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P03951 (FA11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor XI

Short name=FXI
EC=3.4.21.27
Alternative name(s):
Plasma thromboplastin antecedent
Short name=PTA
Gene names
Name:F11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.

Catalytic activity

Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.

Enzyme regulation

Inhibited by SERPINA5. Ref.9

Subunit structure

Homodimer; disulfide-linked. Forms a heterodimer with SERPINA5. After activation the heavy and light chains are also linked by a disulfide bond. Ref.8 Ref.13

Subcellular location

Secreted.

Tissue specificity

Isoform 2 is produced by platelets and megakaryocytes but absent from other blood cells.

Post-translational modification

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36

Sequence similarities

Belongs to the peptidase S1 family. Plasma kallikrein subfamily.

Contains 4 apple domains.

Contains 1 peptidase S1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ecoP238273EBI-1041019,EBI-1029159From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P03951-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P03951-2)

Also known as: Platelet;

The sequence of this isoform differs from the canonical sequence as follows:
     109-162: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 387369Coagulation factor XIa heavy chain
PRO_0000027825
Chain388 – 625238Coagulation factor XIa light chain
PRO_0000027826

Regions

Domain20 – 10384Apple 1
Domain110 – 19384Apple 2
Domain200 – 28384Apple 3
Domain291 – 37484Apple 4
Domain388 – 623236Peptidase S1
Region547 – 5504Heparin-binding

Sites

Active site4311Charge relay system
Active site4801Charge relay system
Active site5751Charge relay system

Amino acid modifications

Glycosylation901N-linked (GlcNAc...)
Glycosylation1261N-linked (GlcNAc...) Ref.11
Glycosylation3531N-linked (GlcNAc...)
Glycosylation4501N-linked (GlcNAc...) Ref.11 Ref.12
Glycosylation4911N-linked (GlcNAc...) Ref.8 Ref.11 Ref.12
Disulfide bond20 ↔ 103 Potential
Disulfide bond29Interchain Ref.8 Ref.13
Disulfide bond46 ↔ 76 Ref.8 Ref.13
Disulfide bond50 ↔ 56 Ref.8 Ref.13
Disulfide bond110 ↔ 193 Ref.8 Ref.13
Disulfide bond136 ↔ 165 Ref.8 Ref.13
Disulfide bond140 ↔ 146 Ref.8 Ref.13
Disulfide bond200 ↔ 283 Ref.8 Ref.13
Disulfide bond226 ↔ 255 Ref.8 Ref.13
Disulfide bond230 ↔ 236 Ref.8 Ref.13
Disulfide bond291 ↔ 374 Ref.8 Ref.13
Disulfide bond317 ↔ 346 Ref.8 Ref.13
Disulfide bond321 ↔ 327 Ref.8 Ref.13
Disulfide bond339Interchain Potential
Disulfide bond380 ↔ 500Interchain (between heavy and light chains) Ref.8 Ref.13
Disulfide bond416 ↔ 432 Ref.8 Ref.13
Disulfide bond514 ↔ 581 Ref.8 Ref.13
Disulfide bond545 ↔ 560 Ref.8 Ref.13
Disulfide bond571 ↔ 599 Ref.8 Ref.13

Natural variations

Alternative sequence109 – 16254Missing in isoform 2.
VSP_005388
Natural variant321G → R in FA11D. Ref.31
Corresponds to variant rs281875259 [ dbSNP | Ensembl ].
VAR_067929
Natural variant341D → H in FA11D. Ref.16
Corresponds to variant rs281875267 [ dbSNP | Ensembl ].
VAR_012085
Natural variant431A → T in FA11D; dominant-negative mutation that results in severely decreased protein secretion. Ref.32
Corresponds to variant rs281875264 [ dbSNP | Ensembl ].
VAR_067930
Natural variant461C → F in FA11D. Ref.28
Corresponds to variant rs281875271 [ dbSNP | Ensembl ].
VAR_054894
Natural variant511T → I in FA11D. Ref.30
Corresponds to variant rs281875252 [ dbSNP | Ensembl ].
VAR_067931
Natural variant511T → P in FA11D. Ref.30 Ref.36
Corresponds to variant rs281875243 [ dbSNP | Ensembl ].
VAR_067932
Natural variant531H → Q in FA11D. Ref.31
Corresponds to variant rs281875261 [ dbSNP | Ensembl ].
VAR_067933
Natural variant561C → R in FA11D; secretion of the mutant protein is impaired. Ref.25 Ref.36
Corresponds to variant rs121965069 [ dbSNP | Ensembl ].
VAR_054895
Natural variant631A → V in FA11D. Ref.36
Corresponds to variant rs281875244 [ dbSNP | Ensembl ].
VAR_067934
Natural variant661P → L. Ref.23
Corresponds to variant rs5968 [ dbSNP | Ensembl ].
VAR_011774
Natural variant1011K → R in FA11D. Ref.28
Corresponds to variant rs281875272 [ dbSNP | Ensembl ].
VAR_054896
Natural variant1401C → Y in FA11D. Ref.29
Corresponds to variant rs281875256 [ dbSNP | Ensembl ].
VAR_067935
Natural variant1511Y → C in FA11D. Ref.28
Corresponds to variant rs281875273 [ dbSNP | Ensembl ].
VAR_054897
Natural variant2221D → Y in FA11D. Ref.36
Corresponds to variant rs281875245 [ dbSNP | Ensembl ].
VAR_067936
Natural variant2281R → Q in FA11D. Ref.36
Corresponds to variant rs281875246 [ dbSNP | Ensembl ].
VAR_067937
Natural variant2411F → L in FA11D; dominant-negative mutation that results in severely decreased protein secretion. Ref.32
Corresponds to variant rs281875265 [ dbSNP | Ensembl ].
VAR_067938
Natural variant2441Q → R Found in a patient with factor XI deficiency that also carries mutation N-266. Ref.19 Ref.23
Corresponds to variant rs5969 [ dbSNP | Ensembl ].
VAR_011775
Natural variant2461W → C in FA11D. Ref.21
Corresponds to variant rs281875279 [ dbSNP | Ensembl ].
VAR_012086
Natural variant2521R → T in FA11D. Ref.31
Corresponds to variant rs281875260 [ dbSNP | Ensembl ].
VAR_067939
Natural variant2551C → Y in FA11D; secretion of the mutant protein is impaired. Ref.25
Corresponds to variant rs281875277 [ dbSNP | Ensembl ].
VAR_054898
Natural variant2631G → E in FA11D. Ref.28
Corresponds to variant rs281875274 [ dbSNP | Ensembl ].
VAR_054899
Natural variant2661S → N in FA11D. Ref.19
Corresponds to variant rs145168351 [ dbSNP | Ensembl ].
VAR_012087
Natural variant2701K → I in FA11D; although the mutant protein is synthesized the secretion is reduced. Ref.27
Corresponds to variant rs121965070 [ dbSNP | Ensembl ].
VAR_054900
Natural variant2761S → C in FA11D. Ref.36
Corresponds to variant rs281875247 [ dbSNP | Ensembl ].
VAR_067940
Natural variant2771G → D in FA11D. Ref.36
Corresponds to variant rs281875248 [ dbSNP | Ensembl ].
VAR_067941
Natural variant3011F → L in FA11D. Ref.14 Ref.15
Corresponds to variant rs121965064 [ dbSNP | Ensembl ].
VAR_006622
Natural variant3081I → F. Ref.23
Corresponds to variant rs5972 [ dbSNP | Ensembl ].
VAR_011776
Natural variant3151E → K in FA11D. Ref.29
Corresponds to variant rs281875257 [ dbSNP | Ensembl ].
VAR_067942
Natural variant3201L → P in FA11D. Ref.16
Corresponds to variant rs281875268 [ dbSNP | Ensembl ].
VAR_012088
Natural variant3221T → I in FA11D. Ref.16
Corresponds to variant rs281875269 [ dbSNP | Ensembl ].
VAR_012089
Natural variant3261R → C in FA11D. Ref.22
Corresponds to variant rs28934608 [ dbSNP | Ensembl ].
VAR_012090
Natural variant3311T → I in FA11D. Ref.30
Corresponds to variant rs281875253 [ dbSNP | Ensembl ].
VAR_067943
Natural variant3391C → F. Ref.4 Ref.23 Ref.25
Corresponds to variant rs5967 [ dbSNP | Ensembl ].
VAR_011777
Natural variant3411E → K in FA11D. Ref.16
Corresponds to variant rs281875270 [ dbSNP | Ensembl ].
VAR_012091
Natural variant3601L → P in FA11D. Ref.30
Corresponds to variant rs281875254 [ dbSNP | Ensembl ].
VAR_067944
Natural variant3991W → R.
Corresponds to variant rs1800439 [ dbSNP | Ensembl ].
VAR_011778
Natural variant4011W → R in FA11D. Ref.31
Corresponds to variant rs281875262 [ dbSNP | Ensembl ].
VAR_067945
Natural variant4031V → M in FA11D; dominant-negative mutation that results in severely decreased protein secretion. Ref.32
Corresponds to variant rs281875266 [ dbSNP | Ensembl ].
VAR_067946
Natural variant4041T → N in FA11D. Ref.18
Corresponds to variant rs121965067 [ dbSNP | Ensembl ].
VAR_012092
Natural variant4181G → V in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. Ref.26
Corresponds to variant rs121965071 [ dbSNP | Ensembl ].
VAR_054901
Natural variant4301A → V in FA11D. Ref.22 Ref.28
Corresponds to variant rs121965068 [ dbSNP | Ensembl ].
VAR_012093
Natural variant4541I → K in FA11D. Ref.35
Corresponds to variant rs281875241 [ dbSNP | Ensembl ].
VAR_067947
Natural variant4601F → V in FA11D. Ref.17
Corresponds to variant rs121965065 [ dbSNP | Ensembl ].
VAR_012094
Natural variant4811I → S in FA11D. Ref.34
Corresponds to variant rs281875242 [ dbSNP | Ensembl ].
VAR_067948
Natural variant4931T → I in FA11D. Ref.22
VAR_012095
Natural variant5031S → P in FA11D. Ref.30
Corresponds to variant rs140068026 [ dbSNP | Ensembl ].
VAR_067949
Natural variant5061D → G in FA11D; mild phenotype. Ref.33
Corresponds to variant rs281875258 [ dbSNP | Ensembl ].
VAR_067950
Natural variant5111Y → H in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion. Ref.25
Corresponds to variant rs281875278 [ dbSNP | Ensembl ].
VAR_054902
Natural variant5141C → F in FA11D. Ref.36
Corresponds to variant rs281875249 [ dbSNP | Ensembl ].
VAR_067951
Natural variant5261D → E in FA11D. Ref.31
Corresponds to variant rs281875263 [ dbSNP | Ensembl ].
VAR_067952
Natural variant5381P → L in FA11D. Ref.28
Corresponds to variant rs139695003 [ dbSNP | Ensembl ].
VAR_054903
Natural variant5651E → K in FA11D. Ref.28
Corresponds to variant rs281875275 [ dbSNP | Ensembl ].
VAR_054904
Natural variant5751S → L in FA11D. Ref.36
Corresponds to variant rs281875250 [ dbSNP | Ensembl ].
VAR_067953
Natural variant5871W → S in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. Ref.26
Corresponds to variant rs121965072 [ dbSNP | Ensembl ].
VAR_054905
Natural variant5941S → R in FA11D. Ref.22
Corresponds to variant rs28934609 [ dbSNP | Ensembl ].
VAR_012096
Natural variant5971E → K in FA11D. Ref.29 Ref.36
Corresponds to variant rs281875251 [ dbSNP | Ensembl ].
VAR_067954
Natural variant6081Y → H in FA11D. Ref.30
Corresponds to variant rs281875255 [ dbSNP | Ensembl ].
VAR_067955
Natural variant6181I → S in FA11D. Ref.28
Corresponds to variant rs281875276 [ dbSNP | Ensembl ].
VAR_054906

