   545   560         
DISULFID   571   599        Potential. 
VAR_SEQ   109   162        Missing (in isoform 2). VSP_005388
VARIANT   34    34  1     D -> H (in F11 deficiency). VAR_012085 
VARIANT   66    66  1     P -> L (in dbSNP:rs5968 [NCBI]). VAR_011774 
VARIANT   244   244  1     Q -> R (in F11 deficiency; dbSNP:rs5969 [NCBI]). VAR_011775 
VARIANT   246   246  1     W -> C (in F11 deficiency). VAR_012086 
VARIANT   266   266  1     S -> N (in F11 deficiency). VAR_012087 
VARIANT   301   301  1     F -> L (in F11 deficiency; frequent mutation in Ashkenazi patients). VAR_006622 
VARIANT   308   308  1     I -> F (in dbSNP:rs5972 [NCBI]). VAR_011776 
VARIANT   320   320  1     L -> P (in F11 deficiency). VAR_012088 
VARIANT   322   322  1     T -> I (in F11 deficiency). VAR_012089 
VARIANT   326   326  1     R -> C (in F11 deficiency). VAR_012090 
VARIANT   339   339  1     C -> F (in dbSNP:rs5967 [NCBI]). VAR_011777 
VARIANT   341   341  1     E -> K (in F11 deficiency).