Reviewed, UniProtKB/Swiss-Prot P03951 (FA11_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	625 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Signal
Ligand	Heparin-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Ref.3 Non-traceable author statement. Source: UniProtKB plasminogen activation Inferred from direct assay. Source: UniProtKB positive regulation of fibrinolysis Inferred from direct assay. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from direct assay. Source: UniProtKB membrane Ref.3 Non-traceable author statement. Source: UniProtKB
Molecular function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Ref.3 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

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

Regions

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

Sites

Active site

431

1

Charge relay system

Active site

480

1

Charge relay system

Active site

575

1

Charge relay system

Amino acid modifications

Modified residue

17

1

Phosphoserine Ref.10

Modified residue

22

1

Phosphothreonine Ref.10

Glycosylation

90

1

N-linked (GlcNAc...)

Glycosylation

126

1

N-linked (GlcNAc...) Ref.9

Glycosylation

353

1

N-linked (GlcNAc...)

Glycosylation

450

1

N-linked (GlcNAc...) Ref.9

Glycosylation

491

1

N-linked (GlcNAc...) Ref.7 Ref.9

Disulfide bond

20 ↔ 103

Potential

Disulfide bond

29

Interchain Ref.7

Disulfide bond

46 ↔ 76

Ref.7

Disulfide bond

50 ↔ 56

Ref.7

Disulfide bond

110 ↔ 193

Ref.7

Disulfide bond

136 ↔ 165

Ref.7

Disulfide bond

140 ↔ 146

Ref.7

Disulfide bond

200 ↔ 283

Ref.7

Disulfide bond

226 ↔ 255

Ref.7

Disulfide bond

230 ↔ 236

Ref.7

Disulfide bond

291 ↔ 374

Ref.7

Disulfide bond

317 ↔ 346

Ref.7

Disulfide bond

321 ↔ 327

Ref.7

Disulfide bond

339

Interchain Potential

Disulfide bond

380 ↔ 500

Interchain (between heavy and light chains) Ref.7

Disulfide bond

416 ↔ 432

Ref.7

Disulfide bond

514 ↔ 581

Potential

Disulfide bond

545 ↔ 560

Ref.7

Disulfide bond

571 ↔ 599

Potential

Natural variations

Alternative sequence

109 – 162

54

Missing in isoform 2.

VSP_005388

Natural variant

34

1

D → H in F11 deficiency.

VAR_012085

Natural variant

46

1

C → F in F11 deficiency.

VAR_054894

Natural variant

56

1

C → R in F11 deficiency; autosomal dominant; secretion of the mutant protein is impaired.

VAR_054895

Natural variant

66

1

P → L: dbSNP rs5968. Ref.21

VAR_011774

Natural variant

101

1

K → R in F11 deficiency.

VAR_054896

Natural variant

151

1

Y → C in F11 deficiency.

VAR_054897

Natural variant

244

1

Q → R in F11 deficiency. dbSNP rs5969.

VAR_011775

Natural variant

246

1

W → C in F11 deficiency.

VAR_012086

Natural variant

255

1

C → Y in F11 deficiency; secretion of the mutant protein is impaired.

VAR_054898

Natural variant

263

1

G → E in F11 deficiency.

VAR_054899

Natural variant

266

1

S → N in F11 deficiency.

VAR_012087

Natural variant

270

1

K → I in F11 deficiency; although the mutant protein is synthesized the secretion is reduced.

VAR_054900

Natural variant

301

1

F → L in F11 deficiency; frequent mutation in Ashkenazi patients.

VAR_006622

Natural variant

308

1

I → F: dbSNP rs5972. Ref.21

VAR_011776

Natural variant

320

1

L → P in F11 deficiency.

VAR_012088

Natural variant

322

1

T → I in F11 deficiency.

VAR_012089

Natural variant

326

1

R → C in F11 deficiency.

VAR_012090

Natural variant

339

1

C → F: dbSNP rs5967. Ref.23 Ref.21 Ref.4

VAR_011777

Natural variant

341

1

E → K in F11 deficiency.

VAR_012091

Natural variant

399

1

W → R: dbSNP rs1800439.

VAR_011778

Natural variant

404

1

T → N in F11 deficiency.

VAR_012092

Natural variant

418

1

G → V in F11 deficiency; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect.

VAR_054901

Natural variant

430

1

A → V in F11 deficiency.

VAR_012093

Natural variant

460

1

F → V in F11 deficiency.

VAR_012094

Natural variant

493

1

T → I in F11 deficiency.

VAR_012095

Natural variant

511

1

Y → H in F11 deficiency; transfected cells contain reduced amount of mutant protein and display decreased secretion.

VAR_054902

Natural variant

538

1

P → L in F11 deficiency.

VAR_054903

Natural variant

565

1

E → K in F11 deficiency.

VAR_054904

Natural variant

587

1

W → S in F11 deficiency; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect.

VAR_054905

Natural variant

594

1

S → R in F11 deficiency.

VAR_012096

Natural variant

618

1

I → S in F11 deficiency.

VAR_054906

Experimental info

Sequence conflict

226

1

C → S in AAA51985. Ref.2

Secondary structure

1

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625

Helix Strand Turn

Details...

Beta strand

25 – 30

6

Beta strand

34 – 39

6

Helix

43 – 52

10

Beta strand

53 – 55

3

Beta strand

58 – 62

5

Turn

71 – 74

4

Beta strand

75 – 79

5

Helix

82 – 84

3

Beta strand

88 – 98

11

Beta strand

115 – 121

7

Beta strand

123 – 129

7

Helix

133 – 141

9

Beta strand

143 – 145

3

Beta strand

147 – 152

6

Beta strand

159 – 161

3

Beta strand

164 – 169

6

Beta strand

171 – 174

4

Beta strand

176 – 188

13

Turn

191 – 194

4

Beta strand

205 – 209

5

Beta strand

212 – 219

8

Helix

223 – 231

9

Beta strand

237 – 242

6

Helix

249 – 251

3

Beta strand

254 – 259

6

Beta strand

261 – 264

4

Beta strand

269 – 278

10

Helix

281 – 283

3

Beta strand

304 – 313

10

Helix

316 – 323

8

Beta strand

329 – 333

5

Turn

337 – 339

3

Beta strand

344 – 350

7

Beta strand

352 – 354

3

Beta strand

366 – 369

4

Helix

374 – 376

3

Beta strand

402 – 422

21

Beta strand

425 – 428

4

Helix

430 – 433

4

Helix

439 – 441

3

Beta strand

442 – 447

6

Helix

451 – 453

3

Beta strand

461 – 468

8

Turn

475 – 477

3

Beta strand

482 – 488

7

Beta strand

514 – 519

6

Beta strand

533 – 536

4

Helix

542 – 548

7

Turn

549 – 551

3

Beta strand

558 – 561

4

Beta strand

578 – 583

6

Beta strand

586 – 600

15

Beta strand

606 – 609

4

Helix

611 – 614

4

Helix

615 – 622

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 23, 1986. Version 1. Checksum: 147AFA94B7709E8F	FASTA	625	70,109
	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
	Isoform 2 (Platelet). Checksum: FB9D65D72151755E	FASTA	571	63,840
	10 20 30 40 50 60 MIFLYQVVHF ILFTSVSGEC VTQLLKDTCF EGGDITTVFT PSAKYCQVVC TYHPRCLLFT 70 80 90 100 110 120 FTAESPSEDP TRWFTCVLKD SVTETLPRVN RTAAISGYSF KQCSHQISNI CLLKHTQTGT 130 140 150 160 170 180 PTRITKLDKV VSGFSLKSCA LSNLACIRDI FPNTVFADSN IDSVMAPDAF VCGRICTHHP 190 200 210 220 230 240 GCLFFTFFSQ EWPKESQRNL CLLKTSESGL PSTRIKKSKA LSGFSLQSCR HSIPVFCHSS 250 260 270 280 290 300 FYHDTDFLGE ELDIVAAKSH EACQKLCTNA VRCQFFTYTP AQASCNEGKG KCYLKLSSNG 310 320 330 340 350 360 SPTKILHGRG GISGYTLRLC KMDNECTTKI KPRIVGGTAS VRGEWPWQVT LHTTSPTQRH 370 380 390 400 410 420 LCGGSIIGNQ WILTAAHCFY GVESPKILRV YSGILNQSEI KEDTSFFGVQ EIIIHDQYKM 430 440 450 460 470 480 AESGYDIALL KLETTVNYTD SQRPICLPSK GDRNVIYTDC WVTGWGYRKL RDKIQNTLQK 490 500 510 520 530 540 AKIPLVTNEE CQKRYRGHKI THKMICAGYR EGGKDACKGD SGGPLSCKHN EVWHLVGITS 550 560 570 WGEGCAQRER PGVYTNVVEY VDWILEKTQA V