Experimental info

Sequence conflict2261C → S in AAA51985. Ref.2

Secondary structure

............................................................................................................................... 625
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: 147AFA94B7709E8F

FASTA62570,109
        10         20         30         40         50         60 
MIFLYQVVHF ILFTSVSGEC VTQLLKDTCF EGGDITTVFT PSAKYCQVVC TYHPRCLLFT 

        70         80         90        100        110        120 
FTAESPSEDP TRWFTCVLKD SVTETLPRVN RTAAISGYSF KQCSHQISAC NKDIYVDLDM 

       130        140        150        160        170        180 
KGINYNSSVA KSAQECQERC TDDVHCHFFT YATRQFPSLE HRNICLLKHT QTGTPTRITK 

       190        200        210        220        230        240 
LDKVVSGFSL KSCALSNLAC IRDIFPNTVF ADSNIDSVMA PDAFVCGRIC THHPGCLFFT 

       250        260        270        280        290        300 
FFSQEWPKES QRNLCLLKTS ESGLPSTRIK KSKALSGFSL QSCRHSIPVF CHSSFYHDTD 

       310        320        330        340        350        360 
FLGEELDIVA AKSHEACQKL CTNAVRCQFF TYTPAQASCN EGKGKCYLKL SSNGSPTKIL 

       370        380        390        400        410        420 
HGRGGISGYT LRLCKMDNEC TTKIKPRIVG GTASVRGEWP WQVTLHTTSP TQRHLCGGSI 

       430        440        450        460        470        480 
IGNQWILTAA HCFYGVESPK ILRVYSGILN QSEIKEDTSF FGVQEIIIHD QYKMAESGYD 

       490        500        510        520        530        540 
IALLKLETTV NYTDSQRPIC LPSKGDRNVI YTDCWVTGWG YRKLRDKIQN TLQKAKIPLV 

       550        560        570        580        590        600 
TNEECQKRYR GHKITHKMIC AGYREGGKDA CKGDSGGPLS CKHNEVWHLV GITSWGEGCA 

       610        620 
QRERPGVYTN VVEYVDWILE KTQAV 

« Hide

Isoform 2 (Platelet) [UniParc].

Checksum: FB9D65D72151755E
Show »

FASTA57163,840

References

« Hide 'large scale' references
[1]"Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein."
Fujikawa K., Chung D.W., Hendrickson L.E., Davie E.W.
Biochemistry 25:2417-2424(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Organization of the gene for human factor XI."
Asakai R., Davie E.W., Chung D.W.
Biochemistry 26:7221-7228(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]"Molecular cloning of platelet factor XI, an alternative splicing product of the plasma factor XI gene."
Hsu T.-C., Shore S.K., Seshsmma T., Bagasra O., Walsh P.N.
J. Biol. Chem. 273:13787-13793(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]SeattleSNPs variation discovery resource
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-339.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains."
McMullen B.A., Fujikawa K., Davie E.W.
Biochemistry 30:2056-2060(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
[9]"Inactivation of human plasma kallikrein and factor XIa by protein C inhibitor."
Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M., Bouma B.N.
Biochemistry 27:4231-4237(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
[10]"Localization of a heparin binding site in the catalytic domain of factor XIa."
Badellino K.O., Walsh P.N.
Biochemistry 40:7569-7580(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: HEPARIN-BINDING SITE.
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-450 AND ASN-491.
Tissue: Plasma.
[12]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-491.
Tissue: Liver.
[13]"Clavatadine A, a natural product with selective recognition and irreversible inhibition of factor XIa."
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.
J. Med. Chem. 51:3583-3587(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 388-625 IN COMPLEX WITH INHIBITOR, DISULFIDE BONDS.
[14]"Factor XI (plasma thromboplastin antecedent) deficiency in Ashkenazi Jews is a bleeding disorder that can result from three types of point mutations."
Asakai R., Chung D.W., Ratnoff O.D., Davie E.W.
Proc. Natl. Acad. Sci. U.S.A. 86:7667-7671(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D LEU-301.
[15]"Expression of human blood coagulation factor XI: characterization of the defect in factor XI type III deficiency."
Meijers J.C., Davie E.W., Chung D.W.
Blood 79:1435-1440(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D LEU-301.
[16]"Six point mutations that cause factor XI deficiency."
Pugh R.E., McVey J.H., Tuddenham E.G., Hancock J.F.
Blood 85:1509-1516(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D HIS-34; PRO-320; ILE-322 AND LYS-341.
[17]"Identification of two novel mutations in non-Jewish factor XI deficiency."
Imanaka Y., Lal K., Nishimura T., Bolton-Maggs P.H., Tuddenham E.G., McVey J.H.
Br. J. Haematol. 90:916-920(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D VAL-460.
[18]"Severe factor XI deficiency in an Arab family associated with a novel mutation in exon 11."
Wistinghausen B., Reischer A., Oddoux C., Ostrer H., Nardi M., Karpatkin M.
Br. J. Haematol. 99:575-577(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D ASN-404.
[19]"Identification of mutations and polymorphisms in the factor XI genes of an African American family by dideoxyfingerprinting."
Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A., Gailani D.
Blood 92:3309-3317(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D ASN-266, VARIANT ARG-244.
[20]Erratum
Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A., Gailani D.
Blood 93:1786-1786(1999)
[21]"Identification of a novel mutation in a non-Jewish factor XI deficient kindred."
Alhaq A., Mitchell M., Sethi M., Rahman S., Flynn G., Boulton P., Caeno G., Smith M., Savidge G.
Br. J. Haematol. 104:44-49(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D CYS-246.
[22]"Heterozygous factor XI deficiency associated with three novel mutations."
Mitchell M., Cutler J., Thompson S., Moore G., Jenkins Ap Rees E., Smith M., Savidge G., Alhaq A.
Br. J. Haematol. 107:763-765(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D CYS-326; VAL-430 ILE-493 AND ARG-594.
[23]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
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. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-66; ARG-244; PHE-308 AND PHE-339.
[24]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)
[25]"Factor XI deficiency in French Basques is caused predominantly by an ancestral Cys38Arg mutation in the factor XI gene."
Zivelin A., Bauduer F., Ducout L., Peretz H., Rosenberg N., Yatuv R., Seligsohn U.
Blood 99:2448-2454(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D ARG-56; TYR-255 AND HIS-511, VARIANT PHE-339, CHARACTERIZATION OF VARIANTS FA11D ARG-56; TYR-255 AND HIS-511.
[26]"Dominant factor XI deficiency caused by mutations in the factor XI catalytic domain."
Kravtsov D.V., Wu W., Meijers J.C.M., Sun M.-F., Blinder M.A., Dang T.P., Wang H., Gailani D.
Blood 104:128-134(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D VAL-418 AND SER-587, CHARACTERIZATION OF VARIANTS FA11D VAL-418 AND SER-587.
[27]"Severe factor XI deficiency caused by compound heterozygosity."
Dai L., Mitchell M., Carson P., Creagh D., Cutler J., Savidge G., Alhaq A.
Br. J. Haematol. 125:817-818(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D ILE-270, CHARACTERIZATION OF VARIANT F11 DEFICIENCY ILE-270.
[28]"Genetic analysis in FXI deficiency: six novel mutations and the use of a polymerase chain reaction-based test to define a whole gene deletion."
Hill M., McLeod F., Franks H., Gordon B., Dolan G.
Br. J. Haematol. 129:825-829(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D PHE-46; ARG-101; CYS-151; GLU-263; VAL-430; LEU-538; LYS-565 AND SER-618.
[29]"Identification of five novel mutations in the factor XI gene (F11) of patients with factor XI deficiency."
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.
Blood Coagul. Fibrinolysis 17:69-73(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D TYR-140; LYS-315 AND LYS-597.
[30]"Seven novel point mutations in the F11 gene in Iranian FXI-deficient patients."
Fard-Esfahani P., Lari G.R., Ravanbod S., Mirkhani F., Allahyari M., Rassoulzadegan M., Ala F.
Haemophilia 14:91-95(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D ILE-51; PRO-51; ILE-331; PRO-360; PRO-503 AND HIS-608.
[31]"Population-specific spectrum of the F11 mutations in Koreans: evidence for a founder effect."
Kim J., Song J., Lyu C., Kim Y., Oh S., Choi Y., Yoo J., Choi J., Kim H., Lee K.A.
Clin. Genet. 82:180-186(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D ARG-32; GLN-53; THR-252; ARG-401 AND GLU-526.
[32]"Three dominant-negative mutations in factor XI-deficient patients."
Dai L., Rangarajan S., Mitchell M.
Haemophilia 17:E919-E922(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D THR-43; LEU-241 AND MET-403, CHARACTERIZATION OF VARIANTS FA11D THR-43; LEU-241 AND MET-403.
[33]"A novel missense mutation Asp506Gly in exon 13 of the F11 gene in an asymptomatic Korean woman with mild factor XI deficiency."
Lee J.H., Cho H.S., Hyun M.S., Kim H.Y., Kim H.J.
Korean J. Lab. Med. 31:290-293(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D GLY-506.
[34]"Identification of a novel F11 missense mutation (Ile463Ser) in a family with congenital factor XI deficiency."
Tirefort Y., Uhr M.R., Neerman-Arbez M., de Moerloose P.
Blood Coagul. Fibrinolysis 23:251-252(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D SER-481.
[35]"A cluster of factor XI-deficient patients due to a new mutation (Ile 436 Lys) in northeastern Italy."
Girolami A., Scarparo P., Bonamigo E., Santarossa L., Cristiani A., Moro S., Lombardi A.M.
Eur. J. Haematol. 88:229-236(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA11D LYS-454.
[36]"Revisiting the molecular epidemiology of factor XI deficiency: nine new mutations and an original large 4qTer deletion in western Brittany (France)."
Gueguen P., Chauvin A., Quemener-Redon S., Pan-Petesch B., Ferec C., Abgrall J.F., Le Marechal C.
Thromb. Haemost. 107:44-50(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA11D PRO-51; ARG-56; VAL-63; TYR-222; GLN-228; CYS-276; ASP-277; PHE-514; LEU-575 AND LYS-597.
+Additional computationally mapped references.

Web resources

Wikipedia

Factor XI entry

GeneReviews
SeattleSNPs
Mendelian genes Coagulation factor XI (F11)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13142 mRNA. Translation: AAA52487.1.
M20218 expand/collapse EMBL AC list , M18296, M21184, M18298, M18299, M18300, M18301, M18302, M18303, M18304, M19417, M20217 Genomic DNA. Translation: AAA51985.1.
AF045649 mRNA. Translation: AAC24506.1.
AY191837 Genomic DNA. Translation: AAN85554.1.
AC110771 Genomic DNA. Translation: AAY40901.1.
CH471056 Genomic DNA. Translation: EAX04621.1.
BC119014 mRNA. Translation: AAI19015.1.
BC122863 mRNA. Translation: AAI22864.1.
PIRKFHU1. A27431.
RefSeqNP_000119.1. NM_000128.3.
UniGeneHs.1430.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XX9X-ray2.20A/B388-625[»]
1XXDX-ray2.91A/B388-625[»]
1XXFX-ray2.60A/B388-625[»]
1ZHMX-ray1.96A388-624[»]
1ZHPX-ray2.70A388-625[»]
1ZHRX-ray1.73A388-625[»]
1ZJDX-ray2.60A388-624[»]
1ZLRX-ray2.50A388-624[»]
1ZMJX-ray2.00A388-624[»]
1ZMLX-ray2.25A388-625[»]
1ZMNX-ray2.05A388-625[»]
1ZOMX-ray2.25A388-624[»]
1ZPBX-ray2.10A388-624[»]
1ZPCX-ray2.60A388-624[»]
1ZPZX-ray2.50A388-625[»]
1ZRKX-ray2.30A388-625[»]
1ZSJX-ray1.90A388-625[»]
1ZSKX-ray1.90A388-625[»]
1ZSLX-ray2.05A388-625[»]
1ZTJX-ray2.05A388-625[»]
1ZTKX-ray2.50A388-625[»]
1ZTLX-ray2.60A388-625[»]
2F83X-ray2.87A1-625[»]
2FDAX-ray2.00A388-625[»]
2J8JNMR-A/B290-379[»]
2J8LNMR-A/B290-379[»]
3BG8X-ray1.60A388-625[»]
3SORX-ray1.80A388-625[»]
3SOSX-ray2.58A388-625[»]
ProteinModelPortalP03951.
SMRP03951. Positions 20-623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108458. 3 interactions.
DIPDIP-29085N.
IntActP03951. 1 interaction.
STRING9606.ENSP00000264691.

Chemistry

BindingDBP03951.
ChEMBLCHEMBL2820.
DrugBankDB00100. Coagulation Factor IX.
GuidetoPHARMACOLOGY2360.

Protein family/group databases

MEROPSS01.213.

PTM databases

PhosphoSiteP03951.

Polymorphism databases

DMDM119762.

Proteomic databases

PaxDbP03951.
PeptideAtlasP03951.
PRIDEP03951.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000403665; ENSP00000384957; ENSG00000088926. [P03951-1]
GeneID2160.
KEGGhsa:2160.
UCSCuc003iza.1. human. [P03951-1]

Organism-specific databases

CTD2160.
GeneCardsGC04P187187.
HGNCHGNC:3529. F11.
MIM264900. gene.
612416. phenotype.
neXtProtNX_P03951.
Orphanet329. Congenital factor XI deficiency.
PharmGKBPA27941.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000112467.
HOVERGENHBG000399.
InParanoidP03951.
KOK01323.
OMAVWHLVGI.
OrthoDBEOG75B84T.
PhylomeDBP03951.
TreeFamTF343687.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP03951.
BgeeP03951.
CleanExHS_F11.
GenevestigatorP03951.

Family and domain databases

InterProIPR000177. Apple.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00024. PAN_1. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00005. APPLEDOMAIN.
PR00722. CHYMOTRYPSIN.
SMARTSM00223. APPLE. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS00495. APPLE. 4 hits.
PS50948. PAN. 4 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSF11. human.
EvolutionaryTraceP03951.
GeneWikiFactor_XI.
GenomeRNAi2160.
NextBio8727.
PMAP-CutDBP03951.
PROP03951.
SOURCESearch...

Entry information

Entry nameFA11_HUMAN
AccessionPrimary (citable) accession number: P03951
Secondary accession number(s): D3DP64, Q4W5C2, Q9Y495
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: March 19, 2014
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM