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Protein

Coagulation factor XI

Gene

F11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Inhibited by SERPINA5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei431Charge relay system1
Active sitei480Charge relay system1
Active sitei575Charge relay system1

GO - Molecular functioni

  • heparin binding Source: UniProtKB-KW
  • serine-type aminopeptidase activity Source: Ensembl
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: UniProtKB
  • blood coagulation, intrinsic pathway Source: Reactome
  • plasminogen activation Source: BHF-UCL
  • positive regulation of fibrinolysis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:HS01617-MONOMER.
BRENDAi3.4.21.27. 2681.
ReactomeiR-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
SABIO-RKP03951.

Protein family/group databases

MEROPSiS01.213.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor XI (EC:3.4.21.27)
Short name:
FXI
Alternative name(s):
Plasma thromboplastin antecedent
Short name:
PTA
Cleaved into the following 2 chains:
Gene namesi
Name:F11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3529. F11.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor XI deficiency (FA11D)21 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612416
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07651530F → S in FA11D. 1 Publication1
Natural variantiVAR_06792932G → R in FA11D. 1 PublicationCorresponds to variant rs281875259dbSNPEnsembl.1
Natural variantiVAR_01208534D → H in FA11D. 1 PublicationCorresponds to variant rs281875267dbSNPEnsembl.1
Natural variantiVAR_06793043A → T in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 PublicationCorresponds to variant rs281875264dbSNPEnsembl.1
Natural variantiVAR_05489446C → F in FA11D. 1 PublicationCorresponds to variant rs281875271dbSNPEnsembl.1
Natural variantiVAR_06793151T → I in FA11D. 1 PublicationCorresponds to variant rs281875252dbSNPEnsembl.1
Natural variantiVAR_06793251T → P in FA11D. 2 PublicationsCorresponds to variant rs281875243dbSNPEnsembl.1
Natural variantiVAR_06793353H → Q in FA11D. 1 PublicationCorresponds to variant rs281875261dbSNPEnsembl.1
Natural variantiVAR_05489556C → R in FA11D; secretion of the mutant protein is impaired. 2 PublicationsCorresponds to variant rs121965069dbSNPEnsembl.1
Natural variantiVAR_06793463A → V in FA11D. 1 PublicationCorresponds to variant rs281875244dbSNPEnsembl.1
Natural variantiVAR_054896101K → R in FA11D. 1 PublicationCorresponds to variant rs281875272dbSNPEnsembl.1
Natural variantiVAR_076516109A → T in FA11D. 1 PublicationCorresponds to variant rs768474112dbSNPEnsembl.1
Natural variantiVAR_067935140C → Y in FA11D. 1 PublicationCorresponds to variant rs281875256dbSNPEnsembl.1
Natural variantiVAR_054897151Y → C in FA11D. 1 PublicationCorresponds to variant rs281875273dbSNPEnsembl.1
Natural variantiVAR_076517216D → N in FA11D. 1 Publication1
Natural variantiVAR_067936222D → Y in FA11D. 1 PublicationCorresponds to variant rs281875245dbSNPEnsembl.1
Natural variantiVAR_067937228R → Q in FA11D. 1 PublicationCorresponds to variant rs281875246dbSNPEnsembl.1
Natural variantiVAR_067938241F → L in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 PublicationCorresponds to variant rs281875265dbSNPEnsembl.1
Natural variantiVAR_012086246W → C in FA11D. 1 PublicationCorresponds to variant rs281875279dbSNPEnsembl.1
Natural variantiVAR_067939252R → T in FA11D. 1 PublicationCorresponds to variant rs281875260dbSNPEnsembl.1
Natural variantiVAR_054898255C → Y in FA11D; secretion of the mutant protein is impaired. 1 PublicationCorresponds to variant rs281875277dbSNPEnsembl.1
Natural variantiVAR_054899263G → E in FA11D. 1 PublicationCorresponds to variant rs281875274dbSNPEnsembl.1
Natural variantiVAR_012087266S → N in FA11D. 1 PublicationCorresponds to variant rs145168351dbSNPEnsembl.1
Natural variantiVAR_054900270K → I in FA11D; although the mutant protein is synthesized the secretion is reduced. 1 PublicationCorresponds to variant rs121965070dbSNPEnsembl.1
Natural variantiVAR_067940276S → C in FA11D. 1 PublicationCorresponds to variant rs281875247dbSNPEnsembl.1
Natural variantiVAR_067941277G → D in FA11D. 1 PublicationCorresponds to variant rs281875248dbSNPEnsembl.1
Natural variantiVAR_006622301F → L in FA11D. 2 PublicationsCorresponds to variant rs121965064dbSNPEnsembl.1
Natural variantiVAR_067942315E → K in FA11D. 2 PublicationsCorresponds to variant rs281875257dbSNPEnsembl.1
Natural variantiVAR_012088320L → P in FA11D. 1 PublicationCorresponds to variant rs281875268dbSNPEnsembl.1
Natural variantiVAR_012089322T → I in FA11D. 1 PublicationCorresponds to variant rs281875269dbSNPEnsembl.1
Natural variantiVAR_012090326R → C in FA11D. 1 PublicationCorresponds to variant rs28934608dbSNPEnsembl.1
Natural variantiVAR_067943331T → I in FA11D. 1 PublicationCorresponds to variant rs281875253dbSNPEnsembl.1
Natural variantiVAR_012091341E → K in FA11D. 1 PublicationCorresponds to variant rs281875270dbSNPEnsembl.1
Natural variantiVAR_067944360L → P in FA11D. 1 PublicationCorresponds to variant rs281875254dbSNPEnsembl.1
Natural variantiVAR_067945401W → R in FA11D. 1 PublicationCorresponds to variant rs281875262dbSNPEnsembl.1
Natural variantiVAR_067946403V → M in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 PublicationCorresponds to variant rs281875266dbSNPEnsembl.1
Natural variantiVAR_012092404T → N in FA11D. 1 PublicationCorresponds to variant rs121965067dbSNPEnsembl.1
Natural variantiVAR_054901418G → V in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 PublicationCorresponds to variant rs121965071dbSNPEnsembl.1
Natural variantiVAR_012093430A → V in FA11D. 1 PublicationCorresponds to variant rs121965068dbSNPEnsembl.1
Natural variantiVAR_067947454I → K in FA11D. 1 PublicationCorresponds to variant rs281875241dbSNPEnsembl.1
Natural variantiVAR_012094460F → V in FA11D. 1 PublicationCorresponds to variant rs121965065dbSNPEnsembl.1
Natural variantiVAR_067948481I → S in FA11D. 1 PublicationCorresponds to variant rs281875242dbSNPEnsembl.1
Natural variantiVAR_012095493T → I in FA11D. 1 Publication1
Natural variantiVAR_067949503S → P in FA11D. 1 PublicationCorresponds to variant rs140068026dbSNPEnsembl.1
Natural variantiVAR_067950506D → G in FA11D; mild phenotype. 1 PublicationCorresponds to variant rs281875258dbSNPEnsembl.1
Natural variantiVAR_054902511Y → H in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion. 1 PublicationCorresponds to variant rs281875278dbSNPEnsembl.1
Natural variantiVAR_067951514C → F in FA11D. 1 PublicationCorresponds to variant rs281875249dbSNPEnsembl.1
Natural variantiVAR_067952526D → E in FA11D. 1 PublicationCorresponds to variant rs281875263dbSNPEnsembl.1
Natural variantiVAR_054903538P → L in FA11D. 1 PublicationCorresponds to variant rs139695003dbSNPEnsembl.1
Natural variantiVAR_076518543E → K in FA11D. 1 PublicationCorresponds to variant rs142952627dbSNPEnsembl.1
Natural variantiVAR_076519552H → R in FA11D. 1 PublicationCorresponds to variant rs369935706dbSNPEnsembl.1
Natural variantiVAR_054904565E → K in FA11D. 1 PublicationCorresponds to variant rs281875275dbSNPEnsembl.1
Natural variantiVAR_067953575S → L in FA11D. 1 PublicationCorresponds to variant rs281875250dbSNPEnsembl.1
Natural variantiVAR_054905587W → S in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 PublicationCorresponds to variant rs121965072dbSNPEnsembl.1
Natural variantiVAR_012096594S → R in FA11D. 1 PublicationCorresponds to variant rs28934609dbSNPEnsembl.1
Natural variantiVAR_067954597E → K in FA11D. 2 PublicationsCorresponds to variant rs281875251dbSNPEnsembl.1
Natural variantiVAR_067955608Y → H in FA11D. 1 PublicationCorresponds to variant rs281875255dbSNPEnsembl.1
Natural variantiVAR_054906618I → S in FA11D. 1 PublicationCorresponds to variant rs281875276dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2160.
MalaCardsiF11.
MIMi612416. phenotype.
OpenTargetsiENSG00000088926.
Orphaneti329. Congenital factor XI deficiency.
PharmGKBiPA27941.

Chemistry databases

ChEMBLiCHEMBL2820.
DrugBankiDB00100. Coagulation Factor IX.
GuidetoPHARMACOLOGYi2360.

Polymorphism and mutation databases

BioMutaiF11.
DMDMi119762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000002782519 – 387Coagulation factor XIa heavy chainAdd BLAST369
ChainiPRO_0000027826388 – 625Coagulation factor XIa light chainAdd BLAST238

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20 ↔ 103Sequence analysis
Disulfide bondi29Interchain
Disulfide bondi46 ↔ 761 Publication
Disulfide bondi50 ↔ 561 Publication
Glycosylationi90N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi110 ↔ 1931 Publication
Glycosylationi126N-linked (GlcNAc...) (complex)2 Publications1
Disulfide bondi136 ↔ 1651 Publication
Disulfide bondi140 ↔ 1461 Publication
Glycosylationi163N-linked (GlcNAc...) (complex); atypical1 Publication1
Disulfide bondi200 ↔ 283
Disulfide bondi226 ↔ 2551 Publication
Disulfide bondi230 ↔ 2361 Publication
Disulfide bondi291 ↔ 3741 Publication
Disulfide bondi317 ↔ 3461 Publication
Disulfide bondi321 ↔ 3271 Publication
Disulfide bondi339InterchainSequence analysis
Glycosylationi353N-linked (GlcNAc...)1
Disulfide bondi380 ↔ 500Interchain (between heavy and light chains)
Disulfide bondi416 ↔ 4321 Publication
Glycosylationi450N-linked (GlcNAc...) (complex)3 Publications1
Glycosylationi491N-linked (GlcNAc...) (complex)4 Publications1
Disulfide bondi514 ↔ 581
Disulfide bondi545 ↔ 5601 Publication
Disulfide bondi571 ↔ 599

Post-translational modificationi

N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. Glycosylation at Asn-163 uses a rare non-canonical Asn-X-Cys glycosite.1 Publication
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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP03951.
PeptideAtlasiP03951.
PRIDEiP03951.

PTM databases

iPTMnetiP03951.
PhosphoSitePlusiP03951.

Miscellaneous databases

PMAP-CutDBP03951.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000088926.
CleanExiHS_F11.
ExpressionAtlasiP03951. baseline and differential.
GenevisibleiP03951. HS.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Forms a heterodimer with SERPINA5. After activation the heavy and light chains are also linked by a disulfide bond.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ecoP238273EBI-1041019,EBI-1029159From a different organism.

Protein-protein interaction databases

BioGridi108458. 6 interactors.
DIPiDIP-29085N.
IntActiP03951. 1 interactor.
STRINGi9606.ENSP00000384957.

Chemistry databases

BindingDBiP03951.

Structurei

Secondary structure

1625
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 30Combined sources6
Beta strandi34 – 39Combined sources6
Helixi43 – 52Combined sources10
Beta strandi53 – 55Combined sources3
Beta strandi58 – 62Combined sources5
Helixi70 – 72Combined sources3
Beta strandi75 – 79Combined sources5
Beta strandi82 – 84Combined sources3
Beta strandi88 – 98Combined sources11
Helixi100 – 102Combined sources3
Beta strandi114 – 129Combined sources16
Helixi133 – 142Combined sources10
Beta strandi143 – 145Combined sources3
Beta strandi147 – 152Combined sources6
Turni159 – 163Combined sources5
Beta strandi164 – 169Combined sources6
Beta strandi171 – 174Combined sources4
Beta strandi176 – 188Combined sources13
Helixi190 – 192Combined sources3
Turni193 – 195Combined sources3
Beta strandi205 – 219Combined sources15
Helixi223 – 231Combined sources9
Beta strandi237 – 242Combined sources6
Helixi249 – 251Combined sources3
Beta strandi254 – 259Combined sources6
Beta strandi261 – 264Combined sources4
Beta strandi266 – 278Combined sources13
Helixi281 – 283Combined sources3
Beta strandi294 – 296Combined sources3
Beta strandi299 – 302Combined sources4
Beta strandi304 – 312Combined sources9
Helixi314 – 322Combined sources9
Beta strandi329 – 333Combined sources5
Turni337 – 339Combined sources3
Beta strandi344 – 350Combined sources7
Beta strandi352 – 355Combined sources4
Beta strandi357 – 364Combined sources8
Beta strandi366 – 369Combined sources4
Helixi372 – 376Combined sources5
Helixi379 – 381Combined sources3
Beta strandi390 – 393Combined sources4
Beta strandi402 – 407Combined sources6
Beta strandi409 – 411Combined sources3
Beta strandi413 – 422Combined sources10
Beta strandi425 – 428Combined sources4
Helixi430 – 433Combined sources4
Helixi439 – 441Combined sources3
Beta strandi442 – 445Combined sources4
Helixi451 – 453Combined sources3
Beta strandi456 – 458Combined sources3
Beta strandi461 – 468Combined sources8
Helixi475 – 477Combined sources3
Beta strandi482 – 488Combined sources7
Beta strandi494 – 496Combined sources3
Helixi504 – 506Combined sources3
Beta strandi507 – 509Combined sources3
Beta strandi514 – 519Combined sources6
Beta strandi522 – 525Combined sources4
Beta strandi533 – 536Combined sources4
Helixi542 – 548Combined sources7
Turni549 – 551Combined sources3
Beta strandi558 – 561Combined sources4
Beta strandi578 – 583Combined sources6
Beta strandi586 – 595Combined sources10
Beta strandi597 – 600Combined sources4
Beta strandi606 – 610Combined sources5
Helixi611 – 614Combined sources4
Helixi615 – 622Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.05A388-624[»]
1ZTKX-ray2.50A388-624[»]
1ZTLX-ray2.60A388-624[»]
2F83X-ray2.87A1-625[»]
2FDAX-ray2.00A388-625[»]
2J8JNMR-A/B290-379[»]
2J8LNMR-A/B290-379[»]
3BG8X-ray1.60A388-625[»]
3SORX-ray1.80A388-625[»]
3SOSX-ray2.58A388-625[»]
4CR5X-ray2.00A388-625[»]
4CR9X-ray1.70A388-625[»]
4CRAX-ray1.80A388-625[»]
4CRBX-ray1.85A388-625[»]
4CRCX-ray1.60A388-625[»]
4CRDX-ray2.10A388-625[»]
4CREX-ray1.73A388-625[»]
4CRFX-ray2.30A388-625[»]
4CRGX-ray1.25A388-625[»]
4D76X-ray1.77A388-625[»]
4D7FX-ray1.62A388-625[»]
4D7GX-ray2.33A388-625[»]
4NA7X-ray2.80A388-625[»]
4NA8X-ray2.30A388-625[»]
4TY6X-ray1.85A388-625[»]
H375-387[»]
4TY7X-ray2.09A388-625[»]
4WXIX-ray2.60A388-625[»]
4X6MX-ray2.40A388-625[»]
4X6NX-ray2.10A388-625[»]
H375-387[»]
4X6OX-ray2.10A388-625[»]
4X6PX-ray1.93A/B388-625[»]
4Y8XX-ray1.90A388-625[»]
4Y8YX-ray2.60A388-625[»]
4Y8ZX-ray2.20A388-625[»]
5E2OX-ray2.08A388-625[»]
5E2PX-ray2.11A388-625[»]
5EODX-ray3.10A20-625[»]
5EOKX-ray2.80A20-625[»]
5EXLX-ray2.30A388-625[»]
5EXMX-ray2.09A388-625[»]
5EXNX-ray1.49A388-625[»]
5I25X-ray2.85A19-625[»]
ProteinModelPortaliP03951.
SMRiP03951.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03951.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 103Apple 1PROSITE-ProRule annotationAdd BLAST84
Domaini110 – 193Apple 2PROSITE-ProRule annotationAdd BLAST84
Domaini200 – 283Apple 3PROSITE-ProRule annotationAdd BLAST84
Domaini291 – 374Apple 4PROSITE-ProRule annotationAdd BLAST84
Domaini388 – 623Peptidase S1PROSITE-ProRule annotationAdd BLAST236

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni547 – 550Heparin-binding4

Sequence similaritiesi

Belongs to the peptidase S1 family. Plasma kallikrein subfamily.PROSITE-ProRule annotation
Contains 4 apple domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000112467.
HOVERGENiHBG000399.
InParanoidiP03951.
KOiK01323.
OMAiGWGYRKL.
OrthoDBiEOG091G0AH5.
PhylomeDBiP03951.
TreeFamiTF343687.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR000177. Apple.
IPR003609. Pan_app.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00024. PAN_1. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00005. APPLEDOMAIN.
PR00722. CHYMOTRYPSIN.
SMARTiSM00223. APPLE. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS00495. APPLE. 4 hits.
PS50948. PAN. 4 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P03951-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MIFLYQVVHF ILFTSVSGEC VTQLLKDTCF EGGDITTVFT PSAKYCQVVC
60 70 80 90 100
TYHPRCLLFT FTAESPSEDP TRWFTCVLKD SVTETLPRVN RTAAISGYSF
110 120 130 140 150
KQCSHQISAC NKDIYVDLDM KGINYNSSVA KSAQECQERC TDDVHCHFFT
160 170 180 190 200
YATRQFPSLE HRNICLLKHT QTGTPTRITK LDKVVSGFSL KSCALSNLAC
210 220 230 240 250
IRDIFPNTVF ADSNIDSVMA PDAFVCGRIC THHPGCLFFT FFSQEWPKES
260 270 280 290 300
QRNLCLLKTS ESGLPSTRIK KSKALSGFSL QSCRHSIPVF CHSSFYHDTD
310 320 330 340 350
FLGEELDIVA AKSHEACQKL CTNAVRCQFF TYTPAQASCN EGKGKCYLKL
360 370 380 390 400
SSNGSPTKIL HGRGGISGYT LRLCKMDNEC TTKIKPRIVG GTASVRGEWP
410 420 430 440 450
WQVTLHTTSP TQRHLCGGSI IGNQWILTAA HCFYGVESPK ILRVYSGILN
460 470 480 490 500
QSEIKEDTSF FGVQEIIIHD QYKMAESGYD IALLKLETTV NYTDSQRPIC
510 520 530 540 550
LPSKGDRNVI YTDCWVTGWG YRKLRDKIQN TLQKAKIPLV TNEECQKRYR
560 570 580 590 600
GHKITHKMIC AGYREGGKDA CKGDSGGPLS CKHNEVWHLV GITSWGEGCA
610 620
QRERPGVYTN VVEYVDWILE KTQAV
Length:625
Mass (Da):70,109
Last modified:October 23, 1986 - v1
Checksum:i147AFA94B7709E8F
GO
Isoform 2 (identifier: P03951-2) [UniParc]FASTAAdd to basket
Also known as: Platelet

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

Show »
Length:571
Mass (Da):63,840
Checksum:iFB9D65D72151755E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti226C → S in AAA51985 (PubMed:2827746).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07651530F → S in FA11D. 1 Publication1
Natural variantiVAR_06792932G → R in FA11D. 1 PublicationCorresponds to variant rs281875259dbSNPEnsembl.1
Natural variantiVAR_01208534D → H in FA11D. 1 PublicationCorresponds to variant rs281875267dbSNPEnsembl.1
Natural variantiVAR_06793043A → T in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 PublicationCorresponds to variant rs281875264dbSNPEnsembl.1
Natural variantiVAR_05489446C → F in FA11D. 1 PublicationCorresponds to variant rs281875271dbSNPEnsembl.1
Natural variantiVAR_06793151T → I in FA11D. 1 PublicationCorresponds to variant rs281875252dbSNPEnsembl.1
Natural variantiVAR_06793251T → P in FA11D. 2 PublicationsCorresponds to variant rs281875243dbSNPEnsembl.1
Natural variantiVAR_06793353H → Q in FA11D. 1 PublicationCorresponds to variant rs281875261dbSNPEnsembl.1
Natural variantiVAR_05489556C → R in FA11D; secretion of the mutant protein is impaired. 2 PublicationsCorresponds to variant rs121965069dbSNPEnsembl.1
Natural variantiVAR_06793463A → V in FA11D. 1 PublicationCorresponds to variant rs281875244dbSNPEnsembl.1
Natural variantiVAR_01177466P → L.1 PublicationCorresponds to variant rs5968dbSNPEnsembl.1
Natural variantiVAR_054896101K → R in FA11D. 1 PublicationCorresponds to variant rs281875272dbSNPEnsembl.1
Natural variantiVAR_076516109A → T in FA11D. 1 PublicationCorresponds to variant rs768474112dbSNPEnsembl.1
Natural variantiVAR_067935140C → Y in FA11D. 1 PublicationCorresponds to variant rs281875256dbSNPEnsembl.1
Natural variantiVAR_054897151Y → C in FA11D. 1 PublicationCorresponds to variant rs281875273dbSNPEnsembl.1
Natural variantiVAR_076517216D → N in FA11D. 1 Publication1
Natural variantiVAR_067936222D → Y in FA11D. 1 PublicationCorresponds to variant rs281875245dbSNPEnsembl.1
Natural variantiVAR_067937228R → Q in FA11D. 1 PublicationCorresponds to variant rs281875246dbSNPEnsembl.1
Natural variantiVAR_067938241F → L in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 PublicationCorresponds to variant rs281875265dbSNPEnsembl.1
Natural variantiVAR_011775244Q → R Found in a patient with factor XI deficiency that also carries mutation N-266. 2 PublicationsCorresponds to variant rs5969dbSNPEnsembl.1
Natural variantiVAR_012086246W → C in FA11D. 1 PublicationCorresponds to variant rs281875279dbSNPEnsembl.1
Natural variantiVAR_067939252R → T in FA11D. 1 PublicationCorresponds to variant rs281875260dbSNPEnsembl.1
Natural variantiVAR_054898255C → Y in FA11D; secretion of the mutant protein is impaired. 1 PublicationCorresponds to variant rs281875277dbSNPEnsembl.1
Natural variantiVAR_054899263G → E in FA11D. 1 PublicationCorresponds to variant rs281875274dbSNPEnsembl.1
Natural variantiVAR_012087266S → N in FA11D. 1 PublicationCorresponds to variant rs145168351dbSNPEnsembl.1
Natural variantiVAR_054900270K → I in FA11D; although the mutant protein is synthesized the secretion is reduced. 1 PublicationCorresponds to variant rs121965070dbSNPEnsembl.1
Natural variantiVAR_067940276S → C in FA11D. 1 PublicationCorresponds to variant rs281875247dbSNPEnsembl.1
Natural variantiVAR_067941277G → D in FA11D. 1 PublicationCorresponds to variant rs281875248dbSNPEnsembl.1
Natural variantiVAR_006622301F → L in FA11D. 2 PublicationsCorresponds to variant rs121965064dbSNPEnsembl.1
Natural variantiVAR_011776308I → F.1 PublicationCorresponds to variant rs5972dbSNPEnsembl.1
Natural variantiVAR_067942315E → K in FA11D. 2 PublicationsCorresponds to variant rs281875257dbSNPEnsembl.1
Natural variantiVAR_012088320L → P in FA11D. 1 PublicationCorresponds to variant rs281875268dbSNPEnsembl.1
Natural variantiVAR_012089322T → I in FA11D. 1 PublicationCorresponds to variant rs281875269dbSNPEnsembl.1
Natural variantiVAR_012090326R → C in FA11D. 1 PublicationCorresponds to variant rs28934608dbSNPEnsembl.1
Natural variantiVAR_067943331T → I in FA11D. 1 PublicationCorresponds to variant rs281875253dbSNPEnsembl.1
Natural variantiVAR_011777339C → F.3 PublicationsCorresponds to variant rs5967dbSNPEnsembl.1
Natural variantiVAR_012091341E → K in FA11D. 1 PublicationCorresponds to variant rs281875270dbSNPEnsembl.1
Natural variantiVAR_067944360L → P in FA11D. 1 PublicationCorresponds to variant rs281875254dbSNPEnsembl.1
Natural variantiVAR_011778399W → R.Corresponds to variant rs1800439dbSNPEnsembl.1
Natural variantiVAR_067945401W → R in FA11D. 1 PublicationCorresponds to variant rs281875262dbSNPEnsembl.1
Natural variantiVAR_067946403V → M in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 PublicationCorresponds to variant rs281875266dbSNPEnsembl.1
Natural variantiVAR_012092404T → N in FA11D. 1 PublicationCorresponds to variant rs121965067dbSNPEnsembl.1
Natural variantiVAR_054901418G → V in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 PublicationCorresponds to variant rs121965071dbSNPEnsembl.1
Natural variantiVAR_012093430A → V in FA11D. 1 PublicationCorresponds to variant rs121965068dbSNPEnsembl.1
Natural variantiVAR_067947454I → K in FA11D. 1 PublicationCorresponds to variant rs281875241dbSNPEnsembl.1
Natural variantiVAR_012094460F → V in FA11D. 1 PublicationCorresponds to variant rs121965065dbSNPEnsembl.1
Natural variantiVAR_067948481I → S in FA11D. 1 PublicationCorresponds to variant rs281875242dbSNPEnsembl.1
Natural variantiVAR_012095493T → I in FA11D. 1 Publication1
Natural variantiVAR_067949503S → P in FA11D. 1 PublicationCorresponds to variant rs140068026dbSNPEnsembl.1
Natural variantiVAR_067950506D → G in FA11D; mild phenotype. 1 PublicationCorresponds to variant rs281875258dbSNPEnsembl.1
Natural variantiVAR_054902511Y → H in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion. 1 PublicationCorresponds to variant rs281875278dbSNPEnsembl.1
Natural variantiVAR_067951514C → F in FA11D. 1 PublicationCorresponds to variant rs281875249dbSNPEnsembl.1
Natural variantiVAR_067952526D → E in FA11D. 1 PublicationCorresponds to variant rs281875263dbSNPEnsembl.1
Natural variantiVAR_054903538P → L in FA11D. 1 PublicationCorresponds to variant rs139695003dbSNPEnsembl.1
Natural variantiVAR_076518543E → K in FA11D. 1 PublicationCorresponds to variant rs142952627dbSNPEnsembl.1
Natural variantiVAR_076519552H → R in FA11D. 1 PublicationCorresponds to variant rs369935706dbSNPEnsembl.1
Natural variantiVAR_054904565E → K in FA11D. 1 PublicationCorresponds to variant rs281875275dbSNPEnsembl.1
Natural variantiVAR_067953575S → L in FA11D. 1 PublicationCorresponds to variant rs281875250dbSNPEnsembl.1
Natural variantiVAR_054905587W → S in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 PublicationCorresponds to variant rs121965072dbSNPEnsembl.1
Natural variantiVAR_012096594S → R in FA11D. 1 PublicationCorresponds to variant rs28934609dbSNPEnsembl.1
Natural variantiVAR_067954597E → K in FA11D. 2 PublicationsCorresponds to variant rs281875251dbSNPEnsembl.1
Natural variantiVAR_067955608Y → H in FA11D. 1 PublicationCorresponds to variant rs281875255dbSNPEnsembl.1
Natural variantiVAR_054906618I → S in FA11D. 1 PublicationCorresponds to variant rs281875276dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005388109 – 162Missing in isoform 2. 1 PublicationAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3847.1. [P03951-1]
PIRiA27431. KFHU1.
RefSeqiNP_000119.1. NM_000128.3. [P03951-1]
UniGeneiHs.1430.