References

	« Hide 'large scale' referencesShow '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. , 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

Wikipedia

Factor XI entry

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M13142 mRNA. Translation: AAA52487.1.
M20218 , 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.

IPI

IPI00008556.
IPI00216588.

PIR

KFHU1. A27431.

RefSeq

NP_000119.1.

UniGene

Hs.1430
Hs.714107

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XX9	X-ray	2.20	A/B	388-625	[»]
1XXD	X-ray	2.91	A/B	388-625	[»]
1XXF	X-ray	2.60	A/B	388-625	[»]
1ZHM	X-ray	1.96	A	388-624	[»]
1ZHP	X-ray	2.70	A	388-625	[»]
1ZHR	X-ray	1.73	A	388-625	[»]
1ZJD	X-ray	2.60	A	388-624	[»]
1ZLR	X-ray	2.50	A	388-624	[»]
1ZMJ	X-ray	2.00	A	388-624	[»]
1ZML	X-ray	2.25	A	388-625	[»]
1ZMN	X-ray	2.05	A	388-625	[»]
1ZOM	X-ray	2.25	A	388-624	[»]
1ZPB	X-ray	2.10	A	388-624	[»]
1ZPC	X-ray	2.60	A	388-624	[»]
1ZPZ	X-ray	2.50	A	388-625	[»]
1ZRK	X-ray	2.30	A	388-625	[»]
1ZSJ	X-ray	1.90	A	388-625	[»]
1ZSK	X-ray	1.90	A	388-625	[»]
1ZSL	X-ray	2.05	A	388-625	[»]
1ZTJ	X-ray	2.05	A	388-625	[»]
1ZTK	X-ray	2.50	A	388-625	[»]
1ZTL	X-ray	2.60	A	388-625	[»]
2F83	X-ray	2.87	A	1-625	[»]
2FDA	X-ray	2.00	A	388-625	[»]
2J8J	NMR	-	A/B	290-379	[»]
2J8L	NMR	-	A/B	290-379	[»]
3BG8	X-ray	1.60	A	388-625	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29085N.

Protein family/group databases

MEROPS

S01.213.

PTM databases

PhosphoSite

P03951.

Proteomic databases

PeptideAtlas

P03951.

PRIDE

P03951.

Genome annotation databases

Ensembl

ENSG00000088926. Homo sapiens. [Contig view]

GeneID

2160.

KEGG

hsa:2160.

NMPDR

fig|9606.3.peg.24953.

Organism-specific databases

GeneCards

GC04P187424.

H-InvDB

HIX0031358.

HGNC

HGNC:3529. F11.

MIM

264900. gene.
612416. phenotype.

Orphanet

329. Congenital factor XI deficiency.

PharmGKB

PA24968.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P03951.

HOVERGEN

P03951.

OMA

P03951. QRPICLP.

Enzyme and pathway databases

BRENDA

3.4.21.27. 247.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P03951.

Bgee

P03951.

CleanEx

HS_F11.

GermOnline

ENSG00000088926. Homo sapiens.

Family and domain databases

InterPro

IPR000177. Apple.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]

Pfam

PF00024. PAN_1. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00005. APPLEDOMAIN.
PR00722. CHYMOTRYPSIN.

SMART

SM00223. APPLE. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS00495. APPLE. 4 hits.
PS50948. PAN. 4 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P03951.

DrugBank

DB00100. Coagulation Factor IX.

NextBio

8727.

PMAP-CutDB

P03951.

SOURCE

Search...

Entry information

Entry name

FA11_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)