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P03951

- FA11_HUMAN

UniProt

P03951 - FA11_HUMAN

Protein

Coagulation factor XI

Gene

F11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 1 (23 Oct 1986)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei431 – 4311Charge relay system
    Active sitei480 – 4801Charge relay system
    Active sitei575 – 5751Charge relay system

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. serine-type aminopeptidase activity Source: Ensembl
    4. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: UniProtKB
    2. blood coagulation, intrinsic pathway Source: Reactome
    3. plasminogen activation Source: BHF-UCL
    4. positive regulation of fibrinolysis Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_326. Intrinsic Pathway.

    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
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3529. F11.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Factor XI deficiency (FA11D) [MIM:612416]: 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.20 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321G → R in FA11D. 1 Publication
    Corresponds to variant rs281875259 [ dbSNP | Ensembl ].
    VAR_067929
    Natural varianti34 – 341D → H in FA11D. 1 Publication
    Corresponds to variant rs281875267 [ dbSNP | Ensembl ].
    VAR_012085
    Natural varianti43 – 431A → T in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 Publication
    Corresponds to variant rs281875264 [ dbSNP | Ensembl ].
    VAR_067930
    Natural varianti46 – 461C → F in FA11D. 1 Publication
    Corresponds to variant rs281875271 [ dbSNP | Ensembl ].
    VAR_054894
    Natural varianti51 – 511T → I in FA11D. 1 Publication
    Corresponds to variant rs281875252 [ dbSNP | Ensembl ].
    VAR_067931
    Natural varianti51 – 511T → P in FA11D. 2 Publications
    Corresponds to variant rs281875243 [ dbSNP | Ensembl ].
    VAR_067932
    Natural varianti53 – 531H → Q in FA11D. 1 Publication
    Corresponds to variant rs281875261 [ dbSNP | Ensembl ].
    VAR_067933
    Natural varianti56 – 561C → R in FA11D; secretion of the mutant protein is impaired. 2 Publications
    Corresponds to variant rs121965069 [ dbSNP | Ensembl ].
    VAR_054895
    Natural varianti63 – 631A → V in FA11D. 1 Publication
    Corresponds to variant rs281875244 [ dbSNP | Ensembl ].
    VAR_067934
    Natural varianti101 – 1011K → R in FA11D. 1 Publication
    Corresponds to variant rs281875272 [ dbSNP | Ensembl ].
    VAR_054896
    Natural varianti140 – 1401C → Y in FA11D. 1 Publication
    Corresponds to variant rs281875256 [ dbSNP | Ensembl ].
    VAR_067935
    Natural varianti151 – 1511Y → C in FA11D. 1 Publication
    Corresponds to variant rs281875273 [ dbSNP | Ensembl ].
    VAR_054897
    Natural varianti222 – 2221D → Y in FA11D. 1 Publication
    Corresponds to variant rs281875245 [ dbSNP | Ensembl ].
    VAR_067936
    Natural varianti228 – 2281R → Q in FA11D. 1 Publication
    Corresponds to variant rs281875246 [ dbSNP | Ensembl ].
    VAR_067937
    Natural varianti241 – 2411F → L in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 Publication
    Corresponds to variant rs281875265 [ dbSNP | Ensembl ].
    VAR_067938
    Natural varianti246 – 2461W → C in FA11D. 1 Publication
    Corresponds to variant rs281875279 [ dbSNP | Ensembl ].
    VAR_012086
    Natural varianti252 – 2521R → T in FA11D. 1 Publication
    Corresponds to variant rs281875260 [ dbSNP | Ensembl ].
    VAR_067939
    Natural varianti255 – 2551C → Y in FA11D; secretion of the mutant protein is impaired. 1 Publication
    Corresponds to variant rs281875277 [ dbSNP | Ensembl ].
    VAR_054898
    Natural varianti263 – 2631G → E in FA11D. 1 Publication
    Corresponds to variant rs281875274 [ dbSNP | Ensembl ].
    VAR_054899
    Natural varianti266 – 2661S → N in FA11D. 1 Publication
    Corresponds to variant rs145168351 [ dbSNP | Ensembl ].
    VAR_012087
    Natural varianti270 – 2701K → I in FA11D; although the mutant protein is synthesized the secretion is reduced. 1 Publication
    Corresponds to variant rs121965070 [ dbSNP | Ensembl ].
    VAR_054900
    Natural varianti276 – 2761S → C in FA11D. 1 Publication
    Corresponds to variant rs281875247 [ dbSNP | Ensembl ].
    VAR_067940
    Natural varianti277 – 2771G → D in FA11D. 1 Publication
    Corresponds to variant rs281875248 [ dbSNP | Ensembl ].
    VAR_067941
    Natural varianti301 – 3011F → L in FA11D. 2 Publications
    Corresponds to variant rs121965064 [ dbSNP | Ensembl ].
    VAR_006622
    Natural varianti315 – 3151E → K in FA11D. 1 Publication
    Corresponds to variant rs281875257 [ dbSNP | Ensembl ].
    VAR_067942
    Natural varianti320 – 3201L → P in FA11D. 1 Publication
    Corresponds to variant rs281875268 [ dbSNP | Ensembl ].
    VAR_012088
    Natural varianti322 – 3221T → I in FA11D. 1 Publication
    Corresponds to variant rs281875269 [ dbSNP | Ensembl ].
    VAR_012089
    Natural varianti326 – 3261R → C in FA11D. 1 Publication
    Corresponds to variant rs28934608 [ dbSNP | Ensembl ].
    VAR_012090
    Natural varianti331 – 3311T → I in FA11D. 1 Publication
    Corresponds to variant rs281875253 [ dbSNP | Ensembl ].
    VAR_067943
    Natural varianti341 – 3411E → K in FA11D. 1 Publication
    Corresponds to variant rs281875270 [ dbSNP | Ensembl ].
    VAR_012091
    Natural varianti360 – 3601L → P in FA11D. 1 Publication
    Corresponds to variant rs281875254 [ dbSNP | Ensembl ].
    VAR_067944
    Natural varianti401 – 4011W → R in FA11D. 1 Publication
    Corresponds to variant rs281875262 [ dbSNP | Ensembl ].
    VAR_067945
    Natural varianti403 – 4031V → M in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 Publication
    Corresponds to variant rs281875266 [ dbSNP | Ensembl ].
    VAR_067946
    Natural varianti404 – 4041T → N in FA11D. 1 Publication
    Corresponds to variant rs121965067 [ dbSNP | Ensembl ].
    VAR_012092
    Natural varianti418 – 4181G → V in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 Publication
    Corresponds to variant rs121965071 [ dbSNP | Ensembl ].
    VAR_054901
    Natural varianti430 – 4301A → V in FA11D. 1 Publication
    Corresponds to variant rs121965068 [ dbSNP | Ensembl ].
    VAR_012093
    Natural varianti454 – 4541I → K in FA11D. 1 Publication
    Corresponds to variant rs281875241 [ dbSNP | Ensembl ].
    VAR_067947
    Natural varianti460 – 4601F → V in FA11D. 1 Publication
    Corresponds to variant rs121965065 [ dbSNP | Ensembl ].
    VAR_012094
    Natural varianti481 – 4811I → S in FA11D. 1 Publication
    Corresponds to variant rs281875242 [ dbSNP | Ensembl ].
    VAR_067948
    Natural varianti493 – 4931T → I in FA11D. 1 Publication
    VAR_012095
    Natural varianti503 – 5031S → P in FA11D. 1 Publication
    Corresponds to variant rs140068026 [ dbSNP | Ensembl ].
    VAR_067949
    Natural varianti506 – 5061D → G in FA11D; mild phenotype. 1 Publication
    Corresponds to variant rs281875258 [ dbSNP | Ensembl ].
    VAR_067950
    Natural varianti511 – 5111Y → H in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion. 1 Publication
    Corresponds to variant rs281875278 [ dbSNP | Ensembl ].
    VAR_054902
    Natural varianti514 – 5141C → F in FA11D. 1 Publication
    Corresponds to variant rs281875249 [ dbSNP | Ensembl ].
    VAR_067951
    Natural varianti526 – 5261D → E in FA11D. 1 Publication
    Corresponds to variant rs281875263 [ dbSNP | Ensembl ].
    VAR_067952
    Natural varianti538 – 5381P → L in FA11D. 1 Publication
    Corresponds to variant rs139695003 [ dbSNP | Ensembl ].
    VAR_054903
    Natural varianti565 – 5651E → K in FA11D. 1 Publication
    Corresponds to variant rs281875275 [ dbSNP | Ensembl ].
    VAR_054904
    Natural varianti575 – 5751S → L in FA11D. 1 Publication
    Corresponds to variant rs281875250 [ dbSNP | Ensembl ].
    VAR_067953
    Natural varianti587 – 5871W → S in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 Publication
    Corresponds to variant rs121965072 [ dbSNP | Ensembl ].
    VAR_054905
    Natural varianti594 – 5941S → R in FA11D. 1 Publication
    Corresponds to variant rs28934609 [ dbSNP | Ensembl ].
    VAR_012096
    Natural varianti597 – 5971E → K in FA11D. 2 Publications
    Corresponds to variant rs281875251 [ dbSNP | Ensembl ].
    VAR_067954
    Natural varianti608 – 6081Y → H in FA11D. 1 Publication
    Corresponds to variant rs281875255 [ dbSNP | Ensembl ].
    VAR_067955
    Natural varianti618 – 6181I → S in FA11D. 1 Publication
    Corresponds to variant rs281875276 [ dbSNP | Ensembl ].
    VAR_054906

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi612416. phenotype.
    Orphaneti329. Congenital factor XI deficiency.
    PharmGKBiPA27941.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Chaini19 – 387369Coagulation factor XIa heavy chainPRO_0000027825Add
    BLAST
    Chaini388 – 625238Coagulation factor XIa light chainPRO_0000027826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi20 ↔ 103Sequence Analysis
    Disulfide bondi29 – 29Interchain
    Disulfide bondi46 ↔ 761 Publication
    Disulfide bondi50 ↔ 561 Publication
    Glycosylationi90 – 901N-linked (GlcNAc...)
    Disulfide bondi110 ↔ 1931 Publication
    Glycosylationi126 – 1261N-linked (GlcNAc...)1 Publication
    Disulfide bondi136 ↔ 1651 Publication
    Disulfide bondi140 ↔ 1461 Publication
    Disulfide bondi200 ↔ 283
    Disulfide bondi226 ↔ 2551 Publication
    Disulfide bondi230 ↔ 2361 Publication
    Disulfide bondi291 ↔ 3741 Publication
    Disulfide bondi317 ↔ 3461 Publication
    Disulfide bondi321 ↔ 3271 Publication
    Disulfide bondi339 – 339InterchainSequence Analysis
    Glycosylationi353 – 3531N-linked (GlcNAc...)
    Disulfide bondi380 ↔ 500Interchain (between heavy and light chains)
    Disulfide bondi416 ↔ 4321 Publication
    Glycosylationi450 – 4501N-linked (GlcNAc...)2 Publications
    Glycosylationi491 – 4911N-linked (GlcNAc...)3 Publications
    Disulfide bondi514 ↔ 581
    Disulfide bondi545 ↔ 5601 Publication
    Disulfide bondi571 ↔ 599

    Post-translational modificationi

    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

    PhosphoSiteiP03951.

    Miscellaneous databases

    PMAP-CutDBP03951.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP03951.
    BgeeiP03951.
    CleanExiHS_F11.
    GenevestigatoriP03951.

    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. 3 interactions.
    DIPiDIP-29085N.
    IntActiP03951. 1 interaction.
    STRINGi9606.ENSP00000264691.

    Structurei

    Secondary structure

    1
    625
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 306
    Beta strandi34 – 396
    Helixi43 – 5210
    Beta strandi53 – 553
    Beta strandi58 – 625
    Turni71 – 744
    Beta strandi75 – 795
    Helixi82 – 843
    Beta strandi88 – 9811
    Beta strandi115 – 1217
    Beta strandi123 – 1297
    Helixi133 – 1419
    Beta strandi143 – 1453
    Beta strandi147 – 1526
    Beta strandi159 – 1613
    Beta strandi164 – 1696
    Beta strandi171 – 1744
    Beta strandi176 – 18813
    Turni191 – 1944
    Beta strandi205 – 2095
    Beta strandi212 – 2198
    Helixi223 – 2319
    Beta strandi237 – 2426
    Helixi249 – 2513
    Beta strandi254 – 2596
    Beta strandi261 – 2644
    Beta strandi269 – 27810
    Helixi281 – 2833
    Beta strandi294 – 2963
    Beta strandi298 – 3025
    Beta strandi304 – 31310
    Helixi316 – 3238
    Beta strandi329 – 3335
    Turni337 – 3393
    Beta strandi344 – 3507
    Beta strandi352 – 3543
    Beta strandi358 – 3636
    Beta strandi366 – 3694
    Helixi374 – 3763
    Beta strandi390 – 3934
    Beta strandi402 – 4076
    Beta strandi409 – 4113
    Beta strandi413 – 42210
    Beta strandi425 – 4284
    Helixi430 – 4334
    Helixi439 – 4413
    Beta strandi442 – 4454
    Helixi451 – 4533
    Beta strandi456 – 4583
    Beta strandi461 – 4688
    Helixi475 – 4773
    Beta strandi482 – 4887
    Beta strandi494 – 4963
    Helixi504 – 5074
    Beta strandi514 – 5196
    Beta strandi522 – 5254
    Beta strandi533 – 5364
    Helixi542 – 5487
    Turni549 – 5513
    Beta strandi558 – 5614
    Beta strandi578 – 5836
    Beta strandi586 – 59510
    Beta strandi597 – 6004
    Beta strandi606 – 6105
    Helixi611 – 6144
    Helixi615 – 6228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    4NA7X-ray2.80A388-625[»]
    4NA8X-ray2.30A388-625[»]
    ProteinModelPortaliP03951.
    SMRiP03951. Positions 20-623.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03951.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10384Apple 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini110 – 19384Apple 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini200 – 28384Apple 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini291 – 37484Apple 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini388 – 623236Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni547 – 5504Heparin-binding

    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

    eggNOGiCOG5640.
    HOGENOMiHOG000112467.
    HOVERGENiHBG000399.
    InParanoidiP03951.
    KOiK01323.
    OMAiVWHLVGI.
    OrthoDBiEOG75B84T.
    PhylomeDBiP03951.
    TreeFamiTF343687.

    Family and domain databases

    InterProiIPR000177. Apple.
    IPR003014. PAN-1_domain.
    IPR003609. Pan_app.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [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. Align

    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

    MIFLYQVVHF ILFTSVSGEC VTQLLKDTCF EGGDITTVFT PSAKYCQVVC    50
    TYHPRCLLFT FTAESPSEDP TRWFTCVLKD SVTETLPRVN RTAAISGYSF 100
    KQCSHQISAC NKDIYVDLDM KGINYNSSVA KSAQECQERC TDDVHCHFFT 150
    YATRQFPSLE HRNICLLKHT QTGTPTRITK LDKVVSGFSL KSCALSNLAC 200
    IRDIFPNTVF ADSNIDSVMA PDAFVCGRIC THHPGCLFFT FFSQEWPKES 250
    QRNLCLLKTS ESGLPSTRIK KSKALSGFSL QSCRHSIPVF CHSSFYHDTD 300
    FLGEELDIVA AKSHEACQKL CTNAVRCQFF TYTPAQASCN EGKGKCYLKL 350
    SSNGSPTKIL HGRGGISGYT LRLCKMDNEC TTKIKPRIVG GTASVRGEWP 400
    WQVTLHTTSP TQRHLCGGSI IGNQWILTAA HCFYGVESPK ILRVYSGILN 450
    QSEIKEDTSF FGVQEIIIHD QYKMAESGYD IALLKLETTV NYTDSQRPIC 500
    LPSKGDRNVI YTDCWVTGWG YRKLRDKIQN TLQKAKIPLV TNEECQKRYR 550
    GHKITHKMIC AGYREGGKDA CKGDSGGPLS CKHNEVWHLV GITSWGEGCA 600
    QRERPGVYTN VVEYVDWILE KTQAV 625
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2261C → S in AAA51985. (PubMed:2827746)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321G → R in FA11D. 1 Publication
    Corresponds to variant rs281875259 [ dbSNP | Ensembl ].
    VAR_067929
    Natural varianti34 – 341D → H in FA11D. 1 Publication
    Corresponds to variant rs281875267 [ dbSNP | Ensembl ].
    VAR_012085
    Natural varianti43 – 431A → T in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 Publication
    Corresponds to variant rs281875264 [ dbSNP | Ensembl ].
    VAR_067930
    Natural varianti46 – 461C → F in FA11D. 1 Publication
    Corresponds to variant rs281875271 [ dbSNP | Ensembl ].
    VAR_054894
    Natural varianti51 – 511T → I in FA11D. 1 Publication
    Corresponds to variant rs281875252 [ dbSNP | Ensembl ].
    VAR_067931
    Natural varianti51 – 511T → P in FA11D. 2 Publications
    Corresponds to variant rs281875243 [ dbSNP | Ensembl ].
    VAR_067932
    Natural varianti53 – 531H → Q in FA11D. 1 Publication
    Corresponds to variant rs281875261 [ dbSNP | Ensembl ].
    VAR_067933
    Natural varianti56 – 561C → R in FA11D; secretion of the mutant protein is impaired. 2 Publications
    Corresponds to variant rs121965069 [ dbSNP | Ensembl ].
    VAR_054895
    Natural varianti63 – 631A → V in FA11D. 1 Publication
    Corresponds to variant rs281875244 [ dbSNP | Ensembl ].
    VAR_067934
    Natural varianti66 – 661P → L.1 Publication
    Corresponds to variant rs5968 [ dbSNP | Ensembl ].
    VAR_011774
    Natural varianti101 – 1011K → R in FA11D. 1 Publication
    Corresponds to variant rs281875272 [ dbSNP | Ensembl ].
    VAR_054896
    Natural varianti140 – 1401C → Y in FA11D. 1 Publication
    Corresponds to variant rs281875256 [ dbSNP | Ensembl ].
    VAR_067935
    Natural varianti151 – 1511Y → C in FA11D. 1 Publication
    Corresponds to variant rs281875273 [ dbSNP | Ensembl ].
    VAR_054897
    Natural varianti222 – 2221D → Y in FA11D. 1 Publication
    Corresponds to variant rs281875245 [ dbSNP | Ensembl ].
    VAR_067936
    Natural varianti228 – 2281R → Q in FA11D. 1 Publication
    Corresponds to variant rs281875246 [ dbSNP | Ensembl ].
    VAR_067937
    Natural varianti241 – 2411F → L in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 Publication
    Corresponds to variant rs281875265 [ dbSNP | Ensembl ].
    VAR_067938
    Natural varianti244 – 2441Q → R Found in a patient with factor XI deficiency that also carries mutation N-266. 2 Publications
    Corresponds to variant rs5969 [ dbSNP | Ensembl ].
    VAR_011775
    Natural varianti246 – 2461W → C in FA11D. 1 Publication
    Corresponds to variant rs281875279 [ dbSNP | Ensembl ].
    VAR_012086
    Natural varianti252 – 2521R → T in FA11D. 1 Publication
    Corresponds to variant rs281875260 [ dbSNP | Ensembl ].
    VAR_067939
    Natural varianti255 – 2551C → Y in FA11D; secretion of the mutant protein is impaired. 1 Publication
    Corresponds to variant rs281875277 [ dbSNP | Ensembl ].
    VAR_054898
    Natural varianti263 – 2631G → E in FA11D. 1 Publication
    Corresponds to variant rs281875274 [ dbSNP | Ensembl ].
    VAR_054899
    Natural varianti266 – 2661S → N in FA11D. 1 Publication
    Corresponds to variant rs145168351 [ dbSNP | Ensembl ].
    VAR_012087
    Natural varianti270 – 2701K → I in FA11D; although the mutant protein is synthesized the secretion is reduced. 1 Publication
    Corresponds to variant rs121965070 [ dbSNP | Ensembl ].
    VAR_054900
    Natural varianti276 – 2761S → C in FA11D. 1 Publication
    Corresponds to variant rs281875247 [ dbSNP | Ensembl ].
    VAR_067940
    Natural varianti277 – 2771G → D in FA11D. 1 Publication
    Corresponds to variant rs281875248 [ dbSNP | Ensembl ].
    VAR_067941
    Natural varianti301 – 3011F → L in FA11D. 2 Publications
    Corresponds to variant rs121965064 [ dbSNP | Ensembl ].
    VAR_006622
    Natural varianti308 – 3081I → F.1 Publication
    Corresponds to variant rs5972 [ dbSNP | Ensembl ].
    VAR_011776
    Natural varianti315 – 3151E → K in FA11D. 1 Publication
    Corresponds to variant rs281875257 [ dbSNP | Ensembl ].
    VAR_067942
    Natural varianti320 – 3201L → P in FA11D. 1 Publication
    Corresponds to variant rs281875268 [ dbSNP | Ensembl ].
    VAR_012088
    Natural varianti322 – 3221T → I in FA11D. 1 Publication
    Corresponds to variant rs281875269 [ dbSNP | Ensembl ].
    VAR_012089
    Natural varianti326 – 3261R → C in FA11D. 1 Publication
    Corresponds to variant rs28934608 [ dbSNP | Ensembl ].
    VAR_012090
    Natural varianti331 – 3311T → I in FA11D. 1 Publication
    Corresponds to variant rs281875253 [ dbSNP | Ensembl ].
    VAR_067943
    Natural varianti339 – 3391C → F.3 Publications
    Corresponds to variant rs5967 [ dbSNP | Ensembl ].
    VAR_011777
    Natural varianti341 – 3411E → K in FA11D. 1 Publication
    Corresponds to variant rs281875270 [ dbSNP | Ensembl ].
    VAR_012091
    Natural varianti360 – 3601L → P in FA11D. 1 Publication
    Corresponds to variant rs281875254 [ dbSNP | Ensembl ].
    VAR_067944
    Natural varianti399 – 3991W → R.
    Corresponds to variant rs1800439 [ dbSNP | Ensembl ].
    VAR_011778
    Natural varianti401 – 4011W → R in FA11D. 1 Publication
    Corresponds to variant rs281875262 [ dbSNP | Ensembl ].
    VAR_067945
    Natural varianti403 – 4031V → M in FA11D; dominant-negative mutation that results in severely decreased protein secretion. 1 Publication
    Corresponds to variant rs281875266 [ dbSNP | Ensembl ].
    VAR_067946
    Natural varianti404 – 4041T → N in FA11D. 1 Publication
    Corresponds to variant rs121965067 [ dbSNP | Ensembl ].
    VAR_012092
    Natural varianti418 – 4181G → V in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 Publication
    Corresponds to variant rs121965071 [ dbSNP | Ensembl ].
    VAR_054901
    Natural varianti430 – 4301A → V in FA11D. 1 Publication
    Corresponds to variant rs121965068 [ dbSNP | Ensembl ].
    VAR_012093
    Natural varianti454 – 4541I → K in FA11D. 1 Publication
    Corresponds to variant rs281875241 [ dbSNP | Ensembl ].
    VAR_067947
    Natural varianti460 – 4601F → V in FA11D. 1 Publication
    Corresponds to variant rs121965065 [ dbSNP | Ensembl ].
    VAR_012094
    Natural varianti481 – 4811I → S in FA11D. 1 Publication
    Corresponds to variant rs281875242 [ dbSNP | Ensembl ].
    VAR_067948
    Natural varianti493 – 4931T → I in FA11D. 1 Publication
    VAR_012095
    Natural varianti503 – 5031S → P in FA11D. 1 Publication
    Corresponds to variant rs140068026 [ dbSNP | Ensembl ].
    VAR_067949
    Natural varianti506 – 5061D → G in FA11D; mild phenotype. 1 Publication
    Corresponds to variant rs281875258 [ dbSNP | Ensembl ].
    VAR_067950
    Natural varianti511 – 5111Y → H in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion. 1 Publication
    Corresponds to variant rs281875278 [ dbSNP | Ensembl ].
    VAR_054902
    Natural varianti514 – 5141C → F in FA11D. 1 Publication
    Corresponds to variant rs281875249 [ dbSNP | Ensembl ].
    VAR_067951
    Natural varianti526 – 5261D → E in FA11D. 1 Publication
    Corresponds to variant rs281875263 [ dbSNP | Ensembl ].
    VAR_067952
    Natural varianti538 – 5381P → L in FA11D. 1 Publication
    Corresponds to variant rs139695003 [ dbSNP | Ensembl ].
    VAR_054903
    Natural varianti565 – 5651E → K in FA11D. 1 Publication
    Corresponds to variant rs281875275 [ dbSNP | Ensembl ].
    VAR_054904
    Natural varianti575 – 5751S → L in FA11D. 1 Publication
    Corresponds to variant rs281875250 [ dbSNP | Ensembl ].
    VAR_067953
    Natural varianti587 – 5871W → S in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect. 1 Publication
    Corresponds to variant rs121965072 [ dbSNP | Ensembl ].
    VAR_054905
    Natural varianti594 – 5941S → R in FA11D. 1 Publication
    Corresponds to variant rs28934609 [ dbSNP | Ensembl ].
    VAR_012096
    Natural varianti597 – 5971E → K in FA11D. 2 Publications
    Corresponds to variant rs281875251 [ dbSNP | Ensembl ].
    VAR_067954
    Natural varianti608 – 6081Y → H in FA11D. 1 Publication
    Corresponds to variant rs281875255 [ dbSNP | Ensembl ].
    VAR_067955
    Natural varianti618 – 6181I → S in FA11D. 1 Publication
    Corresponds to variant rs281875276 [ dbSNP | Ensembl ].
    VAR_054906

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei109 – 16254Missing in isoform 2. 1 PublicationVSP_005388Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENST00000403665; ENSP00000384957; ENSG00000088926. [P03951-1]
    GeneIDi2160.
    KEGGihsa:2160.
    UCSCiuc003iza.1. human. [P03951-1]

    Polymorphism databases

    DMDMi119762.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3847.1. [P03951-1 ]
    PIRi A27431. KFHU1.
    RefSeqi NP_000119.1. NM_000128.3. [P03951-1 ]
    UniGenei Hs.1430.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 388-624 [» ]
    1ZTK X-ray 2.50 A 388-624 [» ]
    1ZTL X-ray 2.60 A 388-624 [» ]
    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 [» ]
    3SOR X-ray 1.80 A 388-625 [» ]
    3SOS X-ray 2.58 A 388-625 [» ]
    4NA7 X-ray 2.80 A 388-625 [» ]
    4NA8 X-ray 2.30 A 388-625 [» ]
    ProteinModelPortali P03951.
    SMRi P03951. Positions 20-623.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108458. 3 interactions.
    DIPi DIP-29085N.
    IntActi P03951. 1 interaction.
    STRINGi 9606.ENSP00000264691.

    Chemistry

    BindingDBi P03951.
    ChEMBLi CHEMBL2820.
    DrugBanki DB00100. Coagulation Factor IX.
    GuidetoPHARMACOLOGYi 2360.

    Protein family/group databases

    MEROPSi S01.213.

    PTM databases

    PhosphoSitei P03951.

    Polymorphism databases

    DMDMi 119762.

    Proteomic databases

    PaxDbi P03951.
    PeptideAtlasi P03951.
    PRIDEi P03951.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000403665 ; ENSP00000384957 ; ENSG00000088926 . [P03951-1 ]
    GeneIDi 2160.
    KEGGi hsa:2160.
    UCSCi uc003iza.1. human. [P03951-1 ]

    Organism-specific databases

    CTDi 2160.
    GeneCardsi GC04P187187.
    HGNCi HGNC:3529. F11.
    MIMi 264900. gene.
    612416. phenotype.
    neXtProti NX_P03951.
    Orphaneti 329. Congenital factor XI deficiency.
    PharmGKBi PA27941.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000112467.
    HOVERGENi HBG000399.
    InParanoidi P03951.
    KOi K01323.
    OMAi VWHLVGI.
    OrthoDBi EOG75B84T.
    PhylomeDBi P03951.
    TreeFami TF343687.

    Enzyme and pathway databases

    Reactomei REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    ChiTaRSi F11. human.
    EvolutionaryTracei P03951.
    GeneWikii Factor_XI.
    GenomeRNAii 2160.
    NextBioi 8727.
    PMAP-CutDB P03951.
    PROi P03951.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P03951.
    Bgeei P03951.
    CleanExi HS_F11.
    Genevestigatori P03951.

    Family and domain databases

    InterProi IPR000177. Apple.
    IPR003014. PAN-1_domain.
    IPR003609. Pan_app.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00024. PAN_1. 4 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00005. APPLEDOMAIN.
    PR00722. CHYMOTRYPSIN.
    SMARTi SM00223. APPLE. 4 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-450 AND ASN-491.
      Tissue: Plasma.
    12. "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] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-491.
      Tissue: Liver.
    13. "Clavatadine A, a natural product with selective recognition and irreversible inhibition of factor XIa."
      Buchanan M.S., Carroll A.R., Wessling D., Jobling M., Avery V.M., Davis R.A., Feng Y., Xue Y., Oster L., Fex T., Deinum J., Hooper J.N., Quinn R.J.
      J. Med. Chem. 51:3583-3587(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 388-625 IN COMPLEX WITH INHIBITOR, DISULFIDE BONDS.
    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: VARIANT FA11D ASN-266, VARIANT ARG-244.
    20. "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] [Europe PMC] [Abstract]
      Cited for: VARIANT FA11D CYS-246.
    21. "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] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D CYS-326; VAL-430 ILE-493 AND ARG-594.
    22. Cited for: VARIANTS LEU-66; ARG-244; PHE-308 AND PHE-339.
    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] [Europe PMC] [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.
    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] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D VAL-418 AND SER-587, CHARACTERIZATION OF VARIANTS FA11D 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] [Europe PMC] [Abstract]
      Cited for: VARIANT FA11D 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] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D PHE-46; ARG-101; CYS-151; GLU-263; VAL-430; LEU-538; LYS-565 AND SER-618.
    27. "Identification of five novel mutations in the factor XI gene (F11) of patients with factor XI deficiency."
      Quelin F., Mathonnet F., Potentini-Esnault C., Trigui N., Peynet J., Bastenaire B., Guillon L., Bigel M.L., Sauger A., Mazurier C., de Mazancourt P.
      Blood Coagul. Fibrinolysis 17:69-73(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D TYR-140; LYS-315 AND LYS-597.
    28. "Seven novel point mutations in the F11 gene in Iranian FXI-deficient patients."
      Fard-Esfahani P., Lari G.R., Ravanbod S., Mirkhani F., Allahyari M., Rassoulzadegan M., Ala F.
      Haemophilia 14:91-95(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D ILE-51; PRO-51; ILE-331; PRO-360; PRO-503 AND HIS-608.
    29. "Population-specific spectrum of the F11 mutations in Koreans: evidence for a founder effect."
      Kim J., Song J., Lyu C., Kim Y., Oh S., Choi Y., Yoo J., Choi J., Kim H., Lee K.A.
      Clin. Genet. 82:180-186(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D ARG-32; GLN-53; THR-252; ARG-401 AND GLU-526.
    30. "Three dominant-negative mutations in factor XI-deficient patients."
      Dai L., Rangarajan S., Mitchell M.
      Haemophilia 17:E919-E922(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D THR-43; LEU-241 AND MET-403, CHARACTERIZATION OF VARIANTS FA11D THR-43; LEU-241 AND MET-403.
    31. "A novel missense mutation Asp506Gly in exon 13 of the F11 gene in an asymptomatic Korean woman with mild factor XI deficiency."
      Lee J.H., Cho H.S., Hyun M.S., Kim H.Y., Kim H.J.
      Korean J. Lab. Med. 31:290-293(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA11D GLY-506.
    32. "Identification of a novel F11 missense mutation (Ile463Ser) in a family with congenital factor XI deficiency."
      Tirefort Y., Uhr M.R., Neerman-Arbez M., de Moerloose P.
      Blood Coagul. Fibrinolysis 23:251-252(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA11D SER-481.
    33. "A cluster of factor XI-deficient patients due to a new mutation (Ile 436 Lys) in northeastern Italy."
      Girolami A., Scarparo P., Bonamigo E., Santarossa L., Cristiani A., Moro S., Lombardi A.M.
      Eur. J. Haematol. 88:229-236(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA11D LYS-454.
    34. "Revisiting the molecular epidemiology of factor XI deficiency: nine new mutations and an original large 4qTer deletion in western Brittany (France)."
      Gueguen P., Chauvin A., Quemener-Redon S., Pan-Petesch B., Ferec C., Abgrall J.F., Le Marechal C.
      Thromb. Haemost. 107:44-50(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA11D PRO-51; ARG-56; VAL-63; TYR-222; GLN-228; CYS-276; ASP-277; PHE-514; LEU-575 AND LYS-597.

    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: October 1, 2014
    This is version 182 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

    External Data

    Dasty 3