P03951 (FA11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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. Coagulation factor XIa heavy chain
2. 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.
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.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
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 Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Uncategorized	coagulation factor XIa activity Inferred from electronic annotation. Source: EC
Biological process	blood coagulation, intrinsic pathway Traceable author statement. Source: Reactome plasminogen activation Inferred from direct assay PubMed 89876. Source: BHF-UCL positive regulation of fibrinolysis Inferred from direct assay PubMed 89876. Source: BHF-UCL proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from direct assay PubMed 89876. Source: BHF-UCL plasma membrane Traceable author statement. Source: Reactome
Molecular function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.9. Source: UniProtKB serine-type endopeptidase activity Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
eco	P23827	3	EBI-1041019,EBI-1029159	From 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 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.12

Modified residue

22

1

Phosphothreonine Ref.12

Glycosylation

90

1

N-linked (GlcNAc...)

Glycosylation

126

1

N-linked (GlcNAc...) Ref.11

Glycosylation

353

1

N-linked (GlcNAc...)

Glycosylation

450

1

N-linked (GlcNAc...) Ref.11 Ref.13

Glycosylation

491

1

N-linked (GlcNAc...) Ref.8 Ref.11 Ref.13

Disulfide bond

20 ↔ 103

Potential

Disulfide bond

29

Interchain Ref.8

Disulfide bond

46 ↔ 76

Ref.8

Disulfide bond

50 ↔ 56

Ref.8

Disulfide bond

110 ↔ 193

Ref.8

Disulfide bond

136 ↔ 165

Ref.8

Disulfide bond

140 ↔ 146

Ref.8

Disulfide bond

200 ↔ 283

Ref.8

Disulfide bond

226 ↔ 255

Ref.8

Disulfide bond

230 ↔ 236

Ref.8

Disulfide bond

291 ↔ 374

Ref.8

Disulfide bond

317 ↔ 346

Ref.8

Disulfide bond

321 ↔ 327

Ref.8

Disulfide bond

339

Interchain Potential

Disulfide bond

380 ↔ 500

Interchain (between heavy and light chains) Ref.8

Disulfide bond

416 ↔ 432

Ref.8

Disulfide bond

514 ↔ 581

Potential

Disulfide bond

545 ↔ 560

Ref.8

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 FA11D. Ref.16

VAR_012085

Natural variant

46

1

C → F in FA11D. Ref.28

VAR_054894

Natural variant

56

1

C → R in FA11D; autosomal dominant; secretion of the mutant protein is impaired. Ref.25

VAR_054895

Natural variant

66

1

P → L. Ref.23
Corresponds to variant rs5968 [ dbSNP | Ensembl ].

VAR_011774

Natural variant

101

1

K → R in FA11D. Ref.28

VAR_054896

Natural variant

151

1

Y → C in FA11D. Ref.28

VAR_054897

Natural variant

244

1

Q → R in FA11D. Ref.19 Ref.23
Corresponds to variant rs5969 [ dbSNP | Ensembl ].

VAR_011775

Natural variant

246

1

W → C in FA11D. Ref.21

VAR_012086

Natural variant

255

1

C → Y in FA11D; secretion of the mutant protein is impaired. Ref.25

VAR_054898

Natural variant

263

1

G → E in FA11D. Ref.28

VAR_054899

Natural variant

266

1

S → N in FA11D. Ref.19

VAR_012087

Natural variant

270

1

K → I in FA11D; although the mutant protein is synthesized the secretion is reduced. Ref.27

VAR_054900

Natural variant

301

1

F → L in FA11D. Ref.14 Ref.15

VAR_006622

Natural variant

308

1

I → F. Ref.23
Corresponds to variant rs5972 [ dbSNP | Ensembl ].

VAR_011776

Natural variant

320

1

L → P in FA11D. Ref.16

VAR_012088

Natural variant

322

1

T → I in FA11D. Ref.16

VAR_012089

Natural variant

326

1

R → C in FA11D. Ref.22
Corresponds to variant rs28934608 [ dbSNP | Ensembl ].

VAR_012090

Natural variant

339

1

C → F. Ref.4 Ref.23 Ref.25
Corresponds to variant rs5967 [ dbSNP | Ensembl ].

VAR_011777

Natural variant

341

1

E → K in FA11D. Ref.16

VAR_012091

Natural variant

399

1

W → R.
Corresponds to variant rs1800439 [ dbSNP | Ensembl ].

VAR_011778

Natural variant

404

1

T → N in FA11D. Ref.18

VAR_012092

Natural variant

418

1

G → V in FA11D; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect. Ref.26

VAR_054901

Natural variant

430

1

A → V in FA11D. Ref.22 Ref.28
Corresponds to variant rs28934901 [ dbSNP | Ensembl ].

VAR_012093

Natural variant

460

1

F → V in FA11D. Ref.17

VAR_012094

Natural variant

493

1

T → I in FA11D.

VAR_012095

Natural variant

511

1

Y → H in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion. Ref.25

VAR_054902

Natural variant

538

1

P → L in FA11D. Ref.28

VAR_054903

Natural variant

565

1

E → K in FA11D. Ref.28

VAR_054904

Natural variant

587

1

W → S in FA11D; autosomal dominant; mutant is not secreted by transfected fibroblasts; dominant-negative effect. Ref.26

VAR_054905

Natural variant

594

1

S → R in FA11D. Ref.22
Corresponds to variant rs28934609 [ dbSNP | Ensembl ].

VAR_012096

Natural variant

618

1

I → S in FA11D. Ref.28

VAR_054906

Experimental info

Sequence conflict

226

1

C → S in AAA51985. Ref.2

Secondary structure

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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) [UniParc]. 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]	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. , 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

Wikipedia

Factor XI entry

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CH471056 Genomic DNA. Translation: EAX04621.1.
BC119014 mRNA. Translation: AAI19015.1.
BC122863 mRNA. Translation: AAI22864.1.

IPI

IPI00008556.
IPI00216588.

PIR

KFHU1. A27431.

RefSeq

NP_000119.1. NM_000128.3.

UniGene

Hs.1430.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P03951.

SMR

P03951. Positions 20-624.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29085N.

IntAct

P03951. 1 interaction.

STRING

P03951.

Protein family/group databases

MEROPS

S01.213.

PTM databases

PhosphoSite

P03951.

Polymorphism databases

DMDM

119762.

Proteomic databases

PeptideAtlas

P03951.

PRIDE

P03951.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264691; ENSP00000264691; ENSG00000088926.
ENST00000403665; ENSP00000384957; ENSG00000088926.

GeneID

2160.

KEGG

hsa:2160.

UCSC

uc003iza.1. human.

Organism-specific databases

CTD

2160.

GeneCards

GC04P187187.

H-InvDB

HIX0031358.

HGNC

HGNC:3529. F11.

MIM

264900. gene.
612416. phenotype.

neXtProt

NX_P03951.

Orphanet

329. Congenital factor XI deficiency.

PharmGKB

PA27941.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

GeneTree

ENSGT00650000093010.

HOGENOM

HOG000112467.

HOVERGEN

HBG000399.

InParanoid

P03951.

KO

K01323.

OMA

GWGYRKL.

OrthoDB

EOG4FFD18.

PhylomeDB

P03951.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P03951.

Bgee

P03951.

CleanEx

HS_F11.

Genevestigator

P03951.

GermOnline

ENSG00000088926. Homo sapiens.

Family and domain databases

InterPro

IPR000177. 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]

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]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

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

BindingDB

P03951.

DrugBank

DB00100. Coagulation Factor IX.

EvolutionaryTrace

P03951.

NextBio

8727.

PMAP-CutDB

P03951.

SOURCE

Search...

Entry information

Entry name

FA11_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.