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Reviewed, UniProtKB/Swiss-Prot P03951 (FA11_HUMAN)

Last modified June 16, 2009. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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
Cleaved into the following 2 chains:
    1- Recommended name:
            Coagulation factor XIa heavy chain
    2- Recommended name:
            Coagulation factor XIa light chain
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.

Subunit structure

Homodimer; disulfide-linked. After activation the heavy and light chains are also linked by a disulfide bond. Ref.7

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 F11 deficiency [MIM:612416]; also called plasma thromboplastin antecedent deficiency or Rosenthal syndrome. It is a blood coagulation abnormality occurring in high frequency in Ashkenazi jews. F11-deficient patients are prone to excessive bleeding after haemostatic challenge. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26

Sequence similarities

Belongs to the peptidase S1 family. Plasma kallikrein subfamily.

Contains 4 apple domains.

Contains 1 peptidase S1 domain.

Ontologies

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.10
Modified residue221Phosphothreonine Ref.10
Glycosylation901N-linked (GlcNAc...)
Glycosylation1261N-linked (GlcNAc...) Ref.9
Glycosylation3531N-linked (GlcNAc...)
Glycosylation4501N-linked (GlcNAc...) Ref.9
Glycosylation4911N-linked (GlcNAc...) Ref.7 Ref.9
Disulfide bond20 ↔ 103 Potential
Disulfide bond29Interchain Ref.7
Disulfide bond46 ↔ 76 Ref.7
Disulfide bond50 ↔ 56 Ref.7
Disulfide bond110 ↔ 193 Ref.7
Disulfide bond136 ↔ 165 Ref.7
Disulfide bond140 ↔ 146 Ref.7
Disulfide bond200 ↔ 283 Ref.7
Disulfide bond226 ↔ 255 Ref.7
Disulfide bond230 ↔ 236 Ref.7
Disulfide bond291 ↔ 374 Ref.7
Disulfide bond317 ↔ 346 Ref.7
Disulfide bond321 ↔ 327 Ref.7
Disulfide bond339Interchain Potential
Disulfide bond380 ↔ 500Interchain (between heavy and light chains) Ref.7
Disulfide bond416 ↔ 432 Ref.7
Disulfide bond514 ↔ 581 Potential
Disulfide bond545 ↔ 560 Ref.7
Disulfide bond571 ↔ 599 Potential

Natural variations

Alternative sequence109 – 16254Missing in isoform 2.
VSP_005388
Natural variant341D → H in F11 deficiency.
VAR_012085
Natural variant461C → F in F11 deficiency.
VAR_054894
Natural variant561C → R in F11 deficiency; autosomal dominant; secretion of the mutant protein is impaired.
VAR_054895
Natural variant661P → L: dbSNP rs5968. Ref.21
VAR_011774
Natural variant1011K → R in F11 deficiency.
VAR_054896
Natural variant1511Y → C in F11 deficiency.
VAR_054897
Natural variant2441Q → R in F11 deficiency. dbSNP rs5969.
VAR_011775
Natural variant2461W → C in F11 deficiency.
VAR_012086
Natural variant2551C → Y in F11 deficiency; secretion of the mutant protein is impaired.
VAR_054898
Natural variant2631G → E in F11 deficiency.
VAR_054899
Natural variant2661S → N in F11 deficiency.
VAR_012087
Natural variant2701K → I in F11 deficiency; although the mutant protein is synthesized the secretion is reduced.
VAR_054900
Natural variant3011F → L in F11 deficiency; frequent mutation in Ashkenazi patients.
VAR_006622
Natural variant3081I → F: dbSNP rs5972. Ref.21
VAR_011776
Natural variant3201L → P in F11 deficiency.
VAR_012088
Natural variant3221T → I in F11 deficiency.
VAR_012089
Natural variant3261R → C in F11 deficiency.
VAR_012090
Natural variant3391C → F: dbSNP rs5967. Ref.23 Ref.21 Ref.4
VAR_011777
Natural variant3411E → K in F11 deficiency.
VAR_012091
Natural variant3991W → R: dbSNP rs1800439.
VAR_011778
Natural variant4041T → N in F11 deficiency.
VAR_012092
Natural variant4181G → V in F11 deficiency; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect.
VAR_054901
Natural variant4301A → V in F11 deficiency.
VAR_012093
Natural variant4601F → V in F11 deficiency.
VAR_012094
Natural variant4931T → I in F11 deficiency.
VAR_012095
Natural variant5111Y → H in F11 deficiency; transfected cells contain reduced amount of mutant protein and display decreased secretion.
VAR_054902
Natural variant5381P → L in F11 deficiency.
VAR_054903
Natural variant5651E → K in F11 deficiency.
VAR_054904
Natural variant5871W → S in F11 deficiency; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect.
VAR_054905
Natural variant5941S → R in F11 deficiency.
VAR_012096
Natural variant6181I → S in F11 deficiency.
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).

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]"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].
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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 F11 DEFICIENCY LEU-301.
[13]"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 F11 DEFICIENCY LEU-301.
[14]"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 F11 DEFICIENCY HIS-34; PRO-320; ILE-322 AND LYS-341.
[15]"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 F11 DEFICIENCY VAL-460.
[16]"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 F11 DEFICIENCY ASN-404.
[17]"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 F11 DEFICIENCY ARG-244 AND ASN-266.
[18]Erratum
Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A., Gailani D.
Blood 93:1786-1786(1999)
[19]"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 F11 DEFICIENCY CYS-246.
[20]"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 F11 DEFICIENCY CYS-326; VAL-430 AND ARG-594.
[21]"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.
[22]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)
[23]"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 F11 DEFICIENCY ARG-56; TYR-255 AND HIS-511, VARIANT PHE-339, CHARACTERIZATION OF VARIANTS F11 DEFICIENCY ARG-56; TYR-255 AND HIS-511.
[24]"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 F11 DEFICIENCY VAL-418 AND SER-587, CHARACTERIZATION OF VARIANTS F11 DEFICIENCY VAL-418 AND SER-587.
[25]"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 F11 DEFICIENCY ILE-270, CHARACTERIZATION OF VARIANT F11 DEFICIENCY ILE-270.
[26]"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 F11 DEFICIENCY 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

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.
BC119014 mRNA. Translation: AAI19015.1.
BC122863 mRNA. Translation: AAI22864.1.
IPIIPI00008556.
IPI00216588.
PIRKFHU1. A27431.
RefSeqNP_000119.1.
UniGeneHs.1430
Hs.714107

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29085N.

Protein family/group databases

MEROPSS01.213.

PTM databases

PhosphoSiteP03951.

Proteomic databases

PeptideAtlasP03951.
PRIDEP03951.

Genome annotation databases

EnsemblENSG00000088926. Homo sapiens. [Contig view]
GeneID2160.
KEGGhsa:2160.
NMPDRfig|9606.3.peg.24953.

Organism-specific databases

GeneCardsGC04P187424.
H-InvDBHIX0031358.
HGNCHGNC:3529. F11.
MIM264900. gene.
612416. phenotype.
Orphanet329. Congenital factor XI deficiency.
PharmGKBPA24968.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP03951.
HOVERGENP03951.
OMAP03951. QRPICLP.

Enzyme and pathway databases

BRENDA3.4.21.27. 247.
ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP03951.
BgeeP03951.
CleanExHS_F11.
GermOnlineENSG00000088926. Homo sapiens.

Family and domain databases

InterProIPR000177. Apple.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
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]
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 Resources

BindingDBP03951.
DrugBankDB00100. Coagulation Factor IX.
NextBio8727.
PMAP-CutDBP03951.
SOURCESearch...

Entry information

Entry nameFA11_HUMAN
AccessionPrimary (citable) accession number: P03951
Secondary accession number(s): Q4W5C2, Q9Y495
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: June 16, 2009
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents