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P03951 (FA11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
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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)
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 heterodimer with SERPINA5. After activation the heavy and light chains are also linked by a disulfide bond. Ref.8

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

Defects in F11 are the cause of factor XI deficiency (FA11D) [MIM:612416]; also known as plasma thromboplastin antecedent deficiency or Rosenthal syndrome. It is 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. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28

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

Modified residue171Phosphoserine Ref.12
Modified residue221Phosphothreonine Ref.12
Glycosylation901N-linked (GlcNAc...)
Glycosylation1261N-linked (GlcNAc...) Ref.11
Glycosylation3531N-linked (GlcNAc...)
Glycosylation4501N-linked (GlcNAc...) Ref.11 Ref.13
Glycosylation4911N-linked (GlcNAc...) Ref.8 Ref.11 Ref.13
Disulfide bond20 ↔ 103 Potential
Disulfide bond29Interchain Ref.8
Disulfide bond46 ↔ 76 Ref.8
Disulfide bond50 ↔ 56 Ref.8
Disulfide bond110 ↔ 193 Ref.8
Disulfide bond136 ↔ 165 Ref.8
Disulfide bond140 ↔ 146 Ref.8
Disulfide bond200 ↔ 283 Ref.8
Disulfide bond226 ↔ 255 Ref.8
Disulfide bond230 ↔ 236 Ref.8
Disulfide bond291 ↔ 374 Ref.8
Disulfide bond317 ↔ 346 Ref.8
Disulfide bond321 ↔ 327 Ref.8
Disulfide bond339Interchain Potential
Disulfide bond380 ↔ 500Interchain (between heavy and light chains) Ref.8
Disulfide bond416 ↔ 432 Ref.8
Disulfide bond514 ↔ 581 Potential
Disulfide bond545 ↔ 560 Ref.8
Disulfide bond571 ↔ 599 Potential

Natural variations

Alternative sequence109 – 16254Missing in isoform 2.
VSP_005388
Natural variant341D → H in FA11D. Ref.16
VAR_012085
Natural variant461C → F in FA11D. Ref.28
VAR_054894
Natural variant561C → R in FA11D; autosomal dominant; secretion of the mutant protein is impaired. Ref.25
VAR_054895
Natural variant661P → L. Ref.23
Corresponds to variant rs5968 [ dbSNP | Ensembl ].
VAR_011774
Natural variant1011K → R in FA11D. Ref.28
VAR_054896
Natural variant1511Y → C in FA11D. Ref.28
VAR_054897
Natural variant2441Q → R in FA11D. Ref.19 Ref.23
Corresponds to variant rs5969 [ dbSNP | Ensembl ].
VAR_011775
Natural variant2461W → C in FA11D. Ref.21
VAR_012086
Natural variant2551C → Y in FA11D; secretion of the mutant protein is impaired. Ref.25
VAR_054898
Natural variant2631G → E in FA11D. Ref.28
VAR_054899
Natural variant2661S → N in FA11D. Ref.19
VAR_012087
Natural variant2701K → I in FA11D; although the mutant protein is synthesized the secretion is reduced. Ref.27
VAR_054900
Natural variant3011F → L in FA11D. Ref.14 Ref.15
VAR_006622
Natural variant3081I → F. Ref.23
Corresponds to variant rs5972 [ dbSNP | Ensembl ].
VAR_011776
Natural variant3201L → P in FA11D. Ref.16
VAR_012088
Natural variant3221T → I in FA11D. Ref.16
VAR_012089
Natural variant3261R → C in FA11D. Ref.22
Corresponds to variant rs28934608 [ dbSNP | Ensembl ].
VAR_012090
Natural variant3391C → F. Ref.4 Ref.23 Ref.25
Corresponds to variant rs5967 [ dbSNP | Ensembl ].
VAR_011777
Natural variant3411E → K in FA11D. Ref.16
VAR_012091
Natural variant3991W → R.
Corresponds to variant rs1800439 [ dbSNP | Ensembl ].
VAR_011778
Natural variant4041T → N in FA11D. Ref.18
VAR_012092
Natural variant4181G → V in FA11D; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect. Ref.26
VAR_054901
Natural variant4301A → V in FA11D. Ref.22 Ref.28
Corresponds to variant rs28934901 [ dbSNP | Ensembl ].
VAR_012093
Natural variant4601F → V in FA11D. Ref.17
VAR_012094
Natural variant4931T → I in FA11D.
VAR_012095
Natural variant5111Y → H in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion. Ref.25
VAR_054902
Natural variant5381P → L in FA11D. Ref.28
VAR_054903
Natural variant5651E → K in FA11D. Ref.28
VAR_054904
Natural variant5871W → S in FA11D; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect. Ref.26
VAR_054905
Natural variant5941S → R in FA11D. Ref.22
Corresponds to variant rs28934609 [ dbSNP | Ensembl ].
VAR_012096
Natural variant6181I → S in FA11D. Ref.28
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: 3636155] [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: 2827746] [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: 9593722] [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: 15815621] [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: 15489334] [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: 1998667] [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: 2844223] [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: 11412111] [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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-450 AND ASN-491, MASS SPECTROMETRY.
Tissue: Plasma.
[12]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND THR-22, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-491, MASS SPECTROMETRY.
Tissue: Liver.
[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: 2813350] [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: 1547342] [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: 7888672] [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: 7669672] [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: 9401068] [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: 9787168] [Abstract]
Cited for: VARIANTS FA11D ARG-244 AND ASN-266.
[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: 10027710] [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: 10606881] [Abstract]
Cited for: VARIANTS FA11D CYS-326; VAL-430 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: 10391209] [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: 11895778] [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: 15026311] [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: 15180874] [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: 15953011] [Abstract]
Cited for: VARIANTS FA11D PHE-46; ARG-101; CYS-151; GLU-263; VAL-430; LEU-538; LYS-565 AND SER-618.
+Additional computationally mapped references.

Web resources

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.
IPIIPI00008556.
IPI00216588.
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[»]
ProteinModelPortalP03951.
SMRP03951. Positions 20-624.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29085N.
IntActP03951. 1 interaction.
STRINGP03951.

Protein family/group databases

MEROPSS01.213.

PTM databases

PhosphoSiteP03951.

Polymorphism databases

DMDM119762.

Proteomic databases

PeptideAtlasP03951.
PRIDEP03951.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264691; ENSP00000264691; ENSG00000088926.
ENST00000403665; ENSP00000384957; ENSG00000088926.
GeneID2160.
KEGGhsa:2160.
UCSCuc003iza.1. human.

Organism-specific databases

CTD2160.
GeneCardsGC04P187187.
H-InvDBHIX0031358.
HGNCHGNC:3529. F11.
MIM264900. gene.
612416. phenotype.
neXtProtNX_P03951.
Orphanet329. Congenital factor XI deficiency.
PharmGKBPA27941.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00650000093010.
HOGENOMHOG000112467.
HOVERGENHBG000399.
InParanoidP03951.
KOK01323.
OMAGWGYRKL.
OrthoDBEOG4FFD18.
PhylomeDBP03951.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP03951.
BgeeP03951.
CleanExHS_F11.
GenevestigatorP03951.
GermOnlineENSG00000088926. Homo sapiens.

Family and domain databases

InterProIPR000177. Apple.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[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. Pept_Ser_Cys. 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

BindingDBP03951.
DrugBankDB00100. Coagulation Factor IX.
EvolutionaryTraceP03951.
NextBio8727.
PMAP-CutDBP03951.
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: May 16, 2012
This is version 157 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

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 4

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families