Genome annotation databases

EnsembliENST00000264692; ENSP00000264692; ENSG00000088926. [P03951-2]
ENST00000403665; ENSP00000384957; ENSG00000088926. [P03951-1]
GeneIDi2160.
KEGGihsa:2160.
UCSCiuc003iza.2. human. [P03951-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Factor XI entry

SeattleSNPs
Mendelian genes Coagulation factor XI (F11)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3847.1. [P03951-1]
PIRiA27431. KFHU1.
RefSeqiNP_000119.1. NM_000128.3. [P03951-1]
UniGeneiHs.1430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.05A388-624[»]
1ZTKX-ray2.50A388-624[»]
1ZTLX-ray2.60A388-624[»]
2F83X-ray2.87A1-625[»]
2FDAX-ray2.00A388-625[»]
2J8JNMR-A/B290-379[»]
2J8LNMR-A/B290-379[»]
3BG8X-ray1.60A388-625[»]
3SORX-ray1.80A388-625[»]
3SOSX-ray2.58A388-625[»]
4CR5X-ray2.00A388-625[»]
4CR9X-ray1.70A388-625[»]
4CRAX-ray1.80A388-625[»]
4CRBX-ray1.85A388-625[»]
4CRCX-ray1.60A388-625[»]
4CRDX-ray2.10A388-625[»]
4CREX-ray1.73A388-625[»]
4CRFX-ray2.30A388-625[»]
4CRGX-ray1.25A388-625[»]
4D76X-ray1.77A388-625[»]
4D7FX-ray1.62A388-625[»]
4D7GX-ray2.33A388-625[»]
4NA7X-ray2.80A388-625[»]
4NA8X-ray2.30A388-625[»]
4TY6X-ray1.85A388-625[»]
H375-387[»]
4TY7X-ray2.09A388-625[»]
4WXIX-ray2.60A388-625[»]
4X6MX-ray2.40A388-625[»]
4X6NX-ray2.10A388-625[»]
H375-387[»]
4X6OX-ray2.10A388-625[»]
4X6PX-ray1.93A/B388-625[»]
4Y8XX-ray1.90A388-625[»]
4Y8YX-ray2.60A388-625[»]
4Y8ZX-ray2.20A388-625[»]
5E2OX-ray2.08A388-625[»]
5E2PX-ray2.11A388-625[»]
5EODX-ray3.10A20-625[»]
5EOKX-ray2.80A20-625[»]
5EXLX-ray2.30A388-625[»]
5EXMX-ray2.09A388-625[»]
5EXNX-ray1.49A388-625[»]
5I25X-ray2.85A19-625[»]
ProteinModelPortaliP03951.
SMRiP03951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108458. 6 interactors.
DIPiDIP-29085N.
IntActiP03951. 1 interactor.
STRINGi9606.ENSP00000384957.

Chemistry databases

BindingDBiP03951.
ChEMBLiCHEMBL2820.
DrugBankiDB00100. Coagulation Factor IX.
GuidetoPHARMACOLOGYi2360.

Protein family/group databases

MEROPSiS01.213.

PTM databases

iPTMnetiP03951.
PhosphoSitePlusiP03951.

Polymorphism and mutation databases

BioMutaiF11.
DMDMi119762.

Proteomic databases

PaxDbiP03951.
PeptideAtlasiP03951.
PRIDEiP03951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264692; ENSP00000264692; ENSG00000088926. [P03951-2]
ENST00000403665; ENSP00000384957; ENSG00000088926. [P03951-1]
GeneIDi2160.
KEGGihsa:2160.
UCSCiuc003iza.2. human. [P03951-1]

Organism-specific databases

CTDi2160.
DisGeNETi2160.
GeneCardsiF11.
HGNCiHGNC:3529. F11.
MalaCardsiF11.
MIMi264900. gene.
612416. phenotype.
neXtProtiNX_P03951.
OpenTargetsiENSG00000088926.
Orphaneti329. Congenital factor XI deficiency.
PharmGKBiPA27941.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000112467.
HOVERGENiHBG000399.
InParanoidiP03951.
KOiK01323.
OMAiGWGYRKL.
OrthoDBiEOG091G0AH5.
PhylomeDBiP03951.
TreeFamiTF343687.

Enzyme and pathway databases

BioCyciZFISH:HS01617-MONOMER.
BRENDAi3.4.21.27. 2681.
ReactomeiR-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
SABIO-RKP03951.

Miscellaneous databases

ChiTaRSiF11. human.
EvolutionaryTraceiP03951.
GeneWikiiFactor_XI.
GenomeRNAii2160.
PMAP-CutDBP03951.
PROiP03951.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000088926.
CleanExiHS_F11.
ExpressionAtlasiP03951. baseline and differential.
GenevisibleiP03951. HS.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR000177. Apple.
IPR003609. Pan_app.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00024. PAN_1. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00005. APPLEDOMAIN.
PR00722. CHYMOTRYPSIN.
SMARTiSM00223. APPLE. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS00495. APPLE. 4 hits.
PS50948. PAN. 4 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA11_HUMAN
AccessioniPrimary (citable) accession number: P03951
Secondary accession number(s): D3DP64, Q4W5C2, Q9Y495
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: November 2, 2016
This is version 204 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